Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
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
|
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
|
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-CoA metabolic process [GO:0035336]; negative regulation of prostaglandin secretion [GO:0032307]; neuron differentiation [GO:0030182]; positive regulation of cell growth [GO:0030307]; positive regulation of insulin secretion [GO:0032024]
|
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 membrane [GO:0005778]; plasma membrane [GO:0005886]
|
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 membrane {ECO:0000269|PubMed:24269233}; Single-pass type III membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:24269233}.
|
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|PubMed:22633490, ECO:0000269|PubMed:24269233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000269|PubMed:21242590, ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000269|PubMed:21242590}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000269|PubMed:21242590}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:21242590, ECO:0000269|PubMed:24269233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000269|PubMed:21242590}; CATALYTIC ACTIVITY: Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526, ChEBI:CHEBI:72745, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140; Evidence={ECO:0000269|PubMed:22633490}; CATALYTIC ACTIVITY: Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117; Evidence={ECO:0000250|UniProtKB:O35547}; CATALYTIC ACTIVITY: Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113; Evidence={ECO:0000250|UniProtKB:O35547}; CATALYTIC ACTIVITY: Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109; Evidence={ECO:0000250|UniProtKB:O35547}; CATALYTIC ACTIVITY: Reaction=5,6-epoxy-(8Z,11Z,14Z)-eicosatrienoate + ATP + CoA = 5,6-epoxy-(8Z,11Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52088, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:131992, ChEBI:CHEBI:136351, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52089; Evidence={ECO:0000250|UniProtKB:O35547}; CATALYTIC ACTIVITY: Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52016, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84024, ChEBI:CHEBI:136117, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017; Evidence={ECO:0000250|UniProtKB:O35547}; CATALYTIC ACTIVITY: Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52012, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:76625, ChEBI:CHEBI:136115, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013; Evidence={ECO:0000250|UniProtKB:O35547}; CATALYTIC ACTIVITY: Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + ATP + CoA = 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52008, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84025, ChEBI:CHEBI:136107, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52009; Evidence={ECO:0000250|UniProtKB:O35547};
| 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). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (By similarity). Modulates prostaglandin E2 secretion (PubMed:21242590). {ECO:0000250|UniProtKB:O35547, ECO:0000269|PubMed:21242590, ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233}.
|
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 protein catabolic process [GO:0042177]; negative regulation of protein transport [GO:0051224]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of neuron projection development [GO:0010976]; protein to membrane docking [GO:0022615]; protein transport [GO:0015031]; regulation of Wnt signaling pathway [GO:0030111]; response to bacterium [GO:0009617]
|
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 tubule structures (PubMed:21725319) Colocalizes with EEA1 on nascent phagosomes in dendritic cells but competes with EEA1 for binding to phagosomal membrane (PubMed:23237080). In the case of Salmonella enterica infection localizes to Salmonella-containing vacuoles (SCVs) from which SNX3-containing tubules form 30-60 minutes after infection (PubMed:20482551). {ECO:0000269|PubMed:20482551, ECO:0000269|PubMed:21725319, ECO:0000269|PubMed:23237080}.
| 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 similarity). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC/VPS). May in part act as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (PubMed:21725319, PubMed:24344282, PubMed:30213940). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (PubMed:23237080). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor TFRC presumably by delivering the transferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex (By similarity). In the case of Salmonella enterica infection plays arole in maturation of the Salmonella-containing vacuole (SCV) and promotes recruitment of LAMP1 to SCVs (PubMed:20482551). {ECO:0000250|UniProtKB:O70492, ECO:0000269|PubMed:11433298, ECO:0000269|PubMed:18767904, ECO:0000269|PubMed:21725319, ECO:0000269|PubMed:23237080, ECO:0000269|PubMed:24344282, ECO:0000305|PubMed:21725319}.
|
Homo sapiens (Human)
|
O60494
|
CUBN_HUMAN
|
MMNMSLPFLWSLLTLLIFAEVNGEAGELELQRQKRSINLQQPRMATERGNLVFLTGSAQNIEFRTGSLGKIKLNDEDLSECLHQIQKNKEDIIELKGSAIGLPQNISSQIYQLNSKLVDLERKFQGLQQTVDKKVCSSNPCQNGGTCLNLHDSFFCICPPQWKGPLCSADVNECEIYSGTPLSCQNGGTCVNTMGSYSCHCPPETYGPQCASKYDDCEGGSVARCVHGICEDLMREQAGEPKYSCVCDAGWMFSPNSPACTLDRDECSFQPGPCSTLVQCFNTQGSFYCGACPTGWQGNGYICEDINECEINNGGCSVAPPVECVNTPGSSHCQACPPGYQGDGRVCTLTDICSVSNGGCHPDASCSSTLGSLPLCTCLPGYTGNGYGPNGCVQLSNICLSHPCLNGQCIDTVSGYFCKCDSGWTGVNCTENINECLSNPCLNGGTCVDGVDSFSCECTRLWTGALCQVPQQVCGESLSGINGSFSYRSPDVGYVHDVNCFWVIKTEMGKVLRITFTFFRLESMDNCPHEFLQVYDGDSSSAFQLGRFCGSSLPHELLSSDNALYFHLYSEHLRNGRGFTVRWETQQPECGGILTGPYGSIKSPGYPGNYPPGRDCVWIVVTSPDLLVTFTFGTLSLEHHDDCNKDYLEIRDGPLYQDPLLGKFCTTFSVPPLQTTGPFARIHFHSDSQISDQGFHITYLTSPSDLRCGGNYTDPEGELFLPELSGPFTHTRQCVYMMKQPQGEQIQINFTHVELQCQSDSSQNYIEVRDGETLLGKVCGNGTISHIKSITNSVWIRFKIDASVEKASFRAVYQVACGDELTGEGVIRSPFFPNVYPGERTCRWTIHQPQSQVILLNFTVFEIGSSAHCETDYVEIGSSSILGSPENKKYCGTDIPSFITSVYNFLYVTFVKSSSTENHGFMAKFSAEDLACGEILTESTGTIQSPGHPNVYPHGINCTWHILVQPNHLIHLMFETFHLEFHYNCTNDYLEVYDTDSETSLGRYCGKSIPPSLTSSGNSLMLVFVTDSDLAYEGFLINYEAISAATACLQDYTDDLGTFTSPNFPNNYPNNWECIYRITVRTGQLIAVHFTNFSLEEAIGNYYTDFLEIRDGGYEKSPLLGIFYGSNLPPTIISHSNKLWLKFKSDQIDTRSGFSAYWDGSSTGCGGNLTTSSGTFISPNYPMPYYHSSECYWWLKSSHGSAFELEFKDFHLEHHPNCTLDYLAVYDGPSSNSHLLTQLCGDEKPPLIRSSGDSMFIKLRTDEGQQGRGFKAEYRQTCENVVIVNQTYGILESIGYPNPYSENQHCNWTIRATTGNTVNYTFLAFDLEHHINCSTDYLELYDGPRQMGRYCGVDLPPPGSTTSSKLQVLLLTDGVGRREKGFQMQWFVYGCGGELSGATGSFSSPGFPNRYPPNKECIWYIRTDPGSSIQLTIHDFDVEYHSRCNFDVLEIYGGPDFHSPRIAQLCTQRSPENPMQVSSTGNELAIRFKTDLSINGRGFNASWQAVTGGCGGIFQAPSGEIHSPNYPSPYRSNTDCSWVIRVDRNHRVLLNFTDFDLEPQDSCIMAYDGLSSTMSRLARTCGREQLANPIVSSGNSLFLRFQSGPSRQNRGFRAQFRQACGGHILTSSFDTVSSPRFPANYPNNQNCSWIIQAQPPLNHITLSFTHFELERSTTCARDFVEILDGGHEDAPLRGRYCGTDMPHPITSFSSALTLRFVSDSSISAGGFHTTVTASVSACGGTFYMAEGIFNSPGYPDIYPPNVECVWNIVSSPGNRLQLSFISFQLEDSQDCSRDFVEIREGNATGHLVGRYCGNSFPLNYSSIVGHTLWVRFISDGSGSGTGFQATFMKIFGNDNIVGTHGKVASPFWPENYPHNSNYQWTVNVNASHVVHGRILEMDIEEIQNCYYDKLRIYDGPSIHARLIGAYCGTQTESFSSTGNSLTFHFYSDSSISGKGFLLEWFAVDAPDGVLPTIAPGACGGFLRTGDAPVFLFSPGWPDSYSNRVDCTWLIQAPDSTVELNILSLDIESHRTCAYDSLVIRDGDNNLAQQLAVLCGREIPGPIRSTGEYMFIRFTSDSSVTRAGFNASFHKSCGGYLHADRGIITSPKYPETYPSNLNCSWHVLVQSGLTIAVHFEQPFQIPNGDSSCNQGDYLVLRNGPDICSPPLGPPGGNGHFCGSHASSTLFTSDNQMFVQFISDHSNEGQGFKIKYEAKSLACGGNVYIHDADSAGYVTSPNHPHNYPPHADCIWILAAPPETRIQLQFEDRFDIEVTPNCTSNYLELRDGVDSDAPILSKFCGTSLPSSQWSSGEVMYLRFRSDNSPTHVGFKAKYSIAQCGGRVPGQSGVVESIGHPTLPYRDNLFCEWHLQGLSGHYLTISFEDFNLQNSSGCEKDFVEIWDNHTSGNILGRYCGNTIPDSIDTSSNTAVVRFVTDGSVTASGFRLRFESSMEECGGDLQGSIGTFTSPNYPNPNPHGRICEWRITAPEGRRITLMFNNLRLATHPSCNNEHVIVFNGIRSNSPQLEKLCSSVNVSNEIKSSGNTMKVIFFTDGSRPYGGFTASYTSSEDAVCGGSLPNTPEGNFTSPGYDGVRNYSRNLNCEWTLSNPNQGNSSISIHFEDFYLESHQDCQFDVLEFRVGDADGPLMWRLCGPSKPTLPLVIPYSQVWIHFVTNERVEHIGFHAKYSFTDCGGIQIGDSGVITSPNYPNAYDSLTHCSSLLEAPQGHTITLTFSDFDIEPHTTCAWDSVTVRNGGSPESPIIGQYCGNSNPRTIQSGSNQLVVTFNSDHSLQGGGFYATWNTQTLGCGGIFHSDNGTIRSPHWPQNFPENSRCSWTAITHKSKHLEISFDNNFLIPSGDGQCQNSFVKVWAGTEEVDKALLATGCGNVAPGPVITPSNTFTAVFQSQEAPAQGFSASFVSRCGSNFTGPSGYIISPNYPKQYDNNMNCTYVIEANPLSVVLLTFVSFHLEARSAVTGSCVNDGVHIIRGYSVMSTPFATVCGDEMPAPLTIAGPVLLNFYSNEQITDFGFKFSYRIISCGGVFNFSSGIITSPAYSYADYPNDMHCLYTITVSDDKVIELKFSDFDVVPSTSCSHDYLAIYDGANTSDPLLGKFCGSKRPPNVKSSNNSMLLVFKTDSFQTAKGWKMSFRQTLGPQQGCGGYLTGSNNTFASPDSDSNGMYDKNLNCVWIIIAPVNKVIHLTFNTFALEAASTRQRCLYDYVKLYDGDSENANLAGTFCGSTVPAPFISSGNFLTVQFISDLTLEREGFNATYTIMDMPCGGTYNATWTPQNISSPNSSDPDVPFSICTWVIDSPPHQQVKITVWALQLTSQDCTQNYLQLQDSPQGHGNSRFQFCGRNASAVPVFYSSMSTAMVIFKSGVVNRNSRMSFTYQIADCNRDYHKAFGNLRSPGWPDNYDNDKDCTVTLTAPQNHTISLFFHSLGIENSVECRNDFLEVRNGSNSNSPLLGKYCGTLLPNPVFSQNNELYLRFKSDSVTSDRGYEIIWTSSPSGCGGTLYGDRGSFTSPGYPGTYPNNTYCEWVLVAPAGRLVTINFYFISIDDPGDCVQNYLTLYDGPNASSPSSGPYCGGDTSIAPFVASSNQVFIKFHADYARRPSAFRLTWDS
| 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:0031232]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
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:0000269|PubMed:14576052}. Endosome {ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:29402915}. Lysosome membrane {ECO:0000250|UniProtKB:O70244}; Peripheral membrane protein {ECO:0000305}. Note=Lacks a transmembrane domain and depends on interaction with AMN for location at the plasma membrane (PubMed:29402915, PubMed:30523278). Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells (By similarity). {ECO:0000250|UniProtKB:O70244, ECO:0000269|PubMed:29402915, ECO:0000269|PubMed:30523278}.
| 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. Acts together with AMN to mediate endocytosis of the CBLIF-cobalamin complex (PubMed:14576052, PubMed:9572993). Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the CBLIF-cobalamin complex. Ligand binding requires calcium (PubMed:9572993). Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface. {ECO:0000269|PubMed:10371504, ECO:0000269|PubMed:11606717, ECO:0000269|PubMed:11717447, ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:9572993}.
|
Homo sapiens (Human)
|
O60496
|
DOK2_HUMAN
|
MGDGAVKQGFLYLQQQQTFGKKWRRFGASLYGGSDCALARLELQEGPEKPRRCEAARKVIRLSDCLRVAEAGGEASSPRDTSAFFLETKERLYLLAAPAAERGDWVQAICLLAFPGQRKELSGPEGKQSRPCMEENELYSSAVTVGPHKEFAVTMRPTEASERCHLRGSYTLRAGESALELWGGPEPGTQLYDWPYRFLRRFGRDKVTFSFEAGRRCVSGEGNFEFETRQGNEIFLALEEAISAQKNAAPATPQPQPATIPASLPRPDSPYSRPHDSLPPPSPTTPVPAPRPRGQEGEYAVPFDAVARSLGKNFRGILAVPPQLLADPLYDSIEETLPPRPDHIYDEPEGVAALSLYDSPQEPRGEAWRRQATADRDPAGLQHVQPAGQDFSASGWQPGTEYDNVVLKKGPK
| 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:0000250}.
| 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-stimulated MAP kinase activation (By similarity). {ECO:0000250}.
|
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
|
MALGTTLRASLLLLGLLTEGLAQLAIPASVPRGFWALPENLTVVEGASVELRCGVSTPGSAVQWAKDGLLLGPDPRIPGFPRYRLEGDPARGEFHLHIEACDLSDDAEYECQVGRSEMGPELVSPRVILSILVPPKLLLLTPEAGTMVTWVAGQEYVVNCVSGDAKPAPDITILLSGQTISDISANVNEGSQQKLFTVEATARVTPRSSDNRQLLVCEASSPALEAPIKASFTVNVLFPPGPPVIEWPGLDEGHVRAGQSLELPCVARGGNPLATLQWLKNGQPVSTAWGTEHTQAVARSVLVMTVRPEDHGAQLSCEAHNSVSAGTQEHGITLQVTFPPSAIIILGSASQTENKNVTLSCVSKSSRPRVLLRWWLGWRQLLPMEETVMDGLHGGHISMSNLTFLARREDNGLTLTCEAFSEAFTKETFKKSLILNVKYPAQKLWIEGPPEGQKLRAGTRVRLVCLAIGGNPEPSLMWYKDSRTVTESRLPQESRRVHLGSVEKSGSTFSRELVLVTGPSDNQAKFTCKAGQLSASTQLAVQFPPTNVTILANASALRPGDALNLTCVSVSSNPPVNLSWDKEGERLEGVAAPPRRAPFKGSAAARSVLLQVSSRDHGQRVTCRAHSAELRETVSSFYRLNVLYRPEFLGEQVLVVTAVEQGEALLPVSVSANPAPEAFNWTFRGYRLSPAGGPRHRILSSGALHLWNVTRADDGLYQLHCQNSEGTAEARLRLDVHYAPTIRALQDPTEVNVGGSVDIVCTVDANPILPGMFNWERLGEDEEDQSLDDMEKISRGPTGRLRIHHAKLAQAGAYQCIVDNGVAPPARRLLRLVVRFAPQVEHPTPLTKVAAAGDSTSSATLHCRARGVPNIVFTWTKNGVPLDLQDPRYTEHTYHQGGVHSSLLTIANVSAAQDYALFTCTATNALGSDQTNIQLVSISRPDPPSGLKVVSLTPHSVGLEWKPGFDGGLPQRFCIRYEALGTPGFHYVDVVPPQATTFTLTGLQPSTRYRVWLLASNALGDSGLADKGTQLPITTPGLHQPSGEPEDQLPTEPPSGPSGLPLLPVLFALGGLLLLSNASCVGGVLWQRRLRRLAEGISEKTEAGSEEDRVRNEYEESQWTGERDTQSSTVSTTEAEPYYRSLRDFSPQLPPTQEEVSYSRGFTGEDEDMAFPGHLYDEVERTYPPSGAWGPLYDEVQMGPWDLHWPEDTYQDPRGIYDQVAGDLDTLEPDSLPFELRGHLV
| 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]; skeletal muscle tissue development [GO:0007519]; slit diaphragm assembly [GO:0036060]
|
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:0000250|UniProtKB:Q9R044, ECO:0000269|PubMed:28955049}.
|
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:0000250|UniProtKB:Q9QZS7, ECO:0000250|UniProtKB:Q9R044}.
|
Homo sapiens (Human)
|
O60502
|
OGA_HUMAN
|
MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKNDNQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL
|
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:0102166]; beta-N-acetylglucosaminidase activity [GO:0016231]; hyalurononglucosaminidase activity [GO:0004415]; identical protein binding [GO:0042802]
|
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:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680, ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600, ECO:0000269|PubMed:28939839, ECO:0000305|PubMed:20673219}; CATALYTIC ACTIVITY: Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H2O = L-threonyl-[protein] + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:48892, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:90840, ChEBI:CHEBI:506227; EC=3.2.1.169; Evidence={ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680, ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600, ECO:0000269|PubMed:28939839, ECO:0000305|PubMed:20673219};
|
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-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:20673219). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714). {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:20673219, ECO:0000269|PubMed:22365600, ECO:0000269|PubMed:24088714, ECO:0000269|PubMed:28939839}.; FUNCTION: [Isoform 3]: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1. {ECO:0000269|PubMed:20673219}.
|
Homo sapiens (Human)
|
O60503
|
ADCY9_HUMAN
|
MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDSGGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYALFYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALTLLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHLPLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFVMSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKRHATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMEDGKVIERLGQSVVADQLKGLKTYLISGQRAKESRCSCAEALLSGFEVIDGSQVSSGPRGQGTASSGNVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGAPQNGCQDEHKNSTKASGGPNPKTQNGLLSPPQEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNIREKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTFASPTFSSLLDVFLSTTVFLTLSTTCFLKYEAATVPPPPAALAVFSAALLLEVLSLAVSIRMVFFLEDVMACTKRLLEWIAGWLPRHCIGAILVSLPALAVYSHVTSEYETNIHFPVFTGSAALIAVVHYCNFCQLSSWMRSSLATVVGAGPLLLLYVSLCPDSSVLTSPLDAVQNFSSERNPCNSSVPRDLRRPASLIGQEVVLVFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTKIQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKECYRVLNELIGDFDELLSKPDYSSIEKIKTIGATYMAASGLNTAQAQDGSHPQEHLQILFEFAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDHRVIPQHQLSISPDIRVQVDGSIGRSPTDEIANLVPSVQYVDKTSLGSDSSTQAKDAHLSPKRPWKEPVKAEERGRFGKAIEKDDCDETGIEEANELTKLNVSKSV
|
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 transduction [GO:0007165]
|
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 beta-adrenergic receptors (PubMed:9628827). {ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952, ECO:0000269|PubMed:15879435, ECO:0000269|PubMed:9628827}.
|
Homo sapiens (Human)
|
O60504
|
VINEX_HUMAN
|
MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCNGGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVKYEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQQRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEESWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSPKSSPAPRRAPEQRPPAGPASAWSSSYPHAPYLGSARSLSPHKMADGGSPFLGRRDFVYPSSTRDPSASNGGGSPARREEKKRKAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEGEHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGEAVAQYTFKGDLEVELSFRKGEHICLIRKVNENWYEGRITGTGRQGIFPASYVQVSREPRLRLCDDGPQLPTSPRLTAAARSARHPSSPSALRSPADPIDLGGQTSPRRTGFSFPTQEPRPQTQNLGTPGPALSHSRGPSHPLDLGTSSPNTSQIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKFGTFPGNYVAPV
| 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 assembly [GO:0051496]
|
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 junction {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell-extracellular matrix junctions (By similarity). Both isoforms were localized at focal adhesion and cell-cell adhesion sites, vinexin beta was also found in the nucleus. {ECO:0000250}.
| 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
|
MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKAFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDSKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK
| 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-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000623]; negative regulation of translation [GO:0017148]; osteoblast differentiation [GO:0001649]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of DNA demethylation [GO:1901537]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]
|
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 complex [GO:0045293]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
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 is found in microsomes (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:O43390, ECO:0000250|UniProtKB:Q7TMK9}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7TMK9}. Note=Expressed predominantly in the nucleoplasm. {ECO:0000250|UniProtKB:Q7TMK9}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7TMK9}. Note=Expressed predominantly in the nucleoplasm. {ECO:0000250|UniProtKB:Q7TMK9}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7TMK9}. Note=Expressed predominantly in the nucleoplasm. {ECO:0000250|UniProtKB:Q7TMK9}.
| 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 to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:11134005, ECO:0000269|PubMed:11352648, ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:23071094}.
|
Homo sapiens (Human)
|
O60507
|
TPST1_HUMAN
|
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPVKLESTRTTVRTGLDLKANKTFAYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKEKIRLDEAGVTDEVLDSAMQAFLLEIIVKHGEPAPYLCNKDPFALKSLTYLSRLFPNAKFLLMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLQIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALSKWVGKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKPDPKIIENTRRVYKGEFQLPDFLKEKPQTEQVE
|
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; Evidence={ECO:0000269|PubMed:28821720, ECO:0000269|PubMed:9501187, ECO:0000269|PubMed:9733778};
| 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
|
MSAAIAALAASYGSGSGSESDSDSESSRCPLPAADSLMHLTKSPSSKPSLAVAVDSAPEVAVKEDLETGVHLDPAVKEVQYNPTYETMFAPEFGPENPFRTQQMAAPRNMLSGYAEPAHINDFMFEQQRRTFATYGYALDPSLDNHQVSAKYIGSVEEAEKNQGLTVFETGQKKTEKRKKFKENDASNIDGFLGPWAKYVDEKDVAKPSEEEQKELDEITAKRQKKGKQEEEKPGEEKTILHVKEMYDYQGRSYLHIPQDVGVNLRSTMPPEKCYLPKKQIHVWSGHTKGVSAVRLFPLSGHLLLSCSMDCKIKLWEVYGERRCLRTFIGHSKAVRDICFNTAGTQFLSAAYDRYLKLWDTETGQCISRFTNRKVPYCVKFNPDEDKQNLFVAGMSDKKIVQWDIRSGEIVQEYDRHLGAVNTIVFVDENRRFVSTSDDKSLRVWEWDIPVDFKYIAEPSMHSMPAVTLSPNGKWLACQSMDNQILIFGAQNRFRLNKKKIFKGHMVAGYACQVDFSPDMSYVISGDGNGKLNIWDWKTTKLYSRFKAHDKVCIGAVWHPHETSKVITCGWDGLIKLWD
| 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, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:33220177, ECO:0000269|PubMed:9830021}.
|
Homo sapiens (Human)
|
O60512
|
B4GT3_HUMAN
|
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPLSTANHTALRGSH
|
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={ECO:0000269|PubMed:11588157, ECO:0000269|PubMed:9405390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933; Evidence={ECO:0000269|PubMed:11588157, ECO:0000269|PubMed:9405390}; 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:9405390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746; Evidence={ECO:0000269|PubMed:9405390}; CATALYTIC ACTIVITY: Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275; Evidence={ECO:0000269|PubMed:9405390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500; Evidence={ECO:0000269|PubMed:9405390}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP; Xref=Rhea:RHEA:62552, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:79208, ChEBI:CHEBI:83264; Evidence={ECO:0000269|PubMed:9405390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553; Evidence={ECO:0000269|PubMed:9405390}; CATALYTIC ACTIVITY: Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer + H(+) + UDP; Xref=Rhea:RHEA:62548, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:90357, ChEBI:CHEBI:144378; Evidence={ECO:0000269|PubMed:9405390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549; Evidence={ECO:0000269|PubMed:9405390};
|
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 towards UDP-galactose {ECO:0000269|PubMed:9405390}; Vmax=66.25 pmol/min/mg enzyme towards for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390}; Vmax=60.85 pmol/min/mg enzyme towards D-GlcNAc {ECO:0000269|PubMed:9405390};
|
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
|
MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEIPKAKEFMANFHKTLILGKGKTLTNEASTKKVELDNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYRPQECKALQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLEALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSREQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVFHTRDKGNEVNAERMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITVDFWFGA
|
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}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746; Evidence={ECO:0000269|PubMed:9792633}; CATALYTIC ACTIVITY: Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275; Evidence={ECO:0000269|PubMed:9792633}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500; Evidence={ECO:0000269|PubMed:9792633}; CATALYTIC ACTIVITY: Reaction=3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + UDP-alpha-D-galactose = 3-O-{beta-D-galactosyl-(1->3)-[beta-D-galactosyl-(1->4)-6-O-sulfo-N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:67948, Rhea:RHEA-COMP:17367, Rhea:RHEA-COMP:17398, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:176494, ChEBI:CHEBI:176635; Evidence={ECO:0000305|PubMed:12511560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67949; Evidence={ECO:0000305|PubMed:12511560}; CATALYTIC ACTIVITY: Reaction=3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + UDP-alpha-D-galactose = 3-O-{beta-D-galactosyl-(1->3)-[beta-D-galactosyl-(1->4)-6-O-sulfo-N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:67872, Rhea:RHEA-COMP:17370, Rhea:RHEA-COMP:17397, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:176493, ChEBI:CHEBI:176634; Evidence={ECO:0000305|PubMed:12511560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67873; Evidence={ECO:0000305|PubMed:12511560};
|
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->2Manalpha1->3(Manalpha1->6)Manbeta1->4GlcNAcbeta1->4( Fucalpha1->6)GlcNAc (6S-biGP) {ECO:0000269|PubMed:12511560}; KM=7.7 mM for GlcNAcbeta1->2Manalpha1->3(Manalpha1->6)Manbeta1->4GlcNAcbeta1->4(Fuc alpha1->6)GlcNAc (biGP) {ECO:0000269|PubMed:12511560}; KM=0.091 mM for SO3->6GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP (6S-core2-O-pNP) {ECO:0000269|PubMed:12511560}; KM=0.5 mM for GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP (core2-O-pNP) {ECO:0000269|PubMed:12511560}; KM=0.38 mM for SO3->6GlcNAcbeta1->3Galbeta1->4(SO3->6)GlcNAc (agL2L2) {ECO:0000269|PubMed:12511560}; KM=0.63 mM for SO3->6GlcNAcbeta1->3(SO3->6)Galbeta1->4(SO3->6)GlcNAc (agL2L4) {ECO:0000269|PubMed:12511560}; Vmax=3.6 nmol/min/mg enzyme toward SO3->6GlcNAc (6SGN) {ECO:0000269|PubMed:12511560}; Vmax=1.5 nmol/min/mg enzyme toward GlcNAc {ECO:0000269|PubMed:12511560}; Vmax=3.2 nmol/min/mg enzyme toward 6GlcNAcbeta1->2Manalpha1->3(Manalpha1->6)Manbeta1->4GlcNAcbeta1->4(Fu calpha1->6)GlcNAc (6S-biGP) {ECO:0000269|PubMed:12511560}; Vmax=0.42 nmol/min/mg enzyme toward GlcNAcbeta1->2Manalpha1->3(Manalpha1->6)Manbeta1->4GlcNAcbeta1->4(Fuc alpha1->6)GlcNAc (biGP) {ECO:0000269|PubMed:12511560}; Vmax=4.8 nmol/min/mg enzyme toward SO3->6GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP (6S-core2-O-pNP) {ECO:0000269|PubMed:12511560}; Vmax=1.2 nmol/min/mg enzyme toward GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP (core2-O-pNP) {ECO:0000269|PubMed:12511560}; Vmax=7.8 nmol/min/mg enzyme toward SO3->6GlcNAcbeta1->3Galbeta1->4(SO3->6)GlcNAc (agL2L2) {ECO:0000269|PubMed:12511560}; Vmax=7.8 nmol/min/mg enzyme toward SO3->6GlcNAcbeta1->3(SO3->6)Galbeta1->4(SO3->6)GlcNAc (agL2L4) {ECO:0000269|PubMed:12511560};
|
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 the non-reducing terminal N-acetyl glucosamine 6-O-sulfate (6-O-sulfoGlcNAc) in the linearly growing chain of both N- and O-linked keratan sulfate proteoglycans. Cooperates with B3GNT7 N-acetyl glucosamine transferase and CHST6 and CHST1 sulfotransferases to construct and elongate mono- and disulfated disaccharide units [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer (PubMed:17690104). Transfers Gal residue via a beta1->4 linkage to terminal 6-O-sulfoGlcNAc within the LacNac unit of core 2 O-glycans forming 6-sulfo-sialyl-Lewis X (sLex). May contribute to the generation of sLex epitope on mucin-type glycoproteins that serve as ligands for SELL/L-selectin, a major regulator of leukocyte migration (PubMed:12511560). In the biosynthesis pathway of neolacto-series glycosphingolipids, transfers Gal residue via a beta1->4 linkage to terminal GlcNAc of a lactotriaosylceramide (Lc3Cer) acceptor to form a neolactotetraosylceramide (PubMed:9792633). {ECO:0000269|PubMed:12511560, ECO:0000269|PubMed:17690104, ECO:0000269|PubMed:9792633}.
|
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, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (By similarity). Inhibits EIF4E-mediated mRNA nuclear export (PubMed:22684010). {ECO:0000250|UniProtKB:Q13541, ECO:0000269|PubMed:22684010}.
|
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 biosynthetic process [GO:0046889]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; protein stabilization [GO:0050821]; regulation of DNA-templated transcription [GO:0006355]; signal transduction [GO:0007165]
|
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
|
MKSRFSTIDLRAVLAELNASLLGMRVNNVYDVDNKTYLIRLQKPDFKATLLLESGIRIHTTEFEWPKNMMPSSFAMKCRKHLKSRRLVSAKQLGVDRIVDFQFGSDEAAYHLIIELYDRGNIVLTDYEYVILNILRFRTDEADDVKFAVRERYPLDHARAAEPLLTLERLTEIVASAPKGELLKRVLNPLLPYGPALIEHCLLENGFSGNVKVDEKLETKDIEKVLVSLQKAEDYMKTTSNFSGKGYIIQKREIKPSLEADKPVEDILTYEEFHPFLFSQHSQCPYIEFESFDKAVDEFYSKIEGQKIDLKALQQEKQALKKLDNVRKDHENRLEALQQAQEIDKLKGELIEMNLQIVDRAIQVVRSALANQIDWTEIGLIVKEAQAQGDPVASAIKELKLQTNHVTMLLRNPYLLSEEEDDDVDGDVNVEKNETEPPKGKKKKQKNKQLQKPQKNKPLLVDVDLSLSAYANAKKYYDHKRYAAKKTQKTVEAAEKAFKSAEKKTKQTLKEVQTVTSIQKARKVYWFEKFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIKNPTGEPIPPRTLTEAGTMALCYSAAWDARVITSAWWVYHHQVSKTAPTGEYLTTGSFMIRGKKNFLPPSYLMMGFSFLFKVDESCVWRHQGERKVRVQDEDMETLASCTSELISEEMEQLDGGDTSSDEDKEEHETPVEVELMTQVDQEDITLQSGRDELNEELIQEESSEDEGEYEEVRKDQDSVGEMKDEGEETLNYPDTTIDLSHLQPQRSIQKLASKEESSNSSDSKSQSRRHLSAKERREMKKKKLPSDSGDLEALEGKDKEKESTVHIETHQNTSKNVAAVQPMKRGQKSKMKKMKEKYKDQDEEDRELIMKLLGSAGSNKEEKGKKGKKGKTKDEPVKKQPQKPRGGQRVSDNIKKETPFLEVITHELQDFAVDDPHDDKEEQDLDQQGNEENLFDSLTGQPHPEDVLLFAIPICAPYTTMTNYKYKVKLTPGVQKKGKAAKTALNSFMHSKEATAREKDLFRSVKDTDLSRNIPGKVKVSAPNLLNVKRK
| 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:33909987). Thereby, frees 60S subunit ribosomes from the stalled translation complex and prevents the accumulation of nascent polypeptide chains that are potentially toxic for the cell (PubMed:25578875, PubMed:33406423, PubMed:33909987). Within the RQC complex, NEMF specifically binds stalled 60S ribosomal subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety and promotes the recruitment of LTN1 to stalled 60S subunits (PubMed:25578875). Following binding to stalled 60S ribosomal subunits, NEMF mediates CAT tailing by recruiting alanine-charged tRNA to the A-site and directing the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal alanine extensions (CAT tails) (PubMed:33406423, PubMed:33909987). Mainly recruits alanine-charged tRNAs, but can also other amino acid-charged tRNAs (PubMed:33406423, PubMed:33909987). CAT tailing is required to promote ubiquitination of stalled nascent chains by different E3 ubiquitin-protein ligases (PubMed:33909987). In the canonical RQC pathway (RQC-L), CAT tailing facilitates LTN1-dependent ubiquitination by exposing lysine residues that would otherwise remain buried in the ribosomal exit tunnel (By similarity). In the alternative RQC pathway (RQC-C) CAT tailing creates an C-degron mainly composed of alanine that is recognized by the CRL2(KLHDC10) and RCHY1/PIRH2 E3 ligases, leading to ubiquitination and degradation of stalled nascent chains (PubMed:33909987). NEMF may also indirectly play a role in nuclear export (PubMed:16103875). {ECO:0000250|UniProtKB:Q12532, ECO:0000269|PubMed:16103875, ECO:0000269|PubMed:25578875, ECO:0000269|PubMed:32726578, ECO:0000269|PubMed:33406423, ECO:0000269|PubMed:33909987}.
|
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 execution phase of apoptosis [GO:1900118]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of sequestering of triglyceride [GO:0010890]; regulation of apoptotic DNA fragmentation [GO:1902510]; regulation of apoptotic process [GO:0042981]; response to stilbenoid [GO:0035634]; temperature homeostasis [GO:0001659]
|
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 sites between lipid droplets, and mediates atypical lipid droplet fusion by promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (By similarity). The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC (By similarity). May also act as a CEBPB coactivator in epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein (By similarity). By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (By similarity). When overexpressed, induces apoptosis; the physiological significance of its role in apoptosis is unclear (By similarity). {ECO:0000250|UniProtKB:O70302, ECO:0000269|PubMed:19843876, ECO:0000269|PubMed:26118629}.
|
Homo sapiens (Human)
|
O60547
|
GMDS_HUMAN
|
MAHAPARCPSARGSGDGEMGKPRNVALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTGRIEHLYKNPQAHIEGNMKLHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDLAEYTADVDGVGTLRLLDAVKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATGEVHSVREFVEKSFLHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCTKAKQKLNWKPRVAFDELVREMVHADVELMRTNPNA
|
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
|
MTLGSCCCEIMSSESSPAALSEADADIDVVGGGSGGGELPARSGPRAPRDVLPHGHEPPAEEAEADLAEDEEESGGCSDGEPRALASRGAAAAAGSPGPGAAAARGAAGPGPGPPSGGAATRSPLVKPPYSYIALITMAILQSPKKRLTLSEICEFISGRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPESADMFDNGSFLRRRKRFKRQPLPPPHPHPHPHPELLLRGGAAAAGDPGAFLPGFAAYGAYGYGYGLALPAYGAPPPGPAPHPHPHPHAFAFAAAAAAAPCQLSVPPGRAAAPPPGPPTASVFAGAGSAPAPAPASGSGPGPGPAGLPAFLGAELGCAKAFYAASLSPPAAGTAAGLPTALLRQGLKTDAGGGAGGGGAGAGQRPSFSIDHIMGHGGGGAAPPGAGEGSPGPPFAAAAGPGGQAQVLAMLTAPALAPVAGHIRLSHPGDALLSSGSRFASKVAGLSGCHF
| 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-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
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
|
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPNSGGTKSDSASDSQEIKIQQPSKNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVAHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ
|
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:0000269|PubMed:25255805, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:9506952}; CATALYTIC ACTIVITY: Reaction=N-terminal glycyl-L-lysyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-terminal glycyl-(N(6)-tetradecanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:70671, Rhea:RHEA-COMP:17947, Rhea:RHEA-COMP:17948, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:189855, ChEBI:CHEBI:189856; Evidence={ECO:0000269|PubMed:32103017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70672; Evidence={ECO:0000269|PubMed:32103017};
| 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 required to maintain ARF6 on membranes during the GTPase cycle (PubMed:32103017). {ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:9506952}.
|
Homo sapiens (Human)
|
O60563
|
CCNT1_HUMAN
|
MEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFPGNSVAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHEFLQILEKTPNRLKRIWNWRACEAAKKTKADDRGTDEKTSEQTILNMISQSSSDTTIAGLMSMSTSTTSAVPSLPVSEESSSNLTSVEMLPGKRWLSSQPSFKLEPTQGHRTSENLALTGVDHSLPQDGSNAFISQKQNSKSVPSAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLSHHDSHSSVILKMPIEGSENPERPFLEKADKTALKMRIPVAGGDKAASSKPEEIKMRIKVHAAADKHNSVEDSVTKSREHKEKHKTHPSNHHHHHNHHSHKHSHSQLPVGTGNKRPGDPKHSSQTSNLAHKTYSLSSSFSSSSSTRKRGPSEETGGAVFDHPAKIAKSTKSSSLNFSFPSLPTMGQMPGHSSDTSGLSFSQPSCKTRVPHSKLDKGPTGANGHNTTQTIDYQDTVNMLHSLLSAQGVQPTQPTAFEFVRPYSDYLNPRSGGISSRSGNTDKPRPPPLPSEPPPPLPPLPK
| 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 RNA polymerase II [GO:0032968]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of transcription by RNA polymerase II [GO:0006357]; response to xenobiotic stimulus [GO:0009410]; transcription by RNA polymerase II [GO:0006366]
|
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 polymerase binding [GO:0070063]; transcription cis-regulatory region binding [GO:0000976]
|
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 (RNA Pol II) (PubMed:16109376, PubMed:16109377, PubMed:30134174, PubMed:35393539). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II (PubMed:29849146, PubMed:35393539). {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:29849146, ECO:0000269|PubMed:30134174, ECO:0000269|PubMed:35393539}.; FUNCTION: (Microbial infection) In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes. {ECO:0000269|PubMed:10329125, ECO:0000269|PubMed:10329126}.
|
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:0030199]; determination of dorsal identity [GO:0048263]; embryonic limb morphogenesis [GO:0030326]; limb development [GO:0060173]; mesenchymal to epithelial transition involved in metanephros morphogenesis [GO:0003337]; negative regulation of apoptotic process [GO:0043066]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of bone mineralization [GO:0030502]; negative regulation of bone mineralization involved in bone maturation [GO:1900158]; negative regulation of bone remodeling [GO:0046851]; negative regulation of bone trabecula formation [GO:1900155]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell growth [GO:0030308]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of monocyte chemotaxis [GO:0090027]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of osteoclast proliferation [GO:0090291]; negative regulation of SMAD protein signal transduction [GO:0060392]; positive regulation of angiogenesis [GO:0045766]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of peptidyl-tyrosine autophosphorylation [GO:1900086]; positive regulation of receptor internalization [GO:0002092]; positive regulation of signaling receptor activity [GO:2000273]; positive regulation of telomerase activity [GO:0051973]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proximal/distal pattern formation [GO:0009954]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of focal adhesion assembly [GO:0051893]; sequestering of BMP from receptor via BMP binding [GO:0038098]; signal transduction [GO:0007165]; ureteric bud formation [GO:0060676]
|
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:0043184]
|
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; inhibits BMP2-mediated differentiation of osteoblasts (in vitro) (PubMed:27036124). Acts as inhibitor of monocyte chemotaxis. Can inhibit the growth or viability of normal cells but not transformed cells when is overexpressed (By similarity). {ECO:0000250|UniProtKB:O35793, ECO:0000250|UniProtKB:O70326, ECO:0000269|PubMed:27036124}.
|
Homo sapiens (Human)
|
O60566
|
BUB1B_HUMAN
|
MAAVKKEGGALSEAMSLEGDEWELSKENVQPLRQGRIMSTLQGALAQESACNNTLQQQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPLDMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGIQQKAEPLERLQSQHRQFQARVSRQTLLALEKEEEEEVFESSVPQRSTLAELKSKGKKTARAPIIRVGGALKAPSQNRGLQNPFPQQMQNNSRITVFDENADEASTAELSKPTVQPWIAPPMPRAKENELQAGPWNTGRSLEHRPRGNTASLIAVPAVLPSFTPYVEETARQPVMTPCKIEPSINHILSTRKPGKEEGDPLQRVQSHQQASEEKKEKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKEQREAELLTSAEKRAEMQKQIEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQKIPGMTLSSSVCQVNCCARETSLAENIWQEQPHSKGPSVPFSIFDEFLLSEKKNKSPPADPPRVLAQRRPLAVLKTSESITSNEDVSPDVCDEFTGIEPLSEDAIITGFRNVTICPNPEDTCDFARAARFVSTPFHEIMSLKDLPSDPERLLPEEDLDVKTSEDQQTACGTIYSQTLSIKKLSPIIEDSREATHSSGFSGSSASVASTSSIKCLQIPEKLELTNETSENPTQSPWCSQYRRQLLKSLPELSASAELCIEDRPMPKLEIEKEIELGNEDYCIKREYLICEDYKLFWVAPRNSAELTVIKVSSQPVPWDFYINLKLKERLNEDFDHFCSCYQYQDGCIVWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCNKNNQALKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILANCSSPYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLSQNISELKDGELWNKFFVRILNANDEATVSVLGELAAEMNGVFDTTFQSHLNKALWKVGKLTSPGALLFQ
|
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, centromeric region [GO:0071459]
|
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 Lys-250 regulates its degradation and timing in anaphase entry. {ECO:0000269|PubMed:19407811}.; PTM: Ubiquitinated. Degraded by the proteasome. {ECO:0000269|PubMed:19407811}.; PTM: Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the association with CENPE at the kinetochore. {ECO:0000269|PubMed:18374647}.; PTM: Autophosphorylated in vitro. Intramolecular autophosphorylation is stimulated by CENPE. Phosphorylated during mitosis and hyperphosphorylated in mitotically arrested cells. Phosphorylation at Ser-670 and Ser-1043 occurs at kinetochores upon mitotic entry with dephosphorylation at the onset of anaphase. {ECO:0000269|PubMed:10477750, ECO:0000269|PubMed:10593653, ECO:0000269|PubMed:17376779, ECO:0000269|PubMed:17785528, ECO:0000269|PubMed:19015317}.
|
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-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| 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 blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. May play a role for tumor suppression. {ECO:0000269|PubMed:10477750, ECO:0000269|PubMed:11702782, ECO:0000269|PubMed:14706340, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:19411850, ECO:0000269|PubMed:19503101}.
|
Homo sapiens (Human)
|
O60568
|
PLOD3_HUMAN
|
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP
|
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 [GO:0060425]; neural tube development [GO:0021915]; peptidyl-lysine hydroxylation [GO:0017185]; protein localization [GO:0008104]; protein O-linked glycosylation [GO:0006493]; vasodilation [GO:0042311]
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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]; trans-Golgi network [GO:0005802]
|
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 {ECO:0000269|PubMed:21465473}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q9R0E1}. Note=The majority of the secreted protein is associated with the extracellular matrix. {ECO:0000250|UniProtKB:Q9R0E1}.
|
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; Evidence={ECO:0000269|PubMed:10934207, ECO:0000269|PubMed:11956192, ECO:0000269|PubMed:12475640, ECO:0000269|PubMed:18298658, ECO:0000269|PubMed:18834968, ECO:0000269|PubMed:30089812, ECO:0000269|PubMed:9582318, ECO:0000269|PubMed:9724729}; CATALYTIC ACTIVITY: Reaction=(5R)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-galactose = (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + H(+) + UDP; Xref=Rhea:RHEA:12637, Rhea:RHEA-COMP:12752, Rhea:RHEA-COMP:12753, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:133442, ChEBI:CHEBI:133443; EC=2.4.1.50; Evidence={ECO:0000269|PubMed:12475640, ECO:0000269|PubMed:18298658, ECO:0000269|PubMed:18834968, ECO:0000269|PubMed:30089812}; CATALYTIC ACTIVITY: Reaction=(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-glucose = (5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysyl-[collagen] + H(+) + UDP; Xref=Rhea:RHEA:12576, Rhea:RHEA-COMP:12753, Rhea:RHEA-COMP:12754, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:133443, ChEBI:CHEBI:133452; EC=2.4.1.66; Evidence={ECO:0000269|PubMed:10934207, ECO:0000269|PubMed:11896059, ECO:0000269|PubMed:11956192, ECO:0000269|PubMed:12475640, ECO:0000269|PubMed:18298658, ECO:0000269|PubMed:18834968, ECO:0000269|PubMed:30089812};
|
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 for ascorbate {ECO:0000269|PubMed:11956192};
| 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- sequences in collagens (PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812, PubMed:9582318, PubMed:9724729). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:10934207, PubMed:11896059, PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:25419660). Essential for normal biosynthesis and secretion of type IV collagens (Probable) (PubMed:18834968). Essential for normal formation of basement membranes (By similarity). {ECO:0000250|UniProtKB:Q9R0E1, ECO:0000269|PubMed:10934207, ECO:0000269|PubMed:11896059, ECO:0000269|PubMed:11956192, ECO:0000269|PubMed:12475640, ECO:0000269|PubMed:18298658, ECO:0000269|PubMed:18834968, ECO:0000269|PubMed:25419660, ECO:0000269|PubMed:30089812, ECO:0000269|PubMed:9582318, ECO:0000269|PubMed:9724729, ECO:0000305}.
|
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 initiation [GO:0006413]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; P-body [GO:0000932]
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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]
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PF01652;
|
3.30.760.10;
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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 degradation (PubMed:14623119). {ECO:0000269|PubMed:14623119, ECO:0000269|PubMed:25624349}.; PTM: ISGylation enhances its cap structure-binding activity and translation-inhibition activity. {ECO:0000269|PubMed:17289916}.
|
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), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity). In P-bodies, component of a complex that promotes miRNA-mediated translational repression (PubMed:28487484). Involved in virus-induced host response by mediating miRNA MIR34A-induced translational silencing which controls IFNB1 production by a negative feedback mechanism (PubMed:28487484, PubMed:33581076). {ECO:0000250|UniProtKB:Q8BMB3, ECO:0000269|PubMed:17368478, ECO:0000269|PubMed:22751931, ECO:0000269|PubMed:25624349, ECO:0000269|PubMed:28487484, ECO:0000269|PubMed:33581076, ECO:0000269|PubMed:9582349}.; FUNCTION: Component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931, PubMed:35878012). In association with GIGYF2, assists ribosome-associated quality control (RQC) by sequestering the mRNA cap, blocking ribosome initiation and decreasing the translational load on problematic messages. Part of a pathway that works in parallel to RQC-mediated degradation of the stalled nascent polypeptide. GIGYF2 and EIF4E2 work downstream and independently of ZNF598, which seems to work as a scaffold that can recruit them to faulty mRNA even if alternative recruitment mechanisms may exist (PubMed:32726578). {ECO:0000269|PubMed:22751931, ECO:0000269|PubMed:32726578, ECO:0000269|PubMed:35878012}.; FUNCTION: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 infection, the interaction with non-structural protein 2 (nsp2) with GIGYF2 enhances GIGYF2 binding to EIF4E2 and increases repression of translation initiation of genes involved in antiviral innate immune response such as IFNB1. {ECO:0000269|PubMed:35878012}.
|
Homo sapiens (Human)
|
O60583
|
CCNT2_HUMAN
|
MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKNIISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNISVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKISDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTSPIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKSSGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM
| 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 polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of muscle cell differentiation [GO:0051147]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle tissue development [GO:0007519]; transcription by RNA polymerase II [GO:0006366]
|
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]
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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 RNA polymerase II (RNAP II) (PubMed:15563843, PubMed:9499409). The activity of this complex is regulated by binding with 7SK snRNA (PubMed:11713533). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II (By similarity). In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (PubMed:16331689). Involved in early embryo development (By similarity). {ECO:0000250|UniProtKB:Q7TQK0, ECO:0000269|PubMed:11713533, ECO:0000269|PubMed:15563843, ECO:0000269|PubMed:16331689, ECO:0000269|PubMed:9499409}.; FUNCTION: (Microbial infection) Promotes transcriptional activation of early and late herpes simplex virus 1/HHV-1 promoters. {ECO:0000269|PubMed:21509660}.
|
Homo sapiens (Human)
|
O60602
|
TLR5_HUMAN
|
MGDHLDLLLGVVLMAGPVFGIPSCSFDGRIAFYRFCNLTQVPQVLNTTERLLLSFNYIRTVTASSFPFLEQLQLLELGSQYTPLTIDKEAFRNLPNLRILDLGSSKIYFLHPDAFQGLFHLFELRLYFCGLSDAVLKDGYFRNLKALTRLDLSKNQIRSLYLHPSFGKLNSLKSIDFSSNQIFLVCEHELEPLQGKTLSFFSLAANSLYSRVSVDWGKCMNPFRNMVLEILDVSGNGWTVDITGNFSNAISKSQAFSLILAHHIMGAGFGFHNIKDPDQNTFAGLARSSVRHLDLSHGFVFSLNSRVFETLKDLKVLNLAYNKINKIADEAFYGLDNLQVLNLSYNLLGELYSSNFYGLPKVAYIDLQKNHIAIIQDQTFKFLEKLQTLDLRDNALTTIHFIPSIPDIFLSGNKLVTLPKINLTANLIHLSENRLENLDILYFLLRVPHLQILILNQNRFSSCSGDQTPSENPSLEQLFLGENMLQLAWETELCWDVFEGLSHLQVLYLNHNYLNSLPPGVFSHLTALRGLSLNSNRLTVLSHNDLPANLEILDISRNQLLAPNPDVFVSLSVLDITHNKFICECELSTFINWLNHTNVTIAGPPADIYCVYPDSFSGVSLFSLSTEGCDEEEVLKSLKFSLFIVCTVTLTLFLMTILTVTKFRGFCFICYKTAQRLVFKDHPQGTEPDMYKYDAYLCFSSKDFTWVQNALLKHLDTQYSDQNRFNLCFEERDFVPGENRIANIQDAIWNSRKIVCLVSRHFLRDGWCLEAFSYAQGRCLSDLNSALIMVVVGSLSQYQLMKHQSIRGFVQKQQYLRWPEDLQDVGWFLHKLSQQILKKEKEKKKDNNIPLQTVATIS
| 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-associated molecular patterns (MAMPs) usually expressed by resident microbiota (PubMed:29934223). Upon ligand binding such as bacterial flagellins, recruits intracellular adapter proteins MYD88 and TRIF leading to NF-kappa-B activation, cytokine secretion and induction of the inflammatory response (PubMed:11489966, PubMed:20855887). Plays thereby an important role in the relationship between the intestinal epithelium and enteric microbes and contributes to the gut microbiota composition throughout life (By similarity). {ECO:0000250|UniProtKB:Q9JLF7, ECO:0000269|PubMed:11323673, ECO:0000269|PubMed:11489966, ECO:0000269|PubMed:18490781, ECO:0000269|PubMed:20855887, ECO:0000269|PubMed:29934223}.
|
Homo sapiens (Human)
|
O60603
|
TLR2_HUMAN
|
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNIDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS
| 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:0071346]; central nervous system myelin formation [GO:0032289]; defense response to Gram-positive bacterium [GO:0050830]; defense response to virus [GO:0051607]; detection of diacyl bacterial lipopeptide [GO:0042496]; detection of triacyl bacterial lipopeptide [GO:0042495]; I-kappaB phosphorylation [GO:0007252]; immune response [GO:0006955]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; learning [GO:0007612]; leukotriene metabolic process [GO:0006691]; microglia development [GO:0014005]; microglial cell activation [GO:0001774]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of phagocytosis [GO:0050765]; negative regulation of synapse assembly [GO:0051964]; nitric oxide metabolic process [GO:0046209]; positive regulation of cellular response to macrophage colony-stimulating factor stimulus [GO:1903974]; positive regulation of chemokine production [GO:0032722]; positive regulation of gene expression [GO:0010628]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-18 production [GO:0032741]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of matrix metallopeptidase secretion [GO:1904466]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of oligodendrocyte differentiation [GO:0048714]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of Wnt signaling pathway [GO:0030177]; response to fatty acid [GO:0070542]; response to hypoxia [GO:0001666]; response to insulin [GO:0032868]; response to progesterone [GO:0032570]; response to toxic substance [GO:0009636]; signal transduction [GO:0007165]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]
|
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 receptor 1-Toll-like receptor 2 protein complex [GO:0035354]; Toll-like receptor 2-Toll-like receptor 6 protein complex [GO:0035355]
|
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:0042834]; protein-containing complex binding [GO:0044877]; signaling receptor activity [GO:0038023]; Toll-like receptor binding [GO:0035325]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497]
|
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:0000269|PubMed:27805901}.
|
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 before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determines the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000269|PubMed:16880211}.
| 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 NF-kappa-B activation, cytokine secretion and the inflammatory response. May also activate immune cells and promote apoptosis in response to the lipid moiety of lipoproteins (PubMed:10426995, PubMed:10426996). Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6 (PubMed:11441107). Stimulation of monocytes in vitro with M.tuberculosis PstS1 induces p38 MAPK and ERK1/2 activation primarily via this receptor, but also partially via TLR4 (PubMed:16622205). MAPK activation in response to bacterial peptidoglycan also occurs via this receptor (PubMed:16622205). Acts as a receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PstS1, some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36); the lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). M.tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this protein to stimulate NF-kappa-B expression (PubMed:15809303). Recognizes M.tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (shown in mouse) (By similarity). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (PubMed:16880211). Required for normal uptake of M.tuberculosis, a process that is inhibited by M.tuberculosis LppM (By similarity). {ECO:0000250|UniProtKB:Q9QUN7, ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:10426996, ECO:0000269|PubMed:11441107, ECO:0000269|PubMed:15809303, ECO:0000269|PubMed:16622205, ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:17889651, ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:21078852}.
|
Homo sapiens (Human)
|
O60609
|
GFRA3_HUMAN
|
MVRPLNPRPLPPVVLMLLLLLPPSPLPLAAGDPLPTESRLMNSCLQARRKCQADPTCSAAYHHLDSCTSSISTPLPSEEPSVPADCLEAAQQLRNSSLIGCMCHRRMKNQVACLDIYWTVHRARSLGNYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLNDKCDRLRKAYGEACSGPHCQRHVCLRQLLTFFEKAAEPHAQGLLLCPCAPNDRGCGERRRNTIAPNCALPPVAPNCLELRRLCFSDPLCRSRLVDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFVSNVNTSVALSCTCRGSGNLQEECEMLEGFFSHNPCLTEAIAAKMRFHSQLFSQDWPHPTFAVMAHQNENPAVRPQPWVPSLFSCTLPLILLLSLW
| 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|PubMed:9883723}.
|
Homo sapiens (Human)
|
O60610
|
DIAP1_HUMAN
|
MEPPGGSLGPGRGTRDKKKGRSPDELPSAGGDGGKSKKFTLKRLMADELERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYTSKAGMSQKESSKSAMMYIQELRSGLRDMPLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETAGSYDSRNKHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTTIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDLREIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECISQIVLHKNGADPDFKCRHLQIEIEGLIDQMIDKTKVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVPPSVPSRAPVPPAPPLPGDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGDATIPPPPPLPEGVGIPSPSSLPGGTAIPPPPPLPGSARIPPPPPPLPGSAGIPPPPPPLPGEAGMPPPPPPLPGGPGIPPPPPFPGGPGIPPPPPGMGMPPPPPFGFGVPAAPVLPFGLTPKKLYKPEVQLRRPNWSKLVAEDLSQDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQANRKAGCAVTSLLASELTKDDAMAAVPAKVSKNSETFPTILEEAKELVGRAS
| 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]; regulation of microtubule-based process [GO:0032886]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; sensory perception of sound [GO:0007605]
|
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 {ECO:0000269|PubMed:24781755}. Cytoplasm {ECO:0000250|UniProtKB:O08808}. Nucleus {ECO:0000250|UniProtKB:O08808}. Note=Membrane ruffles, especially at the tip of ruffles, of motile cells. {ECO:0000250|UniProtKB:O08808}.
| 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 activation of the serum response factor (By similarity). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (By similarity). Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity). Has neurite outgrowth promoting activity. Acts in a Rho-dependent manner to recruit PFY1 to the membrane (By similarity). In hear cells, it may play a role in the regulation of actin polymerization in hair cells (PubMed:20937854, PubMed:21834987, PubMed:26912466). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854, PubMed:21834987). It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity (PubMed:20937854, PubMed:21834987). In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (PubMed:20937854, PubMed:21834987). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (PubMed:20937854, PubMed:21834987). Plays a role in brain development (PubMed:24781755). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (By similarity). {ECO:0000250|UniProtKB:O08808, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:24781755, ECO:0000269|PubMed:26912466}.
|
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 (PubMed:24415556). {ECO:0000250|UniProtKB:Q923V8, ECO:0000269|PubMed:24415556}.
|
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:30066932, PubMed:30291375). Regulates neuronal differentiation in response to NGF by facilitating NGF-mediated activation of NTRK1/TRKA receptor tyrosine kinase and subsequent downstream signaling pathways (By similarity). Plays a role in the inhibition of TNFalpha-induced apoptosis. Mechanistically, inhibits the NF-kappa-B signaling pathway by blocking phosphorylation of CHUK (PubMed:30291375). Promotes also the stability of the thiamine transporter 1/SLC19A2 in intestinal epithelial cells leading to an increase of thiamine uptake process (PubMed:21836059). {ECO:0000250|UniProtKB:Q6AYR9, ECO:0000269|PubMed:21836059, ECO:0000269|PubMed:30066932, ECO:0000269|PubMed:30291375}.
|
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
|
MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDLFATASAAVPVSTSKPSSDLLDLQPDFSSGGAAAAAAPAPPPPAGGATAWGDLLGEDSLAALSSVPSEAQISDPFAPEPTPPTTTAEIATASASASTTTTVTAVTAEVDLFGDAFAASPGEAPAASEGAAAPATPTPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSVPVVTPTASTAPPVPATAPSPAPAVAAAAAATTAATAAATTTTTTSAATATTAPPALDIFGDLFESTPEVAAAPKPDAAPSIDLFSTDAFSSPPQGASPVPESSLTADLLSVDAFAAPSPATTASPAKVDSSGVIDLFGDAFGSSASEPQPASQAASSSSASADLLAGFGGSFMAPSPSPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSVFDGLGDLLMPTMAPAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTTTKKGDLQWNAGEKKLTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDPLADLNIKDFL
| 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 their assembly into 60-70 nm coats (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O60645
|
EXOC3_HUMAN
|
MKETDREAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMYEQYRMDSGNTRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFTILERTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLIVAKNLMVQCFPPHYEIFKNLLNMYHQALSTRMQDLASEDLEANEIVSLLTWVLNTYTSTEMMRNVELAPEVDVGTLEPLLSPHVVSELLDTYMSTLTSNIIAWLRKALETDKKDWVKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKDEAQLYKEEHLRNRQHPHCYVQYMIAIINNCQTFKESIVSLKRKYLKNEVEEGVSPSQPSMDGILDAIAKEGCSGLLEEVFLDLEQHLNELMTKKWLLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSPEERKEGAEKMVREAEQLRFLFRKLASGFGEDVDGYCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLAVRGDASRDMKQTIMETLEQGPAQASPSYVPLFKDIVVPSLNVAKLLK
| 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|UniProtKB:Q62825}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). During mitosis, early recruitment to the midbody requires RALA, but not RALB, and EXOC2. In late stages of cytokinesis, localization to the midbody is RALB-dependent (PubMed:18756269). {ECO:0000250|UniProtKB:O54921, ECO:0000269|PubMed:18756269}.
| 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
|
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMPEVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLFFSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEGAQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVTEYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
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 glucuronosyltransferase activity [GO:1904224]; retinoic acid metabolic process [GO:0042573]; xenobiotic glucuronidation [GO:0052697]; xenobiotic metabolic process [GO:0006805]
|
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, ECO:0000269|PubMed:15472229, ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:18052087, ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:19545173}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033; Evidence={ECO:0000305|PubMed:12181437, ECO:0000305|PubMed:15470161, ECO:0000305|PubMed:15472229, ECO:0000305|PubMed:18004212, ECO:0000305|PubMed:18052087, ECO:0000305|PubMed:18674515, ECO:0000305|PubMed:19545173}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 2-hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53004, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136931; Evidence={ECO:0000269|PubMed:15472229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53005; Evidence={ECO:0000305|PubMed:15472229}; CATALYTIC ACTIVITY: Reaction=4-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol 4-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53040, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:62845, ChEBI:CHEBI:136937; Evidence={ECO:0000269|PubMed:15472229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53041; Evidence={ECO:0000305|PubMed:15472229}; CATALYTIC ACTIVITY: Reaction=2-hydroxyestrone + UDP-alpha-D-glucuronate = 2-hydroxyestrone 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53048, ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136967; Evidence={ECO:0000269|PubMed:15472229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53049; Evidence={ECO:0000305|PubMed:15472229}; CATALYTIC ACTIVITY: Reaction=4-hydroxyestrone + UDP-alpha-D-glucuronate = estrone 4-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53060, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:87602, ChEBI:CHEBI:136970; Evidence={ECO:0000269|PubMed:15472229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53061; Evidence={ECO:0000305|PubMed:15472229}; CATALYTIC ACTIVITY: Reaction=prunetin + UDP-alpha-D-glucuronate = prunetin-5-O-beta-D-glucuronide + UDP; Xref=Rhea:RHEA:63612, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:147403, ChEBI:CHEBI:147405; Evidence={ECO:0000269|PubMed:18052087}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63613; Evidence={ECO:0000305|PubMed:18052087}; CATALYTIC ACTIVITY: Reaction=candesartan + UDP-alpha-D-glucuronate = candesartan O-beta-D-glucuronoside + UDP; Xref=Rhea:RHEA:63724, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:149509, ChEBI:CHEBI:149522; Evidence={ECO:0000269|PubMed:18674515}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63725; Evidence={ECO:0000305|PubMed:18674515}; CATALYTIC ACTIVITY: Reaction=SN-38 + UDP-alpha-D-glucuronate = H(+) + SN-38 O-beta-D-glucuronide + UDP; Xref=Rhea:RHEA:63696, ChEBI:CHEBI:8988, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:149482; Evidence={ECO:0000269|PubMed:12181437}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63697; Evidence={ECO:0000305|PubMed:12181437}; CATALYTIC ACTIVITY: Reaction=mycophenolate + UDP-alpha-D-glucuronate = H(+) + mycophenolate 7-O-beta-D-glucuronide + UDP; Xref=Rhea:RHEA:63704, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:62932, ChEBI:CHEBI:149486; Evidence={ECO:0000269|PubMed:15470161, ECO:0000269|PubMed:18004212}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63705; Evidence={ECO:0000305|PubMed:15470161, ECO:0000305|PubMed:18004212};
|
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 glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; KM=43 uM for 2-hydroxy-estrone (when assaying glucuronidation at position 2) {ECO:0000269|PubMed:15472229}; KM=58 uM for 2-hydroxy-estrone (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; KM=53 uM for 2-methoxy-17beta-estradiol (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; KM=126 uM for 2-methoxy-estrone (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; KM=55 uM for 4-hydroxy-17beta-estradiol (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; KM=53 uM for 4-hydroxy-17beta-estradiol (when assaying glucuronidation at position 4) {ECO:0000269|PubMed:15472229}; KM=241 uM for 4-hydroxy-estrone (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; KM=142 uM for 4-hydroxy-estrone (when assaying glucuronidation at position 4) {ECO:0000269|PubMed:15472229}; KM=2.09 uM for genistein {ECO:0000269|PubMed:19545173}; KM=0.7 uM for SN-38 (when assaying glucuronidation at position 10) {ECO:0000269|PubMed:12181437}; KM=160 uM for mycophenolate (when assaying glucuronidation at position 7) {ECO:0000269|PubMed:15470161}; Vmax=4 pmol/min/mg enzyme for the formation of estrone 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=6 pmol/min/mg enzyme for the formation of 2-hydroxy-17beta-estradiol 2-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=145 pmol/min/mg enzyme for the formation of 2-hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=11 pmol/min/mg enzyme for the formation of 2-hydroxy-estrone 2-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=118 pmol/min/mg enzyme for the formation of 2-hydroxy-estrone 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=7 pmol/min/mg enzyme for the formation of 2-methoxy-17beta-estradiol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=41 pmol/min/mg enzyme for the formation of 2-methoxyestrone 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=17 pmol/min/mg enzyme for the formation of 4-hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=1673 pmol/min/mg enzyme for the formation of 4-hydroxy-17beta-estradiol 4-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=63 pmol/min/mg enzyme for the formation of 4-hydroxy-estrone 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=524 pmol/min/mg enzyme for the formation of 4-hydroxy-estrone 4-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; Vmax=5.3 pmol/min/mg enzyme for the formation of 17alpha-estradiol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=3.5 pmol/min/mg enzyme for the formation of 17alpha-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=1.29 nmol/min/mg enzyme for the formation of genistein glucuronide {ECO:0000269|PubMed:19545173}; Vmax=0.25 nmol/min/mg enzyme for the formation of prunetin-5-O-(beta-D-glucuronoside) {ECO:0000269|PubMed:18052087}; Vmax=0.012 pmol/min/mg enzyme with 5alpha-dihydrotestosterone 17-O-(beta-D-glucuronate) as substrate, for the formation of 5alpha-dihydrotestosterone 17-O-[beta-D-glucuronosyl-(1->2)-glucuronate] {ECO:0000269|PubMed:16595710}; Vmax=2.4 pmol/min/mg enzyme for the formation of SN-38 glucuronide {ECO:0000269|PubMed:12181437}; Vmax=11.82 nmol/min/mg enzyme for the formation of mycophenolate 7-O-glucuronide {ECO:0000269|PubMed:15470161}; Note=Some kinetic parameters were assessed using commercial enzymes, which may represent a mix of both active and inactive protein forms, and therefore modify the kinetic values. {ECO:0000305|PubMed:15470161, ECO:0000305|PubMed:16595710, ECO:0000305|PubMed:18052087};
| 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, PubMed:15472229, PubMed:18004212, PubMed:18052087, PubMed:18674515, PubMed:19545173). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:12181437, PubMed:18004212). Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol and estrone (PubMed:15472229). Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (PubMed:18052087, PubMed:19545173). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist caderastan, a drug which can inhibit the effect of angiotensin II (PubMed:18674515). Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan (PubMed:12181437, PubMed:20610558). Also metabolizes mycophenolate, an immunosuppressive agent (PubMed:15470161, PubMed:18004212). {ECO:0000269|PubMed:12181437, ECO:0000269|PubMed:15470161, ECO:0000269|PubMed:15472229, ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:18052087, ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:19545173, ECO:0000269|PubMed:20610558}.; FUNCTION: [Isoform 2]: Lacks UGT glucuronidation activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:20610558}.
|
Homo sapiens (Human)
|
O60658
|
PDE8A_HUMAN
|
MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSGKKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGFTRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSLDVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLEILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPISLDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRSWLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE
|
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' inhibitory-phosphorylation and stimulates RAF1-dependent EGF-activated ERK-signaling (PubMed:23509299). Protects against cell death induced by hydrogen peroxide and staurosporine (PubMed:23509299). {ECO:0000269|PubMed:18983167, ECO:0000269|PubMed:23509299}.
|
Homo sapiens (Human)
|
O60662
|
KLH41_HUMAN
|
MDSQRELAEELRLYQSTLLQDGLKDLLDEKKFIDCTLKAGDKSLPCHRLILSACSPYFREYFLSEIDEAKKKEVVLDNVDPAILDLIIKYLYSASIDLNDGNVQDIFALASRFQIPSVFTVCVSYLQKRLAPGNCLAILRLGLLLDCPRLAISAREFVSDRFVQICKEEDFMQLSPQELISVISNDSLNVEKEEAVFEAVMKWVRTDKENRVKNLSEVFDCIRFRLMTEKYFKDHVEKDDIIKSNPDLQKKIKVLKDAFAGKLPEPSKNAAKTGAGEVNGDVGDEDLLPGYLNDIPRHGMFVKDLILLVNDTAAVAYDPTENECYLTALAEQIPRNHSSIVTQQNQIYVVGGLYVDEENKDQPLQSYFFQLDSIASEWVGLPPLPSARCLFGLGEVDDKIYVVAGKDLQTEASLDSVLCYDPVAAKWNEVKKLPIKVYGHNVISHKGMIYCLGGKTDDKKCTNRVFIFNPKKGDWKDLAPMKIPRSMFGVAVHKGKIVIAGGVTEDGLSASVEAFDLTTNKWDVMTEFPQERSSISLVSLAGSLYAIGGFAMIQLESKEFAPTEVNDIWKYEDDKKEWAGMLKEIRYASGASCLATRLNLFKLSKL
| 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:0035914]; striated muscle contraction [GO:0006941]
|
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 membrane [GO:0033017]
| 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}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:24268659}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24268659}. Note=Predominantly cytoplasmic but can colocalize with F-actin at the membrane ruffle-like structures at the tips of transformation-specific pseudopodia. {ECO:0000269|PubMed:19424503}.
| 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|UniProtKB:A2AUC9}.
|
Homo sapiens (Human)
|
O60663
|
LMX1B_HUMAN
|
MDIATGPESLERCFPRGQTDCAKMLDGIKMEEHALRPGPATLGVLLGSDCPHPAVCEGCQRPISDRFLMRVNESSWHEECLQCAACQQALTTSCYFRDRKLYCKQDYQQLFAAKCSGCMEKIAPTEFVMRALECVYHLGCFCCCVCERQLRKGDEFVLKEGQLLCKGDYEKEKDLLSSVSPDESDSVKSEDEDGDMKPAKGQGSQSKGSGDDGKDPRRPKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLSVRVVQVWFQNQRAKMKKLARRHQQQQEQQNSQRLGQEVLSSRMEGMMASYTPLAPPQQQIVAMEQSPYGSSDPFQQGLTPPQMPGDHMNPYGNDSIFHDIDSDTSLTSLSDCFLGSSDVGSLQARVGNPIDRLYSMQSSYFAS
| 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:0006357]
|
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:1990837]
|
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
|
MSADGAEADGSTQVTVEEPVQQPSVVDRVASMPLISSTCDMVSAAYASTKESYPHIKTVCDAAEKGVRTLTAAAVSGAQPILSKLEPQIASASEYAHRGLDKLEENLPILQQPTEKVLADTKELVSSKVSGAQEMVSSAKDTVATQLSEAVDATRGAVQSGVDKTKSVVTGGVQSVMGSRLGQMVLSGVDTVLGKSEEWADNHLPLTDAELARIATSLDGFDVASVQQQRQEQSYFVRLGSLSERLRQHAYEHSLGKLRATKQRAQEALLQLSQVLSLMETVKQGVDQKLVEGQEKLHQMWLSWNQKQLQGPEKEPPKPEQVESRALTMFRDIAQQLQATCTSLGSSIQGLPTNVKDQVQQARRQVEDLQATFSSIHSFQDLSSSILAQSRERVASAREALDHMVEYVAQNTPVTWLVGPFAPGITEKAPEEKK
| 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, ECO:0000269|PubMed:9590177}. Note=Membrane associated on endosomes (PubMed:15545278). Detected in the envelope and the core of lipid bodies and in lipid sails (PubMed:15545278). {ECO:0000269|PubMed:15545278}.
| 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|PubMed:9590177}.
|
Homo sapiens (Human)
|
O60667
|
FCMR_HUMAN
|
MDFWLWPLYFLPVSGALRILPEVKVEGELGGSVTIKCPLPEMHVRIYLCREMAGSGTCGTVVSTTNFIKAEYKGRVTLKQYPRKNLFLVEVTQLTESDSGVYACGAGMNTDRGKTQKVTLNVHSEYEPSWEEQPMPETPKWFHLPYLFQMPAYASSSKFVTRVTTPAQRGKVPPVHHSSPTTQITHRPRVSRASSVAGDKPRTFLPSTTASKISALEGLLKPQTPSYNHHTRLHRQRALDYGSQSGREGQGFHILIPTILGLFLLALLGLVVKRAVERRKALSRRARRLAVRMRALESSQRPRGSPRPRSQNNIYSACPRRARGADAAGTGEAPVPGPGAPLPPAPLQVSESPWLHAPSLKTSCEYVSLYHQPAAMMEDSDSDDYINVPA
| 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 receptor signaling pathway [GO:0050855]
|
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-Golgi network membrane {ECO:0000269|PubMed:21908732}; Single-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:21908732}; Single-pass membrane protein {ECO:0000255}. Note=Continuously recycles between cytoplasmic pool and the plasma membrane to bind as much IgM as possible. {ECO:0000269|PubMed:30840890}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:21908424}. Note=Detected in the serum. {ECO:0000269|PubMed:21908424}.
| 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 membrane-bound IgM on the plasma membrane as well as endocytosis of IgM-antigen complexes toward lysosomes for degradation. In mucosal epithelium, mediates retrotranscytosis of antigen-IgM complexes across mucosal M cells toward antigen-presenting cells in mucosal lymphoid tissues (PubMed:21908732, PubMed:28230186). Triggers costimulatory signaling and mediates most of IgM effector functions involved in B cell development and primary immune response to infection. Likely limits tonic IgM BCR signaling to self-antigens for proper negative selection of autoreactive B cells in the bone marrow and for the maintenance of regulatory B cell pool in peripheral lymphoid organs. Mediates antibody responses to T cell-dependent and T cell-independent antigens and promotes induction of an efficient neutralizing IgG response. Engages in cross-talk with antigen-receptor signaling via the non-canonical NF-kappa-B, MAP kinases and calcium signaling pathways (PubMed:19858324, PubMed:22675200, PubMed:25601920, PubMed:30840890). {ECO:0000269|PubMed:19858324, ECO:0000269|PubMed:21908732, ECO:0000269|PubMed:22675200, ECO:0000269|PubMed:25601920, ECO:0000269|PubMed:28230186, ECO:0000269|PubMed:30840890, ECO:0000269|PubMed:36949194, ECO:0000269|PubMed:37095205}.
|
Homo sapiens (Human)
|
O60669
|
MOT2_HUMAN
|
MPPMPSAPPVHPPPDGGWGWIVVGAAFISIGFSYAFPKAVTVFFKEIQQIFHTTYSEIAWISSIMLAVMYAGGPVSSVLVNKYGSRPVVIAGGLLCCLGMVLASFSSSVVQLYLTMGFITGLGLAFNLQPALTIIGKYFYRKRPMANGLAMAGSPVFLSSLAPFNQYLFNTFGWKGSFLILGSLLLNACVAGSLMRPLGPNQTTSKSKNKTGKTEDDSSPKKIKTKKSTWEKVNKYLDFSLFKHRGFLIYLSGNVIMFLGFFAPIIFLAPYAKDQGIDEYSAAFLLSVMAFVDMFARPSVGLIANSKYIRPRIQYFFSFAIMFNGVCHLLCPLAQDYTSLVLYAVFFGLGFGSVSSVLFETLMDLVGAPRFSSAVGLVTIVECGPVLLGPPLAGKLVDLTGEYKYMYMSCGAIVVAASVWLLIGNAINYRLLAKERKEENARQKTRESEPLSKSKHSEDVNVKVSNAQSVTSERETNI
| 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 collateral - CA1 synapse [GO:0098685]
|
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=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (By similarity). {ECO:0000250|UniProtKB:O70451, ECO:0000250|UniProtKB:Q63344}.
|
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}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64722; Evidence={ECO:0000305|PubMed:32415067}; CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate(out) + H(+)(out) = 3-methyl-2-oxobutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71783, ChEBI:CHEBI:11851, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out); Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=acetoacetate(out) + H(+)(out) = acetoacetate(in) + H(+)(in); Xref=Rhea:RHEA:71775, ChEBI:CHEBI:13705, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=(R)-3-hydroxybutanoate(out) + H(+)(out) = (R)-3-hydroxybutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71795, ChEBI:CHEBI:10983, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=4-methyl-2-oxopentanoate(out) + H(+)(out) = 4-methyl-2-oxopentanoate(in) + H(+)(in); Xref=Rhea:RHEA:71779, ChEBI:CHEBI:15378, ChEBI:CHEBI:17865; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=(S)-3-hydroxybutanoate(out) + H(+)(out) = (S)-3-hydroxybutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71871, ChEBI:CHEBI:11047, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344};
|
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 cooperatively in transporting substrate (PubMed:32415067). {ECO:0000269|PubMed:32415067, ECO:0000269|PubMed:9786900}.
|
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 on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:15871698). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates (PubMed:15314187, PubMed:15556996, PubMed:15871698). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603). {ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:12578958, ECO:0000269|PubMed:15314187, ECO:0000269|PubMed:15556996, ECO:0000269|PubMed:15871698, ECO:0000269|PubMed:21659603}.
|
Homo sapiens (Human)
|
O60673
|
REV3L_HUMAN
|
MFSVRIVTADYYMASPLQGLDTCQSPLTQAPVKKVPVVRVFGATPAGQKTCLHLHGIFPYLYVPYDGYGQQPESYLSQMAFSIDRALNVALGNPSSTAQHVFKVSLVSGMPFYGYHEKERHFMKIYLYNPTMVKRICELLQSGAIMNKFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAVKFRKARRKSNTLHATGSCKNHLSGNSLADTLFRWEQDEIPSSLILEGVEPQSTCELEVDAVAADILNRLDIEAQIGGNPGLQAIWEDEKQRRRNRNETSQMSQPESQDHRFVPATESEKKFQKRLQEILKQNDFSVTLSGSVDYSDGSQEFSAELTLHSEVLSPEMLQCTPANMVEVHKDKESSKGHTRHKVEEALINEEAILNLMENSQTFQPLTQRLSESPVFMDSSPDEALVHLLAGLESDGYRGERNRMPSPCRSFGNNKYPQNSDDEENEPQIEKEEMELSLVMSQRWDSNIEEHCAKKRSLCRNTHRSSTEDDDSSSGEEMEWSDNSLLLASLSIPQLDGTADENSDNPLNNENSRTHSSVIATSKLSVKPSIFHKDAATLEPSSSAKITFQCKHTSALSSHVLNKEDLIEDLSQTNKNTEKGLDNSVTSFTNESTYSMKYPGSLSSTVHSENSHKENSKKEILPVSSCESSIFDYEEDIPSVTRQVPSRKYTNIRKIEKDSPFIHMHRHPNENTLGKNSFNFSDLNHSKNKVSSEGNEKGNSTALSSLFPSSFTENCELLSCSGENRTMVHSLNSTADESGLNKLKIRYEEFQEHKTEKPSLSQQAAHYMFFPSVVLSNCLTRPQKLSPVTYKLQPGNKPSRLKLNKRKLAGHQETSTKSSETGSTKDNFIQNNPCNSNPEKDNALASDLTKTTRGAFENKTPTDGFIDCHFGDGTLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLKSRKRRKMSKKLPPVIIKYIIINRFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPLKDFWPKVPDSPATKYPIYPLTPKKSHRRKSKHKSAKKKTGKQQRTNNENIKRTLSFRKKRSHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTDPRAEEIMAAAEKEAMLFKGPNVYKKTVNSRIGKTSRARAQIKKSKAKLANPSIVTKKRNKRNQTNKLVDDGKKKPRAKQKTNEKGTSRKHTTLKDEKIKSQSGAEVKFVLKHQNVSEFASSSGGSQLLFKQKDMPLMGSAVDHPLSASLPTGINAQQKLSGCFSSFLESKKSVDLQTFPSSRDDLHPSVVCNSIGPGVSKINVQRPHNQSAMFTLKESTLIQKNIFDLSNHLSQVAQNTQISSGMSSKIEDNANNIQRNYLSSIGKLSEYRNSLESKLDQAYTPNFLHCKDSQQQIVCIAEQSKHSETCSPGNTASEESQMPNNCFVTSLRSPIKQIAWEQKQRGFILDMSNFKPERVKPRSLSEAISQTKALSQCKNRNVSTPSAFGEGQSGLAVLKELLQKRQQKAQNANTTQDPLSNKHQPNKNISGSLEHNKANKRTRSVTSPRKPRTPRSTKQKEKIPKLLKVDSLNLQNSSQLDNSVSDDSPIFFSDPGFESCYSLEDSLSPEHNYNFDINTIGQTGFCSFYSGSQFVPADQNLPQKFLSDAVQDLFPGQAIEKNEFLSHDNQKCDEDKHHTTDSASWIRSGTLSPEIFEKSTIDSNENRRHNQWKNSFHPLTTRSNSIMDSFCVQQAEDCLSEKSRLNRSSVSKEVFLSLPQPNNSDWIQGHTRKEMGQSLDSANTSFTAILSSPDGELVDVACEDLELYVSRNNDMLTPTPDSSPRSTSSPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHDLSETIYQEPFCSNPSDVPEKPREIGGRLLMVETRLANDLAEFEGDFSLEGLRLWKTAFSAMTQNPRPGSPLRSGQGVVNKGSSNSPKMVEDKKIVIMPCKCAPSRQLVQVWLQAKEEYERSKKLPKTKPTGVVKSAENFSSSVNPDDKPVVPPKMDVSPCILPTTAHTKEDVDNSQIALQAPTTGCSQTASESQMLPPVASASDPEKDEDDDDNYYISYSSPDSPVIPPWQQPISPDSKALNGDDRPSSPVEELPSLAFENFLKPIKDGIQKSPCSEPQEPLVISPINTRARTGKCESLCFHSTPIIQRKLLERLPEAPGLSPLSTEPKTQKLSNKKGSNTDTLRRVLLTQAKNQFAAVNTPQKETSQIDGPSLNNTYGFKVSIQNLQEAKALHEIQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPDTEKTELTGVIVIDKDKTVFSQDIRYQTPLLIRSGITGLEVTYAADEKALFHEIANIIKRYDPDILLGYEIQMHSWGYLLQRAAALSIDLCRMISRVPDDKIENRFAAERDEYGSYTMSEINIVGRITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHYVSRVRGNLQMLEQLDLIGKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNYIPVTPSVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVENLGKYDEFKFGCTSLRVPPDLLYQVRHDITVSPNGVAFVKPSVRKGVLPRMLEEILKTRFMVKQSMKAYKQDRALSRMLDARQLGLKLIANVTFGYTSANFSGRMPCIEVGDSIVHKARETLERAIKLVNDTKKWGARVVYGDTDSMFVLLKGATKEQSFKIGQEIAEAVTATNPKPVKLKFEKVYLPCVLQTKKRYVGYMYETLDQKDPVFDAKGIETVRRDSCPAVSKILERSLKLLFETRDISLIKQYVQRQCMKLLEGKASIQDFIFAKEYRGSFSYKPGACVPALELTRKMLTYDRRSEPQVGERVPYVIIYGTPGVPLIQLVRRPVEVLQDPTLRLNATYYITKQILPPLARIFSLIGIDVFSWYHELPRIHKATSSSRSEPEGRKGTISQYFTTLHCPVCDDLTQHGICSKCRSQPQHVAVILNQEIRELERQQEQLVKICKNCTGCFDRHIPCVSLNCPVLFKLSRVNRELSKAPYLRQLLDQF
|
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
|
MGMACLTMTEMEGTSTSSIYQNGDISGNANSMKQIDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQEGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIQSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENEEYNLSGTKKNFSSLKDLLNCYQMETVRSDNIIFQFTKCCPPKPKDKSNLLVFRTNGVSDVPTSPTLQRPTHMNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCVCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWAELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG
|
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 [GO:0002250]; apoptotic process [GO:0006915]; axon regeneration [GO:0031103]; cell differentiation [GO:0030154]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to interleukin-3 [GO:0036016]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to virus [GO:0098586]; collagen-activated signaling pathway [GO:0038065]; cytokine-mediated signaling pathway [GO:0019221]; enzyme-linked receptor protein signaling pathway [GO:0007167]; erythrocyte differentiation [GO:0030218]; extrinsic apoptotic signaling pathway [GO:0097191]; G protein-coupled receptor signaling pathway [GO:0007186]; granulocyte-macrophage colony-stimulating factor signaling pathway [GO:0038157]; growth hormone receptor signaling pathway [GO:0060396]; growth hormone receptor signaling pathway via JAK-STAT [GO:0060397]; immune response [GO:0006955]; interleukin-12-mediated signaling pathway [GO:0035722]; interleukin-3-mediated signaling pathway [GO:0038156]; interleukin-35-mediated signaling pathway [GO:0070757]; interleukin-5-mediated signaling pathway [GO:0038043]; interleukin-6-mediated signaling pathway [GO:0070102]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; mammary gland epithelium development [GO:0061180]; mesoderm development [GO:0007498]; microglial cell activation [GO:0001774]; mineralocorticoid receptor signaling pathway [GO:0031959]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of DNA binding [GO:0043392]; negative regulation of neuron apoptotic process [GO:0043524]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell migration [GO:0030335]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of epithelial cell apoptotic process [GO:1904037]; positive regulation of growth factor dependent skeletal muscle satellite cell proliferation [GO:1902728]; positive regulation of growth hormone receptor signaling pathway [GO:0060399]; positive regulation of insulin secretion [GO:0032024]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of leukocyte proliferation [GO:0070665]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of natural killer cell proliferation [GO:0032819]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of NK T cell proliferation [GO:0051142]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of platelet activation [GO:0010572]; positive regulation of platelet aggregation [GO:1901731]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of signaling receptor activity [GO:2000273]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of T-helper 17 type immune response [GO:2000318]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; post-embryonic hemopoiesis [GO:0035166]; post-translational protein modification [GO:0043687]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of apoptotic process [GO:0042981]; regulation of inflammatory response [GO:0050727]; regulation of nitric oxide biosynthetic process [GO:0045428]; regulation of postsynapse to nucleus signaling pathway [GO:1905539]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]; response to amine [GO:0014075]; response to antibiotic [GO:0046677]; response to hydroperoxide [GO:0033194]; response to interleukin-12 [GO:0070671]; response to lipopolysaccharide [GO:0032496]; response to tumor necrosis factor [GO:0034612]; signal transduction [GO:0007165]; symbiont-induced defense-related programmed cell death [GO:0034050]; transcription by RNA polymerase II [GO:0006366]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; type II interferon-mediated signaling pathway [GO:0060333]; tyrosine phosphorylation of STAT protein [GO:0007260]
|
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 synapse [GO:0098978]; granulocyte macrophage colony-stimulating factor receptor complex [GO:0030526]; interleukin-12 receptor complex [GO:0042022]; interleukin-23 receptor complex [GO:0072536]; membrane raft [GO:0045121]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]
|
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-12 receptor binding [GO:0005143]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; peptide hormone receptor binding [GO:0051428]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713]; SH2 domain binding [GO:0042169]; signaling receptor binding [GO:0005102]; type 1 angiotensin receptor binding [GO:0031702]
|
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 in response to growth hormone (GH) are required for maximal kinase activity (By similarity). Also phosphorylated by TEC (By similarity). Phosphorylated on tyrosine residues in response to interferon gamma signaling (PubMed:7615558, PubMed:7673114). Phosphorylated on tyrosine residues in response to a signaling cascade that is activated by increased cellular retinol (PubMed:21368206). {ECO:0000250|UniProtKB:Q62120, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7673114}.; PTM: Undergoes Notch-induced ubiquitination and subsequent proteasomal degradation which is mediated by ASB1 or ASB2, the substrate-recognition components of probable ECS E3 ubiquitin-protein ligase complexes. {ECO:0000269|PubMed:21119685}.
|
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:PRU10028, ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:9618263};
| 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 receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins (PubMed:7615558). Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins (PubMed:9618263). Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B) (PubMed:21368206). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation (PubMed:20098430). Plays a role in cell cycle by phosphorylating CDKN1B (PubMed:21423214). Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin (PubMed:19783980). {ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:19783980, ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:21423214, ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:9618263}.
|
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-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
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 and NFE2L3/NRF3, and recruiting them to specific DNA-binding sites (PubMed:8932385, PubMed:9150357). Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor (PubMed:9150357). {ECO:0000269|PubMed:8932385, ECO:0000269|PubMed:9150357}.
|
Homo sapiens (Human)
|
O60678
|
ANM3_HUMAN
|
MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIKHIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ
|
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={ECO:0000305|PubMed:33495566}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101; Evidence={ECO:0000305|PubMed:33495566}; CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319; Evidence={ECO:0000305|PubMed:33495566}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097; Evidence={ECO:0000305|PubMed:33495566};
| 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 inhibiting ALDH1A1 retinal dehydrogenase activity (PubMed:33495566). {ECO:0000269|PubMed:33495566, ECO:0000305|PubMed:33495566}.
|
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:0006357]; roof of mouth development [GO:0060021]; skeletal muscle tissue development [GO:0007519]
|
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-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837]
|
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
|
MAPAAASPPEVIRAAQKDEYYRGGLRSAAGGALHSLAGARKWLEWRKEVELLSDVAYFGLTTLAGYQTLGEEYVSIIQVDPSRIHVPSSLRRGVLVTLHAVLPYLLDKALLPLEQELQADPDSGRPLQGSLGPGGRGCSGARRWMRHHTATLTEQQRRALLRAVFVLRQGLACLQRLHVAWFYIHGVFYHLAKRLTGITYLRVRSLPGEDLRARVSYRLLGVISLLHLVLSMGLQLYGFRQRQRARKEWRLHRGLSHRRASLEERAVSRNPLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCREKFPPQKLIYLRHYR
|
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 peroxisome matrix, substrate release [GO:0044721]; protein polyubiquitination [GO:0000209]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]
|
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 subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX10 also regulates PEX5 recycling by acting as a E3 ubiquitin-protein ligase (PubMed:24662292). When PEX5 recycling is compromised, PEX10 catalyzes polyubiquitination of PEX5 during its passage through the retrotranslocation channel, leading to its degradation (By similarity). {ECO:0000250|UniProtKB:Q05568, ECO:0000269|PubMed:24662292}.
|
Homo sapiens (Human)
|
O60684
|
IMA7_HUMAN
|
METMASPGKDNYRMKSYKNNALNPEEMRRRREEEGIQLRKQKREQQLFKRRNVELINEEAAMFDSLLMDSYVSSTTGESVITREMVEMLFSDDSDLQLATTQKFRKLLSKEPSPPIDEVINTPRVVDRFVEFLKRNENCTLQFEAAWALTNIASGTSQQTKIVIEAGAVPIFIELLNSDFEDVQEQAVWALGNIAGDSSVCRDYVLNCSILNPLLTLLTKSTRLTMTRNAVWALSNLCRGKNPPPEFAKVSPCLPVLSRLLFSSDSDLLADACWALSYLSDGPNEKIQAVIDSGVCRRLVELLMHNDYKVASPALRAVGNIVTGDDIQTQVILNCSALPCLLHLLSSPKESIRKEACWTISNITAGNRAQIQAVIDANIFPVLIEILQKAEFRTRKEAAWAITNATSGGTPEQIRYLVSLGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQEGKRSGSGVNPYCGLIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGVEDDDSSLAPQVDETQQQFIFQQPEAPMEGFQL
| 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 of transcription by RNA polymerase II [GO:0045944]; positive regulation of viral life cycle [GO:1903902]; protein import into nucleus [GO:0006606]; transcription by RNA polymerase II [GO:0006366]; viral genome replication [GO:0019079]
|
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 FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:10523667}.
|
Homo sapiens (Human)
|
O60687
|
SRPX2_HUMAN
|
MASQLTQRGALFLLFFLTPAVTPTWYAGSGYYPDESYNEVYAEEVPQAPALDYRVPRWCYTLNIQDGEATCYSPKGGNYHSSLGTRCELSCDRGFRLIGRRSVQCLPSRRWSGTAYCRQMRCHALPFITSGTYTCTNGVLLDSRCDYSCSSGYHLEGDRSRICMEDGRWSGGEPVCVDIDPPKIRCPHSREKMAEPEKLTARVYWDPPLVKDSADGTITRVTLRGPEPGSHFPEGEHVIRYTAYDRAYNRASCKFIVKVQVRRCPTLKPPQHGYLTCTSAGDNYGATCEYHCDGGYDRQGTPSRVCQSSRQWSGSPPICAPMKINVNVNSAAGLLDQFYEKQRLLIISAPDPSNRYYKMQISMLQQSTCGLDLRHVTIIELVGQPPQEVGRIREQQLSANIIEELRQFQRLTRSYFNMVLIDKQGIDRDRYMEPVTPEEIFTFIDDYLLSNQELTQRREQRDICE
| 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 the mitogenic activity of HGF. Promotes synapse formation. May have a role in the perisylvian region, critical for language and cognitive development. {ECO:0000269|PubMed:16497722, ECO:0000269|PubMed:18718938, ECO:0000269|PubMed:19065654, ECO:0000269|PubMed:24179158}.
|
Homo sapiens (Human)
|
O60701
|
UGDH_HUMAN
|
MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV
|
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 biosynthetic process [GO:0006065]
|
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:21961565, ECO:0000269|PubMed:22123821, ECO:0000269|PubMed:23106432, ECO:0000269|PubMed:25478983, ECO:0000269|PubMed:27966912, ECO:0000269|PubMed:30420606, ECO:0000269|PubMed:30457329, ECO:0000269|PubMed:32001716};
|
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:30457329}; KM=384 uM for NAD(+) {ECO:0000269|PubMed:23106432}; Note=kcat is 0.55 sec(-1) with UDP-glucose as substrate. {ECO:0000269|PubMed:27966912};
|
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:0000269|PubMed:30420606, ECO:0000269|PubMed:30457329}.
|
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. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716). {ECO:0000250|UniProtKB:O70475, 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:0000269|PubMed:30420606, ECO:0000269|PubMed:30457329, ECO:0000269|PubMed:32001716}.
|
Homo sapiens (Human)
|
O60704
|
TPST2_HUMAN
|
MRLSVRRVLLAAGCALVLVLAVQLGQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQLVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPGDVVRDMAQIAPMLAQLGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLKGYFQVNQNSTSSHLGSS
|
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; Evidence={ECO:0000269|PubMed:9733778};
| 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
|
MSLSFCGNNISSYNINDGVLQNSCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNLRWILTFALLFVHVCEIAEGIVSDSRRESRHLHLFMPAVMGFVATTTSIVYYHNIETSNFPKLLLALFLYWVMAFITKTIKLVKYCQSGLDISNLRFCITGMMVILNGLLMAVEINVIRVRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEIGDDSWRTGESSLPFESCKKHTGVQPKTINRKQPGRYHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMPWKTCWRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK
| 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:0098662]; monoatomic cation transmembrane transport [GO:0098655]; negative regulation of blood pressure [GO:0045776]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transmembrane transport [GO:0071805]; response to ATP [GO:0033198]; response to xenobiotic stimulus [GO:0009410]; transmembrane transport [GO:0055085]; transport across blood-brain barrier [GO:0150104]
|
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 [GO:0042626]; potassium channel activity [GO:0005267]; potassium channel regulator activity [GO:0015459]; sulfonylurea receptor activity [GO:0008281]; transmembrane transporter binding [GO:0044325]
|
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
|
MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKESPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELHYHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL
| 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-containing complex assembly [GO:0065003]; regulation of cell adhesion mediated by integrin [GO:0033628]; signal transduction [GO:0007165]; substrate adhesion-dependent cell spreading [GO:0034446]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
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]; podosome [GO:0002102]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
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 adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin.
| 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 (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. {ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:20543562}.
|
Homo sapiens (Human)
|
O60716
|
CTND1_HUMAN
|
MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANPLMANGTLTRRHQNGRFVGDADLERQKFSDLKLNGPQDHSHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETSDDGTTRRTETTVKKVVKTVTTRTVQPVAMGPDGLPVDASSVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYSRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRSYEDMIGEEVPSDQYYWAPLAQHERGSLASLDSLRKGGPPPPNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPVLVGLLDHPKKEVHLGACGALKNISFGRDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDALIFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEAAPNVANNTGPHAASCFGAKKGKDEWFSRGKKPIEDPANDTVDFPKRTSPARGYELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAIADLLTNEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVISILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKELRKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIQMSNMGSNTKSLDNNYSTPNERGDHNRTLDRSGDLGDMEPLKGTTPLMQDEGQESLEEELDVLVLDDEGGQVSYPSMQKI
| 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 signaling pathway [GO:0016055]
|
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 to CA3 synapse [GO:0098686]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density, intracellular component [GO:0099092]; presynaptic active zone cytoplasmic component [GO:0098831]; Schaffer collateral - CA1 synapse [GO:0098685]; zonula adherens [GO:0005915]
|
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 GLIS2 promotes nuclear translocation (By similarity). Detected at cell-cell contacts (PubMed:15240885, PubMed:17047063). NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm (PubMed:17047063). CDH1 enhances cell membrane localization (PubMed:15240885). Isoforms 4A and 1AB are excluded from the nucleus (PubMed:11896187). {ECO:0000250|UniProtKB:P30999, ECO:0000269|PubMed:11896187, ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:17047063}.; SUBCELLULAR LOCATION: [Isoform 1A]: Nucleus {ECO:0000269|PubMed:11896187}.; SUBCELLULAR LOCATION: [Isoform 2A]: Nucleus {ECO:0000269|PubMed:11896187}.; SUBCELLULAR LOCATION: [Isoform 3A]: Nucleus {ECO:0000269|PubMed:11896187}.
| 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 including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors (PubMed:17344476). {ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:14610055, ECO:0000269|PubMed:17344476, ECO:0000269|PubMed:20371349}.
|
Homo sapiens (Human)
|
O60721
|
NCKX1_HUMAN
|
MGKLIRMGPQERWLLRTKRLHWSRLLFLLGMLIIGSTYQHLRRPRGLSSLWAAVSSHQPIKLASRDLSSEEMMMMSSSPSKPSSEMGGKMLVPQASVGSDEATLSMTVENIPSMPKRTAKMIPTTTKNNYSPTAAGTERRKEDTPTSSRTLTYYTSTSSRQIVKKYTPTPRGEMKSYSPTQVREKVKYTPSPRGRRVGTYVPSTFMTMETSHAITPRTTVKDSDITATYKILETNSLKRIMEETTPTTLKGMFDSTPTFLTHEVEANVLTSPRSVMEKNNLFPPRRVESNSSAHPWGLVGKSNPKTPQGTVLLHTPATSEGQVTISTMTGSSPAETKAFTAAWSLRNPSPRTSVSAIKTAPAIVWRLAKKPSTAPSTSTTPTVRAKLTMQVHHCVVVKPTPAMLTTPSPSLTTALLPEELSPSPSVLPPSLPDLHPKGEYPPDLFSVEERRQGWVVLHVFGMMYVFVALAIVCDEYFVPALGVITDKLQISEDVAGATFMAAGGSAPELFTSLIGVFISHSNVGIGTIVGSAVFNILFVIGTCSLFSREILNLTWWPLFRDVSFYILDLIMLILFFLDSLIAWWESLLLLLAYAFYVFTMKWNKHIEVWVKEQLSRRPVAKVMALEDLSKPGDGAIAVDELQDNKKLKLPSLLTRGSSSTSLHNSTIRSTIYQLMLHSLDPLREVRLAKEKEEESLNQGARAQPQAKAESKPEEEEPAKLPAVTVTPAPVPDIKGDQKENPGGQEDVAEAESTGEMPGEEGETAGEGETEEKSGGETQPEGEGETETQGKGEECEDENEAEGKGDNEGEDEGEIHAEDGEMKGNEGETESQELSAENHGEAKNDEKGVEDGGGSDGGDSEEEEEEEEEQEEEEEEEEQEEEEEEEEEEEEKGNEEPLSLDWPETRQKQAIYLFLLPIVFPLWLTVPDVRRQESRKFFVFTFLGSIMWIAMFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPVPWLLFSLINGLQPVPVSSNGLFCAIVLLFLMLLFVISSIASCKWRMNKILGFTMFLLYFVFLIISVMLEDRIISCPVSV
| 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]; potassium ion transmembrane transport [GO:0071805]; response to light intensity [GO:0009642]; sodium ion transmembrane transport [GO:0035725]; visual perception [GO:0007601]
|
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 cytosolic free calcium in the outer segment of both retinal rod and cone photoreceptors and the light-induced lowering of calcium is caused by extrusion via this protein which plays a key role in the process of light adaptation (PubMed:20850105). {ECO:0000269|PubMed:20850105, ECO:0000269|PubMed:26631410}.
|
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:90510, ChEBI:CHEBI:90511; EC=2.1.1.100; Evidence={ECO:0000269|PubMed:9614111};
| 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
|
MKRKSERRSSWAAAPPCSRRCSSTSPGVKKIRSSTQQDPRRRDPQDDVYLDITDRLCFAILYSRPKSASNVHYFSIDNELEYENFYADFGPLNLAMVYRYCCKINKKLKSITMLRKKIVHFTGSDQRKQANAAFLVGCYMVIYLGRTPEEAYRILIFGETSYIPFRDAAYGSCNFYITLLDCFHAVKKAMQYGFLNFNSFNLDEYEHYEKAENGDLNWIIPDRFIAFCGPHSRARLESGYHQHSPETYIQYFKNHNVTTIIRLNKRMYDAKRFTDAGFDHHDLFFADGSTPTDAIVKEFLDICENAEGAIAVHCKAGLGRTGTLIACYIMKHYRMTAAETIAWVRICRPGSVIGPQQQFLVMKQTNLWLEGDYFRQKLKGQENGQHRAAFSKLLSGVDDISINGVENQDQQEPEPYSDDDEINGVTQGDRLRALKSRRQSKTNAIPLTVILQSSVQSCKTSEPNISGSAGITKRTTRSASRKSSVKSLSISRTKTVLR
|
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:0006470]; regulation of exit from mitosis [GO:0007096]
|
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|PubMed:12134069}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:12134069}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:12134069};
| 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. Dephosphorylation of FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1, preventing entry into mitosis. Preferentially dephosphorylates proteins modified by proline-directed kinases. {ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:9367992}.
|
Homo sapiens (Human)
|
O60733
|
PLPL9_HUMAN
|
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLVNPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHGVPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLLLSP
|
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 process [GO:0034638]; phosphatidylethanolamine catabolic process [GO:0046338]; platelet activating factor metabolic process [GO:0046469]; positive regulation of ceramide biosynthetic process [GO:2000304]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]
|
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 activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A2 activity [GO:0004623]; serine hydrolase activity [GO:0017171]
|
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|PubMed:18208975}.
|
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}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:20886109}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:20886109}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000305|PubMed:20886109}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:P97819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:P97819}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000269|PubMed:10092647, ECO:0000269|PubMed:23533611}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000305|PubMed:10092647, ECO:0000305|PubMed:23533611}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:P97819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:P97819}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-sn-glycero-3-phosphate + H(+) + hexadecanoate; Xref=Rhea:RHEA:63304, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72859; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63305; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:20886109}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000305|PubMed:20886109}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:20886109}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000305|PubMed:20886109}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40831, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395, ChEBI:CHEBI:74344; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40832; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40827, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395, ChEBI:CHEBI:76079; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40828; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:55430, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000250|UniProtKB:A0A3L7I2I8}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:20886109}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:20886109}; CATALYTIC ACTIVITY: Reaction=1',3'-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-octadecenoate + 1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H(+); Xref=Rhea:RHEA:40463, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77253, ChEBI:CHEBI:77259; Evidence={ECO:0000269|PubMed:23533611}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40464; Evidence={ECO:0000305|PubMed:23533611}; CATALYTIC ACTIVITY: Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-octadecenoate + 1',3'-bis-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H(+); Xref=Rhea:RHEA:40467, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77256, ChEBI:CHEBI:77259; Evidence={ECO:0000269|PubMed:23533611}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40468; Evidence={ECO:0000305|PubMed:23533611}; CATALYTIC ACTIVITY: Reaction=1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H(+); Xref=Rhea:RHEA:52812, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:83580, ChEBI:CHEBI:83581; Evidence={ECO:0000250|UniProtKB:P97819}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:52814; Evidence={ECO:0000250|UniProtKB:P97819}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoethanolamine + 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+); Xref=Rhea:RHEA:63256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75036, ChEBI:CHEBI:78832, ChEBI:CHEBI:146277; Evidence={ECO:0000250|UniProtKB:P97570}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63257; Evidence={ECO:0000250|UniProtKB:P97570};
| 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 respectively), producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:10092647, PubMed:10336645, PubMed:20886109, PubMed:9417066). Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position (PubMed:10092647, PubMed:10336645, PubMed:20886109). Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity) (PubMed:20886109). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (PubMed:23533611). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species (By similarity). Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (By similarity). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (PubMed:20886109). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (By similarity). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (PubMed:18208975). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-protein receptors in various cell types (By similarity). Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent pro-inflammatory signaling lipid (By similarity). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (By similarity). {ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:P97570, ECO:0000250|UniProtKB:P97819, ECO:0000269|PubMed:10092647, ECO:0000269|PubMed:10336645, ECO:0000269|PubMed:18208975, ECO:0000269|PubMed:20886109, ECO:0000269|PubMed:23533611, ECO:0000269|PubMed:9417066}.; FUNCTION: [Isoform Ankyrin-iPLA2-1]: Lacks the catalytic domain and may act as a negative regulator of the catalytically active isoforms. {ECO:0000269|PubMed:9417066}.; FUNCTION: [Isoform Ankyrin-iPLA2-2]: Lacks the catalytic domain and may act as a negative regulator of the catalytically active isoforms. {ECO:0000269|PubMed:9417066}.
|
Homo sapiens (Human)
|
O60741
|
HCN1_HUMAN
|
MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFKVDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILNELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIAPINYPQMTTLNSTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPVQSPLAARTFHYASPTASQLSLMQQQPQQQVQQSQPPQTQPQQPSPQPQTPGSSTPKNEVHKSTQALHNTNLTREVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVTAVPGTGLQAGGRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAALPRESSSVLNTDPDAEKPRFASNL
| 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:0003254]; regulation of membrane potential [GO:0042391]; retinal cone cell development [GO:0046549]; sodium ion transmembrane transport [GO:0035725]
|
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 monoatomic cation channel activity [GO:0022843]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated sodium channel activity [GO:0005248]
|
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 neuron excitability (PubMed:29936235, PubMed:30351409). Participates in cerebellar mechanisms of motor learning (By similarity). May mediate responses to sour stimuli (By similarity). {ECO:0000250|UniProtKB:O88704, ECO:0000269|PubMed:15351778, ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:29936235, ECO:0000269|PubMed:30351409}.
|
Homo sapiens (Human)
|
O60749
|
SNX2_HUMAN
|
MAAEREPPPLGDGKPTDFEDLEDGEDLFTSTVSTLESSPSSPEPASLPAEDISANSNGPKPTEVVLDDDREDLFAEATEEVSLDSPEREPILSSEPSPAVTPVTPTTLIAPRIESKSMSAPVIFDRSREEIEEEANGDIFDIEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKVGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESSELPRAVNTQALSGAGILRMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHVSVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANKPDKIQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAKAIA
| 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:0030905]
|
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 activity [GO:0042803]; transferrin receptor binding [GO:1990459]
|
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|PubMed:20604901}. Note=Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles (PubMed:18088323). Colocalized with F-actin at the leading edge of lamellipodia in cells in a KALRN-dependent manner (PubMed:20604901). {ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:20604901}.
| 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:17101778). The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Required for retrograde endosome-to-TGN transport of TGN38 (PubMed:20138391). Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901). {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778, ECO:0000269|PubMed:20138391, ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:23085988, ECO:0000303|PubMed:16179610}.
|
Homo sapiens (Human)
|
O60755
|
GALR3_HUMAN
|
MADAQNISLDSPGSVGAVAVPVVFALIFLLGTVGNGLVLAVLLQPGPSAWQEPGSTTDLFILNLAVADLCFILCCVPFQATIYTLDAWLFGALVCKAVHLLIYLTMYASSFTLAAVSVDRYLAVRHPLRSRALRTPRNARAAVGLVWLLAALFSAPYLSYYGTVRYGALELCVPAWEDARRRALDVATFAAGYLLPVAVVSLAYGRTLRFLWAAVGPAGAAAAEARRRATGRAGRAMLAVAALYALCWGPHHALILCFWYGRFAFSPATYACRLASHCLAYANSCLNPLVYALASRHFRARFRRLWPCGRRRRHRARRALRRVRPASSGPPGCPGDARPSGRLLAGGGQGPEPREGPVHGGEAARGPE
| 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]; learning or memory [GO:0007611]; neuropeptide signaling pathway [GO:0007218]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
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
|
MSLQRLLQHSSNGNLADFCAGPAYSSYSTLTGSLTMDDNRRIQMLADTVATLPRGRKQLALTRSSSLSDFSWSQRKLVTVEKQDNETFGFEIQSYRPQNQNACSSEMFTLICKIQEDSPAHCAGLQAGDVLANINGVSTEGFTYKQVVDLIRSSGNLLTIETLNGTMILKRTELEAKLQVLKQTLKQKWVEYRSLQLQEHRLLHGDAANCPSLENMDLDELSLFGPLPGPGPALVDRNRLSSESSCKSWLSSMTMDSEDGYQTCVSEDSSRGAFSRQTSTDDECFIPKEGDDFLRRSSSRRNRSISNTSSGSMSPLWEGNLSSMFGTLPRKSRKGSVRKQLLKFIPGLHRAVEEEESRF
| 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|PubMed:9353279, ECO:0000269|PubMed:9425264};
|
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:19939518, ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10601; Evidence={ECO:0000305|PubMed:10824118, ECO:0000305|PubMed:12244105}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:15113825}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin D2; Xref=Rhea:RHEA:51232, ChEBI:CHEBI:85166, ChEBI:CHEBI:133979; Evidence={ECO:0000269|PubMed:12244105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51233; Evidence={ECO:0000305|PubMed:12244105};
|
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:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; KM=0.14 mM for glutathione for the prostaglandin D synthase activity in the presence of magnesium ions {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; Vmax=8.6 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; Vmax=5.1 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; Vmax=44.3 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; Vmax=10.7 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; Vmax=6.8 umol/min/mg enzyme with allyl isothiocyanate as substrate {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; Vmax=6.3 umol/min/mg enzyme with benzyl isothiocyanate as substrate {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; Vmax=0.05 umol/min/mg enzyme with cumene hydroperoxide as substrate {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
| 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 glutathione-peroxidase activity towards cumene hydroperoxide. {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12244105, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:19939518, ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}.
|
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 mannosylation [GO:0035269]
|
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}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21185; Evidence={ECO:0000305|PubMed:10835346};
| 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 (DPM) synthase complex. {ECO:0000269|PubMed:10835346}.
|
Homo sapiens (Human)
|
O60763
|
USO1_HUMAN
|
MNFLRGVMGGQSAGPQHTEAETIQKLCDRVASSTLLDDRRNAVRALKSLSKKYRLEVGIQAMEHLIHVLQTDRSDSEIIGYALDTLYNIISNEEEEEVEENSTRQSEDLGSQFTEIFIKQQENVTLLLSLLEEFDFHVRWPGVKLLTSLLKQLGPQVQQIILVSPMGVSRLMDLLADSREVIRNDGVLLLQALTRSNGAIQKIVAFENAFERLLDIISEEGNSDGGIVVEDCLILLQNLLKNNNSNQNFFKEGSYIQRMKPWFEVGDENSGWSAQKVTNLHLMLQLVRVLVSPTNPPGATSSCQKAMFQCGLLQQLCTILMATGVPADILTETINTVSEVIRGCQVNQDYFASVNAPSNPPRPAIVVLLMSMVNERQPFVLRCAVLYCFQCFLYKNQKGQGEIVSTLLPSTIDATGNSVSAGQLLCGGLFSTDSLSNWCAAVALAHALQENATQKEQLLRVQLATSIGNPPVSLLQQCTNILSQGSKIQTRVGLLMLLCTWLSNCPIAVTHFLHNSANVPFLTGQIAENLGEEEQLVQGLCALLLGISIYFNDNSLESYMKEKLKQLIEKRIGKENFIEKLGFISKHELYSRASQKPQPNFPSPEYMIFDHEFTKLVKELEGVITKAIYKSSEEDKKEEEVKKTLEQHDNIVTHYKNMIREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQMNGIQPEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDSEQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDELESGDQEDEDDESEDPGKDLDHI
| 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 signal transduction [GO:0007264]; transcytosis [GO:0045056]; vesicle fusion with Golgi apparatus [GO:0048280]
|
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 cytoplasm [GO:0048471]; transport vesicle [GO:0030133]
|
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 apparatus during interphase. During interphase, the phosphorylated form is found exclusively in cytosol; the unphosphorylated form is associated with Golgi apparatus membranes. {ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}.
| 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 membranes in proximity. {ECO:0000250|UniProtKB:P41542}.
|
Homo sapiens (Human)
|
O60779
|
S19A2_HUMAN
|
MDVPGPVSRRAAAAAATVLLRTARVRRECWFLPTALLCAYGFFASLRPSEPFLTPYLLGPDKNLTEREVFNEIYPVWTYSYLVLLFPVFLATDYLRYKPVVLLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYSVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVAGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSTCQRVNGIKVQNGGIVTDTPASNHLPGWEDIESKIPLNMEEPPVEEPEPKPDRLLVLKVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYTQGLWEKVMPSRYAAIYNGGVEAVSTLLGAVAVFAVGYIKISWSTWGEMTLSLFSLLIAAAVYIMDTVGNIWVCYASYVVFRIIYMLLITIATFQIAANLSMERYALVFGVNTFIALALQTLLTLIVVDASGLGLEITTQFLIYASYFALIAVVFLASGAVSVMKKCRKLEDPQSSSQVTTS
| 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: Reaction=n H(+)(out) + pyridoxine(out) = n H(+)(in) + pyridoxine(in); Xref=Rhea:RHEA:76203, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709; Evidence={ECO:0000269|PubMed:33008889, ECO:0000269|PubMed:35512554, ECO:0000269|PubMed:35724964};
|
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 pmol/min/mg enzyme for pyridoxine (at pH 5.5) {ECO:0000269|PubMed:33008889}; Vmax=100 pmol/min/mg enzyme for thiamine (at pH 5.5) {ECO:0000269|PubMed:33008889}; Vmax=106 pmol/min/mg enzyme for thiamine (at pH 7.4) {ECO:0000269|PubMed:33008889};
| 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:10542220, ECO:0000269|PubMed:21836059, ECO:0000269|PubMed:33008889, ECO:0000269|PubMed:35512554, ECO:0000269|PubMed:35724964}.
|
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
|
MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDALRAVKKRIVGNKNFHEVMLALTVLETCVKNCGHRFHVLVASQDFVESVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVTIYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETQSGQDSVGTDSSQQEDSGQHAAPLPAPPILSGDTPIAPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQAEPADLELLQELNRTCRAMQQRVLELIPQIANEQLTEELLIVNDNLNNVFLRHERFERFRTGQTTKAPSEAEPAADLIDMGPDPAATGNLSSQLAGMNLGSSSVRAGLQSLEASGRLEDEFDMFALTRGSSLADQRKEVKYEAPQATDGLAGALDARQQSTGAIPVTQACLMEDIEQWLSTDVGNDAEEPKGVTSEEFDKFLEERAKAADRLPNLSSPSAEGPPGPPSGPAPRKKTQEKDDDMLFAL
| 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 autophagosome [GO:0061753]
|
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 membrane [GO:0035579]
|
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:0000269|PubMed:31263572}; Peripheral membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:15047686, ECO:0000269|PubMed:25588840, ECO:0000269|PubMed:26320582}; Peripheral membrane protein {ECO:0000305}. Note=Localized to endo/exosomal vesicles (PubMed:31263572). Enriched on signaling endosomes (PubMed:25588840). Recruited to early endosomes by TOLLIP and by PtdIns(5)P (PubMed:15047686, PubMed:25588840, PubMed:26320582). {ECO:0000269|PubMed:15047686, ECO:0000269|PubMed:25588840, ECO:0000269|PubMed:26320582, ECO:0000269|PubMed:31263572}.
| 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). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (PubMed:23023224). Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes (PubMed:23023224). MYO6 links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (PubMed:31371777). Binds to polyubiquitinated proteins via its GAT domain (PubMed:14563850). In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes (PubMed:15047686). The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin (PubMed:14563850, PubMed:15047686). Mediates clathrin recruitment to early endosomes by ZFYVE16 (PubMed:15657082). Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition; the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking (PubMed:26320582). Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation (PubMed:25588840). PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation (PubMed:25588840). Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling (PubMed:15047686, PubMed:26320582). {ECO:0000269|PubMed:14563850, ECO:0000269|PubMed:15047686, ECO:0000269|PubMed:15657082, ECO:0000269|PubMed:23023224, ECO:0000269|PubMed:25588840, ECO:0000269|PubMed:26320582, ECO:0000269|PubMed:31371777}.
|
Homo sapiens (Human)
|
O60806
|
TBX19_HUMAN
|
MAMSELGTRKPSDGTVSHLLNVVESELQAGREKGDPTEKQLQIILEDAPLWQRFKEVTNEMIVTKNGRRMFPVLKISVTGLDPNAMYSLLLDFVPTDSHRWKYVNGEWVPAGKPEVSSHSCVYIHPDSPNFGAHWMKAPISFSKVKLTNKLNGGGQIMLNSLHKYEPQVHIVRVGSAHRMVTNCSFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERNHLRDVPEAISESQHVTYSHLGGWIFSNPDGVCTAGNSNYQYAAPLPLPAPHTHHGCEHYSGLRGHRQAPYPSAYMHRNHSPSVNLIESSSNNLQVFSGPDSWTSLSSTPHASILSVPHTNGPINPGPSPYPCLWTISNGAGGPSGPGPEVHASTPGAFLLGNPAVTSPPSVLSTQAPTSAGVEVLGEPSLTSIAVSTWTAVASHPFAGWGGPGAGGHHSPSSLDG
| 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 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, 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 another organism [GO:0031640]
|
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 specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons. {ECO:0000269|PubMed:16627869}.; PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation (PubMed:12757711). Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. {ECO:0000250|UniProtKB:Q64475, ECO:0000269|PubMed:12757711}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.; PTM: ADP-ribosylated by PARP1 or PARP2 on Ser-7 (H2BS6ADPr) in response to DNA damage (PubMed:34874266). H2BS6ADPr promotes recruitment of CHD1L (PubMed:34874266). Mono-ADP-ribosylated on Glu-3 (H2BE2ADPr) by PARP3 in response to single-strand breaks (PubMed:27530147). Poly ADP-ribosylation on Glu-36 (H2BE35ADPr) by PARP1 regulates adipogenesis: it inhibits phosphorylation at Ser-37 (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). {ECO:0000250|UniProtKB:Q6ZWY9, ECO:0000269|PubMed:27530147, ECO:0000269|PubMed:34874266}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000269|PubMed:31645732}.
|
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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; FUNCTION: Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.
|
Homo sapiens (Human)
|
O60825
|
F262_HUMAN
|
MSGASSSEQNNNSYETKTPNLRMSEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYRPLDPDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHRDKPTNNFPKNQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKPLSPLRAQDMQEGAD
|
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; Evidence={ECO:0000305|PubMed:11069105}; CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579, ChEBI:CHEBI:456216; EC=2.7.1.105; Evidence={ECO:0000269|PubMed:11069105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15654; Evidence={ECO:0000269|PubMed:11069105};
|
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-fructose 6-phosphate (in presence of PKB) {ECO:0000269|PubMed:11069105}; KM=4.7 uM for beta-D-fructose 2,6-bisphosphate (in presence of AMPK) {ECO:0000269|PubMed:11069105};
| null | null | null |
FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000269|PubMed:11069105}.
|
Homo sapiens (Human)
|
O60826
|
CCD22_HUMAN
|
MEEADRILIHSLRQAGTAVPPDVQTLRAFTTELVVEAVVRCLRVINPAVGSGLSPLLPLAMSARFRLAMSLAQACMDLGYPLELGYQNFLYPSEPDLRDLLLFLAERLPTDASEDADQPAGDSAILLRAIGSQIRDQLALPWVPPHLRTPKLQHLQGSALQKPFHASRLVVPELSSRGEPREFQASPLLLPVPTQVPQPVGRVASLLEHHALQLCQQTGRDRPGDEDWVHRTSRLPPQEDTRAQRQRLQKQLTEHLRQSWGLLGAPIQARDLGELLQAWGAGAKTGAPKGSRFTHSEKFTFHLEPQAQATQVSDVPATSRRPEQVTWAAQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAEREQALRLKSRAVELLPDGTANLAKLQLVVENSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETELGKKTLSNLEKIREDYRALRQENAGLLGRVREA
| 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 transduction [GO:0043123]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; protein transport [GO:0015031]
|
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 activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10 (PubMed:23563313). Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. The CCC complex associates with SNX17, retriever and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGA5:ITGB1 (PubMed:25355947, PubMed:28892079). Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes (PubMed:25355947). {ECO:0000269|PubMed:23563313, ECO:0000269|PubMed:25355947, ECO:0000269|PubMed:28892079}.; FUNCTION: (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface. {ECO:0000269|PubMed:28892079}.
|
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 to virus by host [GO:0002230]; positive regulation of type I interferon production [GO:0032481]; regulation of dendrite morphogenesis [GO:0048814]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA splicing [GO:0043484]
|
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). Colocalized with POU3F2 (PubMed:10332029). Colocalized with ATXN1 in nuclear inclusion bodies (PubMed:12062018). Localizes to cytoplasmic stress granules (PubMed:21933836). {ECO:0000250|UniProtKB:Q91VJ5, ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:21933836}.
| 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-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species (PubMed:10332029, PubMed:12062018, PubMed:20410308, PubMed:23512658). May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery (PubMed:10198427). May be involved in ATXN1 mutant-induced cell death (PubMed:12062018). The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit (PubMed:12062018). Involved in the assembly of cytoplasmic stress granule, possibly by participating in the transport of neuronal RNA granules (PubMed:21933836). Also acts as an innate immune sensor of infection by retroviruses, such as HIV, by detecting the presence of reverse-transcribed DNA in the cytosol (PubMed:26046437). Directly binds retroviral reverse-transcribed DNA in the cytosol and interacts with CGAS, leading to activate the cGAS-STING signaling pathway, triggering type-I interferon production (PubMed:26046437). {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:20410308, ECO:0000269|PubMed:21933836, ECO:0000269|PubMed:23512658, ECO:0000269|PubMed:26046437}.
|
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 multiple Ser and Thr residues attenuates its ability to potentiate JUN transcriptional activator activity (PubMed:28289210). {ECO:0000269|PubMed:24559171, ECO:0000269|PubMed:26242913, ECO:0000269|PubMed:28289210}.
|
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:25374899, PubMed:30658679). {ECO:0000269|PubMed:21357425, ECO:0000269|PubMed:24263171, ECO:0000269|PubMed:25374899, ECO:0000269|PubMed:28289210, ECO:0000269|PubMed:30658679}.
|
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
|
MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFDKLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGVLRYEDGIEVNQEIVVITTKGEAICMAIALMTTAVISTCDHGIVAKIKRVIMERDTYPRKWGLGPKASQKKLMIKQGLLDKHGKPTDSTPATWKQEYVDYSESAKKEVVAEVVKAPQVVAEAAKTAKRKRESESESDETPPAAPQLIKKEKKKSKKDKKAKAGLESGAEPGDGDSDTTKKKKKKKKAKEVELVSE
|
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 regulation of telomerase activity [GO:0051973]; positive regulation of telomerase RNA localization to Cajal body [GO:1904874]; positive regulation of telomere maintenance via telomerase [GO:0032212]; regulation of telomerase RNA localization to Cajal body [GO:1904872]; RNA processing [GO:0006396]; rRNA processing [GO:0006364]; rRNA pseudouridine synthesis [GO:0031118]; scaRNA localization to Cajal body [GO:0090666]; snRNA pseudouridine synthesis [GO:0031120]; telomerase RNA stabilization [GO:0090669]; telomere maintenance via telomerase [GO:0007004]
|
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:25219674). Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance (PubMed:19179534, PubMed:25219674). Also required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (PubMed:19179534). {ECO:0000269|PubMed:19179534, ECO:0000269|PubMed:25219674, ECO:0000269|PubMed:32554502}.; FUNCTION: [Isoform 3]: Promotes cell to cell and cell to substratum adhesion, increases the cell proliferation rate and leads to cytokeratin hyper-expression. {ECO:0000269|PubMed:21820037}.
|
Homo sapiens (Human)
|
O60840
|
CAC1F_HUMAN
|
MSESEGGKDTTPEPSPANGAGPGPEWGLCPGPPAVEGESSGASGLGTPKRRNQHSKHKTVAVASAQRSPRALFCLTLANPLRRSCISIVEWKPFDILILLTIFANCVALGVYIPFPEDDSNTANHNLEQVEYVFLVIFTVETVLKIVAYGLVLHPSAYIRNGWNLLDFIIVVVGLFSVLLEQGPGRPGDAPHTGGKPGGFDVKALRAFRVLRPLRLVSGVPSLHIVLNSIMKALVPLLHIALLVLFVIIIYAIIGLELFLGRMHKTCYFLGSDMEAEEDPSPCASSGSGRACTLNQTECRGRWPGPNGGITNFDNFFFAMLTVFQCVTMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKQREKQQMEEDLRGYLDWITQAEELDMEDPSADDNLGSMAEEGRAGHRPQLAELTNRRRGRLRWFSHSTRSTHSTSSHASLPASDTGSMTETQGDEDEEEGALASCTRCLNKIMKTRVCRRLRRANRVLRARCRRAVKSNACYWAVLLLVFLNTLTIASEHHGQPVWLTQIQEYANKVLLCLFTVEMLLKLYGLGPSAYVSSFFNRFDCFVVCGGILETTLVEVGAMQPLGISVLRCVRLLRIFKVTRHWASLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDQTHTKRSTFDTFPQALLTVFQILTGEDWNVVMYDGIMAYGGPFFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLASGDAGTAKDKGGEKSNEKDLPQENEGLVPGVEKEEEEGARREGADMEEEEEEEEEEEEEEEEEGAGGVELLQEVVPKEKVVPIPEGSAFFCLSQTNPLRKGCHTLIHHHVFTNLILVFIILSSVSLAAEDPIRAHSFRNHILGYFDYAFTSIFTVEILLKMTVFGAFLHRGSFCRSWFNMLDLLVVSVSLISFGIHSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYTCTDEAKHTPQECKGSFLVYPDGDVSRPLVRERLWVNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDAYAEDHGPIYNYRVEISVFFIVYIIIIAFFMMNIFVGFVIITFRAQGEQEYQNCELDKNQRQCVEYALKAQPLRRYIPKNPHQYRVWATVNSAAFEYLMFLLILLNTVALAMQHYEQTAPFNYAMDILNMVFTGLFTIEMVLKIIAFKPKHYFTDAWNTFDALIVVGSIVDIAVTEVNNGGHLGESSEDSSRISITFFRLFRVMRLVKLLSKGEGIRTLLWTFIKSFQALPYVALLIAMIFFIYAVIGMQMFGKVALQDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLASLPGNRCDPESDFGPGEEFTCGSNFAIAYFISFFMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPGAKGRIKHLDVVALLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVTFNATLFALVRTSLKIKTEGNLEQANQELRIVIKKIWKRMKQKLLDEVIPPPDEEEVTVGKFYATFLIQDYFRKFRRRKEKGLLGNDAAPSTSSALQAGLRSLQDLGPEMRQALTCDTEEEEEEGQEGVEEEDEKDLETNKATMVSQPSARRGSGISVSLPVGDRLPDSLSFGPSDDDRGTPTSSQPSVPQAGSNTHRRGSGALIFTIPEEGNSQPKGTKGQNKQDEDEEVPDRLSYLDEQAGTPPCSVLLPPHRAQRYMDGHLVPRRRLLPPTPAGRKPSFTIQCLQRQGSCEDLPIPGTYHRGRNSGPNRAQGSWATPPQRGRLLYAPLLLVEEGAAGEGYLGRSSGPLRTFTCLHVPGTHSDPSHGKRGSADSLVEAVLISEGLGLFARDPRFVALAKQEIADACRLTLDEMDNAASDLLAQGTSSLYSDEESILSRFDEEDLGDEMACVHAL
| 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 isoform alpha-1F gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines. Activates at more negative voltages and does not undergo calcium-dependent inactivation (CDI), due to incoming calcium ions, during depolarization. {ECO:0000269|PubMed:27226626}.; FUNCTION: [Isoform 4]: Voltage-dependent L-type calcium channel activates at more hyperpolarized voltages and exhibits a robust calcium-dependent inactivation (CDI), due to incoming calcium ions, during depolarizations. {ECO:0000269|PubMed:27226626}.; FUNCTION: [Isoform 6]: Voltage-dependent L-type calcium channel activates at more hyperpolarized voltages and exhibits a robust calcium-dependent inactivation (CDI), due to incoming calcium ions, during depolarizations. {ECO:0000269|PubMed:27226626}.
|
Homo sapiens (Human)
|
O60841
|
IF2P_HUMAN
|
MGKKQKNKSEDSTKDDIDLDALAAEIEGAGAAKEQEPQKSKGKKKKEKKKQDFDEDDILKELEELSLEAQGIKADRETVAVKPTENNEEEFTSKDKKKKGQKGKKQSFDDNDSEELEDKDSKSKKTAKPKVEMYSGSDDDDDFNKLPKKAKGKAQKSNKKWDGSEEDEDNSKKIKERSRINSSGESGDESDEFLQSRKGQKKNQKNKPGPNIESGNEDDDASFKIKTVAQKKAEKKERERKKRDEEKAKLRKLKEKEELETGKKDQSKQKESQRKFEEETVKSKVTVDTGVIPASEEKAETPTAAEDDNEGDKKKKDKKKKKGEKEEKEKEKKKGPSKATVKAMQEALAKLKEEEERQKREEEERIKRLEELEAKRKEEERLEQEKRERKKQKEKERKERLKKEGKLLTKSQREARARAEATLKLLQAQGVEVPSKDSLPKKRPIYEDKKRKKIPQQLESKEVSESMELCAAVEVMEQGVPEKEETPPPVEPEEEEDTEDAGLDDWEAMASDEETEKVEGNKVHIEVKENPEEEEEEEEEEEEDEESEEEEEEEGESEGSEGDEEDEKVSDEKDSGKTLDKKPSKEMSSDSEYDSDDDRTKEERAYDKAKRRIEKRRLEHSKNVNTEKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKEDEIPVLKDELIHELKQTLNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKIKILPQYIFNSRDPIVMGVTVEAGQVKQGTPMCVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPGESPKMFGRHFEATDILVSKISRQSIDALKDWFRDEMQKSDWQLIVELKKVFEII
|
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|UniProtKB:G0S8G9};
|
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:19670; Evidence={ECO:0000269|PubMed:10659855, ECO:0000305|PubMed:35732735};
|
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:10659855, PubMed:35732735). Together with eIF1A (EIF1AX), actively orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex (PubMed:12569173, PubMed:35732735). Is released after formation of the 80S initiation complex (PubMed:35732735). Its GTPase activity is not essential for ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A (EIF1AX) ejection quickly followed by EIF5B release to form elongation-competent ribosomes (PubMed:10659855, PubMed:35732735). In contrast to its procaryotic homolog, does not promote recruitment of Met-rRNA to the small ribosomal subunit (PubMed:10659855). {ECO:0000269|PubMed:10659855, ECO:0000269|PubMed:12569173, ECO:0000269|PubMed:35732735}.
|
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
|
MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGSVRNSLWRPAPFKCPTCRKETSATGINSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCLTDMQLICGICATRGEHTKHVFCSIEDAYAQERDAFESLFQSFETWRRGDALSRLDTLETSKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQAYDPEINKLNTILQEQRMAFNIAEAFKDVSEPIVFLQQMQEFREKIKVIKETPLPPSNLPASPLMKNFDTSQWEDIKLVDVDKLSLPQDTGTFISKIPWSFYKLFLLILLLGLVIVFGPTMFLEWSLFDDLATWKGCLSNFSSYLTKTADFIEQSVFYWEQVTDGFFIFNERFKNFTLVVLNNVAEFVCKYKLL
|
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 of NF-kappaB transcription factor activity [GO:0051092]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; suppression of viral release by host [GO:0044790]
|
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 colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.
|
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 folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor (PubMed:22178386). Also plays a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation (PubMed:28087809). Participates as well in T-cell receptor-mediated NF-kappa-B activation (PubMed:25088585). In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B (PubMed:25152375). {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:25088585, ECO:0000269|PubMed:25152375, ECO:0000269|PubMed:28087809}.
|
Homo sapiens (Human)
|
O60861
|
GAS7_HUMAN
|
MSGARCRTLYPFSGERHGQGLRFAAGELITLLQVPDGGWWEGEKEDGLRGWFPASYVQLLEKPGMVPPPPGEESQTVILPPGWQSYLSPQGRRYYVNTTTNETTWERPSSSPGIPASPGSHRSSLPPTVNGYHASGTPAHPPETAHMSVRKSTGDSQNLGSSSPSKKQSKENTITINCVTFPHPDTMPEQQLLKPTEWSYCDYFWADKKDPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEDYAKNLAKLSQNSLASQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQRDLEMKTQQLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQLLRKVDPAKDRELWVREHKTGNIRPVDMEI
| 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 differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism. {ECO:0000269|PubMed:10567391, ECO:0000269|PubMed:12040021, ECO:0000269|PubMed:15112053, ECO:0000269|PubMed:9813014}.
|
Homo sapiens (Human)
|
O60870
|
KIN17_HUMAN
|
MGKSDFLTPKAIANRIKSKGLQKLRWYCQMCQKQCRDENGFKCHCMSESHQRQLLLASENPQQFMDYFSEEFRNDFLELLRRRFGTKRVHNNIVYNEYISHREHIHMNATQWETLTDFTKWLGREGLCKVDETPKGWYIQYIDRDPETIRRQLELEKKKKQDLDDEEKTAKFIEEQVRRGLEGKEQEVPTFTELSRENDEEKVTFNLSKGACSSSGATSSKSSTLGPSALKTIGSSASVKRKESSQSSTQSKEKKKKKSALDEIMEIEEEKKRTARTDYWLQPEIIVKIITKKLGEKYHKKKAIVKEVIDKYTAVVKMIDSGDKLKLDQTHLETVIPAPGKRILVLNGGYRGNEGTLESINEKTFSATIVIETGPLKGRRVEGIQYEDISKLA
| 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|PubMed:15831485}. Note=During S phase, strongly associated with the nuclear matrix, and to chromosomal DNA in the presence of DNA damage. Also shows cytoplasmic localization in elongated spermatids. {ECO:0000250|UniProtKB:Q8K339, ECO:0000269|PubMed:11880372, ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299, ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485}.
| 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 in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro. {ECO:0000250|UniProtKB:Q8K339, ECO:0000269|PubMed:11880372, ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299, ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485, ECO:0000269|PubMed:17045609}.
|
Homo sapiens (Human)
|
O60879
|
DIAP2_HUMAN
|
MEQPGAAASGAGGGSEEPGGGRSNKRSAGNRAANEEETKNKPKLNIQIKTLADDVRDRITSFRKSTVKKEKPLIQHPIDSQVAMSEFPAAQPLYDERSLNLSEKEVLDLFEKMMEDMNLNEEKKAPLRNKDFTTKREMVVQYISATAKSGGLKNSKHECTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSNPVSWVNNFGHEGLGLLLDELEKLLDKKQQENIDKKNQYKLIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQPNMMTEIVKILSAICIVGEENILDKLLGAITTAAERNNRERFSPIVEGLENQEALQLQVACMQFINALVTSPYELDFRIHLRNEFLRSGLKTMLPDLKEKENDELDIQLKVFDENKEDDLTELSHRLNDIRAEMDDMNEVYHLLYNMLKDTAAENYFLSILQHFLLIRNDYYIRPQYYKIIEECVSQIVLHCSGMDPDFKYRQRLDIDLTHLIDSCVNKAKVEESEQKAAEFSKKFDEEFTARQEAQAELQKRDEKIKELEAEIQQLRTQAQVLSSSSGIPGPPAAPPLPGVGPPPPPPAPPLPGGAPLPPPPPPLPGMMGIPPPPPPPLLFGGPPPPPPLGGVPPPPGISLNLPYGMKQKKMYKPEVSMKRINWSKIEPTELSENCFWLRVKEDKFENPDLFAKLALNFATQIKVQKNAEALEEKKTGPTKKKVKELRILDPKTAQNLSIFLGSYRMPYEDIRNVILEVNEDMLSEALIQNLVKHLPEQKILNELAELKNEYDDLCEPEQFGVVMSSVKMLQPRLSSILFKLTFEEHINNIKPSIIAVTLACEELKKSESFNRLLELVLLVGNYMNSGSRNAQSLGFKINFLCKIRDTKSADQKTTLLHFIADICEEKYRDILKFPEELEHVESASKVSAQILKSNLASMEQQIVHLERDIKKFPQAENQHDKFVEKMTSFTKTAREQYEKLSTMHNNMMKLYENLGEYFIFDSKTVSIEEFFGDLNNFRTLFLEAVRENNKRREMEEKTRRAKLAKEKAEQEKLERQKKKKQLIDINKEGDETGVMDNLLEALQSGAAFRDRRKRIPRNPDNRRVPLERSRSRHNGAISSK
| 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:12577064}.
|
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 mediated cytotoxicity [GO:0045954]; regulation of immune response [GO:0050776]
|
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 effectors including INPP5D/SHIP1 and PTPN11/SHP-2 (PubMed:11806999). However, by simultaneous interactions, recruits FYN which subsequently phosphorylates and activates SLAMF1 (PubMed:12458214). Positively regulates CD244/2B4- and CD84-mediated natural killer (NK) cell functions. Can also promote CD48-, SLAMF6 -, LY9-, and SLAMF7-mediated NK cell activation. In the context of NK cell-mediated cytotoxicity enhances conjugate formation with target cells (By similarity). May also regulate the activity of the neurotrophin receptors NTRK1, NTRK2 and NTRK3. {ECO:0000250|UniProtKB:O88890, ECO:0000269|PubMed:11806999, ECO:0000269|PubMed:12458214, ECO:0000305|PubMed:21219180}.
|
Homo sapiens (Human)
|
O60882
|
MMP20_HUMAN
|
MKVLPASGLAVFLIMALKFSTAAPSLVAASPRTWRNNYRLAQAYLDKYYTNKEGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVIKKPRCGVPDVANYRLFPGEPKWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTMGTNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYGPRKVFLGKPTLPHAPHHKPSIPDLCDSSSSFDAVTMLGKELLLFKDRIFWRRQVHLRTGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRGFQMQGPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVELNGYIYFFSGPKTYKYDTEKEDVVSVVKSSSWIGC
|
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' site. {ECO:0000269|PubMed:10922468, ECO:0000269|PubMed:9398237}.
|
Homo sapiens (Human)
|
O60883
|
G37L1_HUMAN
|
MRWLWPLAVSLAVILAVGLSRVSGGAPLHLGRHRAETQEQQSRSKRGTEDEEAKGVQQYVPEEWAEYPRPIHPAGLQPTKPLVATSPNPGKDGGTPDSGQELRGNLTGAPGQRLQIQNPLYPVTESSYSAYAIMLLALVVFAVGIVGNLSVMCIVWHSYYLKSAWNSILASLALWDFLVLFFCLPIVIFNEITKQRLLGDVSCRAVPFMEVSSLGVTTFSLCALGIDRFHVATSTLPKVRPIERCQSILAKLAVIWVGSMTLAVPELLLWQLAQEPAPTMGTLDSCIMKPSASLPESLYSLVMTYQNARMWWYFGCYFCLPILFTVTCQLVTWRVRGPPGRKSECRASKHEQCESQLNSTVVGLTVVYAFCTLPENVCNIVVAYLSTELTRQTLDLLGLINQFSTFFKGAITPVLLLCICRPLGQAFLDCCCCCCCEECGGASEASAANGSDNKLKTEVSSSIYFHKPRESPPLLPLGTPC
| 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]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of systemic arterial blood pressure [GO:0003085]; positive regulation of cerebellar granule cell precursor proliferation [GO:0021940]; positive regulation of MAPK cascade [GO:0043410]; smoothened signaling pathway [GO:0007224]
|
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:Q99JG2}.
| 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:27072655, PubMed:28688853). It has been suggested that GPR37L1 is a constitutively active receptor which signals through the guanine nucleotide-binding protein G(s) subunit alpha (PubMed:27072655). Participates in the regulation of postnatal cerebellar development by modulating the Shh pathway (By similarity). Regulates baseline blood pressure in females and protects against cardiovascular stress in males (By similarity). Mediates inhibition of astrocyte glutamate transporters and reduction in neuronal N-methyl-D-aspartate receptor activity (By similarity). {ECO:0000250|UniProtKB:Q99JG2, ECO:0000269|PubMed:23690594, ECO:0000269|PubMed:27072655, ECO:0000269|PubMed:28688853}.
|
Homo sapiens (Human)
|
O60884
|
DNJA2_HUMAN
|
MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDGRQIVVKYPPGKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPEVPNIIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ
| 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
|
MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETEMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF
| 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 [GO:0045893]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of T-helper 17 cell lineage commitment [GO:2000330]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of inflammatory response [GO:0050727]; regulation of transcription by RNA polymerase II [GO:0006357]
|
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 activity [GO:0008353]; transcription cis-regulatory region binding [GO:0000976]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]
|
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 promoters, phosphorylation promoting recruitment to p53/TP53 target promoters. {ECO:0000269|PubMed:23317504}.
|
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 different signals such as activation of the JNK pathway or nocodazole treatment (PubMed:16109376, PubMed:21890894). Preferentially localizes to mitotic chromosomes, while it does not localize to meiotic chromosomes (PubMed:16109376, PubMed:21890894). {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:21890894}.; SUBCELLULAR LOCATION: [Isoform B]: Chromosome {ECO:0000269|PubMed:23728299}.
| 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 entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504). {ECO:0000250|UniProtKB:Q9ESU6, ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:19103749, ECO:0000269|PubMed:19596240, ECO:0000269|PubMed:22334664, ECO:0000269|PubMed:22509028, ECO:0000269|PubMed:23086925, ECO:0000269|PubMed:23317504, ECO:0000269|PubMed:23589332, ECO:0000269|PubMed:24360279, ECO:0000269|PubMed:29176719}.; FUNCTION: [Isoform B]: Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AX/H2A.x phosphorylation. {ECO:0000269|PubMed:23728299}.
|
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
|
MGHPPLEFSDCYLDSPDFRERLKCYEQELERTNKFIKDVIKDGNALISAMRNYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLNEVENERMMMVHNASDLLIKPLENFRKEQIGFTKERKKKFEKDGERFYSLLDRHLHLSSKKKESQLQEADLQVDKERHNFFESSLDYVYQIQEVQESKKFNIVEPVLAFLHSLFISNSLTVELTQDFLPYKQQLQLSLQNTRNHFSSTREEMEELKKRMKEAPQTCKLPGQPTIEGYLYTQEKWALGISWVKYYCQYEKETKTLTMTPMEQKPGAKQGPLDLTLKYCVRRKTESIDKRFCFDIETNERPGTITLQALSEANRRLWMEAMDGKEPIYHSPITKQQEMELNEVGFKFVRKCINIIETKGIKTEGLYRTVGSNIQVQKLLNAFFDPKCPGDVDFHNSDWDIKTITSSLKFYLRNLSEPVMTYRLHKELVSAAKSDNLDYRLGAIHSLVYKLPEKNREMLELLIRHLVNVCEHSKENLMTPSNMGVIFGPTLMRAQEDTVAAMMNIKFQNIVVEILIEHFGKIYLGPPEESAAPPVPPPRVTARRHKPITISKRLLRERTVFYTSSLDESEDEIQHQTPNGTITSSIEPPKPPQHPKLPIQRSGETDPGRKSPSRPILDGKLEPCPEVDVGKLVSRLQDGGTKITPKATNGPMPGSGPTKTPSFHIKRPAPRPLAHHKEGDADSFSKVRPPGEKPTIIRPPVRPPDPPCRAATPQKPEPKPDIVAGNAGEITSSVVASRTRFFETASRKTGSSQGRLPGDES
| 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 apical/basal polarity [GO:0045198]; maintenance of postsynaptic specialization structure [GO:0098880]; negative regulation of proteasomal protein catabolic process [GO:1901799]; nervous system development [GO:0007399]; neuron differentiation [GO:0030182]; neuron projection development [GO:0031175]; regulation of endocytosis [GO:0030100]; regulation of postsynaptic neurotransmitter receptor internalization [GO:0099149]; regulation of Rho protein signal transduction [GO:0035023]; regulation of synaptic transmission, glutamatergic [GO:0051966]; regulation of synaptic vesicle endocytosis [GO:1900242]; signal transduction [GO:0007165]; substrate-dependent cell migration, cell extension [GO:0006930]; synaptic vesicle endocytosis [GO:0048488]
|
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:Q99J31}.
| 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 vesicle endocytosis at presynaptic terminals. Required for the localization of NR1D1 to dendrites, can suppress its repressor activity and protect it from proteasomal degradation (By similarity). {ECO:0000250}.
|
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:0032870]; G protein-coupled receptor signaling pathway [GO:0007186]; intracellular protein transport [GO:0006886]; positive regulation of protein glycosylation [GO:0060050]; protein localization to plasma membrane [GO:0072659]; protein transport [GO:0015031]; receptor internalization [GO:0031623]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]
|
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 transport [GO:0006816]; cellular response to hormone stimulus [GO:0032870]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; G protein-coupled receptor signaling pathway [GO:0007186]; heart development [GO:0007507]; intracellular protein transport [GO:0006886]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of vascular permeability [GO:0043116]; positive regulation of angiogenesis [GO:0045766]; positive regulation of gene expression [GO:0010628]; positive regulation of vasculogenesis [GO:2001214]; protein localization to plasma membrane [GO:0072659]; protein transport [GO:0015031]; receptor internalization [GO:0031623]; regulation of blood pressure [GO:0008217]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; sprouting angiogenesis [GO:0002040]; vascular associated smooth muscle cell development [GO:0097084]; vasculogenesis [GO:0001570]
|
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 [GO:0032870]; cross-receptor inhibition within G protein-coupled receptor heterodimer [GO:0038041]; G protein-coupled receptor signaling pathway [GO:0007186]; G protein-coupled receptor signaling pathway involved in heart process [GO:0086103]; intracellular protein transport [GO:0006886]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein kinase A signaling [GO:0010739]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of receptor recycling [GO:0001921]; protein localization to plasma membrane [GO:0072659]; protein transport [GO:0015031]; receptor internalization [GO:0031623]; response to amyloid-beta [GO:1904645]
|
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-dependent manner.
| 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:23674134, ECO:0000269|PubMed:9620797}.
|
Homo sapiens (Human)
|
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