Datasets:
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Sequence
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35.2k
EC number
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118
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Cofactor
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1.77k
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Gene Ontology (biological process)
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11.3k
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Gene Ontology (molecular function)
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2.09k
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Pfam
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232
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Gene3D
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250
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Protein families
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Post-translational modification
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8.52k
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Subcellular location [CC]
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6.18k
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Catalytic activity
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Pathway
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908
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pH dependence
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955
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Temperature dependence
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Function [CC]
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196
O60487
MPZL2_HUMAN
MYGKSSTRAVLLLLGIQLTALWPIAAVEIYTSRVLEAVNGTDARLKCTFSSFAPVGDALTVTWNFRPLDGGPEQFVFYYHIDPFQPMSGRFKDRVSWDGNPERYDASILLWKLQFDDNGTYTCQVKNPPDVDGVIGEIRLSVVHTVRFSEIHFLALAIGSACALMIIIVIVVVLFQHYRKKRWAERAHKVVEIKSKEEERLNQEKKVSVYLEDTD
null
null
anatomical structure morphogenesis [GO:0009653]; cell-cell adhesion [GO:0098609]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]
cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]
null
PF07686;
2.60.40.10;
Myelin P0 protein family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Mediates homophilic cell-cell adhesion.
Homo sapiens (Human)
O60488
ACSL4_HUMAN
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLP...
6.2.1.15; 6.2.1.3
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
embryonic process involved in female pregnancy [GO:0060136]; fatty acid metabolic process [GO:0006631]; 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]; long-chain fatty-acyl-...
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; lipid droplet [GO:0005811]; membrane [GO:0016020]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; mitochondrial outer membrane [GO:0005741]; peroxisomal memb...
arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; palmitoyl-CoA ligase activity [GO:0090433]; very long-chain fatty acid-CoA ligase activity [GO:0031957]
PF00501;
3.30.300.30;3.40.50.12780;
ATP-dependent AMP-binding enzyme family
null
SUBCELLULAR 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 memb...
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:21242590, ECO:0000269|PubM...
null
null
null
null
FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:21242590, PubMed:22633490, PubMed:24269233). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:21242590). Preferent...
Homo sapiens (Human)
O60493
SNX3_HUMAN
MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRQLPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA
null
null
endocytic recycling [GO:0032456]; intralumenal vesicle formation [GO:0070676]; late endosome to Golgi transport [GO:0034499]; membrane invagination [GO:0010324]; negative regulation of early endosome to late endosome transport [GO:2000642]; negative regulation of phagocytosis [GO:0050765]; negative regulation of protei...
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]; retromer complex [GO:0030904]
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]; retromer complex binding [GO:1905394]
PF00787;
3.30.1520.10;
Sorting nexin family
PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10 (By similarity). {ECO:0000250|UniProtKB:O70492}.
SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:11433298, ECO:0000269|PubMed:21725319, ECO:0000269|PubMed:30213940}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:23237080}. Note=Colocalizes to clathrin-coated endosomal vesicles morphologically distinct from retromer-decorated non-branched endosomal tubul...
null
null
null
null
null
FUNCTION: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (By...
Homo sapiens (Human)
O60494
CUBN_HUMAN
MMNMSLPFLWSLLTLLIFAEVNGEAGELELQRQKRSINLQQPRMATERGNLVFLTGSAQNIEFRTGSLGKIKLNDEDLSECLHQIQKNKEDIIELKGSAIGLPQNISSQIYQLNSKLVDLERKFQGLQQTVDKKVCSSNPCQNGGTCLNLHDSFFCICPPQWKGPLCSADVNECEIYSGTPLSCQNGGTCVNTMGSYSCHCPPETYGPQCASKYDDCEGGSVARCVHGICEDLMREQAGEPKYSCVCDAGWMFSPNSPACTLDRDECSFQPGPCSTLVQCFNTQGSFYCGACPTGWQGNGYICEDINECEINNGGCSVAP...
null
null
cholesterol metabolic process [GO:0008203]; cobalamin metabolic process [GO:0009235]; cobalamin transport [GO:0015889]; establishment of localization in cell [GO:0051649]; lipoprotein transport [GO:0042953]; receptor-mediated endocytosis [GO:0006898]; response to bacterium [GO:0009617]; tissue homeostasis [GO:0001894]
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; clathrin-coated pit [GO:0005905]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extrinsic component of external side of plasma membrane [GO:0031...
calcium ion binding [GO:0005509]; cargo receptor activity [GO:0038024]; cobalamin binding [GO:0031419]; protein homodimerization activity [GO:0042803]; signaling receptor activity [GO:0038023]
PF00431;PF00008;PF12947;PF07645;
2.10.25.10;2.60.120.290;
null
PTM: The precursor is cleaved by a trans-Golgi proteinase furin, removing a propeptide. {ECO:0000269|PubMed:9572993}.; PTM: N-glycosylated. {ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:20237569, ECO:0000269|PubMed:29402915}.
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q9JLB4}; Peripheral membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:29402915, ECO:0000269|PubMed:30523278}; Peripheral membrane protein {ECO:0000305, ECO:0000305|PubMed:30523278}. Membrane, coated pit {ECO:0...
null
null
null
null
null
FUNCTION: Endocytic receptor which plays a role in lipoprotein, vitamin and iron metabolism by facilitating their uptake (PubMed:10371504, PubMed:11606717, PubMed:11717447, PubMed:14576052, PubMed:9572993). Acts together with LRP2 to mediate endocytosis of high-density lipoproteins, GC, hemoglobin, ALB, TF and SCGB1A1....
Homo sapiens (Human)
O60496
DOK2_HUMAN
MGDGAVKQGFLYLQQQQTFGKKWRRFGASLYGGSDCALARLELQEGPEKPRRCEAARKVIRLSDCLRVAEAGGEASSPRDTSAFFLETKERLYLLAAPAAERGDWVQAICLLAFPGQRKELSGPEGKQSRPCMEENELYSSAVTVGPHKEFAVTMRPTEASERCHLRGSYTLRAGESALELWGGPEPGTQLYDWPYRFLRRFGRDKVTFSFEAGRRCVSGEGNFEFETRQGNEIFLALEEAISAQKNAAPATPQPQPATIPASLPRPDSPYSRPHDSLPPPSPTTPVPAPRPRGQEGEYAVPFDAVARSLGKNFRGILAV...
null
null
cell surface receptor signaling pathway [GO:0007166]; positive regulation of MAPK cascade [GO:0043410]; Ras protein signal transduction [GO:0007265]; signal transduction [GO:0007165]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
cytoplasm [GO:0005737]; cytosol [GO:0005829]
transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068]
PF02174;
2.30.29.30;
DOK family, Type A subfamily
PTM: On immunoreceptor stimulation, phosphorylated on C-terminal tyrosine residues. Phosphorylation on Tyr-345 is required for binding to the SH2 domain of NCK. Phosphorylation on both Tyr-271 and Tyr-299 is required for interaction with RASGAP. Phosphorylated on tyrosine residues by TEK/TIE2 (By similarity). {ECO:0000...
null
null
null
null
null
null
FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-...
Homo sapiens (Human)
O60499
STX10_HUMAN
MSLEDPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGDLQERKVFVERMREAVQEMKDHMVSPTAVAFLERNNREILAGKPAAQKSPSDLLDASAVSATSRYIEEQQATQQLIMDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSDRRQWCAIAVLVGVLLLVLILLFSL
null
null
Golgi vesicle transport [GO:0048193]; intracellular protein transport [GO:0006886]; regulation of protein localization [GO:0032880]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]
cytosol [GO:0005829]; endomembrane system [GO:0012505]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]; vesicle [GO:0031982]
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
PF05739;PF09177;
1.20.5.110;1.20.58.90;
Syntaxin family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}.
Homo sapiens (Human)
O60500
NPHN_HUMAN
MALGTTLRASLLLLGLLTEGLAQLAIPASVPRGFWALPENLTVVEGASVELRCGVSTPGSAVQWAKDGLLLGPDPRIPGFPRYRLEGDPARGEFHLHIEACDLSDDAEYECQVGRSEMGPELVSPRVILSILVPPKLLLLTPEAGTMVTWVAGQEYVVNCVSGDAKPAPDITILLSGQTISDISANVNEGSQQKLFTVEATARVTPRSSDNRQLLVCEASSPALEAPIKASFTVNVLFPPGPPVIEWPGLDEGHVRAGQSLELPCVARGGNPLATLQWLKNGQPVSTAWGTEHTQAVARSVLVMTVRPEDHGAQLSCEAH...
null
null
cell-cell adhesion [GO:0098609]; gene expression [GO:0010467]; glomerular basement membrane development [GO:0032836]; JNK cascade [GO:0007254]; myoblast fusion [GO:0007520]; podocyte development [GO:0072015]; positive regulation of actin filament polymerization [GO:0030838]; protein localization to synapse [GO:0035418]...
cell projection [GO:0042995]; cell-cell junction [GO:0005911]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; slit diaphragm [GO:0036057]
cell adhesion molecule binding [GO:0050839]; myosin binding [GO:0017022]
PF08205;PF00041;PF07679;PF13927;PF07686;
2.60.40.10;
Immunoglobulin superfamily
PTM: Phosphorylated at Tyr-1193 by FYN, leading to the recruitment and activation of phospholipase C-gamma-1/PLCG1 (By similarity). Tyrosine phosphorylation is reduced by high glucose levels (PubMed:28955049). Dephosphorylated by tensin TNS2 which leads to reduced binding of NPHN1 to PIK3R1 (PubMed:28955049). {ECO:0000...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly located at podocyte slit diaphragm between podocyte foot processes. Also associated with podocyte apical plasma membrane. {ECO:0000269|PubMed:10393930, ECO:0000269|PubMed:10550324}.
null
null
null
null
null
FUNCTION: Seems to play a role in the development or function of the kidney glomerular filtration barrier. Regulates glomerular vascular permeability. May anchor the podocyte slit diaphragm to the actin cytoskeleton. Plays a role in skeletal muscle formation through regulation of myoblast fusion (By similarity). {ECO:0...
Homo sapiens (Human)
O60502
OGA_HUMAN
MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEA...
3.2.1.169
null
glycoprotein catabolic process [GO:0006516]; glycoprotein metabolic process [GO:0009100]; N-acetylglucosamine metabolic process [GO:0006044]; protein deglycosylation [GO:0006517]; protein O-linked glycosylation [GO:0006493]
cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]
[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity [GO:0102167]; [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity [GO:0102571]; [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity [GO:...
PF07555;
3.40.630.30;3.20.20.80;
Glycosyl hydrolase 84 family
PTM: Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity. {ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680}.
SUBCELLULAR 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}.
CATALYTIC ACTIVITY: Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:48876, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:90838, ChEBI:CHEBI:506227; EC=3.2.1.169; Evidence={ECO:0000269|PubMed:1...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 mM for pNP-GlcNAc {ECO:0000269|PubMed:11788610}; Vmax=652 umol/min/mg enzyme with pNP-GLcNAc as substrate {ECO:0000269|PubMed:11788610};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.7-7. {ECO:0000269|PubMed:11148210};
null
FUNCTION: [Isoform 1]: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins (PubMed:11148210, PubMed:11788610, PubMed:20673219, PubMed:22365600, PubMed:24088714, PubMed:28939839). Deglycosylates a large and diverse number of proteins, such as CRYAB, ELK1, LMNB1 and TAB1 (PubMed:28939839). Can use p-nitrophenyl-be...
Homo sapiens (Human)
O60503
ADCY9_HUMAN
MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDSGGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYALFYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALTLLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHLPLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFVMSQVRSRSTFLKVGQSIMHG...
4.6.1.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P30803}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P30803}; Note=Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP biosynthetic process [GO:0006171]; in utero embryonic development [GO:0001701]; intracellular signal transduction [GO:0035556]; signal transductio...
axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; plasma membrane [GO:0005886]
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]
PF00211;
3.30.70.1230;
Adenylyl cyclase class-4/guanylyl cyclase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:9628827}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952, ECO:0000269|PubMed:15879435, ECO:0000269|PubMed:9628827};
null
null
null
null
FUNCTION: Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors (PubMed:10987815, PubMed:12972952, PubMed:15879435, PubMed:9628827). Contributes to signaling cascades activated by CRH (corticotropin-releasing factor), corticosteroids and be...
Homo sapiens (Human)
O60504
VINEX_HUMAN
MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCNGGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVKYEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQQRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEESWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSPKSSPAPRRAPEQRPPAGPAS...
null
null
cell adhesion [GO:0007155]; cell-substrate adhesion [GO:0031589]; MAPK cascade [GO:0000165]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cytoskeleton organization [GO:0051495]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of stress fiber assemb...
cell-substrate junction [GO:0030055]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]
structural constituent of cytoskeleton [GO:0005200]; vinculin binding [GO:0017166]
PF00018;PF14604;PF02208;
2.30.30.40;
null
PTM: Phosphorylated at Ser-530 by MAPK1/ERK2 during cell spreading. {ECO:0000250}.
SUBCELLULAR 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 juncti...
null
null
null
null
null
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.
Homo sapiens (Human)
O60506
HNRPQ_HUMAN
MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTV...
null
null
cellular response to type II interferon [GO:0071346]; CRD-mediated mRNA stabilization [GO:0070934]; mRNA modification [GO:0016556]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900152]; negative regulation of nuclear-t...
catalytic step 2 spliceosome [GO:0071013]; CRD-mediated mRNA stability complex [GO:0070937]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; GAIT complex [GO:0097452]; histone pre-mRNA 3'end processing complex [GO:0071204]; mCRD-mediated mRNA stability complex [GO:0106002]; membrane [GO:0016020]; mRNA editing...
mRNA 5'-UTR binding [GO:0048027]; RNA binding [GO:0003723]
PF18360;PF00076;
3.30.70.330;
null
PTM: Phosphorylated on tyrosine. The membrane-bound form found in microsomes is phosphorylated in vitro by insulin receptor tyrosine kinase (INSR). Phosphorylation is inhibited upon binding to RNA, whereas the cytoplasmic form is poorly phosphorylated (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:35538151}. Microsome {ECO:0000250|UniProtKB:Q7TMK9}. Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000250|UniProtKB:Q7TMK9}. Note=The tyrosine phosphorylated form bound to RNA ...
null
null
null
null
null
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 t...
Homo sapiens (Human)
O60507
TPST1_HUMAN
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPVKLESTRTTVRTGLDLKANKTFAYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKEKIRLDEAGVTDEVLDSAMQAFLLEIIVKHGEPAPYLCNKDPFALKSLTYLSRLFPNAKFLLMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLQIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALSKWVGKIPPDVLQDMAVIAPM...
2.8.2.20
null
3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; post-translational protein modification [GO:0043687]
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
protein homodimerization activity [GO:0042803]; protein-tyrosine sulfotransferase activity [GO:0008476]
PF13469;
3.40.50.300;
Protein sulfotransferase family
PTM: N-glycosylated. {ECO:0000269|PubMed:16859706, ECO:0000269|PubMed:9501187}.
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:16859706, ECO:0000269|PubMed:25660941}; Single-pass type II membrane protein {ECO:0000269|PubMed:25660941, ECO:0000305|PubMed:16859706}.
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]; Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20...
null
null
null
null
FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000269|PubMed:28821720, ECO:0000269|PubMed:9501187, ECO:0000269|PubMed:9733778}.
Homo sapiens (Human)
O60508
PRP17_HUMAN
MSAAIAALAASYGSGSGSESDSDSESSRCPLPAADSLMHLTKSPSSKPSLAVAVDSAPEVAVKEDLETGVHLDPAVKEVQYNPTYETMFAPEFGPENPFRTQQMAAPRNMLSGYAEPAHINDFMFEQQRRTFATYGYALDPSLDNHQVSAKYIGSVEEAEKNQGLTVFETGQKKTEKRKKFKENDASNIDGFLGPWAKYVDEKDVAKPSEEEQKELDEITAKRQKKGKQEEEKPGEEKTILHVKEMYDYQGRSYLHIPQDVGVNLRSTMPPEKCYLPKKQIHVWSGHTKGVSAVRLFPLSGHLLLSCSMDCKIKLWEVYG...
null
null
embryonic brain development [GO:1990403]; mRNA splicing, via spliceosome [GO:0000398]
catalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; U2-type catalytic step 2 spliceosome [GO:0071007]
mRNA binding [GO:0003729]; RNA binding [GO:0003723]
PF00400;
2.130.10.10;
null
PTM: Undergoes isomerization of the peptide bond between Gly-94 and Pro-95. The reaction is catalyzed by PPIL1. {ECO:0000269|PubMed:33220177}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154}. Nucleus speckle {ECO:0000269|PubMed:9830021}.
null
null
null
null
null
FUNCTION: Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:33220177). Plays an important role in embryonic brain development; this function does not require proline isomerization (PubMed:33220177). {ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, EC...
Homo sapiens (Human)
O60512
B4GT3_HUMAN
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMN...
2.4.1.-; 2.4.1.275; 2.4.1.38; 2.4.1.90
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
carbohydrate metabolic process [GO:0005975]; galactosylceramide biosynthetic process [GO:0006682]; glycosylation [GO:0070085]; protein glycosylation [GO:0006486]
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]
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]
PF02709;PF13733;
null
Glycosyltransferase 7 family
null
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Trans cisternae of Golgi stack.
CATALYTIC ACTIVITY: Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507; EC=2.4.1.38; Evidence={...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=63 uM for GlcNAc-B-S-pNP {ECO:0000269|PubMed:11588157}; KM=0.084 mM for UDP-galactose {ECO:0000269|PubMed:9405390}; KM=0.58 mM for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390}; KM=13.1 mM for D-GlcNAc {ECO:0000269|PubMed:9405390}; Vmax=64.35 pmol/min/mg enzyme...
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:11588157, ECO:0000269|PubMed:9405390}.
null
null
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:11588157, ECO:0000269|PubMed:9405390}.
Homo sapiens (Human)
O60513
B4GT4_HUMAN
MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEIPKAKEFMANFHKTLILGKGKTLTNEASTKKVELDNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYRPQECKALQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLEALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSREQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVFHTRDKGNEVNAERMKLLHQVSRVWRTDGLSSC...
2.4.1.-; 2.4.1.275; 2.4.1.90
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
carbohydrate metabolic process [GO:0005975]; glycosylation [GO:0070085]; keratan sulfate biosynthetic process [GO:0018146]; lactosylceramide biosynthetic process [GO:0001572]; membrane lipid metabolic process [GO:0006643]; protein glycosylation [GO:0006486]
extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
galactosyltransferase activity [GO:0008378]; metal ion binding [GO:0046872]; N-acetyllactosamine synthase activity [GO:0003945]; UDP-galactosyltransferase activity [GO:0035250]
PF02709;PF13733;
null
Glycosyltransferase 7 family
PTM: N-glycosylated. {ECO:0000269|PubMed:32827291}.
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:32827291}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:32827291}.
CATALYTIC ACTIVITY: Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP; Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227; EC=2.4.1.90; Evidence={ECO:0000269|PubMed:9792633}; Physiologi...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.031 mM for UDP-Gal {ECO:0000269|PubMed:9792633}; KM=238 uM for GlcNAc-B-S-pNP {ECO:0000269|PubMed:11588157}; KM=0.43 mM for SO3->6GlcNAc (6SGN) {ECO:0000269|PubMed:12511560}; KM=330 mM for GlcNAc {ECO:0000269|PubMed:12511560}; KM=0.11 mM for SO3 ->6GlcNAcbeta1->2...
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:12511560}.; PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:9792633}.
null
null
FUNCTION: Galactose (Gal) transferase involved in the synthesis of terminal N-acetyllactosamine (LacNac) unit present on glycan chains of glycoproteins and glycosphingolipids (PubMed:12511560, PubMed:17690104, PubMed:32827291, PubMed:9792633). Catalyzes the transfer of Gal residue via a beta1->4 linkage from UDP-Gal to...
Homo sapiens (Human)
O60516
4EBP3_HUMAN
MSTSTSCPIPGGRDQLPDCYSTTPGGTLYATTPGGTRIIYDRKFLLECKNSPIARTPPCCLPQIPGVTTPPTAPLSKLEELKEQETEEEIPDDAQFEMDI
null
null
negative regulation of translational initiation [GO:0045947]
cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; membrane [GO:0016020]; nucleus [GO:0005634]
eukaryotic initiation factor 4E binding [GO:0008190]; translation repressor activity [GO:0030371]
PF05456;
null
EIF4E-binding protein family
PTM: Phosphorylated. {ECO:0000269|PubMed:9593750}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22684010}. Nucleus {ECO:0000269|PubMed:22684010}.
null
null
null
null
null
FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: the hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repression of translation. In contrast, the hyperphosphorylated form dissociates from EIF4E, allo...
Homo sapiens (Human)
O60519
CRBL2_HUMAN
MDDSKVVGGKVKKPGKRGRKPAKIDLKAKLERSRQSARECRARKKLRYQYLEELVSSRERAICALREELEMYKQWCMAMDQGKIPSEIKALLTGEEQNKSQQNSSRHTKAGKTDANSNSW
null
null
cell cycle [GO:0007049]; cell differentiation [GO:0030154]; DNA-templated transcription [GO:0006351]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of glucose import [GO:0046326]; positive regulation of lipid biosynthet...
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]
PF07716;
1.20.5.170;
BZIP family, ATF subfamily
PTM: Phosphorylated by AMPK. {ECO:0000269|PubMed:18063805}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle. Identification in a chromosomal region frequently deleted in various cancers suggests that it might act as a tumor suppressor. {ECO:0000269|PubMed:9693048...
Homo sapiens (Human)
O60524
NEMF_HUMAN
MKSRFSTIDLRAVLAELNASLLGMRVNNVYDVDNKTYLIRLQKPDFKATLLLESGIRIHTTEFEWPKNMMPSSFAMKCRKHLKSRRLVSAKQLGVDRIVDFQFGSDEAAYHLIIELYDRGNIVLTDYEYVILNILRFRTDEADDVKFAVRERYPLDHARAAEPLLTLERLTEIVASAPKGELLKRVLNPLLPYGPALIEHCLLENGFSGNVKVDEKLETKDIEKVLVSLQKAEDYMKTTSNFSGKGYIIQKREIKPSLEADKPVEDILTYEEFHPFLFSQHSQCPYIEFESFDKAVDEFYSKIEGQKIDLKALQQEKQAL...
null
null
CAT tailing [GO:0140708]; nuclear export [GO:0051168]; protein-containing complex assembly [GO:0065003]; rescue of stalled ribosome [GO:0072344]; ribosome-associated ubiquitin-dependent protein catabolic process [GO:1990116]
cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; nucleus [GO:0005634]; RQC complex [GO:1990112]
alpha-aminoacyl-tRNA binding [GO:1904678]; ribosomal large subunit binding [GO:0043023]; tRNA binding [GO:0000049]
PF11923;PF05670;PF05833;
2.30.310.10;
NEMF family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25578875}. Nucleus {ECO:0000305|PubMed:16103875}.
null
null
null
null
null
FUNCTION: Key component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes as well as their ubiquitin-mediated proteasomal degradation (PubMed:25578875, PubMed:32726578, PubMed:33406423, PubMed:33909...
Homo sapiens (Human)
O60543
CIDEA_HUMAN
MEAARDYAGALIRPLTFMGSQTKRVLFTPLMHPARPFRVSNHDRSSRRGVMASSLQELISKTLDALVIATGLVTLVLEEDGTVVDTEEFFQTLGDNTHFMILEKGQKWMPGSQHVPTCSPPKRSGIARVTFDLYRLNPKDFIGCLNVKATMYEMYSVSYDIRCTGLKGLLRSLLRFLSYSAQVTGQFLIYLGTYMLRVLDDKEERPSLRSQAKGRFTCG
null
null
apoptotic process [GO:0006915]; cellular response to cold [GO:0070417]; lipid droplet fusion [GO:0160077]; lipid metabolic process [GO:0006629]; lipid storage [GO:0019915]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of cytokine production [GO:0001818]; negative regulation of exe...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; mitochondrial envelope [GO:0005740]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
lipid transfer activity [GO:0120013]; phosphatidic acid binding [GO:0070300]; protein homodimerization activity [GO:0042803]
PF02017;
3.10.20.10;
CIDE family
null
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18509062}. Nucleus {ECO:0000250|UniProtKB:O70302}. Note=Enriched at lipid droplet contact sites. {ECO:0000269|PubMed:18509062}.
CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out); Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615; Evidence={ECO:0000250|UniProtKB:O70302};
null
null
null
null
FUNCTION: Lipid transferase that promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed:19843876, PubMed:26118629). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:19843876). Localizes on the lipid droplet surface, at focal contact...
Homo sapiens (Human)
O60547
GMDS_HUMAN
MAHAPARCPSARGSGDGEMGKPRNVALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTGRIEHLYKNPQAHIEGNMKLHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDLAEYTADVDGVGTLRLLDAVKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATGEVHSVREFVEKSFLHIGKTIVWEGKNENEVGRCKETGKVHVTVD...
4.2.1.47
COFACTOR: Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000269|Ref.9};
'de novo' GDP-L-fucose biosynthetic process [GO:0042351]; GDP-mannose metabolic process [GO:0019673]; Notch signaling pathway [GO:0007219]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]
GDP-mannose 4,6-dehydratase activity [GO:0008446]; identical protein binding [GO:0042802]; NADP+ binding [GO:0070401]
PF16363;
3.40.50.720;3.90.25.10;
NAD(P)-dependent epimerase/dehydratase family, GDP-mannose 4,6-dehydratase subfamily
null
null
CATALYTIC ACTIVITY: Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O; Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527, ChEBI:CHEBI:57964; EC=4.2.1.47; Evidence={ECO:0000269|PubMed:9525924}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23821; Evidence={ECO:0000305|PubMed:9525924};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=80 uM for GDP-mannose {ECO:0000269|PubMed:9525924}; Vmax=0.11 umol/min/mg enzyme {ECO:0000269|PubMed:9525924};
PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2. {ECO:0000305|PubMed:9525924}.
null
null
FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose. {ECO:0000269|PubMed:9525924, ECO:0000269|PubMed:9603974}.
Homo sapiens (Human)
O60548
FOXD2_HUMAN
MTLGSCCCEIMSSESSPAALSEADADIDVVGGGSGGGELPARSGPRAPRDVLPHGHEPPAEEAEADLAEDEEESGGCSDGEPRALASRGAAAAAGSPGPGAAAARGAAGPGPGPPSGGAATRSPLVKPPYSYIALITMAILQSPKKRLTLSEICEFISGRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPESADMFDNGSFLRRRKRFKRQPLPPPHPHPHPHPELLLRGGAAAAGDPGAFLPGFAAYGAYGYGYGLALPAYGAPPPGPAPHPHPHPHAFAFAAAAAAAPCQLSVPPGRAAAPPP...
null
null
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-...
PF00250;
1.10.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
null
null
null
null
null
FUNCTION: Probable transcription factor involved in embryogenesis and somatogenesis. {ECO:0000250}.
Homo sapiens (Human)
O60551
NMT2_HUMAN
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPNSGGTKSDSASDSQEIKIQQPSKNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFSHLSRNM...
2.3.1.-; 2.3.1.97
null
intracellular transport of virus [GO:0075733]; N-terminal peptidyl-glycine N-myristoylation [GO:0018008]; regulation of rhodopsin mediated signaling pathway [GO:0022400]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; host cell [GO:0043657]; plasma membrane [GO:0005886]
glycylpeptide N-tetradecanoyltransferase activity [GO:0004379]; peptidyl-lysine N6-myristoyltransferase activity [GO:0018030]
PF01233;PF02799;
3.40.630.170;
NMT family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9506952}. Membrane {ECO:0000269|PubMed:9506952}; Peripheral membrane protein {ECO:0000269|PubMed:9506952}.
CATALYTIC ACTIVITY: Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723, ChEBI:CHEBI:133050; EC=2.3.1.97; Evidence={ECO:000026...
null
null
null
null
FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins (PubMed:25255805, PubMed:9506952). Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' (PubMed:32103017). Lysine myristoylation is require...
Homo sapiens (Human)
O60563
CCNT1_HUMAN
MEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFPGNSVAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHEFLQILEKTPNRLKRIWNWRACEAAKKTKADDRGTDEKTSEQTILNMISQSSSDTTIAGLMSMSTSTTSAVPSLPVSEESS...
null
null
cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RN...
cyclin/CDK positive transcription elongation factor complex [GO:0008024]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-TEFb complex [GO:0070691]
7SK snRNA binding [GO:0097322]; chromatin binding [GO:0003682]; cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; molecular condensate scaffold activity [GO:0140693]; protein kinase binding [GO:0019901]; RNA...
PF00134;PF21797;
1.10.472.10;
Cyclin family, Cyclin C subfamily
PTM: ADP-ribosylation on serine residues by PARP1 in response to DNA damage disrupts the phase separation activity of CCNT1, thereby preventing activation of CDK9. {ECO:0000269|PubMed:35393539}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944466, ECO:0000269|PubMed:29849146}.
null
null
null
null
null
FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) 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 (RN...
Homo sapiens (Human)
O60565
GREM1_HUMAN
MSRTAYTVGALLLLLGTLLPAAEGKKKGSQGAIPPPDKAQHNDSEQTQSPQQPGSRNRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD
null
null
animal organ morphogenesis [GO:0009887]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [GO:0060379]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell morphogenesis [GO:0000902]; cell-cell signaling [GO:0007267]; collagen fibril organization [GO:003019...
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; morphogen activity [GO:0016015]; protein homodimerization activity [GO:0042803]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; vascular endothelial growth factor receptor 2 binding [GO:0043...
PF03045;
2.10.90.10;
DAN family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: 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 (By similarity). Antagonist of BMP2;...
Homo sapiens (Human)
O60566
BUB1B_HUMAN
MAAVKKEGGALSEAMSLEGDEWELSKENVQPLRQGRIMSTLQGALAQESACNNTLQQQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPLDMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGIQQKAEPLERLQSQHRQFQARVSRQTLLALEKEEEEEVFESSVPQRSTLAELKSKGKKTARAPIIRVGGALKAPSQNRGLQNPFPQQMQNNSRITVFDENADEASTAELSKPTVQPWIAPPMPRAKENELQAGPWNTGRSLE...
2.7.11.1
null
apoptotic process [GO:0006915]; cell division [GO:0051301]; meiotic sister chromatid cohesion, centromeric [GO:0051754]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; mitotic spindle assembly checkpoint signaling [GO:0007094]; phosphorylation [GO:0016310]; protein localization to chromosome, centrom...
anaphase-promoting complex [GO:0005680]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinetochore [GO:0000776]; mitotic checkpoint complex [GO:0033597]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF08311;
1.25.40.430;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, BUB1 subfamily
PTM: Proteolytically cleaved by caspase-3 in a cell cycle specific manner. The cleavage might be involved in the durability of the cell cycle delay. Caspase-3 cleavage is associated with abrogation of the mitotic checkpoint. The major site of cleavage is at Asp-610. {ECO:0000269|PubMed:16227576}.; PTM: Acetylation at L...
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 KNL1.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
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 b...
Homo sapiens (Human)
O60568
PLOD3_HUMAN
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLL...
1.14.11.4; 2.4.1.50; 2.4.1.66
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:30089812, ECO:0000269|PubMed:9724729}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:30089812, ECO:0000269|PubMed:9724729}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:30089812}...
basement membrane assembly [GO:0070831]; collagen fibril organization [GO:0030199]; collagen metabolic process [GO:0032963]; endothelial cell morphogenesis [GO:0001886]; epidermis morphogenesis [GO:0048730]; hydroxylysine biosynthetic process [GO:0046947]; in utero embryonic development [GO:0001701]; lung morphogenesis...
collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; rough endoplasmic reticulum [GO:0005791]; ...
iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; metal ion binding [GO:0046872]; procollagen galactosyltransferase activity [GO:0050211]; procollagen glucosyltransferase activity [GO:0033823]; procollagen-lysine 5-dioxygenase activity [GO:0008475]; small molecule binding [GO:0036094]
PF03171;
2.60.120.620;
null
null
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000269|PubMed:10934207}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:20470363}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9R0E1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9R0E1}; Lumenal side {ECO:0000250|UniProtKB:Q9R0E1}. Secreted {EC...
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4; ...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=35 uM for UDP-galactose {ECO:0000269|PubMed:12475640}; KM=17 uM for UDP-glucose {ECO:0000269|PubMed:12475640}; KM=100 uM for 2-oxoglutarate {ECO:0000269|PubMed:11956192, ECO:0000269|PubMed:9724729}; KM=300 uM for ascorbate {ECO:0000269|PubMed:9724729}; KM=350 uM fo...
null
null
null
FUNCTION: Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen (PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- seque...
Homo sapiens (Human)
O60573
IF4E2_HUMAN
MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP
null
null
miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; negative regulation of translation [GO:0017148]; negative regulation of translational initiation [GO:0045947]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; rescue of stalled ribosome [GO:0072344]; translational...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; P-body [GO:0000932]
mRNA cap binding [GO:0098808]; RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; RNA cap binding [GO:0000339]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]; ubiquitin protein ligase binding [GO:0031625]
PF01652;
3.30.760.10;
Eukaryotic initiation factor 4E family
PTM: Ubiquitinated by ARIH1 (PubMed:14623119, PubMed:25624349). The consequences of ubiquitination are however unclear: according to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report ubiquitination leads to its subsequent de...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23991149}. Cytoplasm, P-body {ECO:0000269|PubMed:23991149}.
null
null
null
null
null
FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation (PubMed:17368478, PubMed:22751931, PubMed:25624349, PubMed:33581076, PubMed:9582349). In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3)...
Homo sapiens (Human)
O60583
CCNT2_HUMAN
MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKNIISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNI...
null
null
cell cycle [GO:0007049]; cell division [GO:0051301]; early viral transcription [GO:0019085]; late viral transcription [GO:0019086]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription by RNA po...
cyclin/CDK positive transcription elongation factor complex [GO:0008024]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
7SK snRNA binding [GO:0097322]; chromatin binding [GO:0003682]; cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; protein kinase binding [GO:0019901]; RNA polymerase binding [GO:0070063]; transcription coactivator binding [GO:0001223]
PF00134;PF21797;
1.10.472.10;
Cyclin family, Cyclin C subfamily
null
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TQK0}. Nucleus {ECO:0000250|UniProtKB:Q7TQK0}. Note=Nucleus in differentiating cells. {ECO:0000250|UniProtKB:Q7TQK0}.
null
null
null
null
null
FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RN...
Homo sapiens (Human)
O60602
TLR5_HUMAN
MGDHLDLLLGVVLMAGPVFGIPSCSFDGRIAFYRFCNLTQVPQVLNTTERLLLSFNYIRTVTASSFPFLEQLQLLELGSQYTPLTIDKEAFRNLPNLRILDLGSSKIYFLHPDAFQGLFHLFELRLYFCGLSDAVLKDGYFRNLKALTRLDLSKNQIRSLYLHPSFGKLNSLKSIDFSSNQIFLVCEHELEPLQGKTLSFFSLAANSLYSRVSVDWGKCMNPFRNMVLEILDVSGNGWTVDITGNFSNAISKSQAFSLILAHHIMGAGFGFHNIKDPDQNTFAGLARSSVRHLDLSHGFVFSLNSRVFETLKDLKVLNLA...
null
null
cellular response to mechanical stimulus [GO:0071260]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of interleukin-8 production [GO:0032757]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor signaling pathway [GO:0002224]
plasma membrane [GO:0005886]
interleukin-1 receptor binding [GO:0005149]; pattern recognition receptor activity [GO:0038187]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]
PF00560;PF13855;PF01582;
3.80.10.10;3.40.50.10140;
Toll-like receptor family
PTM: Phosphorylated at Ser-805 by PKD/PRKD1; phosphorylation induces the production of inflammatory cytokines. {ECO:0000269|PubMed:17157808, ECO:0000269|PubMed:17442957}.; PTM: Phosphorylated at Tyr-798 upon flagellin binding; required for signaling. {ECO:0000269|PubMed:17157808, ECO:0000269|PubMed:17442957}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24778236}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Pattern recognition receptor (PRR) located on the cell surface that participates in the activation of innate immunity and inflammatory response (PubMed:11323673, PubMed:18490781). Recognizes small molecular motifs named pathogen-associated molecular pattern (PAMPs) expressed by pathogens and microbe-associate...
Homo sapiens (Human)
O60603
TLR2_HUMAN
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIP...
null
null
apoptotic process [GO:0006915]; cellular response to bacterial lipopeptide [GO:0071221]; cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; cellular response to type II interferon [GO:00713...
cell body [GO:0044297]; cell projection [GO:0042995]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; secretory granule membrane [GO:0030667]; Toll-like rec...
amyloid-beta binding [GO:0001540]; identical protein binding [GO:0042802]; lipopolysaccharide binding [GO:0001530]; lipopolysaccharide immune receptor activity [GO:0001875]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; pattern recognition receptor activity [GO:0038187]; peptidoglycan binding [GO:004283...
PF00560;PF13855;PF01463;PF01582;
3.80.10.10;3.40.50.10140;
Toll-like receptor family
PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000269|PubMed:15173186, ECO:0000269|PubMed:17889651}.; PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation (PubMed:27805901). Deubiquitinated by USP2 (By similarity). {ECO:0000250|UniProtKB:Q9QUN7, ECO:0...
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:16880211}. Note=Does not reside in lipid rafts be...
null
null
null
null
null
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides (PubMed:17889651, PubMed:21078852). Acts via MYD88 and TRAF6, leading to N...
Homo sapiens (Human)
O60609
GFRA3_HUMAN
MVRPLNPRPLPPVVLMLLLLLPPSPLPLAAGDPLPTESRLMNSCLQARRKCQADPTCSAAYHHLDSCTSSISTPLPSEEPSVPADCLEAAQQLRNSSLIGCMCHRRMKNQVACLDIYWTVHRARSLGNYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLNDKCDRLRKAYGEACSGPHCQRHVCLRQLLTFFEKAAEPHAQGLLLCPCAPNDRGCGERRRNTIAPNCALPPVAPNCLELRRLCFSDPLCRSRLVDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFVSNVNTSVALSCTCRG...
null
null
glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; nervous system development [GO:0007399]; neuron migration [GO:0001764]; peripheral nervous system development [GO:0007422]; signal transduction [GO:0007165]; sympathetic nervous system development [GO:0048485]
cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extrinsic component of membrane [GO:0019898]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
axon guidance receptor activity [GO:0008046]; glial cell-derived neurotrophic factor receptor activity [GO:0016167]; signaling receptor activity [GO:0038023]; signaling receptor binding [GO:0005102]
PF02351;
1.10.220.110;
GDNFR family
PTM: N-glycosylated. {ECO:0000269|PubMed:16765900}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9576965}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:9576965}.
null
null
null
null
null
FUNCTION: Receptor for artemin (ARTN), a growth factor that supports the survival of sensory and sympathetic peripheral neurons (PubMed:31535977, PubMed:9883723). ARTN-binding leads to autophosphorylation and activation of the RET receptor (PubMed:31535977, PubMed:9883723). {ECO:0000269|PubMed:31535977, ECO:0000269|Pub...
Homo sapiens (Human)
O60610
DIAP1_HUMAN
MEPPGGSLGPGRGTRDKKKGRSPDELPSAGGDGGKSKKFTLKRLMADELERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYTSKAGMSQKESSKSAMMYIQELRSGLRDMPLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETAGSYDSRNKHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTTIALKVGCLQLINA...
null
null
actin cytoskeleton organization [GO:0030036]; 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 cytoskeleton organization [GO:0051493]; re...
actin filament [GO:0005884]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; ficolin-1-rich granule membrane [GO:0101003]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; secretory granule membrane [GO:0030667]
actin binding [GO:0003779]; RNA binding [GO:0003723]; signaling receptor binding [GO:0005102]; small GTPase binding [GO:0031267]; transmembrane transporter binding [GO:0044325]
PF06346;PF06367;PF06371;PF02181;
1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10;
Formin homology family, Diaphanous subfamily
PTM: Phosphorylation at Thr-768 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement. {ECO:0000269|PubMed:23325789}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08808}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O08808}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24781755}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24781755}. Cytoplasm, cytoskeleton, spindle {...
null
null
null
null
null
FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (By similarity). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (By similarity). Required for cytokinesis, and transcriptional ...
Homo sapiens (Human)
O60613
SEP15_HUMAN
MVAMAAGPSGCLVPAFGLRLLLATVLQAVSAFGAEFSSEACRELGFSSNLLCSSCDLLGQFNLLQLDPDCRGCCQEEAQFETKKLYAGAILEVCGUKLGRFPQVQAFVRSDKPKLFRGLQIKYVRGSDPVLKLLDDNGNIAEELSILKWNTDSVEEFLSEKLERI
null
null
'de novo' post-translational protein folding [GO:0051084]; sperm DNA condensation [GO:0035092]
endoplasmic reticulum lumen [GO:0005788]
oxidoreductase activity [GO:0016491]; selenium binding [GO:0008430]; thioredoxin peroxidase activity [GO:0008379]
PF08806;
3.40.30.50;
Selenoprotein M/F family
PTM: The N-terminus is blocked.
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:11278576}. Note=The association with UGGT1/UGCGL1 is essential for its retention in the endoplasmic reticulum.
null
null
null
null
null
FUNCTION: May be involved in redox reactions associated with the formation of disulfide bonds (By similarity). May contribute to the quality control of protein folding in the endoplasmic reticulum (PubMed:24415556). May regulate protein folding by enhancing the catalytic activity of UGGT1/UGCGL1 and UGGT2/UGCGL2 (PubMe...
Homo sapiens (Human)
O60635
TSN1_HUMAN
MQCFSFIKTMMILFNLLIFLCGAALLAVGIWVSIDGASFLKIFGPLSSSAMQFVNVGYFLIAAGVVVFALGFLGCYGAKTESKCALVTFFFILLLIFIAEVAAAVVALVYTTMAEHFLTLLVVPAIKKDYGSQEDFTQVWNTTMKGLKCCGFTNYTDFEDSPYFKENSAFPPFCCNDNVTNTANETCTKQKAHDQKVEGCFNQLLYDIRTNAVTVGGVAAGIGGLELAAMIVSMYLYCNLQ
null
null
protein stabilization [GO:0050821]
cell junction [GO:0030054]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; vesicle [GO:0031982...
null
PF00335;
1.10.1450.10;
Tetraspanin (TM4SF) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21836059, ECO:0000269|PubMed:30291375}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19508227}; Multi-pass membrane protein {ECO:0000269|PubMed:19508227}.
null
null
null
null
null
FUNCTION: Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Participates thereby in diverse biological functions such as cell signal transduction, adhesion, migration and protein trafficking (PubMed...
Homo sapiens (Human)
O60636
TSN2_HUMAN
MGRFRGGLRCIKYLLLGFNLLFWLAGSAVIAFGLWFRFGGAIKELSSEDKSPEYFYVGLYVLVGAGALMMAVGFFGCCGAMRESQCVLGSFFTCLLVIFAAEVTTGVFAFIGKGVAIRHVQTMYEEAYNDYLKDRGKGNGTLITFHSTFQCCGKESSEQVQPTCPKELLGHKNCIDEIETIISVKLQLIGIVGIGIAGLTIFGMIFSMVLCCAIRNSRDVI
null
null
astrocyte development [GO:0014002]; axon development [GO:0061564]; inflammatory response [GO:0006954]; microglia development [GO:0014005]; myelination [GO:0042552]; oligodendrocyte differentiation [GO:0048709]
membrane [GO:0016020]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
null
PF00335;
1.10.1450.10;
Tetraspanin (TM4SF) family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: May play a role in signalling in oligodendrocytes in the early stages of their terminal differentiation into myelin-forming glia and may also function in stabilizing the mature sheath. {ECO:0000250}.
Homo sapiens (Human)
O60641
AP180_HUMAN
MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAK...
null
null
clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; protein transport [GO:0015031]; regulation of clathrin-dependent endocytosis [GO:2000369]; synaptic vesicle budding from presynaptic endocytic zone membrane [GO:0016185]
clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; extrinsic component of presynaptic endocytic zone membrane [GO:0098894]; synaptic vesicle [GO:0008021]
1-phosphatidylinositol binding [GO:0005545]; clathrin heavy chain binding [GO:0032050]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein kinase binding [GO:0019901]; SNARE binding [GO:0000149]
PF07651;
1.25.40.90;1.20.58.150;
PICALM/SNAP91 family
PTM: Thr-310 can be modified by the addition of N-acetylglucosamine which can be further phosphorylated. There is no evidence for direct Thr-310 phosphorylation (By similarity). {ECO:0000250}.
SUBCELLULAR 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}.
null
null
null
null
null
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 the...
Homo sapiens (Human)
O60645
EXOC3_HUMAN
MKETDREAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMYEQYRMDSGNTRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFTILERTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLIVAKNLMVQCFPPHYEIFKNLLNMYHQALS...
null
null
exocyst localization [GO:0051601]; exocytosis [GO:0006887]; membrane fission [GO:0090148]; mitotic cytokinesis [GO:0000281]; protein transport [GO:0015031]; vesicle docking involved in exocytosis [GO:0006904]; vesicle tethering involved in exocytosis [GO:0090522]
cytosol [GO:0005829]; exocyst [GO:0000145]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; midbody [GO:0030496]; perinuclear region of cytoplasm [GO:0048471]; presynaptic membrane [GO:0042734]; secretory granule membrane [GO:0030667]
cadherin binding [GO:0045296]; SNARE binding [GO:0000149]
PF06046;
1.10.357.50;1.10.357.70;
SEC6 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54921}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54921}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54921}. Midbody {ECO:0000269|PubMed:18756269}. Golgi apparatus {ECO:0000305|PubMed:18756269}. Cell projection, neuron projection {ECO:0000250...
null
null
null
null
null
FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Homo sapiens (Human)
O60656
UD19_HUMAN
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMPEVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLFFSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEGAQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVTEYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIA...
2.4.1.17
null
cellular glucuronidation [GO:0052695]; flavone metabolic process [GO:0051552]; flavonoid glucuronidation [GO:0052696]; liver development [GO:0001889]; negative regulation of cellular glucuronidation [GO:2001030]; negative regulation of fatty acid metabolic process [GO:0045922]; negative regulation of glucuronosyltransf...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
enzyme binding [GO:0019899]; enzyme inhibitor activity [GO:0004857]; glucuronosyltransferase activity [GO:0015020]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; retinoic acid binding [GO:0001972]
PF00201;
3.40.50.2000;
UDP-glycosyltransferase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17179145}; Single-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; Evidence={ECO:0000269|PubMed:12181437, ECO:0000269|PubMed:15470161...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4 uM for estrone (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; KM=17 uM for 2-hydroxy-17beta-estradiol (when assaying glucuronidation at position 2) {ECO:0000269|PubMed:15472229}; KM=24 uM for 2-hydroxy-17beta-estradiol (when assaying...
null
null
null
FUNCTION: [Isoform 1]: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:12181437, PubMed:15470161, P...
Homo sapiens (Human)
O60658
PDE8A_HUMAN
MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSGKKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGFTRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPVIGQGGKIRHYV...
3.1.4.53
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:18983167}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000269|PubMed:18983167};
cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; cellular response to epidermal growth factor stimulus [GO:0071364]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; regulation of DNA-templated transcription [GO:0006355]
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; protein kinase activator activity [GO:0030295]
PF00989;PF00233;
3.40.50.2300;1.10.1300.10;3.30.450.20;
Cyclic nucleotide phosphodiesterase family, PDE8 subfamily
PTM: Phosphorylated at Ser-359 by PKA under elevated cAMP conditions, this enhances catalytic activity. {ECO:0000269|PubMed:22673573}.
null
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000250|UniProtKB:O95263};
null
PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
null
null
FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (PubMed:18983167). May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development (PubMed:18983167). Binding to RAF1 reduces RAF1 'Ser-259' inhi...
Homo sapiens (Human)
O60662
KLH41_HUMAN
MDSQRELAEELRLYQSTLLQDGLKDLLDEKKFIDCTLKAGDKSLPCHRLILSACSPYFREYFLSEIDEAKKKEVVLDNVDPAILDLIIKYLYSASIDLNDGNVQDIFALASRFQIPSVFTVCVSYLQKRLAPGNCLAILRLGLLLDCPRLAISAREFVSDRFVQICKEEDFMQLSPQELISVISNDSLNVEKEEAVFEAVMKWVRTDKENRVKNLSEVFDCIRFRLMTEKYFKDHVEKDDIIKSNPDLQKKIKVLKDAFAGKLPEPSKNAAKTGAGEVNGDVGDEDLLPGYLNDIPRHGMFVKDLILLVNDTAAVAYDPT...
null
null
myofibril assembly [GO:0030239]; protein ubiquitination [GO:0016567]; pseudopodium assembly [GO:0031269]; regulation of myoblast differentiation [GO:0045661]; regulation of myoblast proliferation [GO:2000291]; regulation of skeletal muscle cell differentiation [GO:2001014]; skeletal muscle cell differentiation [GO:0035...
Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; M band [GO:0031430]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]; ruffle [GO:0001726]; sarcoplasmic reticulum membr...
null
PF07707;PF00651;PF01344;
1.25.40.420;2.120.10.80;
null
PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination. {ECO:0000269|PubMed:15983046}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19424503}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A2AUC9}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:Q9ER30}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9ER30}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:A2AUC9}. Sarcoplasmi...
null
null
null
null
null
FUNCTION: Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells. {ECO:0000250|U...
Homo sapiens (Human)
O60663
LMX1B_HUMAN
MDIATGPESLERCFPRGQTDCAKMLDGIKMEEHALRPGPATLGVLLGSDCPHPAVCEGCQRPISDRFLMRVNESSWHEECLQCAACQQALTTSCYFRDRKLYCKQDYQQLFAAKCSGCMEKIAPTEFVMRALECVYHLGCFCCCVCERQLRKGDEFVLKEGQLLCKGDYEKEKDLLSSVSPDESDSVKSEDEDGDMKPAKGQGSQSKGSGDDGKDPRRPKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLSVRVVQVWFQNQRAKMKKLARRHQQQQEQQNSQRLGQEVLSSRMEGMMASYTPLAPPQQQIV...
null
null
dopaminergic neuron differentiation [GO:0071542]; dorsal/ventral pattern formation [GO:0009953]; neuron differentiation [GO:0030182]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:00063...
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990...
PF00046;PF00412;
2.10.110.10;1.10.10.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: Transcription factor involved in the regulation of podocyte-expressed genes (PubMed:24042019, PubMed:28059119). Essential for the specification of dorsal limb fate at both the zeugopodal and autopodal levels. {ECO:0000269|PubMed:24042019, ECO:0000269|PubMed:28059119}.
Homo sapiens (Human)
O60664
PLIN3_HUMAN
MSADGAEADGSTQVTVEEPVQQPSVVDRVASMPLISSTCDMVSAAYASTKESYPHIKTVCDAAEKGVRTLTAAAVSGAQPILSKLEPQIASASEYAHRGLDKLEENLPILQQPTEKVLADTKELVSSKVSGAQEMVSSAKDTVATQLSEAVDATRGAVQSGVDKTKSVVTGGVQSVMGSRLGQMVLSGVDTVLGKSEEWADNHLPLTDAELARIATSLDGFDVASVQQQRQEQSYFVRLGSLSERLRQHAYEHSLGKLRATKQRAQEALLQLSQVLSLMETVKQGVDQKLVEGQEKLHQMWLSWNQKQLQGPEKEPPKPE...
null
null
cellular response to glucose starvation [GO:0042149]; lipid droplet disassembly [GO:1905691]; lipid storage [GO:0019915]; positive regulation of sequestering of triglyceride [GO:0010890]; vesicle-mediated transport [GO:0016192]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; lipid droplet [GO:0005811]; membrane [GO:0016020]; transport vesicle [GO:0030133]
cadherin binding [GO:0045296]
PF03036;
1.20.120.340;3.30.720.170;
Perilipin family
PTM: Phosphorylation at Tyr-251 by isoform 1 of CHKA (CHKalpha2) promotes dissociation from lipid droplets: dissociation is followed by recruitment of autophagosome machinery to lipid droplets and subsequent lipid droplet lipolysis. {ECO:0000269|PubMed:34077757}.
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:15545278, ECO:0000269|PubMed:34077757}. Endosome membrane {ECO:0000269|PubMed:15545278}; Peripheral membrane protein {ECO:0000269|PubMed:15545278}; Cytoplasmic side {ECO:0000269|PubMed:15545278}. Cytoplasm {ECO:0000269|PubMed:15545278, ECO:0000269|PubMed:26357594,...
null
null
null
null
null
FUNCTION: Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets (PubMed:34077757). Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network (PubMed:9590177). {ECO:0000269|PubMed:34077757, ECO:0000269|PubMe...
Homo sapiens (Human)
O60667
FCMR_HUMAN
MDFWLWPLYFLPVSGALRILPEVKVEGELGGSVTIKCPLPEMHVRIYLCREMAGSGTCGTVVSTTNFIKAEYKGRVTLKQYPRKNLFLVEVTQLTESDSGVYACGAGMNTDRGKTQKVTLNVHSEYEPSWEEQPMPETPKWFHLPYLFQMPAYASSSKFVTRVTTPAQRGKVPPVHHSSPTTQITHRPRVSRASSVAGDKPRTFLPSTTASKISALEGLLKPQTPSYNHHTRLHRQRALDYGSQSGREGQGFHILIPTILGLFLLALLGLVVKRAVERRKALSRRARRLAVRMRALESSQRPRGSPRPRSQNNIYSACPR...
null
null
cellular defense response [GO:0006968]; Fc receptor-mediated immune complex endocytosis [GO:0160006]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunoglobulin transcytosis in epithelial cells [GO:0002414]; negative regulation of apoptotic process [GO:0043066]; regulation of B cell rec...
early endosome membrane [GO:0031901]; extracellular region [GO:0005576]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]
high-affinity IgM receptor activity [GO:0002172]; IgM binding [GO:0001791]; polymeric immunoglobulin binding [GO:0001790]
PF07686;
2.60.40.10;
null
PTM: Phosphorylated on both Tyr and Ser residues. {ECO:0000269|PubMed:19858324}.; PTM: O-glycosylated. Sialylated. O-linked glycans regulate trafficking to the plasma membrane. {ECO:0000269|PubMed:19858324, ECO:0000269|PubMed:21908732}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19858324, ECO:0000269|PubMed:21908424, ECO:0000269|PubMed:22675200, ECO:0000269|PubMed:30840890}; Single-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:21908732}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-...
null
null
null
null
null
FUNCTION: High-affinity Fc receptor for immunoglobulin M (IgM), both secreted and membrane-bound IgM (PubMed:19858324, PubMed:22675200, PubMed:36949194, PubMed:37095205). Primarily regulates IgM transport and homeostasis. Primarily regulates IgM transport and homeostasis. In lymphoid cells, enables exocytosis of membra...
Homo sapiens (Human)
O60669
MOT2_HUMAN
MPPMPSAPPVHPPPDGGWGWIVVGAAFISIGFSYAFPKAVTVFFKEIQQIFHTTYSEIAWISSIMLAVMYAGGPVSSVLVNKYGSRPVVIAGGLLCCLGMVLASFSSSVVQLYLTMGFITGLGLAFNLQPALTIIGKYFYRKRPMANGLAMAGSPVFLSSLAPFNQYLFNTFGWKGSFLILGSLLLNACVAGSLMRPLGPNQTTSKSKNKTGKTEDDSSPKKIKTKKSTWEKVNKYLDFSLFKHRGFLIYLSGNVIMFLGFFAPIIFLAPYAKDQGIDEYSAAFLLSVMAFVDMFARPSVGLIANSKYIRPRIQYFFSFA...
null
null
lactate transmembrane transport [GO:0035873]; plasma membrane lactate transport [GO:0035879]; pyruvate transmembrane transport [GO:1901475]; transport across blood-brain barrier [GO:0150104]
basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; nucleoplasm [GO:0005654]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; Schaffer coll...
identical protein binding [GO:0042802]; lactate transmembrane transporter activity [GO:0015129]; pyruvate secondary active transmembrane transporter activity [GO:0005477]; pyruvate transmembrane transporter activity [GO:0050833]; symporter activity [GO:0015293]
PF07690;
1.20.1250.20;
Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:32415067}; Multi-pass membrane protein {ECO:0000269|PubMed:32415067}. Basolateral cell membrane {ECO:0000250|UniProtKB:P53988}; Multi-pass membrane protein {ECO:0000269|PubMed:32415067}. Cytoplasm {ECO:0000250|UniProtKB:O70451}. Note=R...
CATALYTIC ACTIVITY: Reaction=H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in); Xref=Rhea:RHEA:64720, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:32415067, ECO:0000269|PubMed:9786900}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64721; Evidence={ECO:0000305|PubMed:32415067}; Physiologi...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for pyruvate {ECO:0000269|PubMed:9786900};
null
null
null
FUNCTION: Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate (PubMed:32415067, PubMed:9786900). Dimerization is functionally required and both subunits work c...
Homo sapiens (Human)
O60671
RAD1_HUMAN
MPLLTQQIQDEDDQYSLVASLDNVRNLSTILKAIHFREHATCFATKNGIKVTVENAKCVQANAFIQAGIFQEFKVQEESVTFRINLTVLLDCLSIFGSSPMPGTLTALRMCYQGYGYPLMLFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLREAFSELDMTSEVLQITMSPDKPYFRLSTFGNAGSSHLDYPKDSDLMEAFHCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGFLSLQYMIRNEDGQICFVEYYCCPDEEVPESES
null
null
cellular response to ionizing radiation [GO:0071479]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; meiotic recombination checkpoint signaling [GO:0051598]; substantia nigra development [GO:0021762]
checkpoint clamp complex [GO:0030896]; chromosome [GO:0005694]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
damaged DNA binding [GO:0003684]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]
PF02144;
3.70.10.10;
Rad1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9716408}.
null
null
null
null
null
FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:10846170, PubMed:10884395). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:12578958). Acts then as a sliding clamp platform...
Homo sapiens (Human)
O60673
REV3L_HUMAN
MFSVRIVTADYYMASPLQGLDTCQSPLTQAPVKKVPVVRVFGATPAGQKTCLHLHGIFPYLYVPYDGYGQQPESYLSQMAFSIDRALNVALGNPSSTAQHVFKVSLVSGMPFYGYHEKERHFMKIYLYNPTMVKRICELLQSGAIMNKFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAVKFRKARRKSNTLHATGSCKNHLSGNSLADTLFRWEQDEIPSSLILEGVEPQSTCELEVDAVAADILNRLDIEAQIGGNPGLQAIWEDEKQRRRNRNETSQMSQPESQDHRFVPATESEKKFQKRLQEILKQNDFSVTLSG...
2.7.7.7
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P14284}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P14284};
DNA-templated DNA replication [GO:0006261]; double-strand break repair via homologous recombination [GO:0000724]; error-prone translesion synthesis [GO:0042276]
nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; zeta DNA polymerase complex [GO:0016035]
4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]
PF00136;PF03104;PF15735;PF14260;
1.10.132.60;3.30.342.10;1.10.287.690;3.90.1600.10;3.30.420.10;
DNA polymerase type-B family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.71 uM for dATP (for Pol-zeta2); KM=1.17 uM for dATP (for Pol-zeta4); Note=kcat is 0.31 min(-1) for DNA synthesis by Pol-zeta4. kcat is 0.05 min(-1) for DNA synthesis by Pol-zeta2. {ECO:0000269|PubMed:24449906};
null
null
null
FUNCTION: Catalytic subunit of the DNA polymerase zeta complex, an error-prone polymerase specialized in translesion DNA synthesis (TLS). Lacks an intrinsic 3'-5' exonuclease activity and thus has no proofreading function. {ECO:0000269|PubMed:24449906}.
Homo sapiens (Human)
O60674
JAK2_HUMAN
MGMACLTMTEMEGTSTSSIYQNGDISGNANSMKQIDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDF...
2.7.10.2
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305|PubMed:7615558};
actin filament polymerization [GO:0030041]; 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 Janus kinase activity [GO:0042976]; adaptive immune response [...
caveola [GO:0005901]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endosome lumen [GO:0031904]; euchromatin [GO:0000791]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; extrinsic component of plasma membrane [GO:0019897]; focal adhesion [GO:0005925]; glutamatergic s...
acetylcholine receptor binding [GO:0033130]; ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; heme binding [GO:0020037]; histone binding [GO:0042393]; histone H3Y41 kinase activity [GO:0035401]; identical protein binding [GO:0042802]; insulin receptor substrate binding [GO:0043560]; interleukin-1...
PF18379;PF18377;PF17887;PF07714;PF00017;
2.30.29.30;3.30.505.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, JAK subfamily
PTM: Autophosphorylated, leading to regulate its activity. Leptin promotes phosphorylation on tyrosine residues, including phosphorylation on Tyr-813 (By similarity). Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity (By similarity). Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972...
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:19783980}. Nucleus {ECO:0000269|PubMed:19783980}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100...
null
null
null
null
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 recepto...
Homo sapiens (Human)
O60675
MAFK_HUMAN
MTTNPKPNKALKVKKEAGENAPVLSDDELVSMSVRELNQHLRGLTKEEVTRLKQRRRTLKNRGYAASCRIKRVTQKEELERQRVELQQEVEKLARENSSMRLELDALRSKYEALQTFARTVARGPVAPSKVATTSVITIVKSTELSSTSVPFSAAS
null
null
negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-...
PF03131;
1.20.5.170;
BZIP family, Maf subfamily
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:9150357). However, they act as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 a...
Homo sapiens (Human)
O60678
ANM3_HUMAN
MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPV...
2.1.1.319
null
methylation [GO:0032259]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of retinoic acid biosynthetic process [GO:1900053]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
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]; protein-arginine omega-N monomethyltransferase activity [GO:0035241]; ribosome binding [GO:0043022]
PF21137;PF21336;PF06325;
2.70.160.11;3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9642256}.
CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65280; Evidence={...
null
null
null
null
FUNCTION: Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (Probable). May regulate retinoic acid synthesis and signaling by inhibi...
Homo sapiens (Human)
O60682
MUSC_HUMAN
MSTGSVSDPEEMELRGLQREYPVPASKRPPLRGVERSYASPSDNSSAEEEDPDGEEERCALGTAGSAEGCKRKRPRVAGGGGAGGSAGGGGKKPLPAKGSAAECKQSQRNAANARERARMRVLSKAFSRLKTSLPWVPPDTKLSKLDTLRLASSYIAHLRQLLQEDRYENGYVHPVNLTWPFVVSGRPDSDTKEVSAANRLCGTTA
null
null
branchiomeric skeletal muscle development [GO:0014707]; cardiac conduction system development [GO:0003161]; cellular response to leukemia inhibitory factor [GO:1990830]; diaphragm development [GO:0060539]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:00063...
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-...
PF00010;
4.10.280.10;
null
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Transcription repressor capable of inhibiting the transactivation capability of TCF3/E47. May play a role in regulating antigen-dependent B-cell differentiation.
Homo sapiens (Human)
O60683
PEX10_HUMAN
MAPAAASPPEVIRAAQKDEYYRGGLRSAAGGALHSLAGARKWLEWRKEVELLSDVAYFGLTTLAGYQTLGEEYVSIIQVDPSRIHVPSSLRRGVLVTLHAVLPYLLDKALLPLEQELQADPDSGRPLQGSLGPGGRGCSGARRWMRHHTATLTEQQRRALLRAVFVLRQGLACLQRLHVAWFYIHGVFYHLAKRLTGITYLRVRSLPGEDLRARVSYRLLGVISLLHLVLSMGLQLYGFRQRQRARKEWRLHRGLSHRRASLEERAVSRNPLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCREKFPPQKLI...
2.3.2.27
null
cellular response to reactive oxygen species [GO:0034614]; peroxisome organization [GO:0007031]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into...
peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]
protein transmembrane transporter activity [GO:0008320]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF04757;PF13639;
3.30.40.10;
Pex2/pex10/pex12 family
null
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:9922452}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:24662292};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:24662292}.
null
null
FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:24662292). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each sub...
Homo sapiens (Human)
O60684
IMA7_HUMAN
METMASPGKDNYRMKSYKNNALNPEEMRRRREEEGIQLRKQKREQQLFKRRNVELINEEAAMFDSLLMDSYVSSTTGESVITREMVEMLFSDDSDLQLATTQKFRKLLSKEPSPPIDEVINTPRVVDRFVEFLKRNENCTLQFEAAWALTNIASGTSQQTKIVIEAGAVPIFIELLNSDFEDVQEQAVWALGNIAGDSSVCRDYVLNCSILNPLLTLLTKSTRLTMTRNAVWALSNLCRGKNPPPEFAKVSPCLPVLSRLLFSSDSDLLADACWALSYLSDGPNEKIQAVIDSGVCRRLVELLMHNDYKVASPALRAVGN...
null
null
entry of viral genome into host nucleus through nuclear pore complex via importin [GO:0075506]; maternal process involved in female pregnancy [GO:0060135]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation...
cytosol [GO:0005829]; host cell [GO:0043657]; membrane [GO:0016020]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]
PF00514;PF16186;PF01749;
1.20.5.690;1.25.10.10;
Importin alpha family
null
null
null
null
null
null
null
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...
Homo sapiens (Human)
O60687
SRPX2_HUMAN
MASQLTQRGALFLLFFLTPAVTPTWYAGSGYYPDESYNEVYAEEVPQAPALDYRVPRWCYTLNIQDGEATCYSPKGGNYHSSLGTRCELSCDRGFRLIGRRSVQCLPSRRWSGTAYCRQMRCHALPFITSGTYTCTNGVLLDSRCDYSCSSGYHLEGDRSRICMEDGRWSGGEPVCVDIDPPKIRCPHSREKMAEPEKLTARVYWDPPLVKDSADGTITRVTLRGPEPGSHFPEGEHVIRYTAYDRAYNRASCKFIVKVQVRRCPTLKPPQHGYLTCTSAGDNYGATCEYHCDGGYDRQGTPSRVCQSSRQWSGSPPICA...
null
null
angiogenesis [GO:0001525]; cell motility [GO:0048870]; cell-cell adhesion [GO:0098609]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of synapse assembly [GO:0051965]; regulation of phosphorylation [GO:0042325]; vocalization behavior [GO:0071625]
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; excitatory synapse [GO:0060076]; extracellular space [GO:0005615]; synaptic membrane [GO:0097060]
hepatocyte growth factor binding [GO:0036458]; identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102]
PF13778;PF02494;PF00084;
2.10.70.10;
null
PTM: Contains chondroitin sulfate chains. {ECO:0000269|PubMed:22242148}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22242148}. Cytoplasm. Cell surface. Synapse {ECO:0000250}.
null
null
null
null
null
FUNCTION: Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases t...
Homo sapiens (Human)
O60701
UGDH_HUMAN
MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIID...
1.1.1.22
null
chondroitin sulfate biosynthetic process [GO:0030206]; gastrulation with mouth forming second [GO:0001702]; glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; neuron development [GO:0048666]; protein hexamerization [GO:0034214]; UDP-glucuronate biosynthe...
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
identical protein binding [GO:0042802]; NAD binding [GO:0051287]; UDP-glucose 6-dehydrogenase activity [GO:0003979]
PF00984;PF03720;PF03721;
1.20.5.100;3.40.50.720;
UDP-glucose/GDP-mannose dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.7 uM for UDP-glucose {ECO:0000269|PubMed:27966912}; KM=7.6 uM for UDP-glucose {ECO:0000269|PubMed:30457329}; KM=25 uM for UDP-glucose {ECO:0000269|PubMed:23106432}; KM=780 uM for NAD {ECO:0000269|PubMed:27966912}; KM=1160 uM for NAD(+) {ECO:0000269|PubMed:3045732...
PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1. {ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21961565, ECO:0000269|PubMed:22123821, ECO:0000269|PubMed:23106432, ECO:0000269|PubMed:25478983, ECO:0000269|PubMed:27966912, ECO:000...
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.6. {ECO:0000269|PubMed:25478983};
null
FUNCTION: Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Re...
Homo sapiens (Human)
O60704
TPST2_HUMAN
MRLSVRRVLLAAGCALVLVLAVQLGQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQLVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPGDVVRDMAQIAPML...
2.8.2.20
null
3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; peptidyl-tyrosine sulfation [GO:0006478]
endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
protein homodimerization activity [GO:0042803]; protein-tyrosine sulfotransferase activity [GO:0008476]
PF13469;
3.40.50.300;
Protein sulfotransferase family
PTM: N-glycosylated. {ECO:0000269|PubMed:9733778}.
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:25660941}; Single-pass type II membrane protein {ECO:0000269|PubMed:25660941}.
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]; Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20...
null
null
null
null
FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000269|PubMed:9733778}.
Homo sapiens (Human)
O60706
ABCC9_HUMAN
MSLSFCGNNISSYNINDGVLQNSCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNLRWILTFALLFVHVCEIAEGIVSDSRRESRHLHLFMPAVMGFVATTTSIVYYHNIETSNFPKLLLALFLYWVMAFITKTIKLVKYCQSGLDISNLRFCITGMMVILNGLLMAVEINVIRVRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISG...
null
null
action potential [GO:0001508]; cardiac conduction [GO:0061337]; cardiac muscle cell contraction [GO:0086003]; coronary vasculature development [GO:0060976]; defense response to virus [GO:0051607]; fibroblast proliferation [GO:0048144]; heart morphogenesis [GO:0003007]; inorganic cation transmembrane transport [GO:00986...
inward rectifying potassium channel [GO:0008282]; membrane [GO:0016020]; plasma membrane [GO:0005886]; potassium ion-transporting ATPase complex [GO:0031004]; sarcomere [GO:0030017]
ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled inorganic anion transmembrane transporter activity [GO:0043225]; ATPase-coupled monoatomic cation transmembrane transporter activity [GO:0019829]; ATPase-coupled transmembrane transporter activity ...
PF00664;PF00005;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
null
null
null
null
null
FUNCTION: Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. {ECO:0000269|PubMed:9831708}.
Homo sapiens (Human)
O60711
LPXN_HUMAN
MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKESPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELH...
null
null
actin cytoskeleton organization [GO:0030036]; cell adhesion [GO:0007155]; endothelial cell migration [GO:0043542]; heart development [GO:0007507]; muscle structure development [GO:0061061]; negative regulation of B cell receptor signaling pathway [GO:0050859]; negative regulation of cell adhesion [GO:0007162]; protein-...
adherens junction [GO:0005912]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; po...
actin binding [GO:0003779]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; transcription coregulator activity [GO:0003712]
PF00412;
2.10.110.10;
Paxillin family
PTM: Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is important for its inhibitory function. Bombesin stimulates phosphorylation on Tyr-22, Tyr-62 and Tyr-72. {ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:20543562}.
SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region {ECO:0000250}. 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...
null
null
null
null
null
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 ...
Homo sapiens (Human)
O60716
CTND1_HUMAN
MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANPLMANGTLTRRHQNGRFVGDADLERQKFSDLKLNGPQDHSHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETSDDGTTRRTETTVKKVVKTVTTRTVQPVAMGPDGLPVDASSVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYSRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRS...
null
null
cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; protein stabilization [GO:0050821]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; Wnt...
adherens junction [GO:0005912]; catenin complex [GO:0016342]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; hippocampal mossy fiber ...
beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; protein sequestering activity [GO:0140311]; protein tyrosine kinase binding [GO:1990782]; signaling receptor binding [GO:0005102]
PF00514;
1.25.10.10;
Beta-catenin family
PTM: Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK5. Dephosphorylated by PTPRJ. {ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:17194753, ECO:0000269|PubMed:20564219, ECO:0000269|PubMed:7623846}.
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:11896187}. Cytoplasm {ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:17047063}. Nucleus {ECO:0000269|PubMed:11896187, ECO:0000269|PubMed:17115030}. Cell membrane {ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:17047063}. Note=Interaction with ...
null
null
null
null
null
FUNCTION: Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability (PubMed:14610055, PubMed:20371349). Beside cell-cell adhesion, regulates gene transcription through several transcription factors inclu...
Homo sapiens (Human)
O60721
NCKX1_HUMAN
MGKLIRMGPQERWLLRTKRLHWSRLLFLLGMLIIGSTYQHLRRPRGLSSLWAAVSSHQPIKLASRDLSSEEMMMMSSSPSKPSSEMGGKMLVPQASVGSDEATLSMTVENIPSMPKRTAKMIPTTTKNNYSPTAAGTERRKEDTPTSSRTLTYYTSTSSRQIVKKYTPTPRGEMKSYSPTQVREKVKYTPSPRGRRVGTYVPSTFMTMETSHAITPRTTVKDSDITATYKILETNSLKRIMEETTPTTLKGMFDSTPTFLTHEVEANVLTSPRSVMEKNNLFPPRRVESNSSAHPWGLVGKSNPKTPQGTVLLHTPATSE...
null
null
calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; long-term synaptic depression [GO:0060292]; long-term synaptic potentiation [GO:0060291]; monoatomic ion transport [GO:0006811...
cell surface [GO:0009986]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; outer membrane [GO:0019867]; plasma membrane [GO:0005886]
calcium channel activity [GO:0005262]; calcium, potassium:sodium antiporter activity [GO:0008273]; symporter activity [GO:0015293]
PF01699;
1.20.1420.30;
Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family, SLC24A subfamily
PTM: The uncleaved signal sequence is required for efficient membrane targeting and proper membrane integration. {ECO:0000269|PubMed:10608890}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26631410}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in) + 4 Na(+)(out); Xref=Rhea:RHEA:69967, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:26631410};
null
null
null
null
FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) (PubMed:26631410). Critical component of the visual transduction cascade, controlling the calcium concentration of outer segments during light and darkness (PubMed:20850105). Light causes a rapid lowering of cytos...
Homo sapiens (Human)
O60725
ICMT_HUMAN
MAGCAARAPPGSEARLSLATFLLGASVLALPLLTRAGLQGRTGLALYVAGLNALLLLLYRPPRYQIAIRACFLGFVFGCGTLLSFSQSSWSHFGWYMCSLSLFHYSEYLVTAVNNPKSLSLDSFLLNHSLEYTVAALSSWLEFTLENIFWPELKQITWLSVTGLLMVVFGECLRKAAMFTAGSNFNHVVQNEKSDTHTLVTSGVYAWFRHPSYVGWFYWSIGTQVMLCNPICGVSYALTVWRFFRDRTEEEEISLIHFFGEEYLEYKKRVPTGLPFIKGVKVDL
2.1.1.100
null
C-terminal protein methylation [GO:0006481]; protein modification process [GO:0036211]; protein targeting to membrane [GO:0006612]; S-adenosylhomocysteine metabolic process [GO:0046498]; S-adenosylmethioninamine metabolic process [GO:0046499]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
protein C-terminal carboxyl O-methyltransferase activity [GO:0003880]; protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity [GO:0004671]
PF04140;
1.20.120.1630;
Class VI-like SAM-binding methyltransferase superfamily, Isoprenylcysteine carboxyl methyltransferase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19158273, ECO:0000269|PubMed:9614111}; Multi-pass membrane protein {ECO:0000269|PubMed:19158273}.
CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21672, Rhea:RHEA-COMP:12125, Rhea:RHEA-COMP:12126, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI...
null
null
null
null
FUNCTION: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues. {ECO:0000269|PubMed:9614111}.
Homo sapiens (Human)
O60729
CC14B_HUMAN
MKRKSERRSSWAAAPPCSRRCSSTSPGVKKIRSSTQQDPRRRDPQDDVYLDITDRLCFAILYSRPKSASNVHYFSIDNELEYENFYADFGPLNLAMVYRYCCKINKKLKSITMLRKKIVHFTGSDQRKQANAAFLVGCYMVIYLGRTPEEAYRILIFGETSYIPFRDAAYGSCNFYITLLDCFHAVKKAMQYGFLNFNSFNLDEYEHYEKAENGDLNWIIPDRFIAFCGPHSRARLESGYHQHSPETYIQYFKNHNVTTIIRLNKRMYDAKRFTDAGFDHHDLFFADGSTPTDAIVKEFLDICENAEGAIAVHCKAGLGR...
3.1.3.16; 3.1.3.48
null
cilium assembly [GO:0060271]; DNA repair [GO:0006281]; microtubule cytoskeleton organization [GO:0000226]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of cytokinesis [GO:0032467]; positive regulation of ubiquitin protein ligase activity [GO:1904668]; protein dephosphorylation [GO:000647...
centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle pole [GO:0000922]
myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]
PF00782;PF14671;
3.90.190.10;
Protein-tyrosine phosphatase family, Non-receptor class CDC14 subfamily
null
SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Following DNA damage, translocates from the nucleolus to the nucleoplasm and interacts with FZR1/CDH1.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMe...
null
null
null
null
FUNCTION: Dual-specificity phosphatase involved in DNA damage response. Essential regulator of the G2 DNA damage checkpoint: following DNA damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a key activator of the anaphase promoting complex/cyclosome (APC/C). Dephosphorylates SIRT2 around early anaphase...
Homo sapiens (Human)
O60733
PLPL9_HUMAN
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLVNPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTA...
3.1.1.4; 3.1.1.5; 3.1.2.2
null
antibacterial humoral response [GO:0019731]; cardiolipin acyl-chain remodeling [GO:0035965]; cardiolipin biosynthetic process [GO:0032049]; chemotaxis [GO:0006935]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; phosphatidic acid metabolic process [GO:0046473]; phosphatidylcholine catabolic ...
cytosol [GO:0005829]; extracellular space [GO:0005615]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]
1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; calcium-independent phospholipase A2 activity [GO:0047499]; calmodulin binding [GO:0005516]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; lysophospholipase activit...
PF00023;PF12796;PF01734;
1.25.40.20;3.40.1090.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18208975}. Cell membrane {ECO:0000269|PubMed:18208975}. Mitochondrion {ECO:0000250|UniProtKB:P97819}. Cell projection, pseudopodium {ECO:0000269|PubMed:18208975}. Note=Recruited to the membrane-enriched pseudopods upon MCP1/CCL2 stimulation in monocytes. {ECO:0000269|...
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:20886109}; Physiological...
null
null
null
null
FUNCTION: Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity resp...
Homo sapiens (Human)
O60741
HCN1_HUMAN
MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFKVDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVP...
null
null
apical protein localization [GO:0045176]; cellular response to cAMP [GO:0071320]; general adaptation syndrome, behavioral process [GO:0051867]; neuronal action potential [GO:0019228]; potassium ion transmembrane transport [GO:0071805]; protein homotetramerization [GO:0051289]; regulation of membrane depolarization [GO:...
axon [GO:0030424]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; HCN channel complex [GO:0098855]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic active zone membrane [GO:0048787]
cAMP binding [GO:0030552]; identical protein binding [GO:0042802]; intracellular cAMP-activated cation channel activity involved in regulation of presynaptic membrane potential [GO:0140232]; intracellularly cAMP-activated cation channel activity [GO:0005222]; potassium channel activity [GO:0005267]; voltage-gated monoa...
PF00027;PF00520;PF08412;
1.10.287.70;1.10.287.630;2.60.120.10;
Potassium channel HCN family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15351778, ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:30351409}; Multi-pass membrane protein {ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376}.
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:28086084}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:28086084};
null
null
null
null
FUNCTION: Hyperpolarization-activated ion channel that are permeable to sodium and potassium ions (PubMed:15351778, PubMed:28086084). Displays lower selectivity for K(+) over Na(+) ions (PubMed:28086084). Contributes to the native pacemaker currents in heart (If) and in the generation of the I(h) current which controls...
Homo sapiens (Human)
O60749
SNX2_HUMAN
MAAEREPPPLGDGKPTDFEDLEDGEDLFTSTVSTLESSPSSPEPASLPAEDISANSNGPKPTEVVLDDDREDLFAEATEEVSLDSPEREPILSSEPSPAVTPVTPTTLIAPRIESKSMSAPVIFDRSREEIEEEANGDIFDIEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKVGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESSELPRAVNTQALSGAGILRMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQL...
null
null
early endosome to Golgi transport [GO:0034498]; intracellular protein transport [GO:0006886]; lamellipodium morphogenesis [GO:0072673]; retrograde transport, endosome to Golgi [GO:0042147]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; lamellipodium [GO:0030027]; lysosome [GO:0005764]; membrane [GO:0016020]; protein-containing complex [GO:0032991]; retromer complex [GO:0030904]; retromer, tubulation complex [GO:00...
cadherin binding [GO:0045296]; 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]; protein heterodimerization activity [GO:0046982]; protein homodimerization...
PF00787;PF03700;PF09325;
1.20.1270.60;3.30.1520.10;
Sorting nexin family
null
SUBCELLULAR 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|PubMe...
null
null
null
null
null
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:1710177...
Homo sapiens (Human)
O60755
GALR3_HUMAN
MADAQNISLDSPGSVGAVAVPVVFALIFLLGTVGNGLVLAVLLQPGPSAWQEPGSTTDLFILNLAVADLCFILCCVPFQATIYTLDAWLFGALVCKAVHLLIYLTMYASSFTLAAVSVDRYLAVRHPLRSRALRTPRNARAAVGLVWLLAALFSAPYLSYYGTVRYGALELCVPAWEDARRRALDVATFAAGYLLPVAVVSLAYGRTLRFLWAAVGPAGAAAAEARRRATGRAGRAMLAVAALYALCWGPHHALILCFWYGRFAFSPATYACRLASHCLAYANSCLNPLVYALASRHFRARFRRLWPCGRRRRHRARRAL...
null
null
adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; chemical synaptic transmission [GO:0007268]; feeding behavior [GO:0007631]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; galanin-activated signaling pathway [GO:0090663]; ...
cilium [GO:0005929]; membrane [GO:0016020]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886]; synapse [GO:0045202]
galanin receptor activity [GO:0004966]; peptide hormone binding [GO:0017046]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Receptor for the hormone galanin (PubMed:25691535). Receptor for the hormone spexin-1 (PubMed:24517231). {ECO:0000269|PubMed:24517231, ECO:0000269|PubMed:25691535, ECO:0000269|PubMed:9722565, ECO:0000269|PubMed:9832121}.
Homo sapiens (Human)
O60759
CYTIP_HUMAN
MSLQRLLQHSSNGNLADFCAGPAYSSYSTLTGSLTMDDNRRIQMLADTVATLPRGRKQLALTRSSSLSDFSWSQRKLVTVEKQDNETFGFEIQSYRPQNQNACSSEMFTLICKIQEDSPAHCAGLQAGDVLANINGVSTEGFTYKQVVDLIRSSGNLLTIETLNGTMILKRTELEAKLQVLKQTLKQKWVEYRSLQLQEHRLLHGDAANCPSLENMDLDELSLFGPLPGPGPALVDRNRLSSESSCKSWLSSMTMDSEDGYQTCVSEDSSRGAFSRQTSTDDECFIPKEGDDFLRRSSSRRNRSISNTSSGSMSPLWEGN...
null
null
regulation of cell adhesion [GO:0030155]
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; nucleoplasm [GO:0005654]
null
PF00595;
2.30.42.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm. Early endosome. Note=Recruited from the cytosol to endosomes by SNX27.
null
null
null
null
null
FUNCTION: By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm.
Homo sapiens (Human)
O60760
HPGDS_HUMAN
MPNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKIPILEVDGLTLHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELLTYNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLLVFKPDLLDNHPRLVTLRKKVQAIPAVANWIKRRPQTKL
2.5.1.18; 5.3.99.2
COFACTOR: Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}; Note=Glutathione is required for the prostaglandin D synthase activity. {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|...
glutathione metabolic process [GO:0006749]; locomotory behavior [GO:0007626]; negative regulation of male germ cell proliferation [GO:2000255]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin metabolic process [GO:0006693]; signal transduction [GO:0007165]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]
calcium ion binding [GO:0005509]; glutathione transferase activity [GO:0004364]; magnesium ion binding [GO:0000287]; prostaglandin-D synthase activity [GO:0004667]; protein homodimerization activity [GO:0042803]
PF14497;PF02798;
1.20.1050.10;3.40.30.10;
GST superfamily, Sigma family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353279}.
CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12244105, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:1993951...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 mM for glutathione for the glutathione-conjugating activity {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; KM=0.6 mM for glutathione for the prostaglandin D synthase activity in the presence of EDTA {ECO:0000269|PubMed:11...
null
null
null
FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathi...
Homo sapiens (Human)
O60762
DPM1_HUMAN
MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT
2.4.1.83
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Note=Binds 1 divalent metal cation. {ECO:0000250|UniProtKB:Q8U4M3};
dolichol metabolic process [GO:0019348]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; GDP-mannose metabolic process [GO:0019673]; GPI anchor biosynthetic process [GO:0006506]; protein mannosylation [GO:0035268]; protein N-linked glycosylation via asparagine [GO:0018279]; protein O-linked mannosyla...
dolichol-phosphate-mannose synthase complex [GO:0033185]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nucleus [GO:0005634]
alcohol binding [GO:0043178]; dolichyl-phosphate beta-D-mannosyltransferase activity [GO:0004582]; dolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]; mannose binding [GO:0005537]; metal ion binding [GO:0046872]
PF00535;
null
Glycosyltransferase 2 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305|PubMed:10835346}.
CATALYTIC ACTIVITY: Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683, ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83; Evidence={ECO:0000305|PubMed:10835346}; Physiolog...
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:10835346}.
null
null
FUNCTION: 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...
Homo sapiens (Human)
O60763
USO1_HUMAN
MNFLRGVMGGQSAGPQHTEAETIQKLCDRVASSTLLDDRRNAVRALKSLSKKYRLEVGIQAMEHLIHVLQTDRSDSEIIGYALDTLYNIISNEEEEEVEENSTRQSEDLGSQFTEIFIKQQENVTLLLSLLEEFDFHVRWPGVKLLTSLLKQLGPQVQQIILVSPMGVSRLMDLLADSREVIRNDGVLLLQALTRSNGAIQKIVAFENAFERLLDIISEEGNSDGGIVVEDCLILLQNLLKNNNSNQNFFKEGSYIQRMKPWFEVGDENSGWSAQKVTNLHLMLQLVRVLVSPTNPPGATSSCQKAMFQCGLLQQLCTIL...
null
null
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi vesicle docking [GO:0048211]; intracellular protein transport [GO:0006886]; membrane fusion [GO:0061025]; regulation of cellular response to insulin stimulus [GO:1900076]; secretory granule localization [GO:0032252]; small GTPase-mediated sig...
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; fibrillar center [GO:0001650]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; perinuclear region of cyto...
cadherin binding [GO:0045296]; RNA binding [GO:0003723]
PF18770;PF04871;PF04869;
1.25.10.10;
VDP/USO1/EDE1 family
PTM: Phosphorylated in a cell cycle-specific manner; phosphorylated in interphase but not in mitotic cells. Dephosphorylated protein associates with the Golgi membrane; phosphorylation promotes dissociation. {ECO:0000269|PubMed:9478999}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}. Golgi apparatus membrane {ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}; Peripheral membrane protein {ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}. Note=Recycles between the cytosol and the Golgi a...
null
null
null
null
null
FUNCTION: 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 ...
Homo sapiens (Human)
O60779
S19A2_HUMAN
MDVPGPVSRRAAAAAATVLLRTARVRRECWFLPTALLCAYGFFASLRPSEPFLTPYLLGPDKNLTEREVFNEIYPVWTYSYLVLLFPVFLATDYLRYKPVVLLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYSVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVAGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSTCQRVNGIKVQNGGIVTDTPASNHLPGWEDIESKIPLNMEEPPVEEPEPKPDRLLVLKVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYTQGLW...
null
null
pyridoxine transport [GO:0031923]; spermatogenesis [GO:0007283]; thiamine diphosphate biosynthetic process [GO:0009229]; thiamine transmembrane transport [GO:0071934]; thiamine transport [GO:0015888]; thiamine-containing compound metabolic process [GO:0042723]; transmembrane transport [GO:0055085]
membrane [GO:0016020]; plasma membrane [GO:0005886]
folic acid transmembrane transporter activity [GO:0008517]; thiamine transmembrane transporter activity [GO:0015234]
PF01770;
1.20.1250.20;
Reduced folate carrier (RFC) transporter (TC 2.A.48) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21836059, ECO:0000305|PubMed:10391222, ECO:0000305|PubMed:10542220}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in); Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385; Evidence={ECO:0000269|PubMed:10391222, ECO:0000269|PubMed:10542220, ECO:0000269|PubMed:33008889, ECO:0000269|PubMed:35512554, ECO:0000269|PubMed:35724964}; CATALYTIC ACTIVITY: Re...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37.8 uM for pyridoxine (at pH 5.5) {ECO:0000269|PubMed:33008889}; KM=3.66 uM for thiamine (at pH 5.5) {ECO:0000269|PubMed:33008889}; KM=2.83 uM for thiamine (at pH 7.4) {ECO:0000269|PubMed:33008889}; KM=2.5 uM for thiamine {ECO:0000269|PubMed:10542220}; Vmax=332 pm...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-8.5. {ECO:0000269|PubMed:10542220};
null
FUNCTION: High-affinity transporter for the intake of thiamine (PubMed:10391222, PubMed:10542220, PubMed:21836059, PubMed:33008889, PubMed:35512554, PubMed:35724964). Mediates H(+)-dependent pyridoxine transport (PubMed:33008889, PubMed:35512554, PubMed:35724964). {ECO:0000269|PubMed:10391222, ECO:0000269|PubMed:105422...
Homo sapiens (Human)
O60783
RT14_HUMAN
MAAFMLGSLLRTFKQMVPSSASGQVRSHYVDWRMWRDVKRRKMAYEYADERLRINSLRKNTILPKILQDVADEEIAALPRDSCPVRIRNRCVMTSRPRGVKRRWRLSRIVFRHLADHGQLSGIQRATW
null
null
mitochondrial translation [GO:0032543]; translation [GO:0006412]
mitochondrial inner membrane [GO:0005743]; mitochondrial ribosome [GO:0005761]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]
RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
PF00253;
1.10.287.1480;
Universal ribosomal protein uS14 family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
null
null
null
null
null
null
Homo sapiens (Human)
O60784
TOM1_HUMAN
MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDALRAVKKRIVGNKNFHEVMLALTVLETCVKNCGHRFHVLVASQDFVESVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVTIYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETQSGQDSVGTDSSQQEDSGQHAAPLPAPPILSGDTPIAPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQAEPADLELLQELNRTCRAMQQRVLELIPQIANEQLTEELLIVNDNLNNVFLRHERFERFRTGQTTKAPSEAEPAA...
null
null
autophagosome-lysosome fusion [GO:0061909]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; positive regulation of autophagosome maturation [GO:1901098]; protein transport [GO:0015031]; regulation of endosome organization [GO:1904978]; signal transduction [GO:0007165]; substrate localization to autophagosom...
azurophil granule membrane [GO:0035577]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; specific granule membr...
clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; myosin VI binding [GO:0070853]; phosphatidylinositol-5-phosphate binding [GO:0010314]; polyubiquitin modification-dependent protein binding [GO:0031593]; ubiquitin binding [GO:0043130]
PF03127;PF00790;
1.20.58.160;1.25.40.90;
TOM1 family
PTM: Monoubiquitinated. {ECO:0000269|PubMed:14563850}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14563850, ECO:0000269|PubMed:14613930, ECO:0000269|PubMed:15047686, ECO:0000269|PubMed:26320582, ECO:0000269|PubMed:31263572}. Endosome membrane {ECO:0000269|PubMed:14613930, ECO:0000269|PubMed:15047686, ECO:0000269|PubMed:23023224, ECO:0000269|PubMed:26320582, ECO:00...
null
null
null
null
null
FUNCTION: Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (PubMed:14563850, PubMed:15047686, PubMed:23023224, PubMed:25588840, PubMed:26320582, PubMed:31371777). ...
Homo sapiens (Human)
O60806
TBX19_HUMAN
MAMSELGTRKPSDGTVSHLLNVVESELQAGREKGDPTEKQLQIILEDAPLWQRFKEVTNEMIVTKNGRRMFPVLKISVTGLDPNAMYSLLLDFVPTDSHRWKYVNGEWVPAGKPEVSSHSCVYIHPDSPNFGAHWMKAPISFSKVKLTNKLNGGGQIMLNSLHKYEPQVHIVRVGSAHRMVTNCSFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERNHLRDVPEAISESQHVTYSHLGGWIFSNPDGVCTAGNSNYQYAAPLPLPAPHTHHGCEHYSGLRGHRQAPYPSAYMHRNHSPSVNLIESSSNNLQVFS...
null
null
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; heart morphogenesis [GO:0003007]; mesoderm formation [GO:0001707]; pituitary gland development [GO:0021983]; regulation of cell differentiation [GO:0045595]; regulation of cell population proliferation [GO:0042127]; regulation of tra...
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
PF00907;
2.60.40.820;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
null
null
null
null
null
FUNCTION: Transcriptional regulator involved in developmental processes. Can activate POMC gene expression and repress the alpha glycoprotein subunit and thyroid-stimulating hormone beta promoters. {ECO:0000269|PubMed:11290323}.
Homo sapiens (Human)
O60812
HNRC1_HUMAN
MASNVTNKMDPHSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIAGCSVHKGFAFVQYDKEKNARAAVAGEDGRMIASQVVDINLAAEPKVNRGNAGVKRSAAEMYGSSFDLDYGFQRDYYDGMYSFPARVPPPPPIALAVVPSKRQRLSGNTSRRGKSGFNSKSGKRGSSKSGKLKGDDLQAIKQELTQIKQKVDSLLENLEKIEKEQSKQEVEVKNAKSEEEQSSSSMKKDETHVKMESEGGAEDSAEEGDPLDDDVNEDQGDDQLELIKDDEKEAEEGEDDRDSTNGQDDS
null
null
null
nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
identical protein binding [GO:0042802]; RNA binding [GO:0003723]
PF00076;
3.30.70.330;
RRM HNRPC family, RALY subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of ribonucleosomes. {ECO:0000250}.
null
null
null
null
null
FUNCTION: May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs. {ECO:0000250}.
Homo sapiens (Human)
O60814
H2B1K_HUMAN
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
null
null
antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response in mucosa [GO:0002227]; killing of cells of anothe...
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
PF00125;
1.10.20.10;
Histone H2B family
PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specif...
SUBCELLULAR LOCATION: Nucleus. Chromosome.
null
null
null
null
null
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 r...
Homo sapiens (Human)
O60825
F262_HUMAN
MSGASSSEQNNNSYETKTPNLRMSEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYRPLDPDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPYEQ...
2.7.1.105; 3.1.3.46
null
fructose 2,6-bisphosphate metabolic process [GO:0006003]; fructose metabolic process [GO:0006000]; glucose catabolic process [GO:0006007]; glycolytic process [GO:0006096]; lactate metabolic process [GO:0006089]; positive regulation of insulin secretion [GO:0032024]; response to glucose [GO:0009749]
cytosol [GO:0005829]; nucleoplasm [GO:0005654]
6-phosphofructo-2-kinase activity [GO:0003873]; ATP binding [GO:0005524]; fructose-2,6-bisphosphate 2-phosphatase activity [GO:0004331]; protein kinase binding [GO:0019901]
PF01591;PF00300;
3.40.50.300;3.40.50.1240;
Phosphoglycerate mutase family
PTM: Phosphorylation by AMPK stimulates activity. {ECO:0000269|PubMed:11069105}.
null
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; Evidence={ECO:0000269|PubMed:11069105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17290...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=57 uM for beta-D-fructose 6-phosphate {ECO:0000269|PubMed:11069105}; KM=5.1 uM for beta-D-fructose 2,6-bisphosphate {ECO:0000269|PubMed:11069105}; KM=46 uM for beta-D-fructose 6-phosphate (in presence of AMPK) {ECO:0000269|PubMed:11069105}; KM=29 uM for beta-D-fruc...
null
null
null
FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000269|PubMed:11069105}.
Homo sapiens (Human)
O60826
CCD22_HUMAN
MEEADRILIHSLRQAGTAVPPDVQTLRAFTTELVVEAVVRCLRVINPAVGSGLSPLLPLAMSARFRLAMSLAQACMDLGYPLELGYQNFLYPSEPDLRDLLLFLAERLPTDASEDADQPAGDSAILLRAIGSQIRDQLALPWVPPHLRTPKLQHLQGSALQKPFHASRLVVPELSSRGEPREFQASPLLLPVPTQVPQPVGRVASLLEHHALQLCQQTGRDRPGDEDWVHRTSRLPPQEDTRAQRQRLQKQLTEHLRQSWGLLGAPIQARDLGELLQAWGAGAKTGAPKGSRFTHSEKFTFHLEPQAQATQVSDVPATSR...
null
null
cytoplasmic sequestering of NF-kappaB [GO:0007253]; endocytic recycling [GO:0032456]; Golgi to plasma membrane transport [GO:0006893]; intracellular copper ion homeostasis [GO:0006878]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; positive regulation of canonical NF-kappaB signal transdu...
centrosome [GO:0005813]; cytosol [GO:0005829]; endosome [GO:0005768]; nucleoplasm [GO:0005654]
cullin family protein binding [GO:0097602]
PF05667;PF21674;
null
CCDC22 family
null
SUBCELLULAR LOCATION: Endosome {ECO:0000305|PubMed:28892079}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26638075}.
null
null
null
null
null
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...
Homo sapiens (Human)
O60828
PQBP1_HUMAN
MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNADTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHDKSDRGHDKSDRSHEKLDRGHDKSDRGHDKSDRDRERGYDKVDRERERDRERDRDRGYDKADREEGKERRHHRREELAPYPKSKKAVSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD
null
null
activation of innate immune response [GO:0002218]; alternative mRNA splicing, via spliceosome [GO:0000380]; cellular response to exogenous dsRNA [GO:0071360]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; neuron projection development [GO:0031175]; positive regulation of defense response ...
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; neuronal ribonucleoprotein granule [GO:0071598]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; lipid binding [GO:0008289]; ribonucleoprotein complex binding [GO:0043021]; transcription coactivator activity [GO:0003713]
null
2.20.70.10;3.40.30.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:23512658}. Nucleus speckle {ECO:0000250|UniProtKB:Q91VJ5}. Cytoplasmic granule {ECO:0000269|PubMed:21933836}. Note=Colocalizes with SRSF2 in nuclear speckles (By similarity). Colocali...
null
null
null
null
null
FUNCTION: Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development (PubMed:10198427, PubMed:10332029, PubMed:12062018, PubMed:20410308, PubMed:23512658). Interacts with splicing-rel...
Homo sapiens (Human)
O60829
PAGE4_HUMAN
MSARVRSRSRGRGDGQEAPDVVAFVAPGESQQEEPPTDNQDIEPGQEREGTPPIEERKVEGDCQEMDLEKTRSERGDGSDVKEKTPPNPKHAKTKEAGDGQP
null
null
intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; regulation of stress-activated MAPK cascade [GO:0032872]; response to starvation [GO:0042594]
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
DNA binding [GO:0003677]; nucleic acid binding [GO:0003676]; transcription coactivator activity [GO:0003713]
PF05831;
null
GAGE family
PTM: HIPK1-mediated phosphorylation at Thr-51 leads to the compaction of its intrinsically disordered conformation and is critical for its ability to potentiate the transcriptional activator activity of JUN inspite of a reduced interaction with JUN (PubMed:24559171, PubMed:26242913). CLK2-mediated phosphorylation at mu...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12489849, ECO:0000269|PubMed:24559171, ECO:0000269|PubMed:25374899}. Nucleus {ECO:0000269|PubMed:24559171}. Mitochondrion {ECO:0000269|PubMed:25374899}. Note=Translocates to mitochondria in response to stress. {ECO:0000269|PubMed:25374899}.
null
null
null
null
null
FUNCTION: Intrinsically disordered protein that potentiates the transcriptional activator activity of JUN (PubMed:24263171, PubMed:28289210). Protects cells from stress-induced apoptosis by inhibiting reactive oxygen species (ROS) production and via regulation of the MAPK signaling pathway (PubMed:21357425, PubMed:2537...
Homo sapiens (Human)
O60830
TI17B_HUMAN
MEEYAREPCPWRIVDDCGGAFTMGVIGGGVFQAIKGFRNAPVGIRHRLRGSANAVRIRAPQIGGSFAVWGGLFSTIDCGLVRLRGKEDPWNSITSGALTGAVLAARSGPLAMVGSAMMGGILLALIEGVGILLTRYTAQQFRNAPPFLEDPSQLPPKDGTPAPGYPSYQQYH
null
null
intracellular protein transport [GO:0006886]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626]
mitochondrial inner membrane [GO:0005743]; TIM23 mitochondrial import inner membrane translocase complex [GO:0005744]
protein transmembrane transporter activity [GO:0008320]
PF02466;
null
Tim17/Tim22/Tim23 family
PTM: Forms one disulfide bond. {ECO:0000269|PubMed:27265872}.
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Homo sapiens (Human)
O60831
PRAF2_HUMAN
MSEVRLPPLRALDDFVLGSARLAAPDPCDPQRWCHRVINNLLYYQTNYLLCFGIGLALAGYVRPLHTLLSALVVAVALGVLVWAAETRAAVRRCRRSHPAACLAAVLAVGLLVLWVAGGACTFLFSIAGPVLLILVHASLRLRNLKNKIENKIESIGLKRTPMGLLLEALGQEQEAGS
null
null
L-glutamate transmembrane transport [GO:0015813]; protein transport [GO:0015031]
endosome membrane [GO:0010008]; membrane [GO:0016020]
null
PF03208;
null
PRA1 family
null
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000305|PubMed:17975142}; Multi-pass membrane protein {ECO:0000305|PubMed:17975142}.
null
null
null
null
null
FUNCTION: May be involved in ER/Golgi transport and vesicular traffic. Plays a proapoptotic role in cerulenin-induced neuroblastoma apoptosis. {ECO:0000269|PubMed:17975142, ECO:0000269|PubMed:18395978}.
Homo sapiens (Human)
O60832
DKC1_HUMAN
MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFDKLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGV...
5.4.99.-
null
box H/ACA RNA 3'-end processing [GO:0000495]; enzyme-directed rRNA pseudouridine synthesis [GO:0000455]; mRNA pseudouridine synthesis [GO:1990481]; positive regulation of establishment of protein localization to telomere [GO:1904851]; positive regulation of protein localization to Cajal body [GO:1904871]; positive regu...
box H/ACA scaRNP complex [GO:0072589]; box H/ACA snoRNP complex [GO:0031429]; box H/ACA telomerase RNP complex [GO:0090661]; cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697]
box H/ACA snoRNA binding [GO:0034513]; pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]; telomerase activity [GO:0003720]; telomerase RNA binding [GO:0070034]
PF08068;PF01472;PF16198;PF01509;
3.30.2350.10;2.30.130.10;
Pseudouridine synthase TruB family
null
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus {ECO:0000269|PubMed:10556300, ECO:0000269|PubMed:10591218, ECO:0000269|PubMed:12429849}. Nucleus, Cajal body {ECO:0000250|UniProtKB:P40615}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:21820037}.
CATALYTIC ACTIVITY: Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA; Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000305|PubMed:25219674};
null
null
null
null
FUNCTION: [Isoform 1]: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA (PubMed:25219674, PubMed:32554502). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (PubMed:25219...
Homo sapiens (Human)
O60840
CAC1F_HUMAN
MSESEGGKDTTPEPSPANGAGPGPEWGLCPGPPAVEGESSGASGLGTPKRRNQHSKHKTVAVASAQRSPRALFCLTLANPLRRSCISIVEWKPFDILILLTIFANCVALGVYIPFPEDDSNTANHNLEQVEYVFLVIFTVETVLKIVAYGLVLHPSAYIRNGWNLLDFIIVVVGLFSVLLEQGPGRPGDAPHTGGKPGGFDVKALRAFRVLRPLRLVSGVPSLHIVLNSIMKALVPLLHIALLVLFVIIIYAIIGLELFLGRMHKTCYFLGSDMEAEEDPSPCASSGSGRACTLNQTECRGRWPGPNGGITNFDNFFFAM...
null
null
calcium ion import across plasma membrane [GO:0098703]; detection of light stimulus involved in visual perception [GO:0050908]; negative regulation of voltage-gated calcium channel activity [GO:1901386]; visual perception [GO:0007601]
membrane [GO:0016020]; perikaryon [GO:0043204]; photoreceptor outer segment [GO:0001750]; voltage-gated calcium channel complex [GO:0005891]
high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]; voltage-gated calcium channel activity [GO:0005245]
PF08763;PF16885;PF16905;PF00520;
1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350;
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1F subfamily
null
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: [Isoform 1]: 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 ...
Homo sapiens (Human)
O60841
IF2P_HUMAN
MGKKQKNKSEDSTKDDIDLDALAAEIEGAGAAKEQEPQKSKGKKKKEKKKQDFDEDDILKELEELSLEAQGIKADRETVAVKPTENNEEEFTSKDKKKKGQKGKKQSFDDNDSEELEDKDSKSKKTAKPKVEMYSGSDDDDDFNKLPKKAKGKAQKSNKKWDGSEEDEDNSKKIKERSRINSSGESGDESDEFLQSRKGQKKNQKNKPGPNIESGNEDDDASFKIKTVAQKKAEKKERERKKRDEEKAKLRKLKEKEELETGKKDQSKQKESQRKFEEETVKSKVTVDTGVIPASEEKAETPTAAEDDNEGDKKKKDKKK...
3.6.5.3
COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000250|UniProtKB:G0S8G9}; Note=Binds 1 monovalent cation per monomer in the active site. Structural cofactor that stabilizes the GTP-bound 'on' state. May also act as a transition state stabilizer of the hydrolysis reaction. {ECO:0000250|UniProt...
regulation of translational initiation [GO:0006446]; ribosome assembly [GO:0042255]; translational initiation [GO:0006413]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; synapse [GO:0045202]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]; tRNA binding [GO:0000049]
PF00009;PF14578;PF11987;
3.40.50.300;2.40.30.10;3.40.50.10050;
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, IF-2 subfamily
PTM: (Microbial infection) Cleaved and inactivated by the protease 3C of poliovirus, Coxsackievirus B3 and Human rhinovirus 14, allowing the virus to shutoff the host cell translation. {ECO:0000269|PubMed:18572216}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05D44}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; Evidence={ECO:0000269|PubMed:10659855, ECO:0000305|PubMed:35732735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:1967...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=1 pmol/min/ug enzyme {ECO:0000269|PubMed:10659855}; Note=Obtained in the presence of 40S and 60S ribosomal subunits. 60S ribosomal subunit is necessary for enzyme activation, while 40S ribosomal subunit is not.;
null
null
null
FUNCTION: Plays a role in translation initiation (PubMed:10659855, PubMed:35732735). Ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit to the pre-initiation complex to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon (PubMed:1...
Homo sapiens (Human)
O60844
ZG16_HUMAN
MLTVALLALLCASASGNAIQARSSSYSGEYGGGGGKRFSHSGNQLDGPITALRVRVNTYYIVGLQVRYGKVWSDYVGGRNGDLEEIFLHPGESVIQVSGKYKWYLKKLVFVTDKGRYLSFGKDSGTSFNAVPLHPNTVLRFISGRSGSLIDAIGLHWDVYPSSCSRC
null
null
defense response to Gram-positive bacterium [GO:0050830]; protein transport [GO:0015031]; suppression of symbiont entry into host [GO:0052373]
collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; mucus layer [GO:0070701]; zymogen granule membrane [GO:0042589]
carbohydrate binding [GO:0030246]; peptidoglycan binding [GO:0042834]
PF01419;
2.100.10.30;
Jacalin lectin family
null
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17307141}. Zymogen granule lumen {ECO:0000250|UniProtKB:Q8CJD3}. Golgi apparatus lumen {ECO:0000269|PubMed:17307141}.
null
null
null
null
null
FUNCTION: May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN. {ECO:0000269|PubMed:17307141}.
Homo sapiens (Human)
O60858
TRI13_HUMAN
MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGSVRNSLWRPAPFKCPTCRKETSATGINSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCLTDMQLICGICATRGEHTKHVFCSIEDAYAQERDAFESLFQSFETWRRGDALSRLDTLETSKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQAYDPEINKLNTILQEQRMAFNIAEAFKDVSEPIVFLQQMQEFREKIKVIKETPLPPSNLPASPLMKNFDTSQWEDIKLVDVDKLSLPQDTGTFISKIPWSFYKLFLL...
2.3.2.27
null
anatomical structure morphogenesis [GO:0009653]; ERAD pathway [GO:0036503]; innate immune response [GO:0045087]; negative regulation of viral transcription [GO:0032897]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of macroautophagy [GO:0016239]; positive regulation o...
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; perinuclear endoplasmic reticulum [GO:0097038]
transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-like protein ligase activity [GO:0061659]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
PF00643;PF13445;
3.30.160.60;3.30.40.10;
TRIM/RBCC family
PTM: Auto-ubiquitinated; requires the RING-type zinc finger. Auto-polyubiquitination leads to proteasomal degradation. {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:25152375}; Single-pass membrane protein {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}. Note=Concentrates and colocaliz...
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly ...
Homo sapiens (Human)
O60861
GAS7_HUMAN
MSGARCRTLYPFSGERHGQGLRFAAGELITLLQVPDGGWWEGEKEDGLRGWFPASYVQLLEKPGMVPPPPGEESQTVILPPGWQSYLSPQGRRYYVNTTTNETTWERPSSSPGIPASPGSHRSSLPPTVNGYHASGTPAHPPETAHMSVRKSTGDSQNLGSSSPSKKQSKENTITINCVTFPHPDTMPEQQLLKPTEWSYCDYFWADKKDPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEDYAKNLAKLSQNSLASQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKDMKKCDH...
null
null
actin filament polymerization [GO:0030041]; neuron projection morphogenesis [GO:0048812]
actin filament [GO:0005884]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
actin filament binding [GO:0051015]; identical protein binding [GO:0042802]
PF00611;PF14604;PF00397;PF16623;
2.20.70.10;1.20.1270.60;2.30.30.40;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
null
null
null
null
null
FUNCTION: May play a role in promoting maturation and morphological differentiation of cerebellar neurons.
Homo sapiens (Human)
O60869
EDF1_HUMAN
MAESDWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQHSITKNTAKLDRETEELHHDRVTLEVGKVIQQGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLRGKDIGKPIEKGPRAK
null
null
endothelial cell differentiation [GO:0045446]; positive regulation of DNA binding [GO:0043388]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of lipid metabolic process [GO:0019216]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
calmodulin binding [GO:0005516]; DNA binding [GO:0003677]; RNA binding [GO:0003723]; TFIID-class transcription factor complex binding [GO:0001094]; transcription coactivator activity [GO:0003713]
PF01381;PF08523;
1.10.260.40;
null
PTM: Phosphorylated (by PKA and PKC). {ECO:0000269|PubMed:10816571, ECO:0000269|PubMed:15112053}.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Also nuclear upon binding to NR5A1 and treatment of cells with TPA or forskolin.
null
null
null
null
null
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 ...
Homo sapiens (Human)
O60870
KIN17_HUMAN
MGKSDFLTPKAIANRIKSKGLQKLRWYCQMCQKQCRDENGFKCHCMSESHQRQLLLASENPQQFMDYFSEEFRNDFLELLRRRFGTKRVHNNIVYNEYISHREHIHMNATQWETLTDFTKWLGREGLCKVDETPKGWYIQYIDRDPETIRRQLELEKKKKQDLDDEEKTAKFIEEQVRRGLEGKEQEVPTFTELSRENDEEKVTFNLSKGACSSSGATSSKSSTLGPSALKTIGSSASVKRKESSQSSTQSKEKKKKKSALDEIMEIEEEKKRTARTDYWLQPEIIVKIITKKLGEKYHKKKAIVKEVIDKYTAVVKMID...
null
null
DNA damage response [GO:0006974]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; mRNA processing [GO:0006397]
cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]
PF10357;PF18131;
2.30.30.140;2.30.30.30;1.10.10.2030;
KIN17 family
null
SUBCELLULAR 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|PubM...
null
null
null
null
null
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...
Homo sapiens (Human)
O60879
DIAP2_HUMAN
MEQPGAAASGAGGGSEEPGGGRSNKRSAGNRAANEEETKNKPKLNIQIKTLADDVRDRITSFRKSTVKKEKPLIQHPIDSQVAMSEFPAAQPLYDERSLNLSEKEVLDLFEKMMEDMNLNEEKKAPLRNKDFTTKREMVVQYISATAKSGGLKNSKHECTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSNPVSWVNNFGHEGLGLLLDELEKLLDKKQQENIDKKNQYKLIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQPNMMTEIVKILSAICIVGEENILDKLLGAITTAAERNNRERFSPIVEGLENQ...
null
null
actin filament polymerization [GO:0030041]; female gamete generation [GO:0007292]; oogenesis [GO:0048477]
actin filament [GO:0005884]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]
actin binding [GO:0003779]; signaling receptor binding [GO:0005102]; small GTPase binding [GO:0031267]
PF06367;PF06371;PF02181;
1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10;
Formin homology family, Diaphanous subfamily
null
SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol. Early endosome. Note=Isoform 3 is cytosolic but when coexpressed with RHOD, the 2 proteins colocalize to early endosomes.
null
null
null
null
null
FUNCTION: 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:12...
Homo sapiens (Human)
O60880
SH21A_HUMAN
MDAVAVYHGKISRETGEKLLLATGLDGSYLLRDSESVPGVYCLCVLYHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP
null
null
adaptive immune response [GO:0002250]; cell-cell signaling [GO:0007267]; cellular defense response [GO:0006968]; humoral immune response [GO:0006959]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of natural killer cell...
cytoplasm [GO:0005737]; cytosol [GO:0005829]
null
PF00017;
3.30.505.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
null
null
null
null
null
FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as SLAMF1, CD244, LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling seems to cooperate with SH2D1B/EAT-2. Initially it has been proposed that association with SLAMF1 prevents SLAMF1 binding to inhibitory...
Homo sapiens (Human)
O60882
MMP20_HUMAN
MKVLPASGLAVFLIMALKFSTAAPSLVAASPRTWRNNYRLAQAYLDKYYTNKEGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVIKKPRCGVPDVANYRLFPGEPKWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTMGTNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYGPRKVFLGKPTLPHAPHHKPSIPDLCDSSSSFDAVTMLGKELLLFKDRIF...
3.4.24.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17869250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:17869250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17869250}; Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:17869250};
amelogenesis [GO:0097186]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; regulation of enamel mineralization [GO:0070173]
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
PF00045;PF00413;PF01471;
3.40.390.10;2.110.10.10;
Peptidase M10A family
PTM: Autoactivates at least at the 107-Asn-|-Tyr-108 site. {ECO:0000250}.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
null
null
null
null
null
FUNCTION: Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' sit...
Homo sapiens (Human)
O60883
G37L1_HUMAN
MRWLWPLAVSLAVILAVGLSRVSGGAPLHLGRHRAETQEQQSRSKRGTEDEEAKGVQQYVPEEWAEYPRPIHPAGLQPTKPLVATSPNPGKDGGTPDSGQELRGNLTGAPGQRLQIQNPLYPVTESSYSAYAIMLLALVVFAVGIVGNLSVMCIVWHSYYLKSAWNSILASLALWDFLVLFFCLPIVIFNEITKQRLLGDVSCRAVPFMEVSSLGVTTFSLCALGIDRFHVATSTLPKVRPIERCQSILAKLAVIWVGSMTLAVPELLLWQLAQEPAPTMGTLDSCIMKPSASLPESLYSLVMTYQNARMWWYFGCYFCL...
null
null
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; Bergmann glial cell differentiation [GO:0060020]; cellular response to reactive oxygen species [GO:0034614]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of neuron differentiation [GO:0045665]; ...
ciliary membrane [GO:0060170]; membrane [GO:0016020]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
G protein-coupled peptide receptor activity [GO:0008528]; G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277]; prosaposin receptor activity [GO:0036505]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.; PTM: Undergoes metalloprotease-mediated cleavage which reduces its constitutive activity. {ECO:0000269|PubMed:27072655}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:28688853}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28688853}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q99JG2}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with the basal membrane of Bergmann glia cell primary cilia. {ECO:0000250|UniProtKB:Q9...
null
null
null
null
null
FUNCTION: G-protein coupled receptor (PubMed:27072655). Has been shown to bind the neuroprotective and glioprotective factor prosaposin (PSAP), leading to endocytosis followed by an ERK phosphorylation cascade (PubMed:23690594). However, other studies have shown that prosaposin does not increase activity (PubMed:270726...
Homo sapiens (Human)
O60884
DNJA2_HUMAN
MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDGRQIVVKYPPGKVIEPGCVRVVRGEGMPQY...
null
null
positive regulation of cell population proliferation [GO:0008284]; protein refolding [GO:0042026]; response to heat [GO:0009408]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]
ATP binding [GO:0005524]; ATPase activator activity [GO:0001671]; Hsp70 protein binding [GO:0030544]; metal ion binding [GO:0046872]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
PF00226;PF01556;PF00684;
1.10.287.110;2.10.230.10;2.60.260.20;
null
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
null
null
null
null
null
FUNCTION: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877). {ECO:0000269|PubMed:24318877}.
Homo sapiens (Human)
O60885
BRD4_HUMAN
MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQ...
null
null
chromatin remodeling [GO:0006338]; DNA damage response [GO:0006974]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of DNA damage checkpoint [GO:2000002]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-templated transcription...
chromatin [GO:0000785]; chromosome [GO:0005694]; condensed nuclear chromosome [GO:0000794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; histone reader activity [GO:0140566]; lysine-acetylated histone binding [GO:0070577]; P-TEFb complex binding [GO:0106140]; p53 binding [GO:0002039]; RNA polymerase II C-terminal domain binding [GO:0099122]; RNA polymerase II CTD heptapeptide repeat kinase act...
PF17035;PF17105;PF00439;
1.20.1270.220;1.20.920.10;
BET family
PTM: Phosphorylation by CK2 disrupt the intramolecular binding between the bromo domain 2 and the NPS region and promotes binding between the NPS and the BID regions, leading to activate the protein and promote binding to acetylated histones. In absence of phosphorylation, BRD4 does not localize to p53/TP53 target gene...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:25593309}. Chromosome {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:21890894}. Note=Associates with acetylated chromatin (PubMed:16109376, PubMed:21890894). Released from chromatin upon deacetylation of histones that can be triggered by d...
null
null
null
null
null
FUNCTION: 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 (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719). Remains associated with acetylated chromatin throughout the ...
Homo sapiens (Human)
O60888
CUTA_HUMAN
MSGGRAPAVLLGGVASLLLSFVWMPALLPVASRLLLLPRVLLTMASGSPPTQPSPASDSGSGYVPGSVSAAFVTCPNEKVAKEIARAVVEKRLAACVNLIPQITSIYEWKGKIEEDSEVLMMIKTQSSLVPALTDFVRSVHPYEVAEVIALPVEQGNFPYLQWVRQVTESVSDSITVLP
null
null
protein localization [GO:0008104]; response to metal ion [GO:0010038]
extracellular exosome [GO:0070062]; membrane [GO:0016020]
copper ion binding [GO:0005507]; enzyme binding [GO:0019899]
PF03091;
3.30.70.120;
CutA family
PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
null
null
null
null
null
null
FUNCTION: May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).
Homo sapiens (Human)
O60890
OPHN1_HUMAN
MGHPPLEFSDCYLDSPDFRERLKCYEQELERTNKFIKDVIKDGNALISAMRNYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLNEVENERMMMVHNASDLLIKPLENFRKEQIGFTKERKKKFEKDGERFYSLLDRHLHLSSKKKESQLQEADLQVDKERHNFFESSLDYVYQIQEVQESKKFNIVEPVLAFLHSLFISNSLTVELTQDFLPYKQQLQLSLQNTRNHFSSTREEMEELKKRMKEAPQTCKLPGQPTIEGYLYTQEKWALGISWVKYYCQYEKETKTLTMTPMEQKPGAKQGPLDLTLKY...
null
null
actin cytoskeleton organization [GO:0030036]; axon guidance [GO:0007411]; cell junction assembly [GO:0034329]; cell morphogenesis involved in neuron differentiation [GO:0048667]; cerebellar granule cell differentiation [GO:0021707]; cerebral cortex neuron differentiation [GO:0021895]; establishment of epithelial cell a...
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; terminal bouton [GO:0043195]
actin binding [GO:0003779]; GTPase activator activity [GO:0005096]; ionotropic glutamate receptor binding [GO:0035255]; phospholipid binding [GO:0005543]
PF16746;PF00169;PF00620;
1.20.1270.60;2.30.29.30;1.10.555.10;
null
null
SUBCELLULAR LOCATION: Postsynapse {ECO:0000250|UniProtKB:P0CAX5}. Presynapse {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, axon {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99J31}. Cytoplasm {ECO:0000250|UniProtKB:Q...
null
null
null
null
null
FUNCTION: Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the regulation of synaptic v...
Homo sapiens (Human)
O60894
RAMP1_HUMAN
MARALCRLPRRGLWLLLAHHLFMTTACQEANYGALLRELCLTQFQVDMEAVGETLWCDWGRTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVRDPPGSILYPFIVVPITVTLLVTALVVWQSKRTEGIV
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; amylin receptor signaling pathway [GO:0097647]; angiogenesis [GO:0001525]; calcitonin gene-related peptide receptor signaling pathway [GO:1990408]; calcium ion transport [GO:0006816]; cellular response to hormone stimulus [GO:003287...
cell surface [GO:0009986]; CGRP receptor complex [GO:1990406]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
amylin receptor activity [GO:0097643]; calcitonin gene-related peptide binding [GO:1990407]; calcitonin gene-related peptide receptor activity [GO:0001635]; coreceptor activity [GO:0015026]
PF04901;
1.10.150.510;
RAMP family
null
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL. {ECO:0000269|PubMed:9620797}.
Homo sapiens (Human)
O60895
RAMP2_HUMAN
MASLRVERAGGPRLPRTRVGRPAALRLLLLLGAVLNPHEALAQPLPTTGTPGSEGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAELFDLGFPNPLAERIIFETHQIHFANCSLVQPTFSDPPEDVLLAMIIAPICLIPFLITLVVWRSKDSEAQA
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adherens junction assembly [GO:0034333]; adrenomedullin receptor signaling pathway [GO:1990410]; angiogenesis [GO:0001525]; basement membrane assembly [GO:0070831]; bicellular tight junction assembly [GO:0070830]; calcium ion transp...
adrenomedullin receptor complex [GO:1903143]; cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
adrenomedullin binding [GO:1990409]; adrenomedullin receptor activity [GO:0001605]; coreceptor activity [GO:0015026]
PF04901;
1.10.150.510;
RAMP family
null
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL. {ECO:0000269|PubMed:22102369, ECO:0000269|PubMed:9620797}.
Homo sapiens (Human)
O60896
RAMP3_HUMAN
METGALRRPQLLPLLLLLCGGCPRAGGCNETGMLERLPLCGKAFADMMGKVDVWKWCNLSEFIVYYESFTNCTEMEANVVGCYWPNPLAQGFITGIHRQFFSNCTVDRVHLEDPPDEVLIPLIVIPVVLTVAMAGLVVWRSKRTDTLL
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adrenomedullin receptor signaling pathway [GO:1990410]; amylin receptor signaling pathway [GO:0097647]; calcium ion transport [GO:0006816]; cellular response to estradiol stimulus [GO:0071392]; cellular response to hormone stimulus ...
adrenomedullin receptor complex [GO:1903143]; amylin receptor complex 3 [GO:0150058]; cell surface [GO:0009986]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
adrenomedullin receptor activity [GO:0001605]; amylin receptor activity [GO:0097643]; amyloid-beta binding [GO:0001540]; coreceptor activity [GO:0015026]
PF04901;
1.10.150.510;
RAMP family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23674134}; Single-pass type I membrane protein {ECO:0000269|PubMed:23674134}. Membrane {ECO:0000269|PubMed:23674134}; Single-pass type I membrane protein {ECO:0000269|PubMed:23674134}. Note=Moves from intracellular puncta to the plasma membrane in a RAMP3-dependen...
null
null
null
null
null
FUNCTION: Plays a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a GPER1-dependent manner. Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) and GPER1 to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL. {ECO:0000269|PubMed...
Homo sapiens (Human)