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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O75844
|
FACE1_HUMAN
|
MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKTMKQH
|
3.4.24.84
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23539603}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23539603};
|
adult walking behavior [GO:0007628]; bone mineralization [GO:0030282]; CAAX-box protein processing [GO:0071586]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; CAMKK-AMPK signaling cascade [GO:0061762]; cardiac conduction [GO:0061337]; cardiac muscle cell development [GO:0055013]; cardiac ventricle development [GO:0003231]; cellular lipid metabolic process [GO:0044255]; cellular response to gamma radiation [GO:0071480]; determination of adult lifespan [GO:0008340]; DNA repair [GO:0006281]; growth plate cartilage development [GO:0003417]; hair follicle development [GO:0001942]; heart morphogenesis [GO:0003007]; inflammatory cell apoptotic process [GO:0006925]; kidney morphogenesis [GO:0060993]; liver development [GO:0001889]; maintenance of rDNA [GO:0043007]; multicellular organism growth [GO:0035264]; negative regulation of miRNA processing [GO:1903799]; neuromuscular process [GO:0050905]; nuclear envelope organization [GO:0006998]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; prenylated protein catabolic process [GO:0030327]; protein maturation [GO:0051604]; proteolysis [GO:0006508]; regulation of autophagy [GO:0010506]; regulation of bone mineralization [GO:0030500]; regulation of cell shape [GO:0008360]; regulation of cellular senescence [GO:2000772]; regulation of defense response to virus [GO:0050688]; regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043516]; regulation of fibroblast proliferation [GO:0048145]; regulation of glucose metabolic process [GO:0010906]; regulation of hormone metabolic process [GO:0032350]; regulation of lipid metabolic process [GO:0019216]; regulation of mitotic cell cycle DNA replication [GO:1903463]; regulation of multicellular organism growth [GO:0040014]; regulation of stress-activated protein kinase signaling cascade [GO:0070302]; regulation of termination of RNA polymerase I transcription [GO:2000730]; regulation of TOR signaling [GO:0032006]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; response to DNA damage checkpoint signaling [GO:0072423]; thymus development [GO:0048538]; ventricular cardiac muscle tissue development [GO:0003229]
|
early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; membrane [GO:0016020]; nuclear inner membrane [GO:0005637]; protein-containing complex [GO:0032991]
|
double-stranded DNA binding [GO:0003690]; endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metalloexopeptidase activity [GO:0008235]
|
PF01435;PF16491;
|
3.30.2010.10;
|
Peptidase M48A family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:35283811}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:35283811}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolyzes the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with aliphatic side chains and P3' is any C-terminal residue.; EC=3.4.24.84; Evidence={ECO:0000269|PubMed:33293369, ECO:0000269|PubMed:33315887};
| null | null | null | null |
FUNCTION: Transmembrane metalloprotease whose catalytic activity is critical for processing lamin A/LMNA on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum (PubMed:33293369, PubMed:33315887). Proteolytically removes the C-terminal three residues of farnesylated proteins (PubMed:33293369, PubMed:33315887). Plays also an antiviral role independently of its protease activity by restricting enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia (PubMed:28169297, PubMed:28246125). Mechanistically, controls IFITM antiviral pathway to hinder viruses from breaching the endosomal barrier by modulating membrane fluidity (PubMed:35283811). {ECO:0000269|PubMed:28169297, ECO:0000269|PubMed:28246125, ECO:0000269|PubMed:33293369, ECO:0000269|PubMed:33315887, ECO:0000269|PubMed:35283811}.
|
Homo sapiens (Human)
|
O75845
|
SC5D_HUMAN
|
MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDHALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELVVSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPYHIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNYGQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE
|
1.14.19.20
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
|
cholesterol biosynthetic process via desmosterol [GO:0033489]; cholesterol biosynthetic process via lathosterol [GO:0033490]; ergosterol biosynthetic process [GO:0006696]; lipid metabolic process [GO:0006629]; sphingolipid biosynthetic process [GO:0030148]
|
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
C-4 methylsterol oxidase activity [GO:0000254]; C-5 sterol desaturase activity [GO:0000248]; delta7-sterol 5(6)-desaturase activity [GO:0050046]; iron ion binding [GO:0005506]; sphingolipid delta-4 desaturase activity [GO:0042284]; sphingosine hydroxylase activity [GO:0000170]
|
PF04116;
| null |
Sterol desaturase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:54320, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:138130, ChEBI:CHEBI:138131; EC=1.14.19.20; Evidence={ECO:0000305|PubMed:10786622}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54321; Evidence={ECO:0000305|PubMed:10786622}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + lathosterol + O2 = 7-dehydrocholesterol + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46556, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17168, ChEBI:CHEBI:17759, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.14.19.20; Evidence={ECO:0000269|PubMed:10786622}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46557; Evidence={ECO:0000305|PubMed:10786622};
| null | null | null | null |
FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol in cholesterol biosynthesis. {ECO:0000269|PubMed:10786622}.
|
Homo sapiens (Human)
|
O75864
|
PPR37_HUMAN
|
MEIAPQEAPPVPGADGDIEEAPAEAGSPSPASPPADGRLKAAAKRVTFPSDEDIVSGAVEPKDPWRHAQNVTVDEVIGAYKQACQKLNCRQIPKLLRQLQEFTDLGHRLDCLDLKGEKLDYKTCEALEEVFKRLQFKVVDLEQTNLDEDGASALFDMIEYYESATHLNISFNKHIGTRGWQAAAHMMRKTSCLQYLDARNTPLLDHSAPFVARALRIRSSLAVLHLENASLSGRPLMLLATALKMNMNLRELYLADNKLNGLQDSAQLGNLLKFNCSLQILDLRNNHVLDSGLAYICEGLKEQRKGLVTLVLWNNQLTHTGMAFLGMTLPHTQSLETLNLGHNPIGNEGVRHLKNGLISNRSVLRLGLASTKLTCEGAVAVAEFIAESPRLLRLDLRENEIKTGGLMALSLALKVNHSLLRLDLDREPKKEAVKSFIETQKALLAEIQNGCKRNLVLAREREEKEQPPQLSASMPETTATEPQPDDEPAAGVQNGAPSPAPSPDSDSDSDSDGEEEEEEEGERDETPCPALVPPTDSLGPGDRSPPGSPSTPTEQRISVSSPGRGHKVFVVTRVESPPERAEPPASPTPPSPPPPPSPPASPSLPPAGAIDTRDTGSSEPQPPPEPPRSGPPLPNGLKPEFALALPPEPPPGPEVKGGSCGLEHELSCSKNEKELEELLLEASQESGQETL
| null | null |
cell migration [GO:0016477]; regulation of Arp2/3 complex-mediated actin nucleation [GO:0034315]
|
lamellipodium [GO:0030027]; plasma membrane [GO:0005886]
|
protein phosphatase inhibitor activity [GO:0004864]
|
PF13516;
|
3.80.10.10;
|
PPP1R37 family
| null | null | null | null | null | null | null |
FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000269|PubMed:19389623}.
|
Homo sapiens (Human)
|
O75865
|
TPC6A_HUMAN
|
MADTVLFEFLHTEMVAELWAHDPDPGPGGQKMSLSVLEGMGFRVGQALGERLPRETLAFREELDVLKFLCKDLWVAVFQKQMDSLRTNHQGTYVLQDNSFPLLLPMASGLQYLEEAPKFLAFTCGLLRGALYTLGIESVVTASVAALPVCKFQVVIPKS
| null | null |
COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; vesicle tethering [GO:0099022]
|
cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; trans-Golgi network [GO:0005802]; TRAPP complex [GO:0030008]; TRAPPIII protein complex [GO:1990072]
| null |
PF04051;
|
3.30.1380.20;
|
TRAPP small subunits family, BET3 subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in vesicular transport during the biogenesis of melanosomes. {ECO:0000250|UniProtKB:Q78XR0}.
|
Homo sapiens (Human)
|
O75871
|
CEAM4_HUMAN
|
MGPPSAAPRGGHRPWQGLLITASLLTFWHPPTTVQFTIEALPSSAAEGKDVLLLACNISETIQAYYWHKGKTAEGSPLIAGYITDIQANIPGAAYSGRETVYPNGSLLFQNITLEDAGSYTLRTINASYDSDQATGQLHVHQNNVPGLPVGAVAGIVTGVLVGVALVAALVCFLLLSRTGRASIQRDLREQPPPASTPGHGPSHRSTFSAPLPSPRTATPIYEELLYSDANIYCQIDHKADVVS
| null | null |
phagocytosis [GO:0006909]; regulation of immune system process [GO:0002682]; signal transduction [GO:0007165]
|
cell surface [GO:0009986]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
protein tyrosine kinase binding [GO:1990782]
|
PF07686;
|
2.60.40.10;
|
Immunoglobulin superfamily, CEA family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:2050678}.; PTM: The cytoplasmic ITAM-like sequence becomes tyrosine phosphorylated by SRC family PTKs upon ligand-mediated receptor clustering and allows to initiate phagocytosis of bound ligand. {ECO:0000269|PubMed:25567962}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Granulocyte orphan receptor that acts as an trigger efficient phagocytosis of attached particles. {ECO:0000269|PubMed:25567962}.
|
Homo sapiens (Human)
|
O75874
|
IDHC_HUMAN
|
MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL
|
1.1.1.42
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19935646}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19935646}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000269|PubMed:19935646};
|
2-oxoglutarate metabolic process [GO:0006103]; female gonad development [GO:0008585]; glutathione metabolic process [GO:0006749]; glyoxylate cycle [GO:0006097]; isocitrate metabolic process [GO:0006102]; NADP metabolic process [GO:0006739]; regulation of phospholipid biosynthetic process [GO:0071071]; regulation of phospholipid catabolic process [GO:0060696]; response to oxidative stress [GO:0006979]; response to steroid hormone [GO:0048545]; tricarboxylic acid cycle [GO:0006099]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]; secretory granule lumen [GO:0034774]; tertiary granule lumen [GO:1904724]
|
cadherin binding [GO:0045296]; identical protein binding [GO:0042802]; isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]
|
PF00180;
|
3.40.718.10;
|
Isocitrate and isopropylmalate dehydrogenases family
|
PTM: Acetylation at Lys-374 dramatically reduces catalytic activity. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10521434}. Peroxisome {ECO:0000269|PubMed:10521434}.
|
CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; Evidence={ECO:0000269|PubMed:10521434, ECO:0000269|PubMed:19935646}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19630; Evidence={ECO:0000269|PubMed:19935646};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=112 uM for NADP(+) {ECO:0000269|PubMed:10521434}; KM=49 uM for NADP(+) {ECO:0000269|PubMed:19935646}; KM=29 uM for magnesium chloride {ECO:0000269|PubMed:19935646}; KM=76 uM for isocitrate {ECO:0000269|PubMed:10521434}; KM=65 uM for isocitrate {ECO:0000269|PubMed:19935646};
| null | null | null |
FUNCTION: Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase (PubMed:10521434, PubMed:19935646). Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways (PubMed:10521434). May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity). {ECO:0000250|UniProtKB:Q9XSG3, ECO:0000269|PubMed:10521434, ECO:0000269|PubMed:19935646, ECO:0000303|PubMed:10521434}.
|
Homo sapiens (Human)
|
O75879
|
GATB_HUMAN
|
MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGEHKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQINELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATSLPAGADPQQVINIDQIRETLPELPSVTREKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRAEPKKVTSWVLNTFLGYLKQQNLAVSESPVTPSALAELLDLLDSRTISSSAAKQVFEELWKREGKTPGQIVSEKQLELMQDQGALEQLCHSVMEAHPQVVMDVKNRNPRAINKLIGLVRKATQSRADPVMIKEILEKKLSL
|
6.3.5.-
| null |
glutaminyl-tRNAGln biosynthesis via transamidation [GO:0070681]; mitochondrial translation [GO:0032543]
|
glutamyl-tRNA(Gln) amidotransferase complex [GO:0030956]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity [GO:0050567]
|
PF02934;PF02637;
|
1.10.10.410;
|
GatB/GatE family, GatB subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:9878253}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate; Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_03147};
| null | null | null | null |
FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:19805282}.
|
Homo sapiens (Human)
|
O75880
|
SCO1_HUMAN
|
MAMLVLVPGRVMRPLGGQLWRFLPRGLEFWGPAEGTARVLLRQFCARQAEAWRASGRPGYCLGTRPLSTARPPPPWSQKGPGDSTRPSKPGPVSWKSLAITFAIGGALLAGMKHVKKEKAEKLEKERQRHIGKPLLGGPFSLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSITTLPDLTPLFISIDPERDTKEAIANYVKEFSPKLVGLTGTREEVDQVARAYRVYYSPGPKDEDEDYIVDHTIIMYLIGPDGEFLDYFGQNKRKGEIAASIATHMRPYRKKS
| null | null |
intracellular copper ion homeostasis [GO:0006878]; mitochondrial cytochrome c oxidase assembly [GO:0033617]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; myofibril [GO:0030016]
|
copper chaperone activity [GO:0016531]; copper ion binding [GO:0005507]
|
PF02630;
|
3.40.30.10;
|
SCO1/2 family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9878253}. Mitochondrion inner membrane {ECO:0000269|PubMed:15229189}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT-CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (PubMed:15229189, PubMed:15659396, PubMed:16735468, PubMed:17189203, PubMed:19336478). Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 (By similarity). {ECO:0000250|UniProtKB:Q5SUC9, ECO:0000269|PubMed:15229189, ECO:0000269|PubMed:15659396, ECO:0000269|PubMed:16735468, ECO:0000269|PubMed:17189203, ECO:0000269|PubMed:19336478}.
|
Homo sapiens (Human)
|
O75881
|
CP7B1_HUMAN
|
MAGEVSAATGRFSLERLGLPGLALAAALLLLALCLLVRRTRRPGEPPLIKGWLPYLGVVLNLRKDPLRFMKTLQKQHGDTFTVLLGGKYITFILDPFQYQLVIKNHKQLSFRVFSNKLLEKAFSISQLQKNHDMNDELHLCYQFLQGKSLDILLESMMQNLKQVFEPQLLKTTSWDTAELYPFCSSIIFEITFTTIYGKVIVCDNNKFISELRDDFLKFDDKFAYLVSNIPIELLGNVKSIREKIIKCFSSEKLAKMQGWSEVFQSRQDVLEKYYVHEDLEIGAHHLGFLWASVANTIPTMFWAMYYLLRHPEAMAAVRDEIDRLLQSTGQKKGSGFPIHLTREQLDSLICLESSIFEALRLSSYSTTIRFVEEDLTLSSETGDYCVRKGDLVAIFPPVLHGDPEIFEAPEEFRYDRFIEDGKKKTTFFKRGKKLKCYLMPFGTGTSKCPGRFFALMEIKQLLVILLTYFDLEIIDDKPIGLNYSRLLFGIQYPDSDVLFRYKVKS
|
1.14.14.26; 1.14.14.29
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P22680};
|
B cell chemotaxis [GO:0035754]; bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; epithelial cell proliferation [GO:0050673]; intracellular estrogen receptor signaling pathway [GO:0030520]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; positive regulation of epithelial cell proliferation [GO:0050679]; prostate gland epithelium morphogenesis [GO:0060740]; sterol metabolic process [GO:0016125]
|
endoplasmic reticulum membrane [GO:0005789]
|
24-hydroxycholesterol 7alpha-hydroxylase activity [GO:0033782]; 25-hydroxycholesterol 7alpha-hydroxylase activity [GO:0033783]; 27-hydroxycholesterol 7-alpha-monooxygenase activity [GO:0047092]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:9802883}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305|PubMed:9802883}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=25-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha,25-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:24308, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:37623, ChEBI:CHEBI:42977, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.29; Evidence={ECO:0000269|PubMed:10588945, ECO:0000269|PubMed:9802883}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24309; Evidence={ECO:0000305|PubMed:10588945, ECO:0000305|PubMed:9802883}; CATALYTIC ACTIVITY: Reaction=(25R)-cholest-5-ene-3beta,26-diol + O2 + reduced [NADPH--hemoprotein reductase] = (25R)-cholest-5-en-3beta,7alpha,26-triol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:19041, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76591, ChEBI:CHEBI:76592; EC=1.14.14.29; Evidence={ECO:0000269|PubMed:10588945}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19042; Evidence={ECO:0000305|PubMed:10588945}; CATALYTIC ACTIVITY: Reaction=(24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24S)-7alpha-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46124, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:34310, ChEBI:CHEBI:37640, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.26; Evidence={ECO:0000250|UniProtKB:Q60991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46125; Evidence={ECO:0000250|UniProtKB:Q60991}; CATALYTIC ACTIVITY: Reaction=(24S)-25-epoxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24S,25)-epoxy-7alpha-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46464, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:41633, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:86146; Evidence={ECO:0000250|UniProtKB:Q60991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46465; Evidence={ECO:0000250|UniProtKB:Q60991}; CATALYTIC ACTIVITY: Reaction=(22R)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22R,7alpha)-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46460, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:67237, ChEBI:CHEBI:86145; Evidence={ECO:0000250|UniProtKB:Q60991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46461; Evidence={ECO:0000250|UniProtKB:Q60991}; CATALYTIC ACTIVITY: Reaction=androst-5-en-3beta,17beta-diol + O2 + reduced [NADPH--hemoprotein reductase] = androst-5-en-3beta,7alpha,17beta-triol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46204, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:2710, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:85810; Evidence={ECO:0000269|PubMed:24491228}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46205; Evidence={ECO:0000305|PubMed:24491228}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3beta,17beta-diol + O2 + reduced [NADPH--hemoprotein reductase] = 5alpha-androstane-3beta,6alpha,17beta-triol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46200, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18329, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:85809; Evidence={ECO:0000269|PubMed:24491228}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46201; Evidence={ECO:0000305|PubMed:24491228}; CATALYTIC ACTIVITY: Reaction=3beta-hydroxyandrost-5-en-17-one + O2 + reduced [NADPH--hemoprotein reductase] = 3beta,7alpha-dihydroxyandrost-5-en-17-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46192, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28689, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:81471; Evidence={ECO:0000269|PubMed:24491228}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46193; Evidence={ECO:0000305|PubMed:24491228}; CATALYTIC ACTIVITY: Reaction=3beta-hydroxy-5alpha-androstan-17-one + O2 + reduced [NADPH--hemoprotein reductase] = 3beta,7alpha-dihydroxy-5alpha-androstan-17-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:43896, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:85816, ChEBI:CHEBI:541975; Evidence={ECO:0000269|PubMed:24491228}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43897; Evidence={ECO:0000305|PubMed:24491228}; CATALYTIC ACTIVITY: Reaction=O2 + pregnenolone + reduced [NADPH--hemoprotein reductase] = 7alpha-hydroxypregnenolone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46196, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16581, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:81467; Evidence={ECO:0000269|PubMed:24491228}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46197; Evidence={ECO:0000305|PubMed:24491228};
| null |
PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000269|PubMed:10588945, ECO:0000269|PubMed:9802883}.; PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:24491228}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of endogenous oxysterols and steroid hormones, including neurosteroids (PubMed:10588945, PubMed:24491228). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:10588945, PubMed:24491228). Catalyzes the hydroxylation of carbon hydrogen bonds of steroids with a preference for 7-alpha position (PubMed:10588945, PubMed:24491228). Usually metabolizes steroids carrying a hydroxy group at position 3, functioning as a 3-hydroxy steroid 7-alpha hydroxylase (PubMed:24491228). Hydroxylates oxysterols, including 25-hydroxycholesterol and (25R)-cholest-5-ene-3beta,26-diol toward 7-alpha hydroxy derivatives, which may be transported to the liver and converted to bile acids (PubMed:10588945, PubMed:9802883). Via its product 7-alpha,25-dihydroxycholesterol, a ligand for the chemotactic G protein-coupled receptor GPR183/EBI2, regulates B cell migration in germinal centers of lymphoid organs, thus guiding efficient maturation of plasma B cells and overall antigen-specific humoral immune response (By similarity). 7-alpha hydroxylates neurosteroids, including 3beta-hydroxyandrost-5-en-17-one (dehydroepiandrosterone) and pregnenolone, both involved in hippocampus-associated memory and learning (PubMed:24491228). Metabolizes androstanoids toward 6- or 7-alpha hydroxy derivatives (PubMed:24491228). {ECO:0000250|UniProtKB:Q60991, ECO:0000269|PubMed:10588945, ECO:0000269|PubMed:24491228, ECO:0000269|PubMed:9802883}.
|
Homo sapiens (Human)
|
O75882
|
ATRN_HUMAN
|
MVAAAAATEARLRRRTAATAALAGRSGGPHWDWDVTRAGRPGLGAGLRLPRLLSPPLRPRLLLLLLLLSPPLLLLLLPCEAEAAAAAAAVSGSAAAEAKECDRPCVNGGRCNPGTGQCVCPAGWVGEQCQHCGGRFRLTGSSGFVTDGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATECSWDHLYVYDGDSIYAPLVAAFSGLIVPERDGNETVPEVVATSGYALLHFFSDAAYNLTGFNITYSFDMCPNNCSGRGECKISNSSDTVECECSENWKGEACDIPHCTDNCGFPHRGICNSSDVRGCSCFSDWQGPGCSVPVPANQSFWTREEYSNLKLPRASHKAVVNGNIMWVVGGYMFNHSDYNMVLAYDLASREWLPLNRSVNNVVVRYGHSLALYKDKIYMYGGKIDSTGNVTNELRVFHIHNESWVLLTPKAKEQYAVVGHSAHIVTLKNGRVVMLVIFGHCPLYGYISNVQEYDLDKNTWSILHTQGALVQGGYGHSSVYDHRTRALYVHGGYKAFSANKYRLADDLYRYDVDTQMWTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDTSMSHGAKCFSSDFMAYDIACDRWSVLPRPDLHHDVNRFGHSAVLHNSTMYVFGGFNSLLLSDILVFTSEQCDAHRSEAACLAAGPGIRCVWNTGSSQCISWALATDEQEEKLKSECFSKRTLDHDRCDQHTDCYSCTANTNDCHWCNDHCVPRNHSCSEGQISIFRYENCPKDNPMYYCNKKTSCRSCALDQNCQWEPRNQECIALPENICGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQSSQSMSKLTLTPWVGLRKINVSYWCWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCERPANHSAKQCRTPCALRTACGDCTSGSSECMWCSNMKQCVDSNAYVASFPFGQCMEWYTMSTCPPENCSGYCTCSHCLEQPGCGWCTDPSNTGKGKCIEGSYKGPVKMPSQAPTGNFYPQPLLNSSMCLEDSRYNWSFIHCPACQCNGHSKCINQSICEKCENLTTGKHCETCISGFYGDPTNGGKCQPCKCNGHASLCNTNTGKCFCTTKGVKGDECQLCEVENRYQGNPLRGTCYYTLLIDYQFTFSLSQEDDRYYTAINFVATPDEQNRDLDMFINASKNFNLNITWAASFSAGTQAGEEMPVVSKTNIKEYKDSFSNEKFDFRNHPNITFFVYVSNFTWPIKIQIAFSQHSNFMDLVQFFVTFFSCFLSLLLVAAVVWKIKQSCWASRRREQLLREMQQMASRPFASVNVALETDEEPPDLIGGSIKTVPKPIALEPCFGNKAAVLSVFVRLPRGLGGIPPPGQSGLAVASALVDISQQMPIVYKEKSGAVRNRKQQPPAQPGTCI
| null | null |
cerebellum development [GO:0021549]; inflammatory response [GO:0006954]; myelination [GO:0042552]; pigmentation [GO:0043473]; regulation of multicellular organism growth [GO:0040014]
|
extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]; signaling receptor activity [GO:0038023]
|
PF00431;PF01344;PF13964;PF01437;
|
2.120.10.80;2.10.25.10;3.10.100.10;2.60.120.290;
| null |
PTM: Heavily glycosylated. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17261078, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7539799}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:7539799}; Single-pass type I membrane protein {ECO:0000269|PubMed:7539799}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:7539799, ECO:0000269|PubMed:9736737}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:7539799}.
| null | null | null | null | null |
FUNCTION: Involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines. May play a role in melanocortin signaling pathways that regulate energy homeostasis and hair color. Low-affinity receptor for agouti (By similarity). Has a critical role in normal myelination in the central nervous system (By similarity). {ECO:0000250, ECO:0000269|PubMed:9736737}.
|
Homo sapiens (Human)
|
O75884
|
RBBP9_HUMAN
|
MASPSKAVIVPGNGGGDVTTHGWYGWVKKELEKIPGFQCLAKNMPDPITARESIWLPFMETELHCDEKTIIIGHSSGAIAAMRYAETHRVYAIVLVSAYTSDLGDENERASGYFTRPWQWEKIKANCPYIVQFGSTDDPFLPWKEQQEVADRLETKLHKFTDCGHFQNTEFHELITVVKSLLKVPA
|
3.-.-.-
| null |
positive regulation of gene expression [GO:0010628]; response to nematode [GO:0009624]; type II pneumocyte differentiation [GO:0060510]
|
nucleoplasm [GO:0005654]
|
hydrolase activity [GO:0016787]
|
PF06821;
|
3.40.50.1820;
|
RBBP9 family
| null | null | null | null | null | null | null |
FUNCTION: Serine hydrolase whose substrates have not been identified yet (PubMed:19329999, PubMed:20080647). May negatively regulate basal or autocrine TGF-beta signaling by suppressing SMAD2-SMAD3 phosphorylation (PubMed:20080647). May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta through interaction with RB1 and the subsequent displacement of E2F1 (PubMed:9697699). {ECO:0000269|PubMed:19329999, ECO:0000269|PubMed:20080647, ECO:0000269|PubMed:9697699}.
|
Homo sapiens (Human)
|
O75886
|
STAM2_HUMAN
|
MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDKVGSTPNGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRAVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGITFPPAGSQTVSAAAKNGTSSNKNKEDEDIAKAIELSLQEQKQQHTETKSLYPSSEIQLNNKVARKVRALYDFEAVEDNELTFKHGEIIIVLDDSDANWWKGENHRGIGLFPSNFVTTNLNIETEAAAVDKLNVIDDDVEEIKKSEPEPVYIDEDKMDRALQVLQSIDPTDSKPDSQDLLDLEDICQQMGPMIDEKLEEIDRKHSELSELNVKVLEALELYNKLVNEAPVYSVYSKLHPPAHYPPASSGVPMQTYPVQSHGGNYMGQSIHQVTVAQSYSLGPDQIGPLRSLPPNVNSSVTAQPAQTSYLSTGQDTVSNPTYMNQNSNLQSATGTTAYTQQMGMSVDMSSYQNTTSNLPQLAGFPVTVPAHPVAQQHTNYHQQPLL
| null | null |
macroautophagy [GO:0016236]; membrane fission [GO:0090148]; multivesicular body assembly [GO:0036258]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; ESCRT-0 complex [GO:0033565]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]
|
phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]
|
PF00018;PF02809;PF00790;
|
1.20.5.1940;1.25.40.90;2.30.30.40;
|
STAM family
|
PTM: Phosphorylated in response to IL-2, GM-CSF, EGF and PDGF.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane {ECO:0000269|PubMed:12551915}; Peripheral membrane protein {ECO:0000269|PubMed:12551915}; Cytoplasmic side {ECO:0000269|PubMed:12551915}.
| null | null | null | null | null |
FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as a sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75888
|
TNF13_HUMAN
|
MPASSPFLLAPKGPPGNMGGPVREPALSVALWLSWGAALGAVACAMALLTQQTELQSLRREVSRLQGTGGPSQNGEGYPWQSLPEQSSDALEAWENGERSRKRRAVLTQKQKKQHSVLHLVPINATSKDDSDVTEVMWQPALRRGRGLQAQGYGVRIQDAGVYLLYSQVLFQDVTFTMGQVVSREGQGRQETLFRCIRSMPSHPDRAYNSCYSAGVFHLHQGDILSVIIPRARAKLNLSPHGTFLGFVKL
| null | null |
immune response [GO:0006955]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]
|
cytokine activity [GO:0005125]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The precursor is cleaved by furin. {ECO:0000269|PubMed:11571266}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11571266}.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA. Plays a role in the regulation of tumor cell growth. May be involved in monocyte/macrophage-mediated immunological processes. {ECO:0000269|PubMed:10973284}.
|
Homo sapiens (Human)
|
O75891
|
AL1L1_HUMAN
|
MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAASSVLELTEAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRLVEEVKELCDGLELENEDVYMASTFGDFIQLLVRKLRGDDEEGECSIDYVEMAVNKRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTFEY
|
1.5.1.6
| null |
10-formyltetrahydrofolate catabolic process [GO:0009258]; biosynthetic process [GO:0009058]; NADPH regeneration [GO:0006740]; one-carbon metabolic process [GO:0006730]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
aldehyde dehydrogenase (NAD+) activity [GO:0004029]; formyltetrahydrofolate dehydrogenase activity [GO:0016155]
|
PF00171;PF02911;PF00551;PF00550;
|
1.10.1200.10;3.10.25.10;3.40.50.170;
|
GART family; Aldehyde dehydrogenase family, ALDH1L subfamily
|
PTM: Phosphopantetheinylation at Ser-354 by AASDHPPT is required for the formyltetrahydrofolate dehydrogenase activity. {ECO:0000269|PubMed:19933275}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:19933275}.
|
CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + H2O + NADP(+) = (6S)-5,6,7,8-tetrahydrofolate + CO2 + H(+) + NADPH; Xref=Rhea:RHEA:10180, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:195366; EC=1.5.1.6; Evidence={ECO:0000269|PubMed:19933275, ECO:0000269|PubMed:21238436}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10181; Evidence={ECO:0000305|PubMed:19933275};
| null | null | null | null |
FUNCTION: Cytosolic 10-formyltetrahydrofolate dehydrogenase that catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate to tetrahydrofolate and carbon dioxide (PubMed:19933275, PubMed:21238436). May also have an NADP(+)-dependent aldehyde dehydrogenase activity towards formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde (By similarity). {ECO:0000250|UniProtKB:P28037, ECO:0000269|PubMed:19933275, ECO:0000269|PubMed:21238436}.
|
Homo sapiens (Human)
|
O75896
|
TUSC2_HUMAN
|
MGASGSKARGLWPFASAAGGGGSEAAGAEQALVRPRGRAVPPFVFTRRGSMFYDEDGDLAHEFYEETIVTKNGQKRAKLRRVHKNLIPQGIVKLDHPRIHVDFPVILYEV
| null | null |
cell cycle [GO:0007049]; cell maturation [GO:0048469]; inflammatory response [GO:0006954]; natural killer cell differentiation [GO:0001779]; negative regulation of interleukin-17 production [GO:0032700]; neutrophil-mediated killing of gram-negative bacterium [GO:0070945]; phagocytosis [GO:0006909]; positive regulation of interleukin-10 production [GO:0032733]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of reactive oxygen species metabolic process [GO:2000377]
|
mitochondrion [GO:0005739]
| null |
PF15000;
| null |
TUSC2 family
|
PTM: Myristoylation is required for tumor suppressor activity. {ECO:0000269|PubMed:15126327}.
| null | null | null | null | null | null |
FUNCTION: May function as a tumor suppressor, inhibiting colony formation, causing G1 arrest and ultimately inducing apoptosis in homozygous 3p21.3 120-kb region-deficient cells.
|
Homo sapiens (Human)
|
O75897
|
ST1C4_HUMAN
|
MALHDMEDFTFDGTKRLSVNYVKGILQPTDTCDIWDKIWNFQAKPDDLLISTYPKAGTTWTQEIVELIQNEGDVEKSKRAPTHQRFPFLEMKIPSLGSGLEQAHAMPSPRILKTHLPFHLLPPSLLEKNCKIIYVARNPKDNMVSYYHFQRMNKALPAPGTWEEYFETFLAGKVCWGSWHEHVKGWWEAKDKHRILYLFYEDMKKNPKHEIQKLAEFIGKKLDDKVLDKIVHYTSFDVMKQNPMANYSSIPAEIMDHSISPFMRKGAVGDWKKHFTVAQNERFDEDYKKKMTDTRLTFHFQF
|
2.8.2.1
| null |
3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; doxorubicin metabolic process [GO:0044598]; ethanol catabolic process [GO:0006068]; flavonoid metabolic process [GO:0009812]; sulfation [GO:0051923]; xenobiotic metabolic process [GO:0006805]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
aryl sulfotransferase activity [GO:0004062]; sulfotransferase activity [GO:0008146]
|
PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28222028}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; Evidence={ECO:0000269|PubMed:17425406, ECO:0000269|PubMed:26948952, ECO:0000269|PubMed:28222028, ECO:0000269|PubMed:9852044}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165; Evidence={ECO:0000305|PubMed:28222028}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta-estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582; Evidence={ECO:0000269|PubMed:28222028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373; Evidence={ECO:0000305|PubMed:28222028}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + bisphenol A = adenosine 3',5'-bisphosphate + bisphenyl A sulfate + H(+); Xref=Rhea:RHEA:66580, ChEBI:CHEBI:15378, ChEBI:CHEBI:33216, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:167171; Evidence={ECO:0000269|PubMed:28222028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66581; Evidence={ECO:0000305|PubMed:28222028};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for PAPS {ECO:0000269|PubMed:28222028}; KM=36.2 uM for 17beta-estradiol (E2) {ECO:0000269|PubMed:28222028}; KM=3.3 uM for genistein {ECO:0000269|PubMed:28222028}; KM=10.5 uM for daidzein {ECO:0000269|PubMed:28222028}; KM=0.9 uM for apigenin {ECO:0000269|PubMed:28222028}; KM=0.97 uM for chrysin {ECO:0000269|PubMed:28222028}; KM=32.8 uM for bisphenol A {ECO:0000269|PubMed:28222028}; KM=1.1 uM for 1-naphthol {ECO:0000269|PubMed:28222028}; Vmax=5.04 nmol/min/ng enzyme with doxorubicin as substrate {ECO:0000269|PubMed:26948952}; Vmax=1.85 nmol/min/ng enzyme with epirubicin as substrate {ECO:0000269|PubMed:26948952};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:28222028};
| null |
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic compounds. Can also sulfonate estrogenic compounds, however, the dietary flavonoids (phytoestrogen) and environmental estrogens, like bisphenol A are better substrates than 17beta-estradiol (E2) (PubMed:17425406, PubMed:26948952, PubMed:28222028, PubMed:9852044). Mediates the sulfation of doxorubicin and its analog epirubicin, two antitumor anthracyclines (PubMed:26948952). {ECO:0000269|PubMed:17425406, ECO:0000269|PubMed:26948952, ECO:0000269|PubMed:28222028, ECO:0000269|PubMed:9852044}.
|
Homo sapiens (Human)
|
O75899
|
GABR2_HUMAN
|
MASPRSSGQPGPPPPPPPPPARLLLLLLLPLLLPLAPGAWGWARGAPRPPPSSPPLSIMGLMPLTKEVAKGSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFSNDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEPSWWEQVHTEANSSRCLRKNLLAAMEGYIGVDFEPLSSKQIKTISGKTPQQYEREYNNKRSGVGPSKFHGYAYDGIWVIAKTLQRAMETLHASSRHQRIQDFNYTDHTLGRIILNAMNETNFFGVTGQVVFRNGERMGTIKFTQFQDSREVKVGEYNAVADTLEIINDTIRFQGSEPPKDKTIILEQLRKISLPLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSEKTFETLCTVRTWILTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVEKYSMEPDPAGRDISIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNVQFCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNRRFQFTQNQKKEDSKTSTSVTSVNQASTSRLEGLQSENHRLRMKITELDKDLEEVTMQLQDTPEKTTYIKQNHYQELNDILNLGNFTESTDGGKAILKNHLDQNPQLQWNTTEPSRTCKDPIEDINSPEHIQRRLSLQLPILHHAYLPSIGGVDASCVSPCVSPTASPRHRHVPPSFRVMVSGL
| null | null |
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; chemical synaptic transmission [GO:0007268]; G protein-coupled receptor signaling pathway [GO:0007186]; gamma-aminobutyric acid signaling pathway [GO:0007214]; negative regulation of adenylate cyclase activity [GO:0007194]; neuron-glial cell signaling [GO:0150099]; synaptic transmission, GABAergic [GO:0051932]
|
cytoplasm [GO:0005737]; G protein-coupled GABA receptor complex [GO:1902712]; G protein-coupled receptor heterodimeric complex [GO:0038039]; GABA receptor complex [GO:1902710]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]
|
G protein-coupled GABA receptor activity [GO:0004965]; protein heterodimerization activity [GO:0046982]; transmembrane signaling receptor activity [GO:0004888]
|
PF00003;PF01094;PF18455;
|
3.40.50.2300;
|
G-protein coupled receptor 3 family, GABA-B receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10328880, ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:9872316}; Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:O88871}; Multi-pass membrane protein {ECO:0000305}. Note=Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane. In contrast, GABBR2 does not depend on GABBR1 for transport to the cell membrane. {ECO:0000269|PubMed:15617512}.
| null | null | null | null | null |
FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:9872316, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016, PubMed:24305054). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644, PubMed:10773016, PubMed:10906333, PubMed:9872744). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (PubMed:22660477, PubMed:9872744). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644, PubMed:22660477, PubMed:9872316, PubMed:9872744). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). {ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10328880, ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744, ECO:0000305}.
|
Homo sapiens (Human)
|
O75900
|
MMP23_HUMAN
|
MGRGARVPSEAPGAGVERRWLGAALVALCLLPALVLLARLGAPAVPAWSAAQGDVAALGLSAVPPTRVPGPLAPRRRRYTLTPARLRWDHFNLTYRILSFPRNLLSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKALSQDELWGLHRLYGCLDRLFVCASWARRGFCDARRRLMKRLCPSSCDFCYEFPFPTVATTPPPPRTKTRLVPEGRNVTFRCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEAHLSIIANAVNEGTYTCVVRRQQRVLTTYSWRVRVRG
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; reproduction [GO:0000003]
|
collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum membrane [GO:0005789]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]
|
PF00413;PF01549;
|
1.10.10.1940;3.40.390.10;2.60.40.10;
|
Peptidase M10A family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:11328856}.; PTM: Proteolytic cleavage might yield an active form. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:11328856}; Single-pass type II membrane protein {ECO:0000269|PubMed:11328856}. Note=A secreted form produced by proteolytic cleavage may also exist. {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75907
|
DGAT1_HUMAN
|
MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVGSGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPAAVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVSVPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLNYEAPAAEA
|
2.3.1.20; 2.3.1.76
| null |
diacylglycerol metabolic process [GO:0046339]; fatty acid homeostasis [GO:0055089]; lipid storage [GO:0019915]; long-chain fatty-acyl-CoA metabolic process [GO:0035336]; monoacylglycerol biosynthetic process [GO:0006640]; triglyceride biosynthetic process [GO:0019432]; triglyceride metabolic process [GO:0006641]; very-low-density lipoprotein particle assembly [GO:0034379]
|
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]
|
2-acylglycerol O-acyltransferase activity [GO:0003846]; acyltransferase activity [GO:0016746]; diacylglycerol O-acyltransferase activity [GO:0004144]; identical protein binding [GO:0042802]; retinol O-fatty-acyltransferase activity [GO:0050252]
|
PF03062;
| null |
Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z2A7}; Multi-pass membrane protein {ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:16214399, ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869; Evidence={ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76; Evidence={ECO:0000269|PubMed:16214399}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:18768481}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912; Evidence={ECO:0000305|PubMed:18768481}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:18768481, ECO:0000269|PubMed:32433610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220; Evidence={ECO:0000269|PubMed:32433610, ECO:0000305|PubMed:18768481}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence={ECO:0000269|PubMed:16214399}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176; Evidence={ECO:0000305|PubMed:16214399}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:197429; Evidence={ECO:0000269|PubMed:28420705}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341; Evidence={ECO:0000305|PubMed:28420705}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:55344, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:138735, ChEBI:CHEBI:197429; Evidence={ECO:0000269|PubMed:28420705}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345; Evidence={ECO:0000305|PubMed:28420705}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915, ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:28420705}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916; Evidence={ECO:0000305|PubMed:28420705}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:53753; Evidence={ECO:0000269|PubMed:28420705}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38380; Evidence={ECO:0000305|PubMed:28420705}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38307, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75728, ChEBI:CHEBI:75729; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38308; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CATALYTIC ACTIVITY: Reaction=hexadecane-1,2-diol + 2 hexadecanoyl-CoA = 1,2-O,O-dihexadecanoyl-1,2-hexadecanediol + 2 CoA; Xref=Rhea:RHEA:38211, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, ChEBI:CHEBI:75608; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38212; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CATALYTIC ACTIVITY: Reaction=hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl hexadecanoate + CoA; Xref=Rhea:RHEA:38171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, ChEBI:CHEBI:75587; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:73990, ChEBI:CHEBI:75466; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75583; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CATALYTIC ACTIVITY: Reaction=hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl hexadecanoate; Xref=Rhea:RHEA:38167, ChEBI:CHEBI:16125, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75584; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CATALYTIC ACTIVITY: Reaction=13-cis-retinol + hexadecanoyl-CoA = 13-cis-retinyl hexadecanoate + CoA; Xref=Rhea:RHEA:55296, ChEBI:CHEBI:45479, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:138722; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55297; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38435, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75735; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38439, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75824; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440; Evidence={ECO:0000250|UniProtKB:Q9Z2A7};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25.9 uM for retinol {ECO:0000269|PubMed:16214399}; KM=13.9 uM for palmitoyl coenzyme A {ECO:0000269|PubMed:16214399}; KM=14.6 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:32433610}; KM=8.6 uM for octadecanoyl-CoA {ECO:0000269|PubMed:32433610}; KM=6.4 uM for hexadecanoyl-coA {ECO:0000269|PubMed:32433610}; KM=6.2 uM for (9Z)-hexadecenoyl-CoA {ECO:0000269|PubMed:32433610}; KM=597.1 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homodimer) {ECO:0000269|PubMed:32433610}; KM=497.5 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homotetramer) {ECO:0000269|PubMed:32433610}; Vmax=956.6 pmol/min/ug enzyme with (9Z)-octadecenoyl-CoA as substrate {ECO:0000269|PubMed:32433610}; Vmax=839.4 pmol/min/ug enzyme with octadecanoyl-CoA as substrate {ECO:0000269|PubMed:32433610}; Vmax=767.8 pmol/min/ug enzyme with hexadecanoyl-coA as substrate {ECO:0000269|PubMed:32433610}; Vmax=838.6 pmol/min/ug enzyme with (9Z)-hexadecenoyl-CoA as substrate {ECO:0000269|PubMed:32433610}; Vmax=3310 pmol/min/ug enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homodimer) as substrate {ECO:0000269|PubMed:32433610}; Vmax=3628 pmol/min/ug enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homotetramer) as substrate {ECO:0000269|PubMed:32433610};
|
PATHWAY: Lipid metabolism; glycerolipid metabolism.
| null | null |
FUNCTION: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates (PubMed:16214399, PubMed:18768481, PubMed:28420705, PubMed:32433610, PubMed:32433611, PubMed:9756920). Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats (PubMed:18768481). In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage (PubMed:16214399). Also present in female mammary glands, where it produces fat in the milk (By similarity). May be involved in VLDL (very low density lipoprotein) assembly (PubMed:18768481). In contrast to DGAT2 it is not essential for survival (By similarity). Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders (PubMed:16214399). Exhibits additional acyltransferase activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705). {ECO:0000250|UniProtKB:Q8MK44, ECO:0000250|UniProtKB:Q9Z2A7, ECO:0000269|PubMed:16214399, ECO:0000269|PubMed:18768481, ECO:0000269|PubMed:28420705, ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611, ECO:0000269|PubMed:9756920}.
|
Homo sapiens (Human)
|
O75908
|
SOAT2_HUMAN
|
MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQLRELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHFRTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLAPYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFLMKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKNFAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLRLLGARARGVAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQRTGPAWNVLMWTMLFLGQGIQVSLYCQEWYARRHCPLPQATFWGLVTPRSWSCHT
|
2.3.1.26
| null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol storage [GO:0010878]; intestinal cholesterol absorption [GO:0030299]; low-density lipoprotein particle clearance [GO:0034383]; macrophage derived foam cell differentiation [GO:0010742]; very-low-density lipoprotein particle assembly [GO:0034379]
|
brush border [GO:0005903]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
|
acyltransferase activity [GO:0016746]; cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772]
|
PF03062;
| null |
Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily
|
PTM: Polyubiquitinated by AMFR/gp78 at Cys-277, leading to its degradation when the lipid levels are low (PubMed:28604676). Association with AMFR/gp78 is mediated via interaction with INSIG1 (PubMed:28604676). High concentration of cholesterol and fatty acid results in Cys-277 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization (PubMed:28604676). {ECO:0000269|PubMed:28604676}.; PTM: Oxidized at Cys-277: high concentration of cholesterol and fatty acid induce reactive oxygen species, which oxidizes Cys-277, preventing ubiquitination at the same site, and resulting in protein stabilization. {ECO:0000269|PubMed:28604676}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O88908}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA; Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26; Evidence={ECO:0000269|PubMed:16647063, ECO:0000305|PubMed:11294643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817; Evidence={ECO:0000269|PubMed:16647063, ECO:0000305|PubMed:11294643}; CATALYTIC ACTIVITY: Reaction=an acyl-CoA + cholesterol = a cholesterol ester + CoA; Xref=Rhea:RHEA:17729, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence={ECO:0000269|PubMed:16647063, ECO:0000305|PubMed:11294643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730; Evidence={ECO:0000269|PubMed:16647063, ECO:0000305|PubMed:11294643}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-octadecenoate) + CoA; Xref=Rhea:RHEA:41436, ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:11294643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437; Evidence={ECO:0000305|PubMed:11294643}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + cholesterol = (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-cholesterol + CoA; Xref=Rhea:RHEA:46612, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:73862, ChEBI:CHEBI:84969; Evidence={ECO:0000269|PubMed:11294643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46613; Evidence={ECO:0000305|PubMed:11294643}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + cholesterol = (9Z,12Z,15Z-octadecatrienoyl)-cholesterol + CoA; Xref=Rhea:RHEA:46620, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:84341; Evidence={ECO:0000269|PubMed:11294643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46621; Evidence={ECO:0000305|PubMed:11294643}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol = cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA; Xref=Rhea:RHEA:42816, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:82751; Evidence={ECO:0000269|PubMed:11294643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817; Evidence={ECO:0000305|PubMed:11294643};
| null | null | null | null |
FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol (PubMed:11294643, PubMed:16647063). Plays a role in lipoprotein assembly and dietary cholesterol absorption (PubMed:11294643). Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates (PubMed:11294643). May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa (PubMed:11294643). {ECO:0000269|PubMed:11294643, ECO:0000269|PubMed:16647063}.; FUNCTION: [Isoform 2]: Has lower enzymatic activity compared to isoform 1. {ECO:0000269|PubMed:16331323}.; FUNCTION: [Isoform 3]: Has lower enzymatic activity compared to isoform 1. {ECO:0000269|PubMed:16331323}.
|
Homo sapiens (Human)
|
O75909
|
CCNK_HUMAN
|
MKENKENSSPSVTSANLDHTKPCWYWDKKDLAHTPSQLEGLDPATEARYRREGARFIFDVGTRLGLHYDTLATGIIYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFGQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLKYAKQLKGDKNKIQKLVQMAWTFVNDSLCTTLSLQWEPEIIAVAVMYLAGRLCKFEIQEWTSKPMYRRWWEQFVQDVPVDVLEDICHQILDLYSQGKQQMPHHTPHQLQQPPSLQPTPQVPQVQQSQPSQSSEPSQPQQKDPQQPAQQQQPAQQPKKPSPQPSSPRQVKRAVVVSPKEENKAAEPPPPKIPKIETTHPPLPPAHPPPDRKPPLAAALGEAEPPGPVDATDLPKVQIPPPAHPAPVHQPPPLPHRPPPPPPSSYMTGMSTTSSYMSGEGYQSLQSMMKTEGPSYGALPPAYGPPAHLPYHPHVYPPNPPPPPVPPPPASFPPPAIPPPTPGYPPPPPTYNPNFPPPPPRLPPTHAVPPHPPPGLGLPPASYPPPAVPPGGQPPVPPPIPPPGMPPVGGLGRAAWMR
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response [GO:0006974]; negative regulation by host of viral genome replication [GO:0044828]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of signal transduction [GO:0009966]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366]
|
cyclin K-CDK12 complex [GO:0002944]; cyclin K-CDK13 complex [GO:0002945]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase binding [GO:0019901]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]
|
PF00134;PF21797;
|
1.10.472.10;
|
Cyclin family, Cyclin C subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22012619}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). {ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:22012619, ECO:0000269|PubMed:9632813}.
|
Homo sapiens (Human)
|
O75911
|
DHRS3_HUMAN
|
MVWKRLGALVMFPLQMIYLVVKAAVGLVLPAKLRDLSRENVLITGGGRGIGRQLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQTAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHINTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVEAVQLNQALLLLPWTMHALVILKSILPQAALEEIHKFSGTYTCMNTFKGRT
|
1.1.1.300
| null |
bone morphogenesis [GO:0060349]; cardiac septum morphogenesis [GO:0060411]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; outflow tract morphogenesis [GO:0003151]; regulation of ossification [GO:0030278]; regulation of retinoic acid receptor signaling pathway [GO:0048385]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; roof of mouth development [GO:0060021]; visual perception [GO:0007601]
|
endoplasmic reticulum membrane [GO:0005789]; lipid droplet [GO:0005811]; photoreceptor outer segment membrane [GO:0042622]
|
electron transfer activity [GO:0009055]; NAD-retinol dehydrogenase activity [GO:0004745]; NADP-retinol dehydrogenase activity [GO:0052650]; nucleotide binding [GO:0000166]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.300; Evidence={ECO:0000269|PubMed:9705317};
| null | null | null | null |
FUNCTION: Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH. {ECO:0000269|PubMed:9705317}.
|
Homo sapiens (Human)
|
O75912
|
DGKI_HUMAN
|
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAGEEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEEKLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENKGRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQELKFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGERLHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSVPDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDCDLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLHFVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGMIAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV
|
2.7.1.107
| null |
diacylglycerol metabolic process [GO:0046339]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; platelet activation [GO:0030168]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of synaptic transmission, glutamatergic [GO:0051966]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991]; synapse [GO:0045202]; synaptic membrane [GO:0097060]; synaptic vesicle membrane [GO:0030672]
|
ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; metal ion binding [GO:0046872]
|
PF12796;PF00130;PF00609;PF00781;
|
2.60.200.40;3.30.60.20;1.25.40.20;
|
Eukaryotic diacylglycerol kinase family
| null |
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:F1MAB7}. Cell projection, dendrite {ECO:0000250|UniProtKB:F1MAB7}. Presynapse {ECO:0000250|UniProtKB:F1MAB7}. Postsynapse {ECO:0000250|UniProtKB:F1MAB7}. Postsynaptic density {ECO:0000250|UniProtKB:F1MAB7}. Synaptic cell membrane {ECO:0000250|UniProtKB:F1MAB7}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:F1MAB7}. Cytoplasm, cytosol {ECO:0000269|PubMed:9830018}. Nucleus {ECO:0000269|PubMed:9830018}. Note=Excluded from inhibitory synapses (By similarity). Localization between cytoplasm and nucleus is regulated by protein kinase C (PubMed:9830018). Both in the detergent soluble and particulate fractions (By similarity). {ECO:0000250|UniProtKB:F1MAB7, ECO:0000269|PubMed:9830018}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9830018}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000305|PubMed:9830018}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9830018}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000305|PubMed:9830018}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:9830018}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000305|PubMed:9830018}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:F1MAB7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340; Evidence={ECO:0000250|UniProtKB:F1MAB7};
| null |
PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000269|PubMed:9830018}.
| null | null |
FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:23949095, PubMed:9830018). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). Has probably no preference for any of the diacylglycerols in terms of the acyl chain composition, especially for the acyl chain at the sn-2 position (PubMed:9830018). By controlling the diacylglycerol/DAG-mediated activation of RASGRP3, negatively regulates the Rap1 signaling pathway. May play a role in presynaptic diacylglycerol/DAG signaling and control neurotransmitter release during metabotropic glutamate receptor-dependent long-term depression (By similarity). {ECO:0000250|UniProtKB:D3YWQ0, ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9830018, ECO:0000305}.
|
Homo sapiens (Human)
|
O75914
|
PAK3_HUMAN
|
MSDGLDNEEKPPAPPLRMNSNNRDSSALNHSSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLYGSQMCPGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHPSSTKTASEPPLAPPVSEEEDEEEEEEEDENEPPPVIAPRPEHTKSIYTRSVVESIASPAVPNKEVTPPSAENANSSTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
axonogenesis [GO:0007409]; cellular response to organic cyclic compound [GO:0071407]; dendrite development [GO:0016358]; dendritic spine morphogenesis [GO:0060997]; ephrin receptor signaling pathway [GO:0048013]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of actin filament polymerization [GO:0030833]; regulation of axonogenesis [GO:0050770]; regulation of MAPK cascade [GO:0043408]; regulation of postsynapse organization [GO:0099175]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; synapse organization [GO:0050808]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; SH3 domain binding [GO:0017124]; small GTPase binding [GO:0031267]
|
PF00786;PF00069;
|
3.90.810.10;1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Autophosphorylated when activated by CDC42/p21.; PTM: Neddylated. {ECO:0000269|PubMed:20596523}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
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: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as a downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development. In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (By similarity). {ECO:0000250|UniProtKB:Q61036, ECO:0000269|PubMed:21177870}.
|
Homo sapiens (Human)
|
O75915
|
PRAF3_HUMAN
|
MDVNIAPLRAWDDFFPGSDRFARPDFRDISKWNNRVVSNLLYYQTNYLVVAAMMISIVGFLSPFNMILGGIVVVLVFTGFVWAAHNKDVLRRMKKRYPTTFVMVVMLASYFLISMFGGVMVFVFGITFPLLLMFIHASLRLRNLKNKLENKMEGIGLKRTPMGIVLDALEQQEEGINRLTDYISKVKE
| null | null |
cellular response to organic cyclic compound [GO:0071407]; cellular response to oxidative stress [GO:0034599]; glutathione metabolic process [GO:0006749]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; L-glutamate import across plasma membrane [GO:0098712]; L-glutamate transmembrane transport [GO:0015813]; learning or memory [GO:0007611]; negative regulation of L-glutamate import across plasma membrane [GO:0002037]; negative regulation of mitochondrial membrane potential [GO:0010917]; negative regulation of transport [GO:0051051]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein localization to plasma membrane [GO:0072659]; protein transport [GO:0015031]
|
cytoskeleton [GO:0005856]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]; presynaptic cytosol [GO:0099523]
| null |
PF03208;
| null |
PRA1 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ES40}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9ES40}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9ES40}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9ES40}. Note=Also exists as a soluble form in the cytoplasm. Associated with microtubules. {ECO:0000250|UniProtKB:Q9ES40}.
| null | null | null | null | null |
FUNCTION: Regulates intracellular concentrations of taurine and glutamate. Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate in a PKC activity-dependent manner. Plays a role in the retention of SLC1A1/EAAC1 in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8R5J9, ECO:0000250|UniProtKB:Q9ES40}.
|
Homo sapiens (Human)
|
O75916
|
RGS9_HUMAN
|
MTIRHQGQQYRPRMAFLQKIEALVKDMQNPETGVRMQNQRVLVTSVPHAMTGSDVLQWIVQRLWISSLEAQNLGNFIVRYGYIYPLQDPKNLILKPDGSLYRFQTPYFWPTQQWPAEDTDYAIYLAKRNIKKKGILEEYEKENYNFLNQKMNYKWDFVIMQAKEQYRAGKERNKADRYALDCQEKAYWLVHRCPPGMDNVLDYGLDRVTNPNEVKVNQKQTVVAVKKEIMYYQQALMRSTVKSSVSLGGIVKYSEQFSSNDAIMSGCLPSNPWITDDTQFWDLNAKLVEIPTKMRVERWAFNFSELIRDPKGRQSFQYFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKDMLAKAIEPQETTKKSSTLPFMRRHLRSSPSPVILRQLEEEAKAREAANTVDITQPGQHMAPSPHLTVYTGTCMPPSPSSPFSSSCRSPRKPFASPSRFIRRPSTTICPSPIRVALESSSGLEQKGECSGSMAPRGPSVTESSEASLDTSWPRSRPRAPPKARMALSFSRFLRRGCLASPVFARLSPKCPAVSHGRVQPLGDVGQQLPRLKSKRVANFFQIKMDVPTGSGTCLMDSEDAGTGESGDRATEKEVICPWESL
| null | null |
dark adaptation [GO:1990603]; dopamine receptor signaling pathway [GO:0007212]; G protein-coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; light adaption [GO:0036367]; negative regulation of signal transduction [GO:0009968]; nervous system development [GO:0007399]; regulation of calcium ion export across plasma membrane [GO:1905912]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; response to amphetamine [GO:0001975]; response to estradiol [GO:0032355]; visual perception [GO:0007601]
|
cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]
|
GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]
|
PF00610;PF00631;PF00615;PF18148;
|
1.10.1240.60;1.10.167.10;4.10.260.10;1.10.10.10;
| null |
PTM: Retinal isoform 3 is light-dependent phosphorylated at 'Ser-478'. Phosphorylation is decreased by light exposition (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Isoform 3]: Membrane; Peripheral membrane protein. Note=Isoform 3 is targeted to the membrane via its interaction with RGS9BP. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction; key element in the recovery phase of visual transduction (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75920
|
SERF1_HUMAN
|
MARGNQRELARQKNMKKTQEISKGKRKEDSLTASQRKQSSGGQKSESKMSAGPHLPLKAPRENPCFPLPAAGGSRYYLAYGSITPISAFVFVVFFSVFFPSFYEDFCCWI
| null | null |
amyloid fibril formation [GO:1990000]; nervous system development [GO:0007399]; protein destabilization [GO:0031648]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
| null |
PF04419;
| null |
SERF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:31034892}. Nucleus {ECO:0000269|PubMed:31034892}.
| null | null | null | null | null |
FUNCTION: Positive regulator of amyloid protein aggregation and proteotoxicity (PubMed:20723760, PubMed:22854022, PubMed:31034892). Induces conformational changes in amyloid proteins, such as APP, HTT, and SNCA, driving them into compact formations preceding the formation of aggregates (PubMed:20723760, PubMed:22854022, PubMed:31034892). {ECO:0000269|PubMed:20723760, ECO:0000269|PubMed:22854022, ECO:0000269|PubMed:31034892}.
|
Homo sapiens (Human)
|
O75923
|
DYSF_HUMAN
|
MLRVFILYAENVHTPDTDISDAYCSAVFAGVKKRTKVIKNSVNPVWNEGFEWDLKGIPLDQGSELHVVVKDHETMGRNRFLGEAKVPLREVLATPSLSASFNAPLLDTKKQPTGASLVLQVSYTPLPGAVPLFPPPTPLEPSPTLPDLDVVADTGGEEDTEDQGLTGDEAEPFLDQSGGPGAPTTPRKLPSRPPPHYPGIKRKRSAPTSRKLLSDKPQDFQIRVQVIEGRQLPGVNIKPVVKVTAAGQTKRTRIHKGNSPLFNETLFFNLFDSPGELFDEPIFITVVDSRSLRTDALLGEFRMDVGTIYREPRHAYLRKWLLLSDPDDFSAGARGYLKTSLCVLGPGDEAPLERKDPSEDKEDIESNLLRPTGVALRGAHFCLKVFRAEDLPQMDDAVMDNVKQIFGFESNKKNLVDPFVEVSFAGKMLCSKILEKTANPQWNQNITLPAMFPSMCEKMRIRIIDWDRLTHNDIVATTYLSMSKISAPGGEIEEEPAGAVKPSKASDLDDYLGFLPTFGPCYINLYGSPREFTGFPDPYTELNTGKGEGVAYRGRLLLSLETKLVEHSEQKVEDLPADDILRVEKYLRRRKYSLFAAFYSATMLQDVDDAIQFEVSIGNYGNKFDMTCLPLASTTQYSRAVFDGCHYYYLPWGNVKPVVVLSSYWEDISHRIETQNQLLGIADRLEAGLEQVHLALKAQCSTEDVDSLVAQLTDELIAGCSQPLGDIHETPSATHLDQYLYQLRTHHLSQITEAALALKLGHSELPAALEQAEDWLLRLRALAEEPQNSLPDIVIWMLQGDKRVAYQRVPAHQVLFSRRGANYCGKNCGKLQTIFLKYPMEKVPGARMPVQIRVKLWFGLSVDEKEFNQFAEGKLSVFAETYENETKLALVGNWGTTGLTYPKFSDVTGKIKLPKDSFRPSAGWTWAGDWFVCPEKTLLHDMDAGHLSFVEEVFENQTRLPGGQWIYMSDNYTDVNGEKVLPKDDIECPLGWKWEDEEWSTDLNRAVDEQGWEYSITIPPERKPKHWVPAEKMYYTHRRRRWVRLRRRDLSQMEALKRHRQAEAEGEGWEYASLFGWKFHLEYRKTDAFRRRRWRRRMEPLEKTGPAAVFALEGALGGVMDDKSEDSMSVSTLSFGVNRPTISCIFDYGNRYHLRCYMYQARDLAAMDKDSFSDPYAIVSFLHQSQKTVVVKNTLNPTWDQTLIFYEIEIFGEPATVAEQPPSIVVELYDHDTYGADEFMGRCICQPSLERMPRLAWFPLTRGSQPSGELLASFELIQREKPAIHHIPGFEVQETSRILDESEDTDLPYPPPQREANIYMVPQNIKPALQRTAIEILAWGLRNMKSYQLANISSPSLVVECGGQTVQSCVIRNLRKNPNFDICTLFMEVMLPREELYCPPITVKVIDNRQFGRRPVVGQCTIRSLESFLCDPYSAESPSPQGGPDDVSLLSPGEDVLIDIDDKEPLIPIQEEEFIDWWSKFFASIGEREKCGSYLEKDFDTLKVYDTQLENVEAFEGLSDFCNTFKLYRGKTQEETEDPSVIGEFKGLFKIYPLPEDPAIPMPPRQFHQLAAQGPQECLVRIYIVRAFGLQPKDPNGKCDPYIKISIGKKSVSDQDNYIPCTLEPVFGKMFELTCTLPLEKDLKITLYDYDLLSKDEKIGETVVDLENRLLSKFGARCGLPQTYCVSGPNQWRDQLRPSQLLHLFCQQHRVKAPVYRTDRVMFQDKEYSIEEIEAGRIPNPHLGPVEERLALHVLQQQGLVPEHVESRPLYSPLQPDIEQGKLQMWVDLFPKALGRPGPPFNITPRRARRFFLRCIIWNTRDVILDDLSLTGEKMSDIYVKGWMIGFEEHKQKTDVHYRSLGGEGNFNWRFIFPFDYLPAEQVCTIAKKDAFWRLDKTESKIPARVVFQIWDNDKFSFDDFLGSLQLDLNRMPKPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGWWPCVAEEGEKKILAGKLEMTLEIVAESEHEERPAGQGRDEPNMNPKLEDPRRPDTSFLWFTSPYKTMKFILWRRFRWAIILFIILFILLLFLAIFIYAFPNYAAMKLVKPFS
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
|
macrophage activation involved in immune response [GO:0002281]; monocyte activation involved in immune response [GO:0002280]; negative regulation of phagocytosis [GO:0050765]; plasma membrane repair [GO:0001778]; regulation of neurotransmitter secretion [GO:0046928]; T-tubule organization [GO:0033292]; vesicle fusion [GO:0006906]
|
centriolar satellite [GO:0034451]; cytoplasmic vesicle membrane [GO:0030659]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; late endosome [GO:0005770]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; synaptic vesicle membrane [GO:0030672]; T-tubule [GO:0030315]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phospholipid binding [GO:0005543]
|
PF00168;PF08165;PF08150;PF08151;PF16165;
|
2.60.40.150;
|
Ferlin family
| null |
SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single-pass type II membrane protein. Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell membrane. Note=Colocalizes, during muscle differentiation, with BIN1 in the T-tubule system of myotubules and at the site of contact between two myotubes or a myoblast and a myotube. Wounding of myotubes led to its focal enrichment to the site of injury and to its relocalization in a Ca(2+)-dependent manner toward the plasma membrane. Colocalizes with AHNAK, AHNAK2 and PARVB at the sarcolemma of skeletal muscle. Detected on the apical plasma membrane of the syncytiotrophoblast. Reaches the plasmma membrane through a caveolin-independent mechanism. Retained by caveolin at the plasmma membrane (By similarity). Colocalizes, during muscle differentiation, with CACNA1S in the T-tubule system of myotubules (By similarity). Accumulates and colocalizes with fusion vesicles at the sarcolemma disruption sites (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75925
|
PIAS1_HUMAN
|
MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRNYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGTWAPMRSKKEVQEVSASYNGVDGCLSSTLEHQVASHHQSSNKNKKVEVIDLTIDSSSDEEEEEPSAKRTCPSLSPTSPLNNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPTTNGSSSGSNSSLVSSNSLRESHSHTVTNRSSTDTASIFGIIPDIISLD
|
2.3.2.-
| null |
fat cell differentiation [GO:0045444]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of apoptotic process [GO:0043066]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein localization to cell periphery [GO:1904377]; positive regulation of protein sumoylation [GO:0033235]; positive regulation of smooth muscle cell differentiation [GO:0051152]; protein sumoylation [GO:0016925]; protein-DNA complex assembly [GO:0065004]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283]; visual learning [GO:0008542]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nuclear periphery [GO:0034399]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; protein domain specific binding [GO:0019904]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF14324;PF02891;
|
2.60.120.780;1.10.720.30;3.30.40.10;
|
PIAS family
|
PTM: Sumoylated. {ECO:0000269|PubMed:11867732, ECO:0000269|PubMed:12393906}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O88907}. Nucleus speckle {ECO:0000269|PubMed:12393906, ECO:0000269|PubMed:9177271}. Nucleus, PML body {ECO:0000250|UniProtKB:O88907}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11672422}. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton (PubMed:11672422). Interaction with MSX1 is required for localization to the nuclear periphery (By similarity). {ECO:0000250|UniProtKB:O88907, ECO:0000269|PubMed:11672422}.
| null | null |
PATHWAY: Protein modification; protein sumoylation.
| null | null |
FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:21965678, PubMed:36050397). Catalyzes sumoylation of various proteins, such as CEBPB, MRE11, MTA1, PTK2 and PML (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:21965678, PubMed:36050397). Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway (PubMed:11583632, PubMed:11867732). In vitro, binds A/T-rich DNA (PubMed:15133049). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:21965678, PubMed:36050397). Mediates sumoylation of MRE11, stabilizing MRE11 on chromatin during end resection (PubMed:36050397). Sumoylates PML (at 'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation (By similarity). PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (PubMed:21965678). Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity). Mediates the nuclear mobility and localization of MSX1 to the nuclear periphery, whereby MSX1 is brought into the proximity of target myoblast differentiation factor genes (By similarity). Also required for the binding of MSX1 to the core enhancer region in target gene promoter regions, independent of its sumoylation activity (By similarity). Capable of binding to the core enhancer region TAAT box in the MYOD1 gene promoter (By similarity). {ECO:0000250|UniProtKB:O88907, ECO:0000269|PubMed:11583632, ECO:0000269|PubMed:11867732, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:15133049, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:36050397}.; FUNCTION: (Microbial infection) Restricts Epstein-Barr virus (EBV) lytic replication by acting as an inhibitor for transcription factors involved in lytic gene expression (PubMed:29262325). The virus can use apoptotic caspases to antagonize PIAS1-mediated restriction and express its lytic genes (PubMed:29262325). {ECO:0000269|PubMed:29262325}.
|
Homo sapiens (Human)
|
O75928
|
PIAS2_HUMAN
|
MADFEELRNMVSSFRVSELQVLLGFAGRNKSGRKHDLLMRALHLLKSGCSPAVQIKIRELYRRRYPRTLEGLSDLSTIKSSVFSLDGGSSPVEPDLAVAGIHSLPSTSVTPHSPSSPVGSVLLQDTKPTFEMQQPSPPIPPVHPDVQLKNLPFYDVLDVLIKPTSLVQSSIQRFQEKFFIFALTPQQVREICISRDFLPGGRRDYTVQVQLRLCLAETSCPQEDNYPNSLCIKVNGKLFPLPGYAPPPKNGIEQKRPGRPLNITSLVRLSSAVPNQISISWASEIGKNYSMSVYLVRQLTSAMLLQRLKMKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESLILDGLFMEILNDCSDVDEIKFQEDGSWCPMRPKKEAMKVSSQPCTKIESSSVLSKPCSVTVASEASKKKVDVIDLTIESSSDEEEDPPAKRKCIFMSETQSSPTKGVLMYQPSSVRVPSVTSVDPAAIPPSLTDYSVPFHHTPISSMSSDLPGLDFLSLIPVDPQYCPPMFLDSLTSPLTASSTSVTTTSSHESSTHVSSSSSRSETGVITSSGSNIPDIISLD
|
2.3.2.-
| null |
DNA-templated transcription [GO:0006351]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; protein sumoylation [GO:0016925]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
DNA binding [GO:0003677]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription coregulator activity [GO:0003712]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF14324;PF02891;
|
2.60.120.780;1.10.720.30;3.30.40.10;
|
PIAS family
|
PTM: Sumoylated. {ECO:0000269|PubMed:11867732, ECO:0000269|PubMed:12393906}.
|
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q8C5D8}. Nucleus, PML body {ECO:0000269|PubMed:12716907, ECO:0000269|PubMed:22406621}. Nucleus {ECO:0000269|PubMed:11477070, ECO:0000269|PubMed:12393906}. Note=Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs) (PubMed:22406621). Colocalizes with SUMO1 in nuclear granules (By similarity). {ECO:0000250|UniProtKB:Q8C5D8, ECO:0000269|PubMed:22406621}.
| null | null |
PATHWAY: Protein modification; protein sumoylation.
| null | null |
FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys-160'. {ECO:0000269|PubMed:15920481, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:22406621}.
|
Homo sapiens (Human)
|
O75934
|
SPF27_HUMAN
|
MAGTGLVAGEVVVDALPYFDQGYEAPGVREAAAALVEEETRRYRPTKNYLSYLTAPDYSAFETDIMRNEFERLAARQPIELLSMKRYELPAPSSGQKNDITAWQECVNNSMAQLEHQAVRIENLELMSQHGCNAWKVYNENLVHMIEHAQKELQKLRKHIQDLNWQRKNMQLTAGSKLREMESNWVSLVSKNYEIERTIVQLENEIYQIKQQHGEANKENIRQDF
| null | null |
mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]
|
catalytic step 2 spliceosome [GO:0071013]; centrosome [GO:0005813]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; U2-type catalytic step 2 spliceosome [GO:0071007]
| null |
PF05700;
| null |
SPF27 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12169396, ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30705154}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
| null | null | null | null | null |
FUNCTION: Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:30705154). Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). {ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30705154}.
|
Homo sapiens (Human)
|
O75935
|
DCTN3_HUMAN
|
MAGLTDLQRLQARVEELERWVYGPGGARGSRKVADGLVKVQVALGNISSKRERVKILYKKIEDLIKYLDPEYIDRIAIPDASKLQFILAEEQFILSQVALLEQVNALVPMLDSAHIKAVPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAATQVKPAEE
| null | null |
cytoskeleton-dependent cytokinesis [GO:0061640]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]
|
centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; kinetochore [GO:0000776]; midbody [GO:0030496]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]
|
structural molecule activity [GO:0005198]
|
PF07426;
| null |
Dynactin subunit 3 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9722614}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:9722614}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:9722614}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:9722614}. Cleavage furrow {ECO:0000269|PubMed:9722614}. Midbody {ECO:0000269|PubMed:9722614}. Note=Localizes to punctate cytoplasmic structures and to the centrosome during interphase, and to kinetochores and to spindle poles throughout mitosis. Colocalizes with dynein to the cleavage furrow and to midbody of dividing cells.
| null | null | null | null | null |
FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Together with dynein may be involved in spindle assembly and cytokinesis (PubMed:9722614). {ECO:0000250|UniProtKB:F1SEC0, ECO:0000269|PubMed:9722614}.
|
Homo sapiens (Human)
|
O75936
|
BODG_HUMAN
|
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIFDVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVENGN
|
1.14.11.1
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000305}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
|
carnitine biosynthetic process [GO:0045329]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]
|
gamma-butyrobetaine dioxygenase activity [GO:0008336]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; zinc ion binding [GO:0008270]
|
PF06155;PF02668;
|
3.30.2020.30;3.60.130.10;
|
Gamma-BBH/TMLD family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate; Xref=Rhea:RHEA:24028, ChEBI:CHEBI:15379, ChEBI:CHEBI:16244, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17126, ChEBI:CHEBI:30031; EC=1.14.11.1; Evidence={ECO:0000269|PubMed:20599753};
| null |
PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
| null | null |
FUNCTION: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
|
Homo sapiens (Human)
|
O75937
|
DNJC8_HUMAN
|
MAASGESGTSGGGGSTEEAFMTFYSEVKQIEKRDSVLTSKNQIERLTRPGSSYFNLNPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDKAYKLLLDQEQKKRALDVIQAGKEYVEHTVKERKKQLKKEGKPTIVEEDDPELFKQAVYKQTMKLFAELEIKRKEREAKEMHERKRQREEEIEAQEKAKREREWQKNFEESRDGRVDSWRNFQANTKGKKEKKNRTFLRPPKVKMEQRE
| null | null | null |
cytosol [GO:0005829]; intercellular bridge [GO:0045171]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
Hsp70 protein binding [GO:0030544]
|
PF00226;
|
1.10.287.110;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27133716}.
| null | null | null | null | null |
FUNCTION: Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells (PubMed:27133716). {ECO:0000269|PubMed:27133716}.
|
Homo sapiens (Human)
|
O75940
|
SPF30_HUMAN
|
MSEDLAKQLASYKAQLQQVEAALSGNGENEDLLKLKKDLQEVIELTKDLLSTQPSETLASSDSFASTQPTHSWKVGDKCMAVWSEDGQCYEAEIEEIDEENGTAAITFAGYGNAEVTPLLNLKPVEEGRKAKEDSGNKPMSKKEMIAQQREYKKKKALKKAQRIKELEQEREDQKVKWQQFNNRAYSKNKKGQVKRSIFASPESVTGKVGVGTCGIADKPMTQYQDTSKYNVRHLMPQ
| null | null |
apoptotic process [GO:0006915]; mRNA processing [GO:0006397]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing, via transesterification reactions [GO:0000375]
|
Cajal body [GO:0015030]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]
|
RNA binding [GO:0003723]
|
PF06003;
|
2.30.30.140;
|
SMN family
| null |
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11331295, ECO:0000269|PubMed:9817934}. Nucleus, Cajal body {ECO:0000269|PubMed:11331295}. Note=Detected in nuclear speckles containing snRNP and in Cajal (coiled) bodies. {ECO:0000269|PubMed:11331295}.
| null | null | null | null | null |
FUNCTION: Involved in spliceosome assembly. {ECO:0000269|PubMed:11331295, ECO:0000269|PubMed:11331595, ECO:0000269|PubMed:9817934}.
|
Homo sapiens (Human)
|
O75943
|
RAD17_HUMAN
|
MSKTFLRPKVSSTKVTDWVDPSFDDFLECSGVSTITATSLGVNNSSHRRKNGPSTLESSRFPARKRGNLSSLEQIYGLENSKEYLSENEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKQGGSILLITGPPGCGKTTTLKILSKEHGIQVQEWINPVLPDFQKDDFKGMFNTESSFHMFPYQSQIAVFKEFLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLRKYVRIGRCPLIFIISDSLSGDNNQRLLFPKEIQEECSISNISFNPVAPTIMMKFLNRIVTIEANKNGGKITVPDKTSLELLCQGCSGDIRSAINSLQFSSSKGENNLRPRKKGMSLKSDAVLSKSKRRKKPDRVFENQEVQAIGGKDVSLFLFRALGKILYCKRASLTELDSPRLPSHLSEYERDTLLVEPEEVVEMSHMPGDLFNLYLHQNYIDFFMEIDDIVRASEFLSFADILSGDWNTRSLLREYSTSIATRGVMHSNKARGYAHCQGGGSSFRPLHKPQWFLINKKYRENCLAAKALFPDFCLPALCLQTQLLPYLALLTIPMRNQAQISFIQDIGRLPLKRHFGRLKMEALTDREHGMIDPDSGDEAQLNGGHSAEESLGEPTQATVPETWSLPLSQNSASELPASQPQPFSAQGDMEENIIIEDYESDGT
| null | null |
DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA replication checkpoint signaling [GO:0000076]; mitotic DNA replication checkpoint signaling [GO:0033314]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; negative regulation of DNA replication [GO:0008156]; protein localization to site of double-strand break [GO:1990166]; regulation of phosphorylation [GO:0042325]
|
nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Rad17 RFC-like complex [GO:0031389]; site of double-strand break [GO:0035861]
|
ATP binding [GO:0005524]; chromatin binding [GO:0003682]; chromatin-protein adaptor activity [GO:0140463]; DNA clamp loader activity [GO:0003689]
|
PF03215;
|
3.40.50.300;
|
Rad17/RAD24 family
|
PTM: Phosphorylation on Ser-646 and Ser-656 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling (PubMed:11418864, PubMed:14500819, PubMed:14871926). Phosphorylation is mediated by ATR upon UV or replication arrest, whereas it may be mediated both by ATR and ATM upon ionizing radiation (PubMed:11418864, PubMed:11799063). Phosphorylation on both sites is required for interaction with RAD1 but dispensable for interaction with RFC3 or RFC4 (PubMed:11687627). Phosphorylation at Thr-633 by ATM in response to DNA damage promotes interaction with NBN and recruitment of the MRN complex to DNA damage sites (PubMed:24534091). {ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:24534091}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10232579, ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:12400013}. Chromosome {ECO:0000269|PubMed:24534091}. Note=Phosphorylated form redistributes to discrete nuclear foci upon DNA damage (PubMed:11799063). Localizes to DNA double-strand breaks (DSBs) (PubMed:24534091). {ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:24534091}.
| null | null | null | null | null |
FUNCTION: Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage (PubMed:10208430, PubMed:11418864, PubMed:11687627, PubMed:11799063, PubMed:12672690, PubMed:14624239, PubMed:15235112). Has a weak ATPase activity required for binding to chromatin (PubMed:10208430, PubMed:11418864, PubMed:11687627, PubMed:11799063, PubMed:12672690, PubMed:14624239, PubMed:15235112). Participates in the recruitment of the 9-1-1 (RAD1-RAD9-HUS1) complex and RHNO1 onto chromatin, and in CHEK1 activation (PubMed:21659603). Involved in homologous recombination by mediating recruitment of the MRN complex to DNA damage sites (PubMed:24534091). May also serve as a sensor of DNA replication progression (PubMed:12578958, PubMed:14500819, PubMed:15538388). {ECO:0000269|PubMed:10208430, ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:12578958, ECO:0000269|PubMed:12672690, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:14624239, ECO:0000269|PubMed:15235112, ECO:0000269|PubMed:15538388, ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:24534091}.
|
Homo sapiens (Human)
|
O75951
|
LYZL6_HUMAN
|
MTKALLIYLVSSFLALNQASLISRCDLAQVLQLEDLDGFEGYSLSDWLCLAFVESKFNISKINENADGSFDYGLFQINSHYWCNDYKSYSENLCHVDCQDLLNPNLLAGIHCAKRIVSGARGMNNWVEWRLHCSGRPLFYWLTGCRLR
|
3.2.1.17
| null |
defense response to bacterium [GO:0042742]; fertilization [GO:0009566]; fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152]
|
acrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; extracellular region [GO:0005576]; sperm flagellum [GO:0036126]; sperm midpiece [GO:0097225]; sperm plasma membrane [GO:0097524]
|
lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28182716}. Cell surface {ECO:0000269|PubMed:28182716}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9DA11}. Note=Detected on the postacrosomal membrane of mature spermatozoa (PubMed:28182716). {ECO:0000269|PubMed:28182716}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17;
| null | null | null | null |
FUNCTION: May be involved sperm-egg plasma membrane adhesion and fusion during fertilization (PubMed:28182716). Exhibits bacteriolytic activity in vitro against Micrococcus luteus and Staphylococcus aureus (PubMed:24013621, PubMed:28182716). Shows weak bacteriolytic activity against Gram-positive bacteria at physiological pH (PubMed:28182716). Bacteriolytic activity is pH-dependent, with a maximum at around pH 5.6 (PubMed:28182716). {ECO:0000269|PubMed:24013621, ECO:0000269|PubMed:28182716}.
|
Homo sapiens (Human)
|
O75952
|
CABYR_HUMAN
|
MISSKPRLVVPYGLKTLLEGISRAVLKTNPSNINQFAAAYFQELTMYRGNTTMDIKDLVKQFHQIKVEKWSEGTTPQKKLECLKEPGKTSVESKVPTQMEKSTDTDEDNVTRTEYSDKTTQFPSVYAVPGTEQTEAVGGLSSKPATPKTTTPPSSPPPTAVSPEFAYVPADPAQLAAQMLGKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVAAPLVCSGKVLEVQVVNQTSVHVDLGSQPKENEAEPSTASSVPLQDEQEPPAYDQAPEVTLQADIEVMSTVHISSVYNDVPVTEGVVYIEQLPEQIVIPFTDQVACLKENEQSKENEQSPRVSPKSVVEKTTSGMSKKSVESVKLAQLEENAKYSSVYMEAEATALLSDTSLKGQPEVPAQLLDAEGAIKIGSEKSLHLEVEITSIVSDNTGQEESGENSVPQEMEGKPVLSGEAAEAVHSGTSVKSSSGPFPPAPEGLTAPEIEPEGESTAE
| null | null |
epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; sperm capacitation [GO:0048240]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular region [GO:0005576]; motile cilium [GO:0031514]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; sperm fibrous sheath [GO:0035686]; sperm principal piece [GO:0097228]
|
calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; SH3 domain binding [GO:0017124]
|
PF02197;
|
1.20.890.10;
| null |
PTM: Isoform 1 is phosphorylated on tyrosine residues during in vitro capacitation. Isoform 3 and isoform 5 are phosphorylated by GSK3B in vitro. Dephosphorylation affects its ability to bind calcium. {ECO:0000269|PubMed:11820818, ECO:0000269|PubMed:15752768}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, cilium, flagellum. Note=Localized to fibrous sheath including the surface of the longitudinal columns and ribs of the principal piece of sperm flagella.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.; SUBCELLULAR LOCATION: [Isoform 5]: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.
| null | null | null | null | null |
FUNCTION: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Isoform 1 binds calcium in vitro. Isoform 2 and isoform 6 probably bind calcium. Isoform 3 and isoform 5 do not bind calcium in vitro. Isoform 4 probably does not bind calcium.
|
Homo sapiens (Human)
|
O75955
|
FLOT1_HUMAN
|
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILTRLPESVERLTGVSISQVNHKPLRTA
| null | null |
axonogenesis [GO:0007409]; cellular response to exogenous dsRNA [GO:0071360]; dsRNA transport [GO:0033227]; extracellular matrix disassembly [GO:0022617]; plasma membrane raft assembly [GO:0044854]; plasma membrane raft organization [GO:0044857]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell junction assembly [GO:1901890]; positive regulation of cell-cell adhesion mediated by cadherin [GO:2000049]; positive regulation of cytokine production [GO:0001819]; positive regulation of endocytosis [GO:0045807]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of protein binding [GO:0032092]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of skeletal muscle tissue development [GO:0048643]; positive regulation of synaptic transmission, dopaminergic [GO:0032226]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; protein kinase C signaling [GO:0070528]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; regulation of neurotransmitter uptake [GO:0051580]; regulation of receptor internalization [GO:0002090]; regulation of Rho protein signal transduction [GO:0035023]; response to endoplasmic reticulum stress [GO:0034976]
|
adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell-cell contact zone [GO:0044291]; cell-cell junction [GO:0005911]; centriolar satellite [GO:0034451]; cytoplasmic vesicle [GO:0031410]; dopaminergic synapse [GO:0098691]; early endosome [GO:0005769]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; flotillin complex [GO:0016600]; focal adhesion [GO:0005925]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; microtubule organizing center [GO:0005815]; plasma membrane [GO:0005886]; presynaptic active zone [GO:0048786]; sarcolemma [GO:0042383]; uropod [GO:0001931]
|
ionotropic glutamate receptor binding [GO:0035255]; protease binding [GO:0002020]
|
PF01145;
|
3.30.479.30;
|
Band 7/mec-2 family, Flotillin subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:20682791}. Endosome {ECO:0000269|PubMed:20682791}. Membrane, caveola {ECO:0000250|UniProtKB:O08917}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08917}. Melanosome {ECO:0000269|PubMed:17081065}. Membrane raft {ECO:0000269|PubMed:25893292}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Membrane-associated protein of caveola (By similarity). {ECO:0000250|UniProtKB:O08917, ECO:0000269|PubMed:17081065}.
| null | null | null | null | null |
FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
|
Homo sapiens (Human)
|
O75956
|
CDKA2_HUMAN
|
MSYKPIAPAPSSTPGSSTPGPGTPVPTGSVPSPSGSVPGAGAPFRPLFNDFGPPSMGYVQAMKPPGAQGSQSTYTDLLSVIEEMGKEIRPTYAGSKSAMERLKRGIIHARALVRECLAETERNART
| null | null |
negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of stem cell division [GO:2000035]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; NuRD complex [GO:0016581]
| null |
PF09806;
|
6.10.140.1300;
|
CDK2AP family
|
PTM: Phosphorylated by MAPK1 and CDK2. {ECO:0000250|UniProtKB:Q9CPY4}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10082655}. Nucleus {ECO:0000269|PubMed:10082655, ECO:0000269|PubMed:33283408}. Note=Accumulates in immature oocytes in the nucleus. During the first meiotic division, accumulates in the cytoplasm and localizes in dots in the vicinity of the chromosomes in a region enriched in microtubules. {ECO:0000250|UniProtKB:Q9CPY4}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:33283408). Inhibits cell cycle G1/S phase transition by repressing CDK2 expression and activation; represses CDK2 activation by inhibiting its interaction with cyclin E and A (PubMed:23781148). Plays a role in regulating the self-renewal of embryonic stem cells (ESCs) and in maintaining cell survival during terminal differentiation of ESCs (By similarity). Regulates microtubule organization of metaphase II oocytes (By similarity). {ECO:0000250|UniProtKB:Q9CPY4, ECO:0000269|PubMed:23781148, ECO:0000269|PubMed:33283408}.
|
Homo sapiens (Human)
|
O75962
|
TRIO_HUMAN
|
MSGSSGGAAAPAASSGPAAAASAAGSGCGGGAGEGAEEAAKDLADIAAFFRSGFRKNDEMKAMDVLPILKEKVAYLSGGRDKRGGPILTFPARSNHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDSIKPLLKILQESFPCCIHVALIIKPDNFWQKQRTNFGSSKFEFETNMVSLEGLTKVVDPSQLTPEFDGCLEYNHEEWIEIRVAFEDYISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKKKVIKAPIEDLDLEGQKLLQRIQSSESFPKKNSGSGNADLQNLLPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWITHNKGLFLNSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIRQIASQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKYMSNVDSWCKACGEVDLPSELQDLEDAIHHHQGIYEHITLAYSEVSQDGKSLLDKLQRPLTPGSSDSLTASANYSKAVHHVLDVIHEVLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAHQLEDRIQDFVRRVEQRKILLDMSVSFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFGQQQQTTLQVTVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLELFLQLRIFERDAIDIISDLESWNDELSQQMNDFDTEDLTIAEQRLQHHADKALTMNNLTFDVIHQGQDLLQYVNEVQASGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYKREEDWCGGADKLGPNSETDHVTPMISKHLEQKEAFLKACTLARRNADVFLKYLHRNSVNMPGMVTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQCQQYVVFERSAKQALEWIHDNGEFYLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVTAVDKRYRDFSLRMEKYRTSLEKALGISSDSNKSSKSLQLDIIPASIPGSEVKLRDAAHELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNKELIIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLILEHAGSYFDEIQQRHGLANSISSYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVMLSVPKRANDAMHLSMLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGDPCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERTIHLKGALKEPIHIPKTAPATRQKGRRDGEDLDSQGDGSSQPDTISIASRTSQNTLDSDKLSGGCELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTTDRSPAAEGLVPCGSLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQPHMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHVKKLAHKHKKSREVRKSADAGSQKDSDDSAATPQDETVEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPPPMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLSSSSPIDEMEERKSSSLKRRHYVLQELVETERDYVRDLGYVVEGYMALMKEDGVPDDMKGKDKIVFGNIHQIYDWHRDFFLGELEKCLEDPEKLGSLFVKHERRLHMYIAYCQNKPKSEHIVSEYIDTFFEDLKQRLGHRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKASLDTSELERAVEVMCIVPRRCNDMMNVGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEENVENDPCKFALTSRTGDVVETFILHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEYQRNHSGGGGGGGSGGSGGGGGSGGGGAPSGGSGHSGGPSSCGGAPSTSRSRPSRIPQPVRHHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAAPEAGPSAPSRRPPGADAEGSEREAEPIPKMKVLESPRKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPSSPLQKGGSFWSSIPASPASRPGSFTFPGDSDSLQRQTPRHAAPGKDTDRMSTCSSASEQSVQSTQSNGSESSSSSNISTMLVTHDYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGHTSAVIVENPDGTLKKSTSWHTALRLRKKSEKKDKDGKREGKLENGYRKSREGLSNKVSVKLLNPNYIYDVPPEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSASLRVLGPGMDGIMVTWKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGRSTGVLDTSRLTSFIERRKHQNDVRPIRSIKNFLQSRLLPRV
|
2.7.11.1
| null |
axon guidance [GO:0007411]; negative regulation of fat cell differentiation [GO:0045599]; neuron projection morphogenesis [GO:0048812]; phosphorylation [GO:0016310]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; regulation of small GTPase mediated signal transduction [GO:0051056]; transmembrane receptor protein tyrosine phosphatase signaling pathway [GO:0007185]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; glutamatergic synapse [GO:0098978]; postsynapse [GO:0098794]; presynaptic active zone [GO:0048786]
|
ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF13716;PF07679;PF00169;PF00069;PF00621;PF16609;PF00018;PF00435;
|
1.20.58.60;3.40.525.10;1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
|
PTM: Phosphorylated on serine residue(s).
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22155786}. Cell projection {ECO:0000250|UniProtKB:Q0KL02}.
|
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: Guanine nucleotide exchange factor (GEF) for RHOA and RAC1 GTPases (PubMed:22155786, PubMed:27418539, PubMed:8643598). Involved in coordinating actin remodeling, which is necessary for cell migration and growth (PubMed:10341202, PubMed:22155786). Plays a key role in the regulation of neurite outgrowth and lamellipodia formation (PubMed:32109419). In developing hippocampal neurons, limits dendrite formation, without affecting the establishment of axon polarity. Once dendrites are formed, involved in the control of synaptic function by regulating the endocytosis of AMPA-selective glutamate receptors (AMPARs) at CA1 excitatory synapses (By similarity). May act as a regulator of adipogenesis (By similarity). {ECO:0000250|UniProtKB:F1M0Z1, ECO:0000269|PubMed:10341202, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:27418539, ECO:0000269|PubMed:32109419, ECO:0000269|PubMed:8643598}.
|
Homo sapiens (Human)
|
O75969
|
AKAP3_HUMAN
|
MSEKVDWLQSQNGVCKVDVYSPGDNQAQDWKMDTSTDPVRVLSWLRRDLEKSTAEFQDVRFKPGESFGGETSNSGDPHKGFSVDYYNTTTKGTPERLHFEMTHKEIPCQGPRAQLGNGSSVDEVSFYANRLTNLVIAMARKEINEKIDGSENKCVYQSLYMGNEPTPTKSLSKIASELVNETVSACSRNAAPDKAPGSGDRVSGSSQSPPNLKYKSTLKIKESTKERQGPDDKPPSKKSFFYKEVFESRNGDYAREGGRFFPRERKRFRGQERPDDFTASVSEGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKKVLLKHAKEVVSDLIDSFLRNLHSVTGTLMTDTQFVSAVKRTVFSHGSQKATDIMDAMLRKLYNVMFAKKVPEHVRKAQDKAESYSLISMKGMGDPKNRNVNFAMKSETKLREKMYSEPKSEEETCAKTLGEHIIKEGLTLWHKTQQKECKSLGFQHAAFEAPNTQRKPASDISFEYPEDIGNLSLPPYPPEKPENFMYDSDSWAEDLIVSALLLIQYHLAQGGRRDARSFVEAAGTTNFPANEPPVAPDESCLKSAPIVGDQEQAEKKDLRSVFFNFIRNLLSETIFKRDQSPEPKVPEQPVKEDRKLCERPLASSPPRLYEDDETPGALSGLTKMAVSQIDGHMSGQMVEHLMNSVMKLCVIIAKSCDASLAELGDDKSGDASRLTSAFPDSLYECLPAKGTGSAEAVLQNAYQAIHNEMRGTSGQPPEGCAAPTVIVSNHNLTDTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSAAAVDKGCSVGEVLQSVLRYEKERQLNEAVGNVTPLQLLDWLMVNL
| null | null |
acrosome reaction [GO:0007340]; blastocyst hatching [GO:0001835]; protein localization [GO:0008104]; single fertilization [GO:0007338]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]
|
acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; sperm fibrous sheath [GO:0035686]; sperm midpiece [GO:0097225]; sperm principal piece [GO:0097228]
|
protein kinase A binding [GO:0051018]
|
PF05716;
| null |
AKAP110 family
|
PTM: Phosphorylated on tyrosine residues.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:O88987}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:O88987}. Note=Dorsal margin of the acrosomal segment. Ribs of the fibrous sheath in the principal piece of the sperm tail. {ECO:0000250|UniProtKB:O88987}.
| null | null | null | null | null |
FUNCTION: Has a role in the maintenance of acrosome structure (PubMed:35228300). May function as a regulator of both spermatozoa motility and head-associated functions such as capacitation and the acrosome reaction. {ECO:0000269|PubMed:35228300}.
|
Homo sapiens (Human)
|
O75970
|
MPDZ_HUMAN
|
MLEAIDKNRALHAAERLQTKLRERGDVANEDKLSLLKSVLQSPLFSQILSLQTSVQQLKDQVNIATSATSNIEYAHVPHLSPAVIPTLQNESFLLSPNNGNLEALTGPGIPHINGKPACDEFDQLIKNMAQGRHVEVFELLKPPSGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQALDQTITHQQAISILQKAKDTVQLVIARGSLPQLVSPIVSRSPSAASTISAHSNPVHWQHMETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQVLRQCGNRVKLMIARGAIEERTAPTALGITLSSSPTSTPELRVDASTQKGEESETFDVELTKNVQGLGITIAGYIGDKKLEPSGIFVKSITKSSAVEHDGRIQIGDQIIAVDGTNLQGFTNQQAVEVLRHTGQTVLLTLMRRGMKQEAELMSREDVTKDADLSPVNASIIKENYEKDEDFLSSTRNTNILPTEEEGYPLLSAEIEEIEDAQKQEAALLTKWQRIMGINYEIVVAHVSKFSENSGLGISLEATVGHHFIRSVLPEGPVGHSGKLFSGDELLEVNGITLLGENHQDVVNILKELPIEVTMVCCRRTVPPTTQSELDSLDLCDIELTEKPHVDLGEFIGSSETEDPVLAMTDAGQSTEEVQAPLAMWEAGIQHIELEKGSKGLGFSILDYQDPIDPASTVIIIRSLVPGGIAEKDGRLLPGDRLMFVNDVNLENSSLEEAVEALKGAPSGTVRIGVAKPLPLSPEEGYVSAKEDSFLYPPHSCEEAGLADKPLFRADLALVGTNDADLVDESTFESPYSPENDSIYSTQASILSLHGSSCGDGLNYGSSLPSSPPKDVIENSCDPVLDLHMSLEELYTQNLLQRQDENTPSVDISMGPASGFTINDYTPANAIEQQYECENTIVWTESHLPSEVISSAELPSVLPDSAGKGSEYLLEQSSLACNAECVMLQNVSKESFERTINIAKGNSSLGMTVSANKDGLGMIVRSIIHGGAISRDGRIAIGDCILSINEESTISVTNAQARAMLRRHSLIGPDIKITYVPAEHLEEFKISLGQQSGRVMALDIFSSYTGRDIPELPEREEGEGEESELQNTAYSNWNQPRRVELWREPSKSLGISIVGGRGMGSRLSNGEVMRGIFIKHVLEDSPAGKNGTLKPGDRIVEVDGMDLRDASHEQAVEAIRKAGNPVVFMVQSIINRPRKSPLPSLLHNLYPKYNFSSTNPFADSLQINADKAPSQSESEPEKAPLCSVPPPPPSAFAEMGSDHTQSSASKISQDVDKEDEFGYSWKNIRERYGTLTGELHMIELEKGHSGLGLSLAGNKDRSRMSVFIVGIDPNGAAGKDGRLQIADELLEINGQILYGRSHQNASSIIKCAPSKVKIIFIRNKDAVNQMAVCPGNAVEPLPSNSENLQNKETEPTVTTSDAAVDLSSFKNVQHLELPKDQGGLGIAISEEDTLSGVIIKSLTEHGVAATDGRLKVGDQILAVDDEIVVGYPIEKFISLLKTAKMTVKLTIHAENPDSQAVPSAAGAASGEKKNSSQSLMVPQSGSPEPESIRNTSRSSTPAIFASDPATCPIIPGCETTIEISKGRTGLGLSIVGGSDTLLGAIIIHEVYEEGAACKDGRLWAGDQILEVNGIDLRKATHDEAINVLRQTPQRVRLTLYRDEAPYKEEEVCDTLTIELQKKPGKGLGLSIVGKRNDTGVFVSDIVKGGIADADGRLMQGDQILMVNGEDVRNATQEAVAALLKCSLGTVTLEVGRIKAGPFHSERRPSQSSQVSEGSLSSFTFPLSGSSTSESLESSSKKNALASEIQGLRTVEMKKGPTDSLGISIAGGVGSPLGDVPIFIAMMHPTGVAAQTQKLRVGDRIVTICGTSTEGMTHTQAVNLLKNASGSIEMQVVAGGDVSVVTGHQQEPASSSLSFTGLTSSSIFQDDLGPPQCKSITLERGPDGLGFSIVGGYGSPHGDLPIYVKTVFAKGAASEDGRLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTLMVLS
| null | null |
microtubule organizing center organization [GO:0031023]; regulation of microtubule cytoskeleton organization [GO:0070507]; tight junction assembly [GO:0120192]
|
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
| null |
PF09045;PF16667;PF00595;
|
2.30.42.10;1.10.287.650;
| null | null |
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Postsynaptic density. Cell projection, dendrite. Cell junction, tight junction. Synapse. Synapse, synaptosome. Note=Colocalizes with HTR2C on the apical membrane of epithelial choroid plexus cells (By similarity). Highly enriched in postsynaptic densities (PSD). Localized to punctae on dendrites of hippocampal neurons and colocalizes with the synaptic marker DLG4. Localized mainly in the Schmidt-Lanterman incisures of myelinating Schwann cells (By similarity). In the retina, localizes to the sub-apical region adjacent to the adherens junction complex at the outer limiting membrane. Enriched at the tight junctions of epithelial cells. Association to the tight junctions depends on CXADR. {ECO:0000250, ECO:0000250|UniProtKB:O55164}.
| null | null | null | null | null |
FUNCTION: Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses (PubMed:11150294, PubMed:15312654). Promotes clustering of HT2RC at the cell surface (By similarity). {ECO:0000250|UniProtKB:O55164, ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:15312654}.
|
Homo sapiens (Human)
|
O75971
|
SNPC5_HUMAN
|
MLSRLQELRKEEETLLRLKAALHDQLNRLKVEELALQSMISSRRGDEMLSSHTVPEQSHDMLVHVDNEASINQTTLELSTKSHVTEEEEEEEEEESDS
| null | null |
snRNA transcription by RNA polymerase II [GO:0042795]; snRNA transcription by RNA polymerase III [GO:0042796]; transcription initiation at RNA polymerase III promoter [GO:0006384]
|
nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
RNA polymerase II general transcription initiation factor activity [GO:0016251]; RNA polymerase III general transcription initiation factor activity [GO:0000995]
|
PF15497;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.
|
Homo sapiens (Human)
|
O75976
|
CBPD_HUMAN
|
MASGRDERPPWRLGRLLLLMCLLLLGSSARAAHIKKAEATTTTTSAGAEAAEGQFDRYYHEEELESALREAAAAGLPGLARLFSIGRSVEGRPLWVLRLTAGLGSLIPEGDAGPDAAGPDAAGPLLPGRPQVKLVGNMHGDETVSRQVLIYLARELAAGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGFGDGGPSGASGRDNSRGRDLNRSFPDQFSTGEPPALDEVPEVRALIEWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKATGIYSKTSDDEVFKYLAKAYASNHPIMKTGEPHCPGDEDETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPASQLRQEWENNRESLITLIEKVHIGVKGFVKDSITGSGLENATISVAGINHNITTGRFGDFYRLLVPGTYNLTVVLTGYMPLTVTNVVVKEGPATEVDFSLRPTVTSVIPDTTEAVSTASTVAIPNILSGTSSSYQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVHNTRIHLMPSMNPDGYEKSQEGDSISVIGRNNSNNFDLNRNFPDQFVQITDPTQPETIAVMSWMKSYPFVLSANLHGGSLVVNYPFDDDEQGLATYSKSPDDAVFQQIALSYSKENSQMFQGRPCKNMYPNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPLEKELPNFWEQNRRSLIQFMKQVHQGVRGFVLDATDGRGILNATISVAEINHPVTTYKTGDYWRLLVPGTYKITASARGYNPVTKNVTVKSEGAIQVNFTLVRSSTDSNNESKKGKGASSSTNDASDPTTKEFETLIKDLSAENGLESLMLRSSSNLALALYRYHSYKDLSEFLRGLVMNYPHITNLTNLGQSTEYRHIWSLEISNKPNVSEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKKNPAVTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKIGQTNARGKDLDTDFTNNASQPETKAIIENLIQKQDFSLSVALDGGSMLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSCPNKSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAARLPSLWADNKRSLLSMLVEVHKGVHGFVKDKTGKPISKAVIVLNEGIKVQTKEGGYFHVLLAPGVHNIIAIADGYQQQHSQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIWCICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH
|
3.4.17.22
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q90240}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q90240};
|
peptide metabolic process [GO:0006518]; protein processing [GO:0016485]
|
extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
metallocarboxypeptidase activity [GO:0004181]; serine-type carboxypeptidase activity [GO:0004185]; zinc ion binding [GO:0008270]
|
PF13620;PF00246;
|
2.60.40.1120;3.40.630.10;
|
Peptidase M14 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Releases C-terminal Arg and Lys from polypeptides.; EC=3.4.17.22;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.5.;
| null | null |
Homo sapiens (Human)
|
O75995
|
SASH3_HUMAN
|
MLRRKPSNASEKEPTQKKKLSLQRSSSFKDFAKSKPSSPVVSEKEFNLDDNIPEDDSGVPTPEDAGKSGKKLGKKWRAVISRTMNRKMGKMMVKALSEEMADTLEEGSASPTSPDYSLDSPGPEKMALAFSEQEEHELPVLSRQASTGSELCSPSPGSGSFGEEPPAPQYTGPFCGRARVHTDFTPSPYDHDSLKLQKGDVIQIIEKPPVGTWLGLLNGKVGSFKFIYVDVLPEEAVGHARPSRRQSKGKRPKPKTLHELLERIGLEEHTSTLLLNGYQTLEDFKELRETHLNELNIMDPQHRAKLLTAAELLLDYDTGSEEAEEGAESSQEPVAHTVSEPKVDIPRDSGCFEGSESGRDDAELAGTEEQLQGLSLAGAP
| null | null |
B cell homeostasis [GO:0001782]; B cell proliferation [GO:0042100]; CD4-positive, alpha-beta T cell differentiation [GO:0043367]; homeostasis of number of cells within a tissue [GO:0048873]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of CD4-positive, alpha-beta T cell differentiation [GO:0043372]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of organ growth [GO:0046622]; positive regulation of T cell cytokine production [GO:0002726]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; T cell proliferation [GO:0042098]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
| null |
PF00536;PF07653;PF12485;
|
2.30.30.40;1.10.150.50;
| null | null | null | null | null | null | null | null |
FUNCTION: May function as a signaling adapter protein in lymphocytes. {ECO:0000250|UniProtKB:Q8K352}.
|
Homo sapiens (Human)
|
O76003
|
GLRX3_HUMAN
|
MAAGAAEAAVAAVEEVGSAGQFEELLRLKAKSLLVVHFWAPWAPQCAQMNEVMAELAKELPQVSFVKLEAEGVPEVSEKYEISSVPTFLFFKNSQKIDRLDGAHAPELTKKVQRHASSGSFLPSANEHLKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKAYSSWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIVKELKENGELLPILRGEN
| null | null |
[2Fe-2S] cluster assembly [GO:0044571]; cell redox homeostasis [GO:0045454]; intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; protein maturation by iron-sulfur cluster transfer [GO:0097428]; regulation of the force of heart contraction [GO:0002026]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; iron-sulfur cluster assembly complex [GO:1990229]; nucleus [GO:0005634]; Z disc [GO:0030018]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein kinase C binding [GO:0005080]; RNA binding [GO:0003723]
|
PF00462;PF00085;
|
3.40.30.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:27519415}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10636891}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q9CQM9}. Note=Under the plasma membrane (By similarity). After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area (By similarity). In the Z line, found associated with CSRP3 (By similarity). {ECO:0000250|UniProtKB:Q9CQM9}.
| null | null | null | null | null |
FUNCTION: Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins (PubMed:26613676, PubMed:27519415). Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Required for hemoglobin maturation (PubMed:23615448). Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. {ECO:0000250|UniProtKB:Q9CQM9, ECO:0000269|PubMed:23615448, ECO:0000269|PubMed:26613676, ECO:0000269|PubMed:27519415}.
|
Homo sapiens (Human)
|
O76011
|
KRT34_HUMAN
|
MSYSCCLPSLGCRTSCSSRPCVPPSCHGYTLPGACNIPANVSNCNWFCEGSFNGSEKETMQFLNDRLASYLEKVRQLERDNAELEKLIQERSQQQEPLLCPSYQSYFKTIEELQQKILCAKAENARLVVNIDNAKLASDDFRSKYQTEQSLRLLVESDINSIRRILDELTLCKSDLESQVESLREELICLKKNHEEEVNTLRSQLGDRLNVEVDTAPTVDLNQVLNETRSQYEALVEINRREVEQWFATQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEAHYSSQLSQVQSLITNVESQLAEIRCDLERQNQEYQVLLDVRARLECEINTYRSLLESEDCKLPCNPCATTNASGNSCGPCGTSQKGCCN
| null | null |
epidermis development [GO:0008544]; epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]
|
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular space [GO:0005615]; intermediate filament [GO:0005882]
|
structural molecule activity [GO:0005198]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O76013
|
KRT36_HUMAN
|
MATQTCTPTFSTGSIKGLCGTAGGISRVSSIRSVGSCRVPSLAGAAGYISSARSGLSGLGSCLPGSYLSSECHTSGFVGSGGWFCEGSFNGSEKETMQFLNDRLANYLEKVRQLERENAELESRIQEWYEFQIPYICPDYQSYFKTIEDFQQKILLTKSENARLVLQIDNAKLAADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELMCLKKNHEEEVSVLRCQLGDRLNVEVDAAPPVDLNKILEDMRCQYEALVENNRRDVEAWFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAETEARYSSQLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEIATYRHLLEGEDCKLPPQPCATACKPVIRVPSVPPVPCVPSVPCTPAPQVGTQIRTITEEIRDGKVISSREHVQSRPL
| null | null |
epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; regulation of keratinocyte differentiation [GO:0045616]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament cytoskeleton [GO:0045111]; keratin filament [GO:0045095]
|
structural constituent of skin epidermis [GO:0030280]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O76014
|
KRT37_HUMAN
|
MTSFYSTSSCPLGCTMAPGARNVFVSPIDVGCQPVAEANAASMCLLANVAHANRVRVGSTPLGRPSLCLPPTSHTACPLPGTCHIPGNIGICGAYGKNTLNGHEKETMKFLNDRLANYLEKVRQLEQENAELETTLLERSKCHESTVCPDYQSYFRTIEELQQKILCSKAENARLIVQIDNAKLAADDFRIKLESERSLHQLVEADKCGTQKLLDDATLAKADLEAQQESLKEEQLSLKSNHEQEVKILRSQLGEKFRIELDIEPTIDLNRVLGEMRAQYEAMVETNHQDVEQWFQAQSEGISLQAMSCSEELQCCQSEILELRCTVNALEVERQAQHTLKDCLQNSLCEAEDRYGTELAQMQSLISNLEEQLSEIRADLERQNQEYQVLLDVKARLENEIATYRNLLESEDCKLPCNPCSTPASCTSCPSCGPVTGGSPSGHGASMGR
| null | null |
epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]
|
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]
|
structural molecule activity [GO:0005198]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O76015
|
KRT38_HUMAN
|
MTSSYSSSSCPLGCTMAPGARNVSVSPIDIGCQPGAEANIAPMCLLANVAHANRVRVGSTPLGRPSLCLPPTCHTACPLPGTCHIPGNIGICGAYGENTLNGHEKETMQFLNDRLANYLEKVRQLEQENAELEATLLERSKCHESTVCPDYQSYFHTIEELQQKILCSKAENARLIVQIDNAKLAADDFRIKLESERSLRQLVEADKCGTQKLLDDATLAKADLEAQQESLKEEQLSLKSNHEQEVKILRSQLGEKLRIELDIEPTIDLNRVLGEMRAQYEAMLETNRQDVEQWFQAQSEGISLQDMSCSEELQCCQSEILELRCTVNALEVERQAQHTLKDCLQNSLCEAEDRFGTELAQMQSLISNVEEQLSEIRADLERQNQEYQVLLDVKTRLENEIATYRNLLESEDCKLPCNPCSTSPSCVTAPCAPRPSCGPCTTCGPTCGASTTGSRF
| null | null |
epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]
|
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]
|
structural molecule activity [GO:0005198]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O76021
|
RL1D1_HUMAN
|
MEDSASASLSSAAATGTSTSTPAAPTARKQLDKEQVRKAVDALLTHCKSRKNNYGLLLNENESLFLMVVLWKIPSKELRVRLTLPHSIRSDSEDICLFTKDEPNSTPEKTEQFYRKLLNKHGIKTVSQIISLQTLKKEYKSYEAKLRLLSSFDFFLTDARIRRLLPSLIGRHFYQRKKVPVSVNLLSKNLSREINDCIGGTVLNISKSGSCSAIRIGHVGMQIEHIIENIVAVTKGLSEKLPEKWESVKLLFVKTEKSAALPIFSSFVSNWDEATKRSLLNKKKKEARRKRRERNFEKQKERKKKRQQARKTASVLSKDDVAPESGDTTVKKPESKKEQTPEHGKKKRGRGKAQVKATNESEDEIPQLVPIGKKTPANEKVEIQKHATGKKSPAKSPNPSTPRGKKRKALPASETPKAAESETPGKSPEKKPKIKEEAVKEKSPSLGKKDARQTPKKPEAKFFTTPSKSVRKASHTPKKWPKKPKVPQST
| null | null |
maturation of LSU-rRNA [GO:0000470]; osteoblast differentiation [GO:0001649]; regulation of apoptotic process [GO:0042981]; regulation of cellular senescence [GO:2000772]; regulation of protein localization [GO:0032880]
|
90S preribosome [GO:0030686]; chromosome [GO:0005694]; cytosolic large ribosomal subunit [GO:0022625]; membrane [GO:0016020]; nucleolus [GO:0005730]
|
cadherin binding [GO:0045296]; mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; RNA binding [GO:0003723]
|
PF00687;
|
3.30.190.20;3.40.50.790;
|
Universal ribosomal protein uL1 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:22419112}. Note=Colocalizes with ING1 in the nucleolus after UV stress. {ECO:0000269|PubMed:22419112}.
| null | null | null | null | null |
FUNCTION: Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage. {ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:22419112}.
|
Homo sapiens (Human)
|
O76024
|
WFS1_HUMAN
|
MDSNTAPLGPSCPQPPPAPQPQARSRLNATASLEQERSERPRAPGPQAGPGPGVRDAAAPAEPQAQHTRSRERADGTGPTKGDMEIPFEEVLERAKAGDPKAQTEVGKHYLQLAGDTDEELNSCTAVDWLVLAAKQGRREAVKLLRRCLADRRGITSENEREVRQLSSETDLERAVRKAALVMYWKLNPKKKKQVAVAELLENVGQVNEHDGGAQPGPVPKSLQKQRRMLERLVSSESKNYIALDDFVEITKKYAKGVIPSSLFLQDDEDDDELAGKSPEDLPLRLKVVKYPLHAIMEIKEYLIDMASRAGMHWLSTIIPTHHINALIFFFIVSNLTIDFFAFFIPLVIFYLSFISMVICTLKVFQDSKAWENFRTLTDLLLRFEPNLDVEQAEVNFGWNHLEPYAHFLLSVFFVIFSFPIASKDCIPCSELAVITGFFTVTSYLSLSTHAEPYTRRALATEVTAGLLSLLPSMPLNWPYLKVLGQTFITVPVGHLVVLNVSVPCLLYVYLLYLFFRMAQLRNFKGTYCYLVPYLVCFMWCELSVVILLESTGLGLLRASIGYFLFLFALPILVAGLALVGVLQFARWFTSLELTKIAVTVAVCSVPLLLRWWTKASFSVVGMVKSLTRSSMVKLILVWLTAIVLFCWFYVYRSEGMKVYNSTLTWQQYGALCGPRAWKETNMARTQILCSHLEGHRVTWTGRFKYVRVTDIDNSAESAINMLPFFIGDWMRCLYGEAYPACSPGNTSTAEEELCRLKLLAKHPCHIKKFDRYKFEITVGMPFSSGADGSRSREEDDVTKDIVLRASSEFKSVLLSLRQGSLIEFSTILEGRLGSKWPVFELKAISCLNCMAQLSPTRRHVKIEHDWRSTVHGAVKFAFDFFFFPFLSAA
| null | null |
calcium ion homeostasis [GO:0055074]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER overload response [GO:0006983]; ERAD pathway [GO:0036503]; glucose homeostasis [GO:0042593]; kidney development [GO:0001822]; negative regulation of apoptotic process [GO:0043066]; negative regulation of ATF6-mediated unfolded protein response [GO:1903892]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of programmed cell death [GO:0043069]; negative regulation of response to endoplasmic reticulum stress [GO:1903573]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of translation [GO:0017148]; negative regulation of type B pancreatic cell apoptotic process [GO:2000675]; nervous system process [GO:0050877]; olfactory behavior [GO:0042048]; pancreas development [GO:0031016]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of ERAD pathway [GO:1904294]; positive regulation of growth [GO:0045927]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein ubiquitination [GO:0031398]; protein maturation by protein folding [GO:0022417]; protein stabilization [GO:0050821]; renal water homeostasis [GO:0003091]; response to endoplasmic reticulum stress [GO:0034976]; sensory perception of sound [GO:0007605]; visual perception [GO:0007601]
|
dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; secretory granule [GO:0030141]; synaptic vesicle membrane [GO:0030672]
|
ATPase binding [GO:0051117]; calcium-dependent protein binding [GO:0048306]; calmodulin binding [GO:0005516]; DNA-binding transcription factor binding [GO:0140297]; proteasome binding [GO:0070628]; ubiquitin protein ligase binding [GO:0031625]
|
PF20053;PF19913;PF19914;PF20023;
|
1.25.40.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:23035048}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:23035048}. Note=Co-localizes with ATP6V1A in the secretory granules in neuroblastoma cell lines. {ECO:0000269|PubMed:23035048}.
| null | null | null | null | null |
FUNCTION: Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store (PubMed:16989814). Negatively regulates the ER stress response and positively regulates the stability of V-ATPase subunits ATP6V1A and ATP1B1 by preventing their degradation through an unknown proteasome-independent mechanism (PubMed:23035048). {ECO:0000269|PubMed:16989814, ECO:0000269|PubMed:23035048}.
|
Homo sapiens (Human)
|
O76027
|
ANXA9_HUMAN
|
MSVTGGKMAPSLTQEILSHLGLASKTAAWGTLGTLRTFLNFSVDKDAQRLLRAITGQGVDRSAIVDVLTNRSREQRQLISRNFQERTQQDLMKSLQAALSGNLERIVMALLQPTAQFDAQELRTALKASDSAVDVAIEILATRTPPQLQECLAVYKHNFQVEAVDDITSETSGILQDLLLALAKGGRDSYSGIIDYNLAEQDVQALQRAEGPSREETWVPVFTQRNPEHLIRVFDQYQRSTGQELEEAVQNRFHGDAQVALLGLASVIKNTPLYFADKLHQALQETEPNYQVLIRILISRCETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCQSALLALCRAEDM
| null | null |
cell-cell adhesion [GO:0098609]
|
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]; vesicle [GO:0031982]
|
acetylcholine receptor activity [GO:0015464]; cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]; phospholipid binding [GO:0005543]; protease binding [GO:0002020]; virion binding [GO:0046790]
|
PF00191;
|
1.10.220.10;
|
Annexin family
| null | null | null | null | null | null | null |
FUNCTION: Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes. {ECO:0000269|PubMed:10899159}.
|
Homo sapiens (Human)
|
O76031
|
CLPX_HUMAN
|
MPSCGACTCGAAAVRLITSSLASAQRGISGGRIHMSVLGRLGTFETQILQRAPLRSFTETPAYFASKDGISKDGSGDGNKKSASEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEVEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQIPQEKRGGEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNILFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPTKESSEEEYDSGVEEEGWPRQADAANS
| null | null |
ATP metabolic process [GO:0046034]; cell division [GO:0051301]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]
|
cytosol [GO:0005829]; endopeptidase Clp complex [GO:0009368]; HslUV protease complex [GO:0009376]; mitochondrial endopeptidase Clp complex [GO:0009841]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; peptidase activator activity [GO:0016504]; protein dimerization activity [GO:0046983]; unfolded protein binding [GO:0051082]; zinc ion binding [GO:0008270]
|
PF07724;PF10431;
|
1.10.8.60;3.40.50.300;
|
ClpX chaperone family
| null |
SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid.
| null | null | null | null | null |
FUNCTION: ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP (PubMed:28874591). Targets specific substrates for degradation by the Clp complex (PubMed:11923310, PubMed:22710082). Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure (PubMed:22841477). ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis (PubMed:28874591). Important for efficient erythropoiesis through up-regulation of heme biosynthesis (PubMed:25957689, PubMed:28874591). {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:22710082, ECO:0000269|PubMed:22841477, ECO:0000269|PubMed:25957689, ECO:0000269|PubMed:28874591}.
|
Homo sapiens (Human)
|
O76036
|
NCTR1_HUMAN
|
MSSTLPALLCVGLCLSQRISAQQQTLPKPFIWAEPHFMVPKEKQVTICCQGNYGAVEYQLHFEGSLFAVDRPKPPERINKVKFYIPDMNSRMAGQYSCIYRVGELWSEPSNLLDLVVTEMYDTPTLSVHPGPEVISGEKVTFYCRLDTATSMFLLLKEGRSSHVQRGYGKVQAEFPLGPVTTAHRGTYRCFGSYNNHAWSFPSEPVKLLVTGDIENTSLAPEDPTFPADTWGTYLLTTETGLQKDHALWDHTAQNLLRMGLAFLVLVALVWFLVEDWLSRKRTRERASRASTWEGRRRLNTQTL
| null | null |
cellular defense response [GO:0006968]; natural killer cell activation [GO:0030101]; regulation of natural killer cell mediated cytotoxicity [GO:0042269]; signal transduction [GO:0007165]
|
plasma membrane [GO:0005886]; SWI/SNF complex [GO:0016514]
| null |
PF00047;
|
2.60.40.10;
|
Natural cytotoxicity receptor (NCR) family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9730896}.; PTM: O-glycosylated. {ECO:0000269|PubMed:9730896}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. {ECO:0000269|PubMed:9730896}.
|
Homo sapiens (Human)
|
O76039
|
CDKL5_HUMAN
|
MKIPNIGNVMNKFEILGVVGEGAYGVVLKCRHKETHEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLELLEEMPNGVPPEKVKSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGNNANYTEYVATRWYRSPELLLGAPYGKSVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPSEQMKLFYSNPRFHGLRFPAVNHPQSLERRYLGILNSVLLDLMKNLLKLDPADRYLTEQCLNHPTFQTQRLLDRSPSRSAKRKPYHVESSTLSNRNQAGKSTALQSHHRSNSKDIQNLSVGLPRADEGLPANESFLNGNLAGASLSPLHTKTYQASSQPGSTSKDLTNNNIPHLLSPKEAKSKTEFDFNIDPKPSEGPGTKYLKSNSRSQQNRHSFMESSQSKAGTLQPNEKQSRHSYIDTIPQSSRSPSYRTKAKSHGALSDSKSVSNLSEARAQIAEPSTSRYFPSSCLDLNSPTSPTPTRHSDTRTLLSPSGRNNRNEGTLDSRRTTTRHSKTMEELKLPEHMDSSHSHSLSAPHESFSYGLGYTSPFSSQQRPHRHSMYVTRDKVRAKGLDGSLSIGQGMAARANSLQLLSPQPGEQLPPEMTVARSSVKETSREGTSSFHTRQKSEGGVYHDPHSDDGTAPKENRHLYNDPVPRRVGSFYRVPSPRPDNSFHENNVSTRVSSLPSESSSGTNHSKRQPAFDPWKSPENISHSEQLKEKEKQGFFRSMKKKKKKSQTVPNSDSPDLLTLQKSIHSASTPSSRPKEWRPEKISDLQTQSQPLKSLRKLLHLSSASNHPASSDPRFQPLTAQQTKNSFSEIRIHPLSQASGGSSNIRQEPAPKGRPALQLPGQMDPGWHVSSVTRSATEGPSYSEQLGAKSGPNGHPYNRTNRSRMPNLNDLKETAL
|
2.7.11.22
| null |
modulation of chemical synaptic transmission [GO:0050804]; neuron migration [GO:0001764]; positive regulation of axon extension [GO:0045773]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of GTPase activity [GO:0043547]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cilium assembly [GO:1902017]; regulation of dendrite development [GO:0050773]; regulation of postsynapse organization [GO:0099175]
|
centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary tip [GO:0097542]; dendrite cytoplasm [GO:0032839]; dendritic growth cone [GO:0044294]; glutamatergic synapse [GO:0098978]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density, intracellular component [GO:0099092]
|
ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; kinase activity [GO:0016301]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
|
PTM: Autophosphorylated.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16935860}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29420175}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:29420175}.
|
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=2.7.11.22; 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=2.7.11.22;
| null | null | null | null |
FUNCTION: Mediates phosphorylation of MECP2 (PubMed:15917271, PubMed:16935860). May regulate ciliogenesis (PubMed:29420175). {ECO:0000269|PubMed:15917271, ECO:0000269|PubMed:16935860, ECO:0000269|PubMed:29420175}.
|
Homo sapiens (Human)
|
O76041
|
NEBL_HUMAN
|
MRVPVFEDIKDETEEEKIGEEENEEDQVFYKPVIEDLSMELARKCTELISDIRYKEEFKKSKDKCTFVTDSPMLNHVKNIGAFISEAKYKGTIKADLSNSLYKRMPATIDSVFAGEVTQLQSEVAYKQKHDAAKGFSDYAHMKEPPEVKHAMEVNKHQSNISYRKDVQDTHTYSAELDRPDIKMATQISKIISNAEYKKGQGIMNKEPAVIGRPDFEHAVEASKLSSQIKYKEKFDNEMKDKKHHYNPLESASFRQNQLAATLASNVKYKKDIQNMHDPVSDLPNLLFLDHVLKASKMLSGREYKKLFEENKGMYHFDADAVEHLHHKGNAVLQSQVKYKEEYEKNKGKPMLEFVETPSYQASKEAQKMQSEKVYKEDFEKEIKGRSSLDLDKTPEFLHVKYITNLLREKEYKKDLENEIKGKGMELNSEVLDIQRAKRASEMASEKEYKKDLESIIKGKGMQAGTDTLEMQHAKKAAEIASEKDYKRDLETEIKGKGMQVSTDTLDVQRAKKASEMASQKQYKKDLENEIKGKGMQVSMDIPDILRAKRTSEIYSQRKYKDEAEKMLSNYSTIADTPEIQRIKTTQQNISAVFYKKEVGAGTAVKDSPEIERVKKNQQNISSVKYKEEIKHATAISDPPELKRVKENQKNISNLQYKEQNYKATPVSMTPEIERVRRNQEQLSAVKYKGELQRGTAISDPPELKRAKENQKNISNVYYRGQLGRATTLSVTPEMERVKKNQENISSVKYTQDHKQMKGRPSLILDTPAMRHVKEAQNHISMVKYHEDFEKTKGRGFTPVVDDPVTERVRKNTQVVSDAAYKGVHPHIVEMDRRPGIIVDLKVWRTDPGSIFDLDPLEDNIQSRSLHMLSEKASHYRRHWSRSHSSSTFGTGLGDDRSEISEIYPSFSCCSEVTRPSDEGAPVLPGAYQQSHSQGYGYMHQTSVSSMRSMQHSPNLRTYRAMYDYSAQDEDEVSFRDGDYIVNVQPIDDGWMYGTVQRTGRTGMLPANYIEFVN
| null | null |
cardiac muscle thin filament assembly [GO:0071691]
|
extracellular exosome [GO:0070062]; I band [GO:0031674]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
actin filament binding [GO:0051015]; cytoskeletal protein binding [GO:0008092]; filamin binding [GO:0031005]; structural constituent of muscle [GO:0008307]; tropomyosin binding [GO:0005523]
|
PF00880;PF14604;
|
2.30.30.40;
| null | null |
SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:15004028}.
| null | null | null | null | null |
FUNCTION: Binds to actin and plays an important role in the assembly of the Z-disk. May functionally link sarcomeric actin to the desmin intermediate filaments in the heart muscle sarcomeres (PubMed:27733623). Isoform 2 might play a role in the assembly of focal adhesion (PubMed:15004028). {ECO:0000269|PubMed:15004028, ECO:0000269|PubMed:27733623}.
|
Homo sapiens (Human)
|
O76050
|
NEUL1_HUMAN
|
MGNNFSSIPSLPRGNPSRAPRGHPQNLKDSIGGPFPVTSHRCHHKQKHCPAVLPSGGLPATPLLFHPHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFHRINDSAVMLFFSGVRTADPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLRREADDARLSVSLCDLNVPGADGDEAAPAAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARVEHGRDERALVFTSRPVRVAETIFVKVTRSGGARPGALSFGVTTCDPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAAAGMQLCVDASQPLWMLFGLHGTITQIRILGSTILAERGIPSLPCSPASTPTSPSALGSRLSDPLLSTCSSGPLGSSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMCLCYACGLRLKKALHACCPICRRPIKDIIKTYRSS
|
2.3.2.27
| null |
cellular response to amino acid stimulus [GO:0071230]; lactation [GO:0007595]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of Notch signaling pathway [GO:0045746]; nervous system development [GO:0007399]; Notch signaling pathway [GO:0007219]; positive regulation of apoptotic process [GO:0043065]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of synapse maturation [GO:0090129]; protein monoubiquitination [GO:0006513]; skeletal muscle tissue development [GO:0007519]; sperm axoneme assembly [GO:0007288]
|
apical dendrite [GO:0097440]; dendritic spine [GO:0043197]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
metal ion binding [GO:0046872]; translation factor activity, non-nucleic acid binding [GO:0045183]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF07177;PF13920;
|
2.60.120.920;3.30.40.10;
| null |
PTM: Myristoylation is a determinant of membrane targeting. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11585928, ECO:0000269|PubMed:20847082}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Perikaryon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Localized in the cell bodies of the pyramidal neurons and distributed along their apical dendrites. Colocalized with PSD95 in postsynaptic sites. Colocalized with CPEB3 at apical dendrites of CA1 neurons (By similarity). Colocalized with JAG1 at the cell surface. {ECO:0000250}.
|
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: Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element-binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor; inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway. {ECO:0000269|PubMed:20847082}.
|
Homo sapiens (Human)
|
O76054
|
S14L2_HUMAN
|
MSGRVGDLSPRQKEALAKFRENVQDVLPALPNPDDYFLLRWLRARSFDLQKSEAMLRKHVEFRKQKDIDNIISWQPPEVIQQYLSGGMCGYDLDGCPVWYDIIGPLDAKGLLFSASKQDLLRTKMRECELLLQECAHQTTKLGRKVETITIIYDCEGLGLKHLWKPAVEAYGEFLCMFEENYPETLKRLFVVKAPKLFPVAYNLIKPFLSEDTRKKIMVLGANWKEVLLKHISPDQVPVEYGGTMTDPDGNPKCKSKINYGGDIPRKYYVRDQVKQQYEHSVQISRGSSHQVEYEILFPGCVLRWQFMSDGADVGFGIFLKTKMGERQRAGEMTEVLPNQRYNSHLVPEDGTLTCSDPGIYVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]; regulation of cholesterol biosynthetic process [GO:0045540]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
phospholipid binding [GO:0005543]; vitamin E binding [GO:0008431]
|
PF00650;PF03765;
|
3.40.525.10;2.60.120.680;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in absence of alpha-tocopherol, and nuclear in presence of alpha-tocopherol.
| null | null | null | null | null |
FUNCTION: Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell.
|
Homo sapiens (Human)
|
O76061
|
STC2_HUMAN
|
MCAERLGQFMTLALVLATFDPARGTDATNPPEGPQDRSSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIRGLHGICMTFLHNAGKFDAQGKSFIKDALKCKAHALRHRFGCISRKCPAIREMVSQLQRECYLKHDLCAAAQENTRVIVEMIHFKDLLLHEPYVDLVNLLLTCGEEVKEAITHSVQVQCEQNWGSLCSILSFCTSAIQKPPTAPPERQPQVDRTKLSRAHHGEAGHHLPEPSSRETGRGAKGERGSKSHPNAHARGRVGGLGAQGPSGSSEWEDEQSEYSDIRR
| null | null |
cellular response to hypoxia [GO:0071456]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; endoplasmic reticulum unfolded protein response [GO:0030968]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of gene expression [GO:0010629]; negative regulation of multicellular organism growth [GO:0040015]; regulation of hormone biosynthetic process [GO:0046885]; regulation of store-operated calcium entry [GO:2001256]; response to oxidative stress [GO:0006979]; response to peptide hormone [GO:0043434]; response to vitamin D [GO:0033280]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]
|
enzyme binding [GO:0019899]; heme binding [GO:0020037]; hormone activity [GO:0005179]; protein homodimerization activity [GO:0042803]
|
PF03298;
| null |
Stanniocalcin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Has an anti-hypocalcemic action on calcium and phosphate homeostasis.
|
Homo sapiens (Human)
|
O76062
|
ERG24_HUMAN
|
MAPTQGPRAPLEFGGPLGAAALLLLLPATMFHLLLAARSGPARLLGPPASLPGLEVLWSPRALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAGLPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSGNPIYDFFLGRELNPRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWHEEAVLTTMDITHDGFGFMLAFGDMAWVPFTYSLQAQFLLHHPQPLGLPMASVICLINATGYYIFRGANSQKNTFRKNPSDPRVAGLETISTATGRKLLVSGWWGMVRHPNYLGDLIMALAWSLPCGVSHLLPYFYLLYFTALLVHREARDERQCLQKYGLAWQEYCRRVPYRIMPYIY
|
1.3.1.70
| null |
cholesterol biosynthetic process [GO:0006695]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; nuclear inner membrane [GO:0005637]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
delta14-sterol reductase activity [GO:0050613]; NADP binding [GO:0050661]
|
PF01222;
|
1.20.120.1630;
|
ERG4/ERG24 family
| null |
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q71KT5}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9878250}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH; Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813, ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70; Evidence={ECO:0000250|UniProtKB:Q8WMV1}; CATALYTIC ACTIVITY: Reaction=5alpha-cholest-8,14-dien-3beta-ol + H(+) + NADPH = 5alpha-cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46456, ChEBI:CHEBI:15378, ChEBI:CHEBI:16608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:86131; Evidence={ECO:0000269|PubMed:16784888}; CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-8,14-cholestadien-3beta-ol + H(+) + NADPH = 4,4-dimethyl-5alpha-cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46812, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78904, ChEBI:CHEBI:87044; Evidence={ECO:0000250|UniProtKB:Q8WMV1};
| null |
PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
| null | null |
FUNCTION: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis. {ECO:0000269|PubMed:16784888}.
|
Homo sapiens (Human)
|
O76064
|
RNF8_HUMAN
|
MGEPGFFVTGDRAGGRSWCLRRVGMSAGWLLLEDGCEVTVGRGFGVTYQLVSKICPLMISRNHCVLKQNPEGQWTIMDNKSLNGVWLNRARLEPLRVYSIHQGDYIQLGVPLENKENAEYEYEVTEEDWETIYPCLSPKNDQMIEKNKELRTKRKFSLDELAGPGAEGPSNLKSKINKVSCESGQPVKSQGKGEVASTPSDNLDPKLTALEPSKTTGAPIYPGFPKVTEVHHEQKASNSSASQRSLQMFKVTMSRILRLKIQMQEKHEAVMNVKKQTQKGNSKKVVQMEQELQDLQSQLCAEQAQQQARVEQLEKTFQEEEQHLQGLEIAQGEKDLKQQLAQALQEHWALMEELNRSKKDFEAIIQAKNKELEQTKEEKEKMQAQKEEVLSHMNDVLENELQCIICSEYFIEAVTLNCAHSFCSYCINEWMKRKIECPICRKDIKSKTYSLVLDNCINKMVNNLSSEVKERRIVLIRERKAKRLF
|
2.3.2.27
| null |
cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response [GO:0006974]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; double-strand break repair via nonhomologous end joining [GO:0006303]; epigenetic regulation of gene expression [GO:0040029]; interstrand cross-link repair [GO:0036297]; isotype switching [GO:0045190]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of DNA repair [GO:0045739]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; protein autoubiquitination [GO:0051865]; protein K48-linked ubiquitination [GO:0070936]; protein K6-linked ubiquitination [GO:0085020]; protein K63-linked ubiquitination [GO:0070534]; response to ionizing radiation [GO:0010212]; signal transduction in response to DNA damage [GO:0042770]; sperm DNA condensation [GO:0035092]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cell division site [GO:0032153]; chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]; ubiquitin ligase complex [GO:0000151]
|
chromatin binding [GO:0003682]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF00498;PF13920;
|
1.20.5.170;2.60.200.20;3.30.40.10;
|
RNF8 family
|
PTM: Autoubiquitinated through 'Lys-48' and 'Lys-63' of ubiquitin. 'Lys-63' polyubiquitination is mediated by UBE2N. 'Lys-29'-type polyubiquitination is also observed, but it doesn't require its own functional RING-type zinc finger. {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:16215985}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:11322894, ECO:0000269|PubMed:14981089, ECO:0000269|PubMed:16215985, ECO:0000269|PubMed:23233665}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03067}. Midbody {ECO:0000255|HAMAP-Rule:MF_03067}. Chromosome, telomere {ECO:0000255|HAMAP-Rule:MF_03067}. Note=Recruited at uncapped telomeres (By similarity). Following DNA damage, such as double-strand breaks, recruited to the sites of damage (PubMed:18001824, PubMed:18077395, PubMed:22266820, PubMed:23233665). During prophase, concomitant with nuclear envelope breakdown, localizes throughout the cell, with a dotted pattern. In telophase, again in the nucleus and also with a discrete dotted pattern in the cytoplasm. In late telophase and during cytokinesis, localizes in the midbody of the tubulin bridge joining the daughter cells. Does not seem to be associated with condensed chromosomes at any time during the cell cycle. During spermatogenesis, sequestered in the cytoplasm by PIWIL1: RNF8 is released following ubiquitination and degradation of PIWIL1. {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:18001824, ECO:0000269|PubMed:18077395, ECO:0000269|PubMed:22266820, ECO:0000269|PubMed:23233665}.
|
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:23115235};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23115235}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF) (PubMed:18001824, PubMed:18006705). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites (PubMed:18077395, PubMed:19202061). Promotes the recruitment of NBN to DNA damage sites by catalyzing 'Lys-6'-linked ubiquitination of NBN (PubMed:23115235). Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non-histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin-conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'-linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites (PubMed:11322894, PubMed:14981089, PubMed:17724460, PubMed:18001825, PubMed:18337245, PubMed:18948756, PubMed:19015238, PubMed:19124460, PubMed:19203578, PubMed:19203579, PubMed:20550933, PubMed:21558560, PubMed:21857671, PubMed:21911360, PubMed:22266820, PubMed:22373579, PubMed:22531782, PubMed:22705371, PubMed:22980979). Following DNA damage, mediates the ubiquitination and degradation of POLD4/p12, a subunit of DNA polymerase delta. In the absence of POLD4, DNA polymerase delta complex exhibits higher proofreading activity (PubMed:23233665). In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis. At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair (PubMed:22865450). May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA-mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2 (PubMed:11322894, PubMed:14981089, PubMed:17724460, PubMed:18001825, PubMed:18337245, PubMed:18948756, PubMed:19015238, PubMed:19124460, PubMed:19203578, PubMed:19203579, PubMed:20550933, PubMed:21558560, PubMed:21857671, PubMed:21911360, PubMed:22266820, PubMed:22373579, PubMed:22531782, PubMed:22705371, PubMed:22980979). {ECO:0000269|PubMed:11322894, ECO:0000269|PubMed:14981089, ECO:0000269|PubMed:17724460, ECO:0000269|PubMed:18001824, ECO:0000269|PubMed:18001825, ECO:0000269|PubMed:18006705, ECO:0000269|PubMed:18077395, ECO:0000269|PubMed:18337245, ECO:0000269|PubMed:18948756, ECO:0000269|PubMed:19015238, ECO:0000269|PubMed:19124460, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19203578, ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:20550933, ECO:0000269|PubMed:21558560, ECO:0000269|PubMed:21857671, ECO:0000269|PubMed:21911360, ECO:0000269|PubMed:22266820, ECO:0000269|PubMed:22373579, ECO:0000269|PubMed:22531782, ECO:0000269|PubMed:22705371, ECO:0000269|PubMed:22865450, ECO:0000269|PubMed:22980979, ECO:0000269|PubMed:23115235, ECO:0000269|PubMed:23233665}.
|
Homo sapiens (Human)
|
O76070
|
SYUG_HUMAN
|
MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD
| null | null |
adult locomotory behavior [GO:0008344]; chemical synaptic transmission [GO:0007268]; protein secretion [GO:0009306]; regulation of dopamine secretion [GO:0014059]; regulation of neurotransmitter secretion [GO:0046928]; synapse organization [GO:0050808]; synaptic vesicle endocytosis [GO:0048488]
|
axon terminus [GO:0043679]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]
|
cuprous ion binding [GO:1903136]
|
PF01387;
|
1.10.287.700;
|
Synuclein family
|
PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on residues distinct from the residue phosphorylated by other kinases. {ECO:0000269|PubMed:10852916}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11746666}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle.
| null | null | null | null | null |
FUNCTION: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O76071
|
CIAO1_HUMAN
|
MKDSLVLLGRVPAHPDSRCWFLAWNPAGTLLASCGGDRRIRIWGTEGDSWICKSVLSEGHQRTVRKVAWSPCGNYLASASFDATTCIWKKNQDDFECVTTLEGHENEVKSVAWAPSGNLLATCSRDKSVWVWEVDEEDEYECVSVLNSHTQDVKHVVWHPSQELLASASYDDTVKLYREEEDDWVCCATLEGHESTVWSLAFDPSGQRLASCSDDRTVRIWRQYLPGNEQGVACSGSDPSWKCICTLSGFHSRTIYDIAWCQLTGALATACGDDAIRVFQEDPNSDPQQPTFSLTAHLHQAHSQDVNCVAWNPKEPGLLASCSDDGEVAFWKYQRPEGL
| null | null |
chromosome segregation [GO:0007059]; iron-sulfur cluster assembly [GO:0016226]; positive regulation of cell population proliferation [GO:0008284]; protein maturation by iron-sulfur cluster transfer [GO:0097428]; regulation of transcription by RNA polymerase II [GO:0006357]
|
CIA complex [GO:0097361]; cytoplasm [GO:0005737]; MMXD complex [GO:0071817]
| null |
PF00400;
|
2.130.10.10;
|
WD repeat CIA1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23585563}.
| null | null | null | null | null |
FUNCTION: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins (PubMed:17937914, PubMed:23891004). As a CIA complex component, interacts specifically with CIAO2A or CIAO2B and MMS19 to assist different branches of iron-sulfur protein assembly, depending of its interactors. The complex CIAO1:CIAO2B:MMS19 binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A specifically matures ACO1 and stabilizes IREB2 (PubMed:23891004). Seems to specifically modulate the transactivation activity of WT1 (PubMed:9556563). As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (PubMed:20797633). {ECO:0000255|HAMAP-Rule:MF_03037, ECO:0000269|PubMed:17937914, ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:9556563}.
|
Homo sapiens (Human)
|
O76074
|
PDE5A_HUMAN
|
MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN
|
3.1.4.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12955149, ECO:0000269|PubMed:15260978}; Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc. {ECO:0000269|PubMed:12955149, ECO:0000269|PubMed:15260978}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12955149}; Note=Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc. {ECO:0000269|PubMed:12955149};
|
cAMP-mediated signaling [GO:0019933]; cGMP catabolic process [GO:0046069]; negative regulation of cardiac muscle contraction [GO:0055118]; negative regulation of T cell proliferation [GO:0042130]; oocyte development [GO:0048599]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of oocyte development [GO:0060282]; regulation of nitric oxide mediated signal transduction [GO:0010749]; relaxation of cardiac muscle [GO:0055119]; T cell proliferation [GO:0042098]
|
cytosol [GO:0005829]
|
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; 3',5'-cyclic-nucleotide phosphodiesterase activity [GO:0004114]; cGMP binding [GO:0030553]; metal ion binding [GO:0046872]
|
PF01590;PF00233;
|
3.30.450.40;1.10.1300.10;
|
Cyclic nucleotide phosphodiesterase family
|
PTM: Phosphorylation is regulated by binding of cGMP to the two allosteric sites (By similarity). Phosphorylation by PRKG1 leads to its activation. {ECO:0000250, ECO:0000269|PubMed:11723116}.
| null |
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:9714779}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000305|PubMed:15260978};
| null |
PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
| null | null |
FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP (PubMed:15489334, PubMed:9714779). Specifically regulates nitric-oxide-generated cGMP (PubMed:15489334). {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9714779}.
|
Homo sapiens (Human)
|
O76075
|
DFFB_HUMAN
|
MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSRIYKPQTRLKRKQPVRKRQ
|
3.-.-.-
| null |
apoptotic chromosome condensation [GO:0030263]; apoptotic DNA fragmentation [GO:0006309]; DNA catabolic process [GO:0006308]; negative regulation of apoptotic DNA fragmentation [GO:1902511]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
disordered domain specific binding [GO:0097718]; DNA binding [GO:0003677]; DNA endonuclease activity [GO:0004520]; DNA nuclease activity [GO:0004536]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]
|
PF02017;PF09230;
|
3.10.20.10;6.10.140.170;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
| null | null | null | null | null |
FUNCTION: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
|
Homo sapiens (Human)
|
O76076
|
CCN5_HUMAN
|
MRGTPKTHLLAFSLLCLLSKVRTQLCPTPCTCPWPPPRCPLGVPLVLDGCGCCRVCARRLGEPCDQLHVCDASQGLVCQPGAGPGGRGALCLLAEDDSSCEVNGRLYREGETFQPHCSIRCRCEDGGFTCVPLCSEDVRLPSWDCPHPRRVEVLGKCCPEWVCGQGGGLGTQPLPAQGPQFSGLVSSLPPGVPCPEWSTAWGPCSTTCGLGMATRVSNQNRFCRLETQRRLCLSRPCPPSRGRSPQNSAF
| null | null |
cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; positive regulation of cell differentiation [GO:0045597]; signal transduction [GO:0007165]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
heparin binding [GO:0008201]; integrin binding [GO:0005178]
|
PF00219;PF19035;PF00093;
|
2.20.100.10;
|
CCN family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May play an important role in modulating bone turnover. Promotes the adhesion of osteoblast cells and inhibits the binding of fibrinogen to integrin receptors. In addition, inhibits osteocalcin production.
|
Homo sapiens (Human)
|
O76080
|
ZFAN5_HUMAN
|
MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADTSLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSTSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI
| null | null |
face development [GO:0060324]; fibroblast migration [GO:0010761]; in utero embryonic development [GO:0001701]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; respiratory system process [GO:0003016]; skeletal system morphogenesis [GO:0048705]; smooth muscle tissue development [GO:0048745]; vasculature development [GO:0001944]
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cytoplasm [GO:0005737]
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DNA binding [GO:0003677]; zinc ion binding [GO:0008270]
|
PF01754;PF01428;
|
1.20.5.4770;4.10.1110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. {ECO:0000269|PubMed:14754897}.
|
Homo sapiens (Human)
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O76081
|
RGS20_HUMAN
|
MPQLSQDNQECLQKHFSRPSIWTQFLPLFRAQRYNTDIHQITENEGDLRAVPDIKSFPPAQLPDSPAAPKLFGLLSSPLSSLARFFSHLLRRPPPEAPRRRLDFSPLLPALPAARLSRGHEELPGRLSLLLGAALALPGRPSGGRPLRPPHPVAKPREEDATAGQSSPMPQMGSERMEMRKRQMPAAQDTPGAAPGQPGAGSRGSNACCFCWCCCCSCSCLTVRNQEDQRPTIASHELRADLPTWEESPAPTLEEVNAWAQSFDKLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKNIIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMVEPSQHIFDDAQLQIYTLMHRDSYPRFMNSAVYKDLLQSLSEKSIEA
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of signal transduction [GO:0009968]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; response to amphetamine [GO:0001975]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]
|
PF00615;
|
1.10.167.10;
| null |
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity). {ECO:0000250}.; PTM: N- and O-glycosylated in synapsomal membranes. {ECO:0000250}.; PTM: Serine phosphorylated in synapsomal membranes. {ECO:0000250}.; PTM: Sumoylated with SUMO1 and SUMO2 in synaptosomes. The sumoylated forms act as a scaffold for sequestering mu-opioid receptor-activated G(alpha) subunits (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Nucleus. Cytoplasm. Note=Shuttles between the cytoplasm/cell membrane and the nucleus. Anchored to the membrane through palmitoylation. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:12379657}.
|
Homo sapiens (Human)
|
O76082
|
S22A5_HUMAN
|
MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFGLSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLVPPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTRMLKDGQERPTILKSTAF
| null | null |
(R)-carnitine transmembrane transport [GO:1902270]; (R)-carnitine transport [GO:1900749]; carnitine transmembrane transport [GO:1902603]; carnitine transport [GO:0015879]; positive regulation of intestinal epithelial structure maintenance [GO:0060731]; quaternary ammonium group transport [GO:0015697]; response to symbiotic bacterium [GO:0009609]; response to tumor necrosis factor [GO:0034612]; response to type II interferon [GO:0034341]; sodium ion transport [GO:0006814]; sodium-dependent organic cation transport [GO:0070715]; transport across blood-brain barrier [GO:0150104]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; brush border membrane [GO:0031526]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]
|
(R)-carnitine transmembrane transporter activity [GO:1901235]; amino-acid betaine transmembrane transporter activity [GO:0015199]; ATP binding [GO:0005524]; carnitine transmembrane transporter activity [GO:0015226]; PDZ domain binding [GO:0030165]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; symporter activity [GO:0015293]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
|
PTM: Glycosylated. Glycosylation affects the expression levels. {ECO:0000269|PubMed:17509700}.; PTM: [Isoform 3]: Not glycosylated. {ECO:0000269|PubMed:17509700}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10679939, ECO:0000269|PubMed:17509700, ECO:0000269|PubMed:33334877}; Multi-pass membrane protein {ECO:0000269|PubMed:10679939}. Apical cell membrane {ECO:0000269|PubMed:10966938, ECO:0000269|PubMed:20722056}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000255}. Note=In intestinal cells, apical expression is induced by TNF. Localized to the basal membrane of Sertoli cells (PubMed:35307651). {ECO:0000269|PubMed:20722056, ECO:0000269|PubMed:35307651}.; SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum {ECO:0000269|PubMed:17509700}.
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CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + Na(+)(out) = (R)-carnitine(in) + Na(+)(in); Xref=Rhea:RHEA:72091, ChEBI:CHEBI:16347, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10454528, ECO:0000269|PubMed:10525100, ECO:0000269|PubMed:17509700, ECO:0000269|PubMed:17855766, ECO:0000269|PubMed:20722056, ECO:0000269|PubMed:33124720}; CATALYTIC ACTIVITY: Reaction=glycine betaine(out) + Na(+)(out) = glycine betaine(in) + Na(+)(in); Xref=Rhea:RHEA:72115, ChEBI:CHEBI:17750, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10966938, ECO:0000269|PubMed:33124720}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(in) + glycine betaine(out) = (R)-carnitine(out) + glycine betaine(in); Xref=Rhea:RHEA:72119, ChEBI:CHEBI:16347, ChEBI:CHEBI:17750; Evidence={ECO:0000269|PubMed:10966938}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-butanoyl-(R)-carnitine(out) = Na(+)(in) + O-butanoyl-(R)-carnitine(in); Xref=Rhea:RHEA:72123, ChEBI:CHEBI:21949, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:17855766}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-acetyl-(R)-carnitine(out) = Na(+)(in) + O-acetyl-(R)-carnitine(in); Xref=Rhea:RHEA:72099, ChEBI:CHEBI:29101, ChEBI:CHEBI:57589; Evidence={ECO:0000269|PubMed:10454528, ECO:0000269|PubMed:10525100}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-propanoyl-(R)-carnitine(out) = Na(+)(in) + O-propanoyl-(R)-carnitine(in); Xref=Rhea:RHEA:72103, ChEBI:CHEBI:29101, ChEBI:CHEBI:53210; Evidence={ECO:0000269|PubMed:10454528}; CATALYTIC ACTIVITY: Reaction=(S)-carnitine(out) + Na(+)(out) = (S)-carnitine(in) + Na(+)(in); Xref=Rhea:RHEA:72095, ChEBI:CHEBI:11060, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10525100}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-acyl-(R)-carnitine(out) = Na(+)(in) + O-acyl-(R)-carnitine(in); Xref=Rhea:RHEA:72107, ChEBI:CHEBI:29101, ChEBI:CHEBI:75659; Evidence={ECO:0000305|PubMed:10525100}; CATALYTIC ACTIVITY: Reaction=L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine(out) + Na(+)(out) = L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine(in) + Na(+)(in); Xref=Rhea:RHEA:72111, ChEBI:CHEBI:29101, ChEBI:CHEBI:191852; Evidence={ECO:0000269|PubMed:18005709}; CATALYTIC ACTIVITY: Reaction=N,N-dimethylglycine(out) + Na(+)(out) = N,N-dimethylglycine(in) + Na(+)(in); Xref=Rhea:RHEA:76591, ChEBI:CHEBI:29101, ChEBI:CHEBI:58251; Evidence={ECO:0000269|PubMed:33124720};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 uM for (R)-carnitine {ECO:0000269|PubMed:10525100}; KM=4.8 uM for (R)-carnitine (at -60 mV holding potential) {ECO:0000269|PubMed:10966938}; KM=2.58 uM for (R)-carnitine (at -90 mV holding potential) {ECO:0000269|PubMed:10966938}; KM=19.9 uM for (R)-carnitine {ECO:0000269|PubMed:33334877}; KM=8.5 uM for O-acetyl-(R)-carnitine {ECO:0000269|PubMed:10525100}; KM=10.9 uM for (S)-carnitine {ECO:0000269|PubMed:10525100}; KM=98.3 uM for (S)-carnitine {ECO:0000269|PubMed:10966938}; KM=18.5 uM for Na(+) {ECO:0000269|PubMed:10525100}; Vmax=0.63 pmol/min/ug enzyme {ECO:0000269|PubMed:33334877};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is from 7 to 8.5. {ECO:0000269|PubMed:10525100, ECO:0000269|PubMed:10966938};
| null |
FUNCTION: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine (PubMed:10454528, PubMed:10525100, PubMed:10966938, PubMed:17509700, PubMed:20722056, PubMed:33124720). Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 11.3 (PubMed:10454528, PubMed:10525100, PubMed:10966938). In intestinal epithelia, transports the quorum-sensing pentapeptide CSF (competence and sporulation factor) from Bacillus Subtilis wich induces cytoprotective heat shock proteins contributing to intestinal homeostasis (PubMed:18005709). May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable). {ECO:0000269|PubMed:10454528, ECO:0000269|PubMed:10525100, ECO:0000269|PubMed:10966938, ECO:0000269|PubMed:17509700, ECO:0000269|PubMed:18005709, ECO:0000269|PubMed:20722056, ECO:0000305|PubMed:35307651}.; FUNCTION: [Isoform 3]: Retained in the ER, unable to perform carnitine uptake. {ECO:0000269|PubMed:17509700}.
|
Homo sapiens (Human)
|
O76083
|
PDE9A_HUMAN
|
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
|
3.1.4.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19919087, ECO:0000269|PubMed:20121115, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:22985069, ECO:0000269|PubMed:23025719, ECO:0000305|PubMed:18757755}; Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc. {ECO:0000269|PubMed:19919087, ECO:0000269|PubMed:20121115, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:22985069, ECO:0000269|PubMed:23025719, ECO:0000305|PubMed:18757755}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19919087, ECO:0000269|PubMed:20121115, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:22985069, ECO:0000269|PubMed:23025719, ECO:0000305|PubMed:18757755}; Note=Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc. {ECO:0000269|PubMed:19919087, ECO:0000269|PubMed:20121115, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:22985069, ECO:0000269|PubMed:23025719, ECO:0000305|PubMed:18757755};
|
cAMP-mediated signaling [GO:0019933]; cGMP catabolic process [GO:0046069]; cGMP metabolic process [GO:0046068]; negative regulation of neural precursor cell proliferation [GO:2000178]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of long-term synaptic potentiation [GO:1900273]; signal transduction [GO:0007165]
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cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; sarcolemma [GO:0042383]
|
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; 3',5'-cyclic-nucleotide phosphodiesterase activity [GO:0004114]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]
|
PF00233;
|
1.10.1300.10;
|
Cyclic nucleotide phosphodiesterase family, PDE9 subfamily
| null |
SUBCELLULAR LOCATION: [Isoform PDE9A1]: Cell projection, ruffle membrane {ECO:0000269|PubMed:17090334}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17090334}. Golgi apparatus {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25799991}.; SUBCELLULAR LOCATION: [Isoform PDE9A2]: Cell projection, ruffle membrane {ECO:0000269|PubMed:17090334}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17090334}.; SUBCELLULAR LOCATION: [Isoform PDE9A3]: Cytoplasm {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}.; SUBCELLULAR LOCATION: [Isoform PDE9A17]: Cytoplasm {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}.
|
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000269|PubMed:18757755, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:9624146};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.113 uM for cGMP {ECO:0000269|PubMed:21483814}; KM=501 uM for cAMP {ECO:0000269|PubMed:21483814}; Vmax=0.285 umol/min/mg enzyme with cGMP as substrate {ECO:0000269|PubMed:21483814}; Vmax=3.7 umol/min/mg enzyme with cAMP as substrate {ECO:0000269|PubMed:21483814}; Note=kcat is 0.18 sec(-1) for cGMP. kcat is 2.37 sec(-1) for cAMP. {ECO:0000269|PubMed:21483814};
|
PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
| null | null |
FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP (PubMed:18757755, PubMed:21483814, PubMed:9624146). Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart (PubMed:25799991). Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (By similarity). {ECO:0000250|UniProtKB:Q8QZV1, ECO:0000269|PubMed:18757755, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624146, ECO:0000305}.
|
Homo sapiens (Human)
|
O76090
|
BEST1_HUMAN
|
MTITYTSQVANARLGSFSRLLLCWRGSIYKLLYGEFLIFLLCYYIIRFIYRLALTEEQQLMFEKLTLYCDSYIQLIPISFVLGFYVTLVVTRWWNQYENLPWPDRLMSLVSGFVEGKDEQGRLLRRTLIRYANLGNVLILRSVSTAVYKRFPSAQHLVQAGFMTPAEHKQLEKLSLPHNMFWVPWVWFANLSMKAWLGGRIRDPILLQSLLNEMNTLRTQCGHLYAYDWISIPLVYTQVVTVAVYSFFLTCLVGRQFLNPAKAYPGHELDLVVPVFTFLQFFFYVGWLKVAEQLINPFGEDDDDFETNWIVDRNLQVSLLAVDEMHQDLPRMEPDMYWNKPEPQPPYTAASAQFRRASFMGSTFNISLNKEEMEFQPNQEDEEDAHAGIIGRFLGLQSHDHHPPRANSRTKLLWPKRESLLHEGLPKNHKAAKQNVRGQEDNKAWKLKAVDAFKSAPLYQRPGYYSAPQTPLSPTPMFFPLEPSAPSKLHSVTGIDTKDKSLKTVSSGAKKSFELLSESDGALMEHPEVSQVRRKTVEFNLTDMPEIPENHLKEPLEQSPTNIHTTLKDHMDPYWALENRDEAHS
| null | null |
chloride transport [GO:0006821]; detection of light stimulus involved in visual perception [GO:0050908]; gamma-aminobutyric acid secretion, neurotransmission [GO:0061534]; glutamate secretion [GO:0014047]; monoatomic ion transmembrane transport [GO:0034220]; protein complex oligomerization [GO:0051259]; regulation of calcium ion transport [GO:0051924]; regulation of synaptic plasticity [GO:0048167]; transepithelial chloride transport [GO:0030321]; visual perception [GO:0007601]
|
basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; chloride channel complex [GO:0034707]; cytosol [GO:0005829]; membrane [GO:0016020]; membrane microdomain [GO:0098857]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
bicarbonate channel activity [GO:0160133]; bicarbonate transmembrane transporter activity [GO:0015106]; chloride channel activity [GO:0005254]; identical protein binding [GO:0042802]; intracellular calcium activated chloride channel activity [GO:0005229]; ligand-gated channel activity [GO:0022834]
|
PF01062;
| null |
Anion channel-forming bestrophin (TC 1.A.46) family, Calcium-sensitive chloride channel subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26200502}; Multi-pass membrane protein {ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156}. Basolateral cell membrane {ECO:0000269|PubMed:19853238, ECO:0000269|PubMed:21330666, ECO:0000269|PubMed:26200502}; Multi-pass membrane protein {ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156}. Note=Localized at the surface membrane of microdomains adjacent to glutamatergic synapses. {ECO:0000250|UniProtKB:O88870}.
|
CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:11904445, ECO:0000269|PubMed:12907679, ECO:0000269|PubMed:18179881, ECO:0000269|PubMed:18400985, ECO:0000269|PubMed:19853238, ECO:0000269|PubMed:21330666, ECO:0000269|PubMed:26200502, ECO:0000269|PubMed:26720466, ECO:0000269|PubMed:35789156}; CATALYTIC ACTIVITY: Reaction=hydrogencarbonate(in) = hydrogencarbonate(out); Xref=Rhea:RHEA:28695, ChEBI:CHEBI:17544; Evidence={ECO:0000269|PubMed:18400985}; CATALYTIC ACTIVITY: Reaction=4-aminobutanoate(in) = 4-aminobutanoate(out); Xref=Rhea:RHEA:35035, ChEBI:CHEBI:59888; Evidence={ECO:0000250|UniProtKB:O88870}; CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:O88870};
| null | null | null | null |
FUNCTION: Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (PubMed:11904445, PubMed:12907679, PubMed:18179881, PubMed:18400985, PubMed:19853238, PubMed:21330666, PubMed:26200502, PubMed:26720466, PubMed:35789156). Allows the movement of chloride and hydrogencarbonate (PubMed:11904445, PubMed:12907679, PubMed:18179881, PubMed:18400985, PubMed:19853238, PubMed:21330666, PubMed:26200502, PubMed:26720466, PubMed:35789156). Found in a partially open conformation leading to significantly smaller chloride movement (PubMed:35789156). Upon F2R/PAR-1 activation, the sequestered calcium is released into the cytosol of astrocytes, leading to the (Ca2+)-dependent release of L-glutamate into the synaptic cleft that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (By similarity). Upon activation of the norepinephrine-alpha-1 adrenergic receptor signaling pathway, transports as well D-serine than L-glutamate in a (Ca2+)-dependent manner, leading to activation of adjacent NMDAR receptors and therefore regulates the heterosynaptic long-term depression and metaplasticity during initial memory acquisition (By similarity). Releases the 4-aminobutanoate neurotransmitter in a (Ca2+)-dependent manner, and participates in its tonic release from cerebellar glial cells (By similarity). {ECO:0000250|UniProtKB:O88870, ECO:0000269|PubMed:11904445, ECO:0000269|PubMed:12907679, ECO:0000269|PubMed:18179881, ECO:0000269|PubMed:18400985, ECO:0000269|PubMed:19853238, ECO:0000269|PubMed:21330666, ECO:0000269|PubMed:26200502, ECO:0000269|PubMed:26720466, ECO:0000269|PubMed:35789156}.
|
Homo sapiens (Human)
|
O76093
|
FGF18_HUMAN
|
MYSAPSACTCLCLHFLLLCFQVQVLVAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQPELQKPFKYTTVTKRSRRIRPTHPA
| null | null |
anatomical structure morphogenesis [GO:0009653]; angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; cell-cell signaling [GO:0007267]; chondrocyte development [GO:0002063]; endochondral ossification [GO:0001958]; ERK1 and ERK2 cascade [GO:0070371]; fibroblast growth factor receptor signaling pathway [GO:0008543]; intramembranous ossification [GO:0001957]; lung development [GO:0030324]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of endothelial cell chemotaxis to fibroblast growth factor [GO:2000546]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; regulation of cell migration [GO:0030334]; signal transduction [GO:0007165]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleolus [GO:0005730]
|
growth factor activity [GO:0008083]; type 1 fibroblast growth factor receptor binding [GO:0005105]; type 2 fibroblast growth factor receptor binding [GO:0005111]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation. {ECO:0000269|PubMed:16597617}.
|
Homo sapiens (Human)
|
O76094
|
SRP72_HUMAN
|
MASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGSFKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLYRLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEKVVPENLGLQEGTHELCYNTACALIGQGQLNQAMKILQKAEDLCRRSLSEDTDGTEEDPQAELAIIHGQMAYILQLQGRTEEALQLYNQIIKLKPTDVGLLAVIANNIITINKDQNVFDSKKKVKLTNAEGVEFKLSKKQLQAIEFNKALLAMYTNQAEQCRKISASLQSQSPEHLLPVLIQAAQLCREKQHTKAIELLQEFSDQHPENAAEIKLTMAQLKISQGNISKACLILRSIEELKHKPGMVSALVTMYSHEEDIDSAIEVFTQAIQWYQNHQPKSPAHLSLIREAANFKLKYGRKKEAISDLQQLWKQNPKDIHTLAQLISAYSLVDPEKAKALSKHLPSSDSMSLKVDVEALENSAGATYIRKKGGKVTGDSQPKEQGQGDLKKKKKKKKGKLPKNYDPKVTPDPERWLPMRERSYYRGRKKGKKKDQIGKGTQGATAGASSELDASKTVSSPPTSPRPGSAATVSASTSNIIPPRHQKPAGAPATKKKQQQKKKKGGKGGW
| null | null |
SRP-dependent cotranslational protein targeting to membrane [GO:0006614]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; signal recognition particle [GO:0048500]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786]
|
7S RNA binding [GO:0008312]; ribosome binding [GO:0043022]; RNA binding [GO:0003723]; signal recognition particle binding [GO:0005047]; TPR domain binding [GO:0030911]
|
PF08492;PF17004;PF13181;
|
1.25.40.10;
|
SRP72 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22541560}. Endoplasmic reticulum {ECO:0000269|PubMed:22541560, ECO:0000269|PubMed:28369529}.
| null | null | null | null | null |
FUNCTION: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (PubMed:34020957). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (PubMed:34020957). Binds the signal recognition particle RNA (7SL RNA) in presence of SRP68 (PubMed:21073748, PubMed:27899666). Can bind 7SL RNA with low affinity (PubMed:21073748, PubMed:27899666). The SRP complex possibly participates in the elongation arrest function (By similarity). {ECO:0000250|UniProtKB:P38688, ECO:0000269|PubMed:21073748, ECO:0000269|PubMed:27899666, ECO:0000269|PubMed:34020957}.
|
Homo sapiens (Human)
|
O76095
|
JTB_HUMAN
|
MLAGAGRPGLPQGRHLCWLLCAFTLKLCQAEAPVQEEKLSASTSNLPCWLVEEFVVAEECSPCSNFRAKTTPECGPTGYVEKITCSSSKRNEFKSCRSALMEQRLFWKFEGAVVCVALIFACLVIIRQRQLDRKALEKVRKQIESI
| null | null |
apoptotic mitochondrial changes [GO:0008637]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; positive regulation of protein kinase activity [GO:0045860]; regulation of cell population proliferation [GO:0042127]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; midbody [GO:0030496]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; spindle [GO:0005819]
|
protein kinase binding [GO:0019901]
|
PF05439;
|
3.30.720.220;
|
JTB family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Mitochondrion {ECO:0000250}. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Detected at the centrosome and along spindle fibers during prophase and metaphase. Detected at the midbody during telophase.
| null | null | null | null | null |
FUNCTION: Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity. Inhibits apoptosis induced by TGFB1 (By similarity). Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential (By similarity). {ECO:0000250, ECO:0000269|PubMed:21225229}.
|
Homo sapiens (Human)
|
O76096
|
CYTF_HUMAN
|
MRAAGTLLAFCCLVLSTTGGPSPDTCSQDLNSRVKPGFPKTIKTNDPGVLQAARYSVEKFNNCTNDMFLFKESRITRALVQIVKGLKYMLEVEIGRTTCKKNQHLRLDDCDFQTNHTLKQTLSCYSEVWVVPWLQHFEVPVLRCH
| null | null |
immune response [GO:0006955]; negative regulation of microglial cell activation [GO:1903979]; negative regulation of peptidase activity [GO:0010466]; positive regulation of myelination [GO:0031643]
|
cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764]; multivesicular body [GO:0005771]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; endopeptidase inhibitor activity [GO:0004866]; peptidase inhibitor activity [GO:0030414]; protein homodimerization activity [GO:0042803]
|
PF00031;
|
3.10.450.10;
|
Cystatin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12423348}. Cytoplasm {ECO:0000269|PubMed:12423348}.
| null | null | null | null | null |
FUNCTION: Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system.
|
Homo sapiens (Human)
|
O76321
|
RACG_ENTH1
|
MRPVKLVIVGDGAVGKTCMLISYTTNAFPNEYIPTVFENYNSSLVVDDVKINLGLWDTAGQEDYDRLRPLSYPSTDVFLVCFSVIAPASYENVEGKWKPEIDQHCPNVPIILVGTKIDIRDDPEQVKRLAEKNIVPIQPPQGDELAKKIGAVKYIECSALTQANLKLVFEEAVRAVLAKAAKEPTGKKEKGGKKGCSLF
|
3.6.5.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q24816};
|
cortical cytoskeleton organization [GO:0030865]; engulfment of apoptotic cell [GO:0043652]; establishment or maintenance of cell polarity [GO:0007163]; mitotic cytokinesis [GO:0000281]; motor neuron axon guidance [GO:0008045]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; small GTPase-mediated signal transduction [GO:0007264]
|
cell projection [GO:0042995]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rho family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63000}; Lipid-anchor {ECO:0000250|UniProtKB:P63000}; Cytoplasmic side {ECO:0000250|UniProtKB:P63000}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:9601102}. Cytoplasm {ECO:0000269|PubMed:9601102}. Note=Localizes to the uroid during capping of surface receptors. {ECO:0000269|PubMed:9601102}.
|
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=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P63000}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P63000};
| null | null | null | null |
FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (By similarity). Involved in actin cytoskeleton remodeling during capping of surface receptors and uroid formation (PubMed:9601102). {ECO:0000250|UniProtKB:P63000, ECO:0000269|PubMed:9601102}.
|
Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
|
O76324
|
DCO_DROME
|
MELRVGNKYRLGRKIGSGSFGDIYLGTTINTGEEVAIKLECIRTKHPQLHIESKFYKTMQGGIGIPRIIWCGSEGDYNVMVMELLGPSLEDLFNFCSRRFSLKTVLLLADQMISRIDYIHSRDFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKFRDARSLKHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGALPWQGLKAANKRQKYERISEKKLSTSIVVLCKGFPSEFVNYLNFCRQMHFDQRPDYCHLRKLFRNLFHRLGFTYDYVFDWNLLKFGGPRNPQAIQQAQDGADGQAGHDAVAAAAAVAAAAAASSHQQQQHKVNAALGGGGGSAAQQQLQGGQTLAMLGGNGGGNGSQLIGGNGLNMDDSMAATNSSRPPYDTPERRPSIRMRQGGGGGGGGVGVGGMPSGGGGGGVGNAK
|
2.7.11.1
| null |
behavioral response to cocaine [GO:0048148]; cell communication [GO:0007154]; cellular response to light stimulus [GO:0071482]; circadian rhythm [GO:0007623]; endocytosis [GO:0006897]; imaginal disc growth [GO:0007446]; locomotor rhythm [GO:0045475]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of smoothened signaling pathway [GO:0045879]; phosphorylation [GO:0016310]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell division [GO:0051781]; positive regulation of cell growth [GO:0030307]; positive regulation of hippo signaling [GO:0035332]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of smoothened signaling pathway [GO:0045880]; positive regulation of Wnt signaling pathway [GO:0030177]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of circadian rhythm [GO:0042752]; regulation of ecdysteroid secretion [GO:0007555]; regulation of establishment of planar polarity [GO:0090175]; signal transduction [GO:0007165]
|
cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26082158}. Cytoplasm, cytosol {ECO:0000269|PubMed:26082158}. Note=Detected in the nucleus and cytoplasm of the small and large lateral neurons (sLNv and lLNv). {ECO:0000269|PubMed:26082158}.
|
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: Serine/threonine-protein kinase which is involved in the circadian rhythm pathway, viability and planar cell polarity (PubMed:10556065, PubMed:26082158, PubMed:32750048, PubMed:9674430, PubMed:9674431). In the circadian rhythm pathway, phosphorylates the clock gene period (per) and targets it for degradation in the absence of timeless (tim), thus contributing to production of the circadian oscillations of the clock genes (PubMed:26082158, PubMed:32750048, PubMed:9674430, PubMed:9674431). Together with CkIalpha, regulates processing of ci by phosphorylating it, which promotes its binding to slmb, the F-box recognition component of the SCF(slmb) E3 ubiquitin-protein ligase (PubMed:16326393). Involved in the inhibition of apoptosis during cell proliferation and growth arrest in imaginal disks (PubMed:10556065). Also functions in planar cell polarity (PubMed:32750048). {ECO:0000269|PubMed:10556065, ECO:0000269|PubMed:16326393, ECO:0000269|PubMed:26082158, ECO:0000269|PubMed:32750048, ECO:0000269|PubMed:9674430, ECO:0000269|PubMed:9674431}.
|
Drosophila melanogaster (Fruit fly)
|
O76329
|
ACTNB_DICDI
|
MEHSTPLNEEIVHKKNDENWVIAQKKVFTNWCNIFLNQRSQKIEDLETDLYDGILLGSLLEILSGKNVILSKCKQLKTRLHYINNLNFSLKFIGDEGLRLVGVASEDITDGNLKLILGLVWTLILRYQIQSMQNSKSSQQNLHSSTKPSELMLNWVKSQISDYGHHIKDLTTSFQNGLLFCALVHKLVPEKLDYKSLSESDSLGNLTLAFEVANKELGIPSILDPHDIITTPDELSILTYISLFPKVYQQTLEPLNNNNNISPSLSSSSSSLLNTPNKRNSIQLSKSTSFEQQNQQQQQQNLLSPNSYRNSISFSKSPSFEGSQSTGSSRSISPISSPIKNSTTGNSNLSKSTSFEKIEASNTTNNNTIIIAEESRVIEKIVEKIIEVEKIVEVEKIVEVEKIVEVEKIVEVEKIVKVDDIEKLTNLQDQLTEQQQQYQEKSLKLVNLELELQEKSNQLVDKSNQLSTMQATNSELMEKIGGLMNDLTDIPTQDIKEKDEIIANLKIESEKNLKCFQDDFNALQSRYSLTIEQTSQLQDRIKQLINELQERDDKFIEFTNSSNQSLADNQRVIDQLTNEKQSITLQLQDQQDIKEKEFQFEKQQLLSQIDSITTNIQEYQDKFNNLQQEFNTQQTLNQQETHRLTQQLYQINTDYNEKQTQLQSEIKDNQTINEQLNKQLSEKDKEIEKLSNQQEQQQDEKINNLLLEIKEKDCLIERINQQLLENIDLNSKYQQLLLEFENFKLNSSKEKENQLNELQSKQDERFNQLNDEKLEKEKQLQSIEDEFNQYKQQQLSSNSNIDQQLQSTIIELSELKEQKELNDSKLIEKEKQLQQLQQEFDQLNEKNQKDHQDQLELLEKQLKQLQQEYDQLNETNQSIENQLNQQNLINKENLNEKEQELLKLQNQLNQQIEKIQFDQQEFSKQNSINIELVNEKNEKLIQLQQDYDQLKQQNRSNDEKDENDLIEKENQLKSIQNELNQLIEKNESDHKEQQLKQQSIENDLIEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNQFDQKEQQLKQQSIENDLFEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNESDQKEQQLKQQSIENDLIEKENQIQQLQLQLNEQRQLQSEVSIDNDKILELEKQLKQCQSDLLKLNDEKQQQDKQLQDKQIEFDQLQLTFNQFKNDKDSQFIQLQDDQKQQLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQFENQEKEKQLSEKDEKLQSIQQNLNQLNDENQEKVKQFSEKDEKLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQQDLNQLNDDQIKKNEKLKEKEEQLLKLQQDFNDQQSQQLKQLEEKLSEKENQLQQLKQENEINQLNQQQQSNEIIQQLKDQLLKQQQQEQQENNNEKEIERLIQEIEQLKQQQEIDQSELSNKEIKIQTTQQEFDQLSHNRSKDQLHLQQLQQELDQLKQSFDDQDHQFKKVIDERYNLQLQLEQSTLSNNQLDQLLKEKLKPLELDSNEKQKTIDDLLSNISNLQISLQNDKDLISERNNSIKTLESRITQQLSLLDEKDNLIKDLQQQKQQQQQPPTASSSPSSSPSLLSSTPTPKPQRPNQIEIDRLVNEIVNRNQDLIRKNKTKFYKLENGDYIVNSIIYRLSLDDDNDSDLIAQEYENGNSTTFEKSLRIFPSKNTRPIFDWRALFFIGAAVLAISTLFSSSRPIKYEKPT
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; cell-cell adhesion [GO:0098609]; sorocarp development [GO:0030587]; spore germination [GO:0009847]
|
actin filament bundle [GO:0032432]; actomyosin contractile ring [GO:0005826]; cell junction [GO:0030054]; cell projection [GO:0042995]; centrosome [GO:0005813]; cortical actin cytoskeleton [GO:0030864]; endoplasmic reticulum membrane [GO:0005789]; Golgi cisterna membrane [GO:0032580]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear outer membrane-endoplasmic reticulum membrane network [GO:0042175]; plasma membrane [GO:0005886]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; actin lateral binding [GO:0003786]
|
PF00307;
|
1.10.418.10;
|
Alpha-actinin family
| null |
SUBCELLULAR LOCATION: Nucleus membrane; Single-pass type IV membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane. Golgi apparatus, Golgi stack membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated either with the nuclear envelope, the Golgi membrane or the endoplasmic reticulum membrane.
| null | null | null | null | null |
FUNCTION: May function as linker between cellular membranes and the actin cytoskeleton. Required for normal development of fruiting bodies. {ECO:0000269|PubMed:10704840}.
|
Dictyostelium discoideum (Social amoeba)
|
O76337
|
CED6_CAEEL
|
MAKDIYKTFKRSVSGIVGGNNINGEGSSSPSTSAPQVKYRGGTGRTWIHPPDYLINGHVEYVARFLGCVETPKANGSDVAREAIHAIRFQRDLKRSEQTRETAKLQKVEIRISIDNVIIADIKTKAPMYTFPLGRISFCADDKDDKRMFSFIARAEGASGKPSCYAFTSEKLAEDITLTIGEAFDLAYKRFLDKNRTSLENQKQIYILKKKIVELETENQVLIERLAEALRANSKADYENTGPPIYPGLGPPALPLSPMPQGPPPNIPPSSIYSMPRANDLPPTEMAPTLPQISTSSNGASPSVSPASTSPSGPAPSIPPPRPPALAPPPPVAPRRNPVVSPKNSTAGLLDGLELGSAEPAKKAPSNIFDDSFDPRAGEKKSTAAEYNPFGADFLSGIQNGKEAPPSASAELLASEAIARLPKPESSSVPPKKTAAEYDAMINEVEKKLAAMSSGSFEFGQLQTGDLGGIEGESDYGTPSDRLNPKMMNLKQ
| null | null |
apoptotic process involved in development [GO:1902742]; engulfment of apoptotic cell [GO:0043652]; establishment of mitotic spindle orientation [GO:0000132]; left/right axis specification [GO:0070986]; positive regulation of apoptotic process involved in development [GO:1904747]; positive regulation of distal tip cell migration [GO:1903356]; positive regulation of engulfment of apoptotic cell [GO:1901076]; programmed cell death [GO:0012501]
|
cytoplasmic side of plasma membrane [GO:0009898]; phagocytic vesicle [GO:0045335]
|
clathrin adaptor activity [GO:0035615]; scavenger receptor binding [GO:0005124]
|
PF00640;
|
2.30.29.30;
|
Ced-6 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15744306}.
| null | null | null | null | null |
FUNCTION: May function as an adapter protein in a pathway that mediates recognition and phagocytosis of apoptotic cells during normal development. Promotes engulfment of cells at both early and late stages of apoptosis. Required for actin reorganization around apoptotic cells. Plays a role in protecting dopaminergic neurons from oxidative stress-induced degeneration (PubMed:29346382). Mediates recruitment of E3 ubiquitin-protein ligase trim-21 to the apoptotic cell surface which promotes ubiquitination and degradation of ced-1 (PubMed:35929733). {ECO:0000269|PubMed:15744306, ECO:0000269|PubMed:29346382, ECO:0000269|PubMed:35929733, ECO:0000269|PubMed:9635426}.
|
Caenorhabditis elegans
|
O76357
|
ILYS3_CAEEL
|
MFVKSLVFLTIAVAYASADCLHCICMRESGCKPIGCNMDVGSLSCGYYQIKLPYYEDCGQPTKKSGETTEAAWKRCANDLSCATTCVENYYNRYKSQCAGTGQGACEVMARNHNGGPQGCKHSGTLGYWNGIKSCCGCS
|
3.2.1.17
| null |
antibacterial innate immune response [GO:0140367]; defense response to Gram-positive bacterium [GO:0050830]; digestion [GO:0007586]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152]
|
extracellular region [GO:0005576]; late endosome lumen [GO:0031906]; lysosomal lumen [GO:0043202]; recycling endosome lumen [GO:0034777]
|
lysozyme activity [GO:0003796]
|
PF05497;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family, Type-I lysozyme subfamily
| null |
SUBCELLULAR LOCATION: Late endosome lumen {ECO:0000269|PubMed:27525822}. Recycling endosome lumen {ECO:0000269|PubMed:27525822}. Lysosome lumen {ECO:0000269|PubMed:27525822}. Secreted {ECO:0000269|PubMed:27525822}. Note=Predominantly localizes to the recycling endosomal network in the basolateral region of intestinal cells. Secreted in the intestinal lumen only during dauer arrest stage, aging, or starvation. {ECO:0000269|PubMed:27525822}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000305|PubMed:27525822};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5. {ECO:0000269|PubMed:27525822};
| null |
FUNCTION: Has bacteriolytic activity against Gram-positive bacteria. Plays a role in defense against bacterial pathogens. Involved in pharyngeal grinder function by enabling proper lysis of ingested bacteria. {ECO:0000269|PubMed:27525822}.
|
Caenorhabditis elegans
|
O76360
|
EGL4_CAEEL
|
MSSGSRPSSGGGGGGGGASGGAGGGAPGGGGGGIRGFFSKLRKPSDQPNGNQVQVGTRTFEAHELQKLIPQLEEAISRKDAQLRQQQTIVEGHIKRISELEGEVTTLQRECDKLRSVLEQKAQSAASPGGQPPSPSPRTDQLGNDLQQKAVLPADGVQRAKKIAVSAEPTNFENKPATLQHYNKTVGAKQMIRDAVQKNDFLKQLAKEQIIELVNCMYEMRARAGQWVIQEGEPGDRLFVVAEGELQVSREGALLGKMRAGTVMGELAILYNCTRTASVQALTDVQLWVLDRSVFQMITQRLGMERHSQLMNFLTKVSIFQNLSEDRISKMADVMDQDYYDGGHYIIRQGEKGDAFFVINSGQVKVTQQIEGETEPREIRVLNQGDFFGERALLGEEVRTANIIAQAPGVEVLTLDRESFGKLIGDLESLKKDYGDKERLAQVVREPPSPVKIVDDFREEFAQVTLKNVKRLATLGVGGFGRVELVCVNGDKAKTFALKALKKKHIVDTRQQEHIFAERNIMMETSTDWIVKLYKTFRDQKFVYMLLEVCLGGELWTTLRDRGHFDDYTARFYVACVLEGLEYLHRKNIVYRDLKPENCLLANTGYLKLVDFGFAKKLASGRKTWTFCGTPEYVSPEIILNKGHDQAADYWALGIYICELMLGRPPFQASDPMKTYTLILKGVDALEIPNRRIGKTATALVKKLCRDNPGERLGSGSGGVNDIRKHRWFMGFDWEGLRSRTLKPPILPKVSNPADVTNFDNYPPDNDVPPDEFSGWDEGF
|
2.7.11.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11181837, ECO:0000269|PubMed:12571101};
|
chemosensory behavior [GO:0007635]; chemotaxis [GO:0006935]; chemotropism [GO:0043577]; determination of adult lifespan [GO:0008340]; insulin receptor signaling pathway [GO:0008286]; larval feeding behavior [GO:0030536]; negative regulation of calcium-mediated signaling [GO:0050849]; negative regulation of cell growth [GO:0030308]; negative regulation of cGMP-mediated signaling [GO:0010754]; negative regulation of dauer larval development [GO:0061067]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of organ growth [GO:0046621]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; olfactory learning [GO:0008355]; phosphorylation [GO:0016310]; positive regulation of cellular response to alcohol [GO:1905959]; positive regulation of cGMP-mediated signaling [GO:0010753]; positive regulation of chemotaxis [GO:0050921]; positive regulation of egg-laying behavior [GO:1901046]; positive regulation of gene expression [GO:0010628]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of eating behavior [GO:1903998]; regulation of egg-laying behavior [GO:0046662]; regulation of gene expression [GO:0010468]; regulation of multicellular organism growth [GO:0040014]; response to alcohol [GO:0097305]; response to hydrogen peroxide [GO:0042542]; response to odorant [GO:1990834]; response to oxygen levels [GO:0070482]; sensory perception of bitter taste [GO:0050913]; signal transduction [GO:0007165]; sleep [GO:0030431]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; cGMP binding [GO:0030553]; cGMP-dependent protein kinase activity [GO:0004692]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]
|
PF00027;PF00069;
|
2.60.120.10;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cGMP subfamily
|
PTM: Autophosphorylated. {ECO:0000269|PubMed:11181837}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20220099, ECO:0000269|PubMed:22319638, ECO:0000269|PubMed:23874221, ECO:0000269|PubMed:23954825, ECO:0000269|PubMed:27383131}. Nucleus {ECO:0000269|PubMed:20220099, ECO:0000269|PubMed:21573134, ECO:0000269|PubMed:22319638, ECO:0000269|PubMed:23874221, ECO:0000269|PubMed:23954825, ECO:0000269|PubMed:27383131}. Note=In resting AWC sensory neurons, localizes in cytoplasm (PubMed:20220099, PubMed:23954825, PubMed:27383131). Prolonged exposure to attractive odorants sensed by AWC neurons results in nuclear translocation (PubMed:20220099, PubMed:23954825, PubMed:27383131). Nuclear translocation is required for the adaptation to prolonged odor exposure and is controlled by G(o)-alpha subunit protein goa-1 (PubMed:20220099, PubMed:23954825, PubMed:27383131). Localization is regulated by cGMP levels: high cGMP levels result in cytoplasmic localization whereas low cGMP levels result in nuclear localization (PubMed:20220099, PubMed:22319638). Nuclear localization in AWC neurons is dependent on age-1 (PubMed:27383131). In addition, an intact sensory cilia structure is required for cytoplasmic localization in resting AWC neurons (PubMed:22319638). In resting AWB sensory neurons, constitutive nuclear localization is dependent on goa-1 (PubMed:23954825). In resting ASH sensory neurons, localizes in both cytoplasm and nucleus (PubMed:23874221). Cytoplasmic localization is important for negative regulation of quinine sensitivity in ASH neurons (PubMed:23874221). {ECO:0000269|PubMed:20220099, ECO:0000269|PubMed:22319638, ECO:0000269|PubMed:23874221, ECO:0000269|PubMed:23954825, ECO:0000269|PubMed:27383131}.
|
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=2.7.11.12; Evidence={ECO:0000269|PubMed:11181837, ECO:0000269|PubMed:12571101, ECO:0000269|PubMed:21573134}; 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=2.7.11.12; Evidence={ECO:0000269|PubMed:11181837, ECO:0000269|PubMed:12571101, ECO:0000269|PubMed:21573134};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=2.1 umol/min/mg enzyme towards cGMP (Isoform c at pH 6.8 and 30 degrees Celsius) {ECO:0000269|PubMed:11181837};
| null | null | null |
FUNCTION: Promotes chemoreceptor gene expression in response to increased cGMP levels by antagonizing the gene repression functions of the class II HDAC hda-4 and the mef-2 transcription factor (PubMed:18832350). Regulates gene expression via recruitment of a histone deacetylase complex containing hda-2, saeg-1 and saeg-2 (PubMed:21573134). Represses body size and lifespan through the dbl-1 and insulin pathways, respectively (PubMed:12571101, PubMed:15330854, PubMed:26434723). May also signal through daf-3 and/or daf-5. Role in egg-laying, dauer formation and motility (PubMed:11181837, PubMed:12571101, PubMed:21573134). Regulates behavioral responses to various chemosensory stimuli in sensory neurons (PubMed:10978280, PubMed:22319638, PubMed:23874221, PubMed:26434723). Required for the initiation of long term adaptation to prolonged odor exposure which results in a decrease in odor seeking behavior (PubMed:12495623, PubMed:20220099, PubMed:26434723). May regulate this process by phosphorylating tax-2, a subunit of cyclic nucleotide-gated channel tax-2/tax-4 (PubMed:12495623). In ASH sensory neurons, negatively regulates avoidance behavior to some bitter tastants, such as quinine, probably by phosphorylating rgs-2 and rgs-3 which are 2 regulator of G-protein signaling proteins (PubMed:23874221). In AWB sensory neurons, involved in avoidance behavior to some repellent odors (PubMed:23954825). In ASE left (ASEL) sensory neuron, involved in the sensing of environmental alkalinity downstream of receptor-type guanylate cyclase gcy-14 (PubMed:23664973). In sensory neurons, involved in the signaling pathway downstream of insulin, TGF-beta and receptor-type guanylate cyclase responsible for inducing quiescence after food intake (PubMed:18316030). Might play a role in aversive olfactory learning in AWC neurons when an odor is associated with food deprivation, depending on the ins-1/age-1 signal from the AIA to the AWC neurons (PubMed:27383131). Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 in ALA neurons, involved in the decrease in locomotion during the quiescent state that precedes each larval molt (PubMed:17891142). {ECO:0000269|PubMed:11181837, ECO:0000269|PubMed:12571101, ECO:0000269|PubMed:15330854, ECO:0000269|PubMed:16547093, ECO:0000269|PubMed:17891142, ECO:0000269|PubMed:18316030, ECO:0000269|PubMed:18832350, ECO:0000269|PubMed:20220099, ECO:0000269|PubMed:21573134, ECO:0000269|PubMed:22319638, ECO:0000269|PubMed:23664973, ECO:0000269|PubMed:23874221, ECO:0000269|PubMed:23954825, ECO:0000269|PubMed:26434723, ECO:0000269|PubMed:27383131, ECO:0000305|PubMed:12495623}.
|
Caenorhabditis elegans
|
O76365
|
CTU1_CAEEL
|
MEKRRGPPPCQSGSGCSNPAKIRKAKDGAQLCGPCFSRNFEDDVHEAIVNNKLFKRGERVAIGASGGKDSTVLAYVMKTLNDRHDYGLDLQLLSIDEGIKGYRDDSLLAVEKNRVEYGLPLTILSYRDLYGWTMDDIVAKIGKKNNCTFCGVFRRQALDRGAFKIGATKLVTGHNADDMAETLLMNVLRGDIARLERCTNIVTGEEGDLPRAKPLKYCFERDIVMYARTNQLEYFYTECIYAPNAYRGYARKYVRDLEKVHPRAILDLIRSGEKVSVKKEVEMPTLKICERCGYMTSQKLCKACLLIEGLNTGNTDLGVRKSKKSKKVTVEADELNKEGGCGSGGGGGGCGCAGAEDAAENEETRQRLKDLQF
|
2.7.7.-
| null |
embryonic morphogenesis [GO:0048598]; oocyte development [GO:0048599]; protein urmylation [GO:0032447]; spermatogenesis [GO:0007283]; translation [GO:0006412]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098]; vulval development [GO:0040025]
|
cytosol [GO:0005829]; cytosolic tRNA wobble base thiouridylase complex [GO:0002144]; mitochondrion [GO:0005739]
|
nucleotidyltransferase activity [GO:0016779]; sulfurtransferase activity [GO:0016783]; tRNA binding [GO:0000049]
|
PF01171;PF16503;
|
3.40.50.620;
|
TtcA family, CTU1/NCS6/ATPBD3 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053}.
| null | null |
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
| null | null |
FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:18391219}.
|
Caenorhabditis elegans
|
O76373
|
CBPC1_CAEEL
|
MPSDSDDVAAVKQPWSQLIVDISNFLSEHPQSKTSQALLPSCNGVWSDEEKLELIEAFGHKKQSHLTKSGVKAVLAAFEGDRTQPDVIFLCRLLHLIFSHFSSENDRKKEKYIVKCDVIATLTRITRKRIIMTLDVTDESSIDHNLDEVLWKLLHKIGLKDPRVSLKVRMGGLISPMCKLFIQKDTLPELFLPFFIKISRSPRNGQAIGRYEGFMTRLLVKIKALDASDQTSQVLLLDKHLQLLFFTMKNKRTRTQLLRENICKYLLEVLRRHLASSSNSRPTRLLSSLFGTFDKSLSAAHTEVVIGTIAILRLLSNFKKARDELKNLQVLDICSRELKEFWSDEWKTGPKSRIVDSLSALCLRCMSPLPYPLETRRFPIDFPLPTATPSTPGGHGRIRNSSSINISFDNGRSSDEDGMDEEDEAFVRDDDDEGKDDRGSDDDDGKDDDEINGALPKTTRLNPQQLAKYAPFFVENEQGTLQPTFSMIYQTNQESWRSICEKTRHVMPIHHHLPIEMFNTPTRIREKTAKTSNNMKKMIIEELDKPERSATSNQVIYDLDTAAFDGLPSPELPFVTGGGKLDTSKDLQFDSRFESGNLRMVIQVAPTHYELFLSPDVNQLRDHYQWFFFQVSNMRKSVKYTFEIVNCLKSTSLYSQGMQPVMYSMMESANGWRRVGENVCYFRNLYINENEEKKNVEEQKKKKYYYSIRFNVTFQNTGDICYIAYHYPYTYSFLNSSLSMLKKRKQENVYCREDVIGHSLAGNPIKMLTITTPASAAEIAAREVIVLSARVHPGETNASWIMQGILENLLCRQSNEMYRLRESFIFKIVPMINPDGVTNGSHRCSLAGIDLNRMWDRPNEALHPEVFATKAIIQYLCEVANKKPFAYVDIHGHSKKWDYFVYGNNASESWRADDVLDVGAAQLEEELHLALPKALEATCPSRFNASECRFNITRAKESSARVNVWRQFGVSTAYTLESTFCGFHKGQNSGYQINTSDLKEIGRDLLHSFLEMTKT
|
3.4.17.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
|
egg-laying behavior [GO:0018991]; proteolysis [GO:0006508]
|
cilium [GO:0005929]; dendrite [GO:0030425]; perikaryon [GO:0043204]
|
metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270]
|
PF18027;PF00246;
|
2.60.40.3120;3.40.630.10;
|
Peptidase M14 family
| null |
SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:21982591}. Cell projection, cilium {ECO:0000269|PubMed:21982591}. Cell projection, dendrite {ECO:0000269|PubMed:21982591}.
| null | null | null | null | null |
FUNCTION: Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia (PubMed:21982591, PubMed:29129530). In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles (PubMed:29129530). Also regulates microtubule dynamics in uterine muscle cells (PubMed:24780738). {ECO:0000269|PubMed:21982591, ECO:0000269|PubMed:24780738, ECO:0000269|PubMed:29129530, ECO:0000305|PubMed:21982591, ECO:0000305|PubMed:29129530}.
|
Caenorhabditis elegans
|
O76411
|
SCD2_CAEEL
|
MRKRRLWWFVVLFRVTLVGAILPNETFDVRRYYADRFLIEDEENGSSRSYYISAESKAKAAEQFALLAPNCSLTSDIQENTCNETSSFCDHRVDSTYKTYHYEQEKCNCFIETCDEETNSTELMVLYPDCYCGKREKHCDLSKEKCHWTPDSDHDDLKFEVFESSNKVLFDYMLQAGSEKANLKMNKVSMVSKFFRQSGFNCSLRFMHHFTHQSSTSRLVVRSILQSGEKKNLYEHWLKPASVFWVPVQVAIGSYAEPFKISIDCETGFPPKKKKNKPFTCSIADIYFENCGEIRDPIEQCSRGDQFLCSISANTRCLQNAQCDSRIDCDDESDEMDCGNINGTMCDFNGQDYCNSWYQVTNVTDYHERLSEPTTVAPLNKLNEVPLHLFRLQSPSAKIKEAMRGSGNMLVFDHKPNPLTRRTSALVSPELPRTNPEAYDEKSPLFKSCKLRFYLCSRTYSKVWQISVISKGINPMESGRTIIYEAGYTLIPKENCTWERVFVNIPRQNAGFRIGIFVTNYFPGSEEYVAIDNLSFSPTCFERDINQSTWDIPDLFINTCGASGFEQPQNCDHNRELDGQTGHFLKEDGTQQWTVPVTGFYRMEICGAGGGSNSKASGDTGDCVTLQVHLIENLSLRMLIGQMGESPCFTEHDDELRPSSCSKISHNYVYDGKRGAAGGGATLLTVEKDLWNVVAGGGAGASWDGFDMEVGYGASAIHVKPDQRCNETCKAVSHTDFIVERRDNRCPGEKGESTVFGGFGGGGNSCGMLGGSGAGYQAGNPFGKSRARSGSSNVSIDFSKSPIYYQSERLDEGYIKIAFCRKRCEPPTVCRFRKDYFEEEYCGCPDGSNVTDTEEACAFPLVCPSSSTNQYRNFTYEPFCLCNNGKEIYDVYNDTCEEIQIWTLYNITFLIFAALTIIGALFVVYHYRNREKQMKQEILDLTQMKSPDYLYDDIYFGRTTRKAALDSLPSISRDSIERGRVLGRGNFGEVYYGEYSGVKLAVKMISRTFSASQASQSDFCNEALCMGTFVDENVVRLIGIDFEKVPYMIALEYMEGGDLLSFVKECRPNQVSLNPFQLAMSDLIKICCDVAAGCKCLETFGYVHRDIAARNILLTTRGPQRVAKIADFGMAKEITYGTEYYRINGRTMMPIKWTPPEAFIDGVFTTKSDIWSFGVLCWEVFSLGVVPYPNRRNEEVMLMLTEGARLEYPYGIPTRVYQLMRDCWKTAAADRPKFVDVVEIFQDIQDDPASVGMPFPIHPAVRATFAHSQSTPVSVETPMTAMTEISLNSTFTDASTVKVSAQQDMQDRIQLHELMLTREHPYTSELTSYVVNSIRKDLARVQYENGLTSVPQPEYLSPENNDESVQLIPQSNTVTDQTPPTSLIDLNRLGVQNTGPTLHRPDSLNFNDPYSSVPLLECQTR
|
2.7.10.1
| null |
chemotaxis [GO:0006935]; dauer larval development [GO:0040024]; phosphorylation [GO:0016310]; regulation of cell population proliferation [GO:0042127]; regulation of neuron differentiation [GO:0045664]; sensory perception of chemical stimulus [GO:0007606]; sensory processing [GO:0050893]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
|
PF12810;PF07714;
|
2.60.120.200;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
|
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=2.7.10.1; Evidence={ECO:0000305};
| null | null | null | null |
FUNCTION: Probable tyrosine-protein kinase receptor which regulates the dauer/non-dauer developmental decision probably by controlling daf-3 transcriptional activity in parallel or together with the TGF-beta pathway (PubMed:11063683, PubMed:18674914). Regulates integration of conflicting sensory cues in AIA interneurons (PubMed:21414922). May act as a receptor for hen-1 (PubMed:18674914, PubMed:21414922). In AWA neurons, together with hen-1, plays a role in regulating olfactory adaptation by controlling the forgetting sensory responses to odorants such as diacetyl (PubMed:28924007). {ECO:0000269|PubMed:11063683, ECO:0000269|PubMed:18674914, ECO:0000269|PubMed:21414922, ECO:0000269|PubMed:28924007}.
|
Caenorhabditis elegans
|
O76460
|
RAD54_DROME
|
MRRSLAPSQRGPLRPESRHSFTPPLLKKNKRSCQQELEREQELDRRRLGALRDASNTSELPLPIRFTANSEYELAIAKVLARKFKVPMDNYVPDYGGKRVLGVRRCISRRPLHDPMACNALVLFHPPAYTEHERMGMDPTKVLVHVVVDPLLSNILRPHQREGVRFMYECVEGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVDQCIIRRTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKSDQVRRSLADCNEKASLTALADITTLKKICSHPDLIYEKLTAREKGFENSQNVLPSNYKPKDLNPELSGKFMLLDFMLAAIRAEGNDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLVASGSIEEKILQRQTHKKSLSSTIIDNNESAEKHFTRDDLKDLFTFDANILSDTHDKLKCKRCVQNIQMKPPPEDTDCTSHLSQWYHCSNNRGLPDNILAQAWMDCKCVSFVFHHRSQAQEIVPSAEEEATDQPEEKPESRKRSSTPASDDSADEDFRGF
|
3.6.4.-
| null |
cell division [GO:0051301]; chromatin remodeling [GO:0006338]; DNA synthesis involved in double-strand break repair via homologous recombination [GO:0043150]; dorsal appendage formation [GO:0046843]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; intracellular mRNA localization [GO:0008298]; meiotic DNA repair synthesis [GO:0000711]; oocyte fate determination [GO:0030716]; oogenesis [GO:0048477]; reciprocal meiotic recombination [GO:0007131]; regulation of translation [GO:0006417]; response to ionizing radiation [GO:0010212]; transcription-coupled nucleotide-excision repair [GO:0006283]
|
nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]
|
PF00271;PF00176;
|
3.40.50.300;1.20.120.850;3.40.50.10810;
|
SNF2/RAD54 helicase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9732269}.
| null | null | null | null | null |
FUNCTION: Involved in mitotic DNA repair and meiotic recombination. Functions in the recombinational DNA repair pathway. Essential for interhomolog gene conversion (GC), but may have a less important role in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51 enhances the ATPase activity of okr/Rad54. {ECO:0000269|PubMed:15105430, ECO:0000269|PubMed:17660539, ECO:0000269|PubMed:9315669, ECO:0000269|PubMed:9732269}.
|
Drosophila melanogaster (Fruit fly)
|
O76512
|
RENT1_CAEEL
|
MDDSDDEYSRSHGETLTFVDPEDDGVSIGNTQDSQFAYEQFSVPTQSSQATDLLPGGTDGTTNDLPFHDVEDDESDSEKSLTEEQHEQKLPEHACRYCGISDPLCVAKCTVCRKWFCNSNDGTSGGHIVHHMVRSQHKEAYTHKDSPCGDTQLECYRCGSKNVFNLGFIPGKKDQVVVIICRTPCASIAFQNDDNWSPEDWKSVIAEKQLLSWIVNVPSEEQVARARKITATQAVRMEELWRDHPEATVDDLNKPGLDREPDHVQLRYVDAHHYSKVFRPLVAIEAEYDRRVKESASQAVGTVRWEQGLRQSVLAFFHLPQFADGVMKLAKGDELRLKHSQTVDGSEWTKIGSVFKIPDNHGDEVGIEIRGAVDKSVMESRIMFTVDVVWNATTFERQYKALAALLNDSKAISPYLYQKLLGHPAEEMMLKFDLPRRLSVAGLPELNSSQMQAVKQVLTRPLSLIQGPPGTGKTVVSATIVYHLVQKTEGNVLVCSPSNIAVDHLAEKIHKTGLKVVRLCARSREHSETTVPYLTLQHQLKVMGGAELQKLIQLKDEAGELEFKDDLRYMQLKRVKEHELLAAADVICCTCSSAADARLSKIRTRTVLIDESTQATEPEILVSIMRGVRQLVLVGDHCQLGPVVICKKAAIAGLSQSLFERLVLLGIRPFRLQVQYRMHPVLSEFPSNVFYDGSLQNGVTENDRHMTGVDWHWPKPNKPAFFWHCSGSEELSASGTSFLNRTEAANVEKLVSKLIKAGVQPHQIGVITSYEGQRSFIVNYMHTQGTLNSKLYENVEIASVDAFQGREKDYIIVTCVRSNDILGIGFLSDPRRLNVAITRAKYGLVLVGNAKVLARHDLWHELINHYKSKEMLYEGPINALKPLNLALPKATIRTKNNIAGNANRFGIKRMQYTFNEYKSNDPSQPRLPPTYSNSQNLLSMSKLAQTFNKNVPIPAHMMDPNVYAAARNQKDRRRGDQRRPPPQAEAAMDLSQGMMSQQSQQYPPQGASSQSQYLLDGASSLSGWSQSQTTTTTTRHHHHRQNRNSQQQMSQDMDDIQQKMDDLLFSQDC
|
3.6.4.12; 3.6.4.13
| null |
DNA duplex unwinding [GO:0032508]; embryonic genitalia morphogenesis [GO:0030538]; ncRNA metabolic process [GO:0034660]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded DNA helicase activity [GO:0036121]; protein phosphatase 2A binding [GO:0051721]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270]
|
PF13086;PF13087;PF18141;PF09416;
|
2.40.30.230;6.10.140.1240;3.40.50.300;
|
DNA2/NAM7 helicase family
|
PTM: Phosphorylated probably by smg-1. Smg-3 and smg-4 are required for phosphorylation.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q92900}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q92900}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q92900}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q92900};
| null | null | null | null |
FUNCTION: RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. The formation of an smg-2-3-4 surveillance complex is believed to activate NMD (By similarity). {ECO:0000250|UniProtKB:Q92900}.
|
Caenorhabditis elegans
|
O76584
|
GPA11_CAEEL
|
MSAADMARKNSLINRQLEKEKIDSKKMLKILLLGGPECGKSTIFKQMKIIHMNGFSDLDYVNFRYLIYSNIMQSMDQLLEAAEFFHFPPDDSPSIRRALNHYKSYKVRYSTSEVELNRELADSLSKLYNAEFIKSVLNRKNELKLLDSAVYFLDDIDRISAHEYKPTEMDVLRARVPTTGITEIEFPFKQASLRMVDVGGQRSEQRKWIHCFDNVNGVLFIAAISGYNLYDEDEENRKDDGTPTKTNRLRYSMELFKRIANHQCFSKKTAMILFLNKIDIFKEKIGKYPLTTCFKNYKGVNAFEPACKYVTDRFSRLVSGDIQHEKPLYTHITNATDTRNIDRVFDSCMDVIFKISMEKVGFM
| null | null |
adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; determination of adult lifespan [GO:0008340]; G protein-coupled receptor signaling pathway [GO:0007186]; serotonin receptor signaling pathway [GO:0007210]
|
cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834]
|
G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]
|
PF00503;
|
1.10.400.10;3.40.50.300;
|
G-alpha family
| null | null | null | null | null | null | null |
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Mediates the transduction of food and serotonin signals, which modulates the avoidance response to the odorant octanol. Has a role in lifespan to promote longevity. {ECO:0000269|PubMed:15492222, ECO:0000269|PubMed:17187771}.
|
Caenorhabditis elegans
|
O76616
|
PID3_CAEEL
|
MVAHQKADFKSKWAMVVTVNNLNDKKRADLREFSEWFIETLRLEGAFIGHYFNYEAAPVTIVETLPGNFDSCTNAYQKIHKEHPQVVLVVHILPQSQSNEYEWMKVLASRYGFVRQGLLYDNCANRFQNVETDQNSVFRNMCQWIYRSGTAIVRNEGNACGILHGKDPKPTFDKVLFNSEDIKDSVFKVLHAEEEPRGADQENMLKISGYPGMLNTFGIAQLLTPYRVNGITITGAQSAVVALENKFQVYQAVQDFNGKKLDRNHKLQVSSLVVSSPAVPLEWPSLKKSKKLVEQVGKPIRLSKVSS
| null | null |
21U-RNA metabolic process [GO:0034585]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; embryo development ending in birth or egg hatching [GO:0009792]; piRNA processing [GO:0034587]; positive regulation of cell division [GO:0051781]; positive regulation of chromosome segregation [GO:0051984]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RNA cap binding complex [GO:0034518]
| null | null |
3.40.50.2300;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31147388}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388}. Nucleus {ECO:0000269|PubMed:31216475}. Note=Dispersedly distributes throughout the cytoplasm in early embryos (PubMed:31147388). During early embryogenesis, localizes to the nucleus at prophase of cell division, and remains in the cytosol at interphase in 2- and 4-cell embryos (PubMed:31216475). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31147388). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
| null | null | null | null | null |
FUNCTION: Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the pid-1 variant of the PETISCO complex may stabilize 21U-RNA precursor molecules (PubMed:31147388). Promotes the biogenesis of 21U-RNAs (PubMed:31216475). Required for chromosome segregation and cell division in early embryos (PubMed:31216475). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475, ECO:0000305|PubMed:31216475}.
|
Caenorhabditis elegans
|
O76689
|
SNF6_CAEEL
|
MSVSSNDPEQRNGRGMASGNNVDMSLYPPFIKQLDAKLPDYTREGDIEYPFEEITGVGDENRIRGNWSNKSDYLLAVIGFTAGVGSFWKFPFLVFQHGGAAFLVPYLCMLCLASLPMFFMEMVLGQFSSSAAISVWKVVPLFKGIGFAQVTISGFFAVFFNIISAWTLFYLINSFSFSIPWSNCANSWSGENCTLGTRIQCKEMNGTLLVNGSCIVEHASSNETTVIPLHDLGSIPSLKYFHNDVLMLSKGVDDFGTLNWYLGLCVLACWIAVFLCLFQGVKSSGKVVYVAVIVPFIILTVLLTRLLTLDGSLAAVFYFLTPKWEILMDLHVWGEAAVQAFYSVSCCSGGLFTIASYSRFHNNIYKDIWLVLIVDVIVSLVGCLLTFSAIGFTCYEFAISLDKFHIRDGFHLVFVFLAEALAGVSVAPLYAGLFFIMILLVVHATQMFVVETIVSSICDEYPERLRRNRRHVLTTVCALFILLSIPFCLSSGLFWMELLTQFVLTWPLVVIAFLECMAINWVYGVDNMLDNAKWIVGYWPPCYIFWKILFKFICPMVYLAILCFLWLDWNSIQYESYQFPYWSILTAWCIASFPLILIPIVGIWQFCIAKGTITQKWWRVLYPDDAWGPAMAIHRAEKFPLQIPEARRLLLPPEVEIASSRGVLQEEMPMSYDYNTSSAADVRSNRSTGHGATDVRSVAATNNTIPKFERETAI
| null | null |
acetylcholine transport [GO:0015870]; amino acid import across plasma membrane [GO:0089718]; choline transport [GO:0015871]; neuromuscular synaptic transmission [GO:0007274]; neurotransmitter uptake [GO:0001504]; positive regulation of locomotion [GO:0040017]; sodium ion transmembrane transport [GO:0035725]
|
plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]
|
acetylcholine transmembrane transporter activity [GO:0005277]; glycine:sodium symporter activity [GO:0015375]; neurotransmitter:sodium symporter activity [GO:0005328]; PDZ domain binding [GO:0030165]
|
PF00209;
| null |
Sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15318222}; Multi-pass membrane protein {ECO:0000269|PubMed:15318222}. Postsynaptic cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The DGC is not necessary to establish snf-6 at the postsynaptic membrane, but it is required for maintenance or stabilization.
| null | null | null | null | null |
FUNCTION: Mediates sodium-dependent uptake of acetylcholine at neuromuscular junctions during periods of increased synaptic activity, may also prevent spillover to adjacent synaptic sites. Not involved in the uptake of other neurotransmitters (GABA, glycine, proline and glutamate) and there was also no inhibition of uptake by adding an excess of other candidate substrates (GABA, glycine, taurine, creatine, proline, alanine, carnitine, glutamate and betaine). Required for muscle integrity; altered transport of acetylcholine due to loss of dystrophin-glycoprotein complex (DGC) function results in muscle degeneration. {ECO:0000269|PubMed:15318222}.
|
Caenorhabditis elegans
|
O76742
|
RAB7_DROME
|
MSGRKKSLLKVIILGDSSVGKTSLMNQYVNKRFSNQYKATIGADFCTKEVVVNDRVVTMQIWDTAGQERFQSLGVAFYRGADCCVLVYDVTAPNSFKNLDSWRDEFLIQASPRDPDHFPFVVLGNKVDLDNRQVSTRRAQQWCQSKNDIPYYETSAKEGINVEMAFQVIAKNALELEAEAEVINDFPDQITLGSQNNRPGNPDNCQC
|
3.6.5.2
| null |
autophagosome-lysosome fusion [GO:0061909]; border follicle cell migration [GO:0007298]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dsRNA transport [GO:0033227]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; endosomal vesicle fusion [GO:0034058]; endosome to lysosome transport [GO:0008333]; endosome to lysosome transport via multivesicular body sorting pathway [GO:0032510]; exosomal secretion [GO:1990182]; phagosome-lysosome fusion [GO:0090385]; positive regulation of endocytic recycling [GO:2001137]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; regulation of vacuole fusion, non-autophagic [GO:0032889]; symbiont entry into host cell [GO:0046718]; T-tubule organization [GO:0033292]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]; wing disc dorsal/ventral pattern formation [GO:0048190]
|
autophagosome membrane [GO:0000421]; cell cortex [GO:0005938]; cell projection [GO:0042995]; early endosome membrane [GO:0031901]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; synapse [GO:0045202]; vesicle [GO:0031982]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
| null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:24327558}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:11136982, ECO:0000269|PubMed:23418349, ECO:0000269|PubMed:24327558}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:24327558}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:27559127, ECO:0000269|PubMed:28483915}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Autolysosome membrane {ECO:0000269|PubMed:28483915}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Presynapse {ECO:0000269|PubMed:24327558, ECO:0000269|PubMed:32658990}. Perikaryon {ECO:0000269|PubMed:24327558}. Note=Partially colocalizes with the early endosomal marker Rab5 and the lysosomal marker spin/spinster (PubMed:24327558). Recruited to endosomal and autophagosomal membranes in a Mon1-Ccz1 guanyl-nucleotide exchange factor complex-dependent mechanism (PubMed:23418349, PubMed:27559127). Recruitment to endosomes is not reliant on phosphatidylinositol 3-phosphate (PtdIns[3]P) enrichment (PubMed:23418349). Colocalizes to autolysosomes with active GTP-bound Rab2 (PubMed:28483915). {ECO:0000269|PubMed:23418349, ECO:0000269|PubMed:24327558, ECO:0000269|PubMed:27559127, ECO:0000269|PubMed:28483915}.
|
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=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P51149}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P51149};
| null | null | null | null |
FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking (Probable). Involved in microtubule minus and plus end-directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (Probable). Governs early-to-late endosomal to lysosomal maturation (PubMed:23418349, PubMed:24327558). Controls endocytic cargo sorting towards the late endosome facilitating its eventual endolysosomal-mediated degradation (PubMed:11136982). Together with Rab2 involved in promoting fusion of autophagosomes and endosomes with lysosomes probably through recruitment of the HOPS tethering complex (PubMed:28063257, PubMed:28483915, PubMed:31194677). Involved in biosynthetic transport to lysosomes (Probable). Involved in establishing morphogen concentration gradients, for example of the TGF-beta homolog dpp/decapentaplegic, during pattern formation and organogenesis (PubMed:11136982). Together with the Mon1-Ccz1 complex, required for autolysosome formation in fat cells and autophagic degradation during starvation-induced basal and developmental autophagy (PubMed:27559127). Together with Mon1, regulates levels of postsynaptic glutamate receptor GluRIIA in the neuromuscular junction (NMJ) presynapse (PubMed:32658990). Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis (PubMed:28063257). {ECO:0000269|PubMed:11136982, ECO:0000269|PubMed:23418349, ECO:0000269|PubMed:24327558, ECO:0000269|PubMed:27559127, ECO:0000269|PubMed:28063257, ECO:0000269|PubMed:28483915, ECO:0000269|PubMed:31194677, ECO:0000269|PubMed:32658990, ECO:0000305, ECO:0000305|PubMed:28483915}.
|
Drosophila melanogaster (Fruit fly)
|
O76743
|
GLH4_CAEEL
|
MSFSDDGWGAEAEVKVAEDVPEKNVPPPVEPPRAPQSTAIKTEPERNSDEPSAGFGIDPITTSKTFGSQTTPKTEFGGAPSLSGFGGNAAAAAANKTSFDQQGNGFGGAAKHGFGGVGGAPSSFGANVIPVNKPSLGHKTTGFGGEPKHVSGGAFSSANNFDQQDKGFGGAASSGFGNGSMLTNQKVGLENQTTGVGASEVPTSKPSSFGQQPAVVSGFGGAAKMGFGGSSSSGFGGQKAGATESSGFPTKETSTSQPGFGGDSSTGFGSGLKAGFGGHGAGAAENSGLPTETTGFGGKLPSAGFGASSSNESAFGQQSKGFGGATKNGFGGDSSSSFGSGSKAGFGGTSSSGIGGQKPGATESSGFPTKETSTSGGTFGSGFGGKPTSTGFGAPSTTDSSSGQQTAGFGGASKPGFGGDSSTGFGSGLKAGFGGHRASTAENSGLPTETTGFGGKLPPAGFGASSSNESAFGQQSKGFGGATKNGFGGDSSNSFGKRDSGFGGPQDQGFGDTDAPSKSGLGSFNTGGGAVKSAFGAAGFGSSSNFGNGNTFGEPSDNQRGNWDGGERPRGCHNCGEEGHISKECDKPKVPRFPCRNCEQLGHFASDCDQPRVPRGPCRNCGIEGHFAVDCDQPKVPRGPCRNCGQEGHFAKDCQNERVRMEPTEPCRRCAEEGHWGYECPTRPKDLQGNFLESYDFVFTPDDKMFEDAVNNDDKIDFDQKVVASTGKVEIPDMASFDGFKILPQDLHDNLKRMKMNRPTPIQRASFFPIMHGNDVVACAHTGSGKTLAFLIPFVIKLMEEFEKDRDVTDEKPSPRLLIVAPTRELVNQTFTTARQLTYETGLKCGLAFGGYSRNANVQHLRSFSQLNILVATMGRLQDFVNAGEVSLSKMKYIVLDEADRMVDSNDFGEEVSKIIGSPGERTQQTVLFSASFSEDLQSDDLPKFVKEGYTMLQVDKFGTANEKIDQKILPVPRTEKRDAIYKLLGIDENTVTLLPDAPIEKQKTLIFVNSVKFCDTLAALISSAGVSTISMHSYQNQEQRDRTLDDFRRGKYQCMVASNVCARGLNIAGLDHVVNYDMPDKNGFDEYVNRIGRTGRAGFTGTSTAFVDVENDTDIIPCLVSILNEAKKEVPEWLTEGAGHQEEGGDDWNEQEQEW
|
3.6.4.13
| null |
gamete generation [GO:0007276]; maturation of SSU-rRNA [GO:0030490]; regulation of cell population proliferation [GO:0042127]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; P granule [GO:0043186]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; JUN kinase binding [GO:0008432]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270]
|
PF00270;PF00271;PF00098;
|
3.40.50.300;4.10.60.10;
|
DEAD box helicase family, DDX4/VASA subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
| null | null | null | null |
FUNCTION: Probable ATP-binding RNA helicase. May act redundantly with the P-granule component glh-1 to regulate the formation of the granular structure of P-granules in embryos (PubMed:21402787, PubMed:24746798). May protect somatic cells from excessive apoptosis during normal development (PubMed:27650246). {ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24746798, ECO:0000269|PubMed:27650246, ECO:0000305}.
|
Caenorhabditis elegans
|
O76745
|
NP_CIMLE
|
MKLLLSAGAALAFVLGLCAAGSPPAQLSVHTVSWNSGHERAPTNLEELLGLNSGETPDVIAVAVQGFGFQTDKPQQGPACVKNFQSLLTSKGYTKLKNTITETMGLTVYCLEKHLDQNTLKNETIIVTVDDQKKSGGIVTSFTIYNKRFSFTTSRMSDEDVTSTNTKYAYDTRLDYSKKDDPSDFLFWIGDLNVRVETNATHAKSLVDQNNIDGLMAFDQLKKAKEQKLFDGWTEPQVTFKPTYKFKPNTDEYDLSATPSWTDRALYKSGTGKTIQPLSYNSLTNYKQTEHRPVLAKFRVTL
| null |
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:15637157, ECO:0000305|PubMed:9716517}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000305|PubMed:15637157};
|
nitric oxide transport [GO:0030185]; phosphatidylinositol dephosphorylation [GO:0046856]; positive regulation of flagellated sperm motility [GO:1902093]; response to abscisic acid [GO:0009737]; response to auxin [GO:0009733]; response to jasmonic acid [GO:0009753]; response to salt stress [GO:0009651]; vasodilation in another organism [GO:0044552]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; non-motile cilium [GO:0097730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
|
heme binding [GO:0020037]; iron ion binding [GO:0005506]; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:0034485]; phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]
| null |
3.60.10.10;
| null |
PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9716517}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16417223, ECO:0000305|PubMed:22305681, ECO:0000305|PubMed:9716517}.
| null | null | null | null | null |
FUNCTION: Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation (Probable). In place of heme, the heme-binding cysteine can also reversibly bind NO when it is present in high concentrations (PubMed:15637157). {ECO:0000269|PubMed:15637157, ECO:0000305}.
|
Cimex lectularius (Bed bug) (Acanthia lectularia)
|
O76818
|
PBAN_AGRIP
|
MYGAVLPGLFFIFISCVVASSNDVKDGGADRGAHSDRGGMWFGPRIGKRSLRMATEDNRQAFFKLLEAADALKYYYDQLPYEMQADEPEARVTKKVIFTPKLGRSLSYEDKMFDNVEFTPRLGRRLADDTPATPADQEMYRPDPEQIDSRTKYFSPRLGRTMNFSPRLGRELAYEMLPSKVRVVRSTNKTQST
| null | null |
neuropeptide signaling pathway [GO:0007218]; pheromone biosynthetic process [GO:0042811]; response to pheromone [GO:0019236]
|
extracellular region [GO:0005576]
|
neuropeptide hormone activity [GO:0005184]
|
PF05874;
| null |
Pyrokinin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9753769}.
| null | null | null | null | null |
FUNCTION: [Pheromone biosynthesis-activating neuropeptide]: A hormone that controls sex pheromone production in female moths and pheromone responsiveness in male (PubMed:9753769). {ECO:0000269|PubMed:9753769}.
|
Agrotis ipsilon (Black cutworm moth)
|
O76840
|
PPN1_CAEEL
|
MRLLLFSAALLLCSVPTWAFSLSSFFGSDVAQKPYLHPNSPPERDPASSRMKRQAYQVYVDGDVSVTVDKSGQKETGNWGPWVPENECSRSCGGGVQLEKRQCSGDCTGASVRYISCNLNACESGTDFRAEQCSKFNDEALDGNYHKWTPYKGKNKCELVCKPESGNFYYKWADKVVDGTKCDSKSNDICVDGECLPVGCDGKLGSSLKFDKCGKCDGDGSTCKTIEGRFDERNLSPGYHDIIKLPEGATNIKIQEARKSTNNLALKNGSDHFYLNGNGLIQVEKEVEVGGTIFVYDDAEPETLSAQGPLSEELTVALLFRKGSRDTAIKYEFSIPLEEEVDYMYKFDNWTPCSVSCGKGVQTRNLYCIDGKNKGRVEDDLCEENNATKPEFEKSCETVDCEAEWFTGDWESCSSTCGDQGQQYRVVYCHQVFANGRRVTVEDGNCTVERPPVKQTCNRFACPEWQAGPWSACSEKCGDAFQYRSVTCRSEKEGEEGKLLAADACPADEQEKFDTERTCNLGPCEGLTFVTGEWNLCTRCNDTEETREVTCKDSQGRAYPLEKCLVDNSTEIPTDTRSCATQPPCEYEWTVSEWSKCTTECGHGHKTRRVICAIHQNGGLEVVDEGHCQAEKPEGKTNCTNEEKCTGTWYTSSWSECTAECGGGSQDRVAVCLNYDKKPVPEWCDEAVKPSEKQDCNVDDCPTCVDSEFGCCPDNSTFATGEFNFGCSNCSETEFGCCADNVTVATGPNSKGCEEFVESPLNLEADVANADAEASGDAPELCSVTNENGEAVDVECATIAPITALLGDGELIGNDTDASNETIHCSKTEFGCCPDWYTAASGKGNEGCPSFTLGGCNETQFGCCHDDVTLARGANLEGCGEPSCAASLYGCCKDRKTIAFGPHYSGCERSSFPCELSDFGCCPDGETAALGKNGTGCGENCLTTKFGCCPDGKTTAKGSHNEGCGCEFAQYGCCPDGKSVAKGAGFYGCPESCAQSQFGCCPDGKTRARGENKEGCPCQYTRYGCCPDGETTALGPRNDGCDNCRYAKHGCCPDGETKALGPDGAGCPPTTTPPFLMGGTVAPHKIAACNQTQESGTVCGAGYKLAWHYDTTEGRCNQFWYGGCGGNDNNFASQDMCETICVEPPGKGRCYLPRVDGPLRCDQLQPRYYYDHSKKHCVAFWWRGCLGNANNFNSFEECSMFCKDVGPYDAPTTAAPPPPPQQNAQQYLPTPEVQQIEIQSAEQPQPQQPQQQQQQQQQQPQQPRQSMEDICRSRQDAGPCETYSDQWFYNAFSQECETFTYGGCGGNLNRFRSKDECEQRCFFVHGAQPSAARQEQAQPAAQPAQPAQPSNIVSPPQQSASPVVVPSNSKQRDACHLNVDQGRCKGAFDSWYYEVATGSCVTFKYTGCGGNANRFASKDQCESLCVKPASEAASAGIDGAAGINSVCDEAKDTGPCTNFVTKWYYNKADGTCNRFHYGGCQGTNNRFDNEQQCKAACQNHKDACQLPKVQGPCSGKHSYYYYNTASHQCETFTYGGCLGNTNRFATIEECQARCPKDDQTTTTSQPEELPSLPLVQEDPQPRPAFSLKQSFAHSRRRDAPFARSVSARHHTPDSEEERVDCYAVPDPGSCGDYRLVWHYSATSNSCRQFYYGGCAGNTNRFETRDKCETSCVAKIEERVESVSEASKSLEEVRLTDPRMDSHFGYHDPEVDQIEEEAEYVIVDTGALPELCMLPEQRGSCYDNILRWRFDSEKSQCVTFMYSGCNPNANHFTSQETCERACGKWRNVAVCELPAEHGDCQLAIPRWYHDPKTSQCQMMMWTGCGGNGNAFSSKADCESLCRVETLWSNNTDFCTLERSAGPCTDSISMWYFDSTHLDCKPFTYGGCRGNQNRFVSKEQCQQSCRPGDTKSEDICTLRPEPGPCRLGLEKYFYDPVIQSCHMFHYGGCEGNANRFDSELDCFRRCSSVKVEASESERVGQLTSASTPVIYIVNKTAIFVGNTFRIRCNSYGVLPITWYKNGGLLQFGSRITEENDDTLEIVDALTADAGVYTCIAGQDSTMSEGVEVVIKRLPGHRTTSRPMLTPSKNFSLGTPPTPSPSTVSTTPFRIYTPGSAPSDARVSRPTSNSCMDVGNASTCDLIVKNGLCGKKRYGTFCCHTCTRVHNFKF
| null | null |
cell morphogenesis [GO:0000902]; distal tip cell migration [GO:0097628]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic morphogenesis [GO:0048598]; extracellular matrix organization [GO:0030198]; nematode larval development [GO:0002119]
|
basement membrane [GO:0005604]; extracellular space [GO:0005615]
|
serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF05986;PF07679;PF00014;PF08686;PF19030;PF00090;
|
2.60.120.830;2.60.40.10;4.10.410.10;2.20.100.10;
|
Papilin family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:19297413}.
| null | null | null | null | null |
FUNCTION: Involved in pharynx morphogenesis probably by remodeling the basement membrane. {ECO:0000269|PubMed:20805556}.; FUNCTION: [Isoform a]: Plays a role in embryogenesis, the second phase of distal cell tip migration and is required for distribution of the metalloproteinase, mig-17, during organogenesis. {ECO:0000269|PubMed:19297413}.; FUNCTION: [Isoform b]: Plays a role in post embryonic distal cell tip migration (PubMed:19297413). Essential extracellular matrix (ECM) protein required for hypodermal enclosure in the embryo (PubMed:11076767). {ECO:0000269|PubMed:11076767, ECO:0000269|PubMed:19297413}.
|
Caenorhabditis elegans
|
O76856
|
CATD_DICDI
|
MKLLILTLFLATIVLAQALTVPLNFHQASRESRRRVPQKWSNRLSALNAGTTIPISDFEDAQYYGAITIGTPGQAFKVVFDTGSSNLWIPSKKCPITVVACDLHNKYNSGASSTYVANGTDFTIQYGSGAMSGFVSQDSVTVGSLTVKDQLFAEATAEPGIAFDFAKFDGILGLAFQSISVNSIPPVFYNMLSQGLVSSTLFSFWLSRTPGANGGELSFGSIDNTKYTGDITYVPLTNETYWEFVMDDFAIDGQSAGFCGTTCHAICDSGTSLIAGPMADITALNEKLGAVILNGEGVFSDCSVINTLPNVTITVAGREFVLTPKEYVLEVTEFGKTECLSGFMGIELNMGNFWILGDVFISAYYTVFDFGNKQVGFATAIQG
|
3.4.23.5
| null |
exocytosis [GO:0006887]; programmed cell death [GO:0012501]; proteolysis [GO:0006508]
|
early endosome [GO:0005769]; early phagosome [GO:0032009]; extracellular region [GO:0005576]; lysosome [GO:0005764]; phagocytic vesicle [GO:0045335]
|
aspartic-type endopeptidase activity [GO:0004190]
|
PF00026;
|
2.40.70.10;
|
Peptidase A1 family
|
PTM: N-glycosylated on 2 out of the 3 potential sites. Glycans contain sulfated Mannose. {ECO:0000269|PubMed:10523518}.
|
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:10523518}. Secreted {ECO:0000269|PubMed:10523518}.
|
CATALYTIC ACTIVITY: Reaction=Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.; EC=3.4.23.5;
| null | null | null | null |
FUNCTION: Protease that may act during cell growth and/or development.
|
Dictyostelium discoideum (Social amoeba)
|
O76902
|
PKHF1_DROME
|
MVDRLVNSEANTRRIASVENCFGSSGVPLAMQGRVLVGEGVLTKMCRKRPKSRQFFLFNDILVYGNIVIGKKKYNKQHIMPLEEVSLESIADNQTYRNGWYIRTTTKSFVVFAATSTEKQEWMAHINKCVEDLLRKSGKKPVENHAAVWVPDTDASVCMHCKKTQFTFIQRRHHCRNCGAVVCAGCSAKKFLLPQQSTKALRVCDACYERLKHVPSSLGSGEDSAAATGAASGNKLNTTAGDSSNDEDSDEETASPGGESHDEPRFYGDNSVLSAVEDSSTITSPSSATTGSLEAPQVTPSVQSSPAAVATTGSHC
| null | null |
endocytosis [GO:0006897]; endosome organization [GO:0007032]; endosome to lysosome transport [GO:0008333]
|
apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; late endosome [GO:0005770]
|
metal ion binding [GO:0046872]; phosphatidylinositol binding [GO:0035091]
|
PF01363;PF00169;
|
2.30.29.30;3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:22160599}. Endosome membrane {ECO:0000269|PubMed:22160599}. Cytoplasm, cell cortex {ECO:0000269|PubMed:22160599}.
| null | null | null | null | null |
FUNCTION: Functions in the regulation of endosome morphology and late endosome formation. Has a role in controlling trafficking from early to late endosomes and from late endosomes to lysosomes. Important for localization of Gdi to the endosomal membranes. May function in controlling the activity of multiple regulators in the endocytic pathway, perhaps by positively controlling those involved in the early steps of endocytosis such as Rab5 and hrs, and negative regulating those involved in the late stages of endocytosis like car and VhaSFD. {ECO:0000269|PubMed:22160599}.
|
Drosophila melanogaster (Fruit fly)
|
O76906
|
CRM_DROME
|
MEELSKQPPPPPLTQPPPPSSSVSIEEPLPNGKGGGAVVVNSIAKLPEEELLGSVTMHNCPGTRASARVIQKMKQDQTRPMTPPPSEREPNKKEEKAAQKTPSQLKTGSGKTTWTNVERNCFFDALNEFGKDFEAVANCINAKLKRRNANSDYSFKTKDQVRQHYYQTHHKICKYVRFSEELKKPAQELYTLINYGEMRRKLQFLTEKHFMKLKQLVYQGQITVRCKGKNIRIKTPSCKALRRLNQLDDSLEDIRLPSKVEVLVTPANMEAFGRVQSLAQNPRGRIIVPLHKKLISFIKTFEYKWRSANQRLHEEKSAYFSSSLPSAASNNNNNNNETEPLQPSVASLDPSMCFQPRPGVAIHRPLLSITAYLSSISICLTAYEERMGFKVRSETLGNLAGMSVAANKRLRTESGSEKRSPETKKPKSSASPPLEKSLDDGPLEGNLMKMENSSGDELGEEIHEFLGDILEAMQHPQAATIPALSATTGDTTNVAVALETSHDPVQQAYPANADLSNAMATSVLQTSCAAAPAPSTPVTGSLAAPSVARSKRKEAKEAAAAAQARNFKPLLSDDILKRIRKGWTQANAADITIGDLYVVFGQDSKLELEYYWCEVDSSTAMASSILTINTVTPSSSSVGTQTGSAASNANQTGASSNCYVSASSNSSTSSTSLPYNPNDCDSVERVRAVTTSSVSNKLKHLLLVANLSERVRKRQCNCGHTCDRKRDLMTKAQQLAEATATGGVGGMVEGNFRTPMLPVRRPISNIDPVRQLSALTRQKISRQVLVQRRLLPPTSAGDRPYDLLSVRQLHSGLFEPIDRVDGTSSAGISTSGSKPDCSMNAMTASQDQEPGDQGALEFLNDEATQVSARDMPNLDICVATNRTDVSSSLNEAAQDGSTTQSFFQGSMSPMHLLRDSTSNARWLEDNINDFSLTSLLGHLDEIDATRDILDPSSSMSVISESSVDFRHKFQEIAALLQQQEKD
| null | null |
pattern specification process [GO:0007389]; regulation of DNA-templated transcription [GO:0006355]; segment specification [GO:0007379]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]
| null |
1.10.10.60;
|
Cramped family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9310333}. Note=During S-phase in early embryogenesis. Colocalizes with PCNA in polytene nuclei during embryogenesis.
| null | null | null | null | null |
FUNCTION: Polycomb group (Pc-G) genes are needed to maintain expression patterns of the homeotic selector genes of the Antennapedia (Antp-C) and Bithorax (Bx-C) complexes, and hence for the maintenance of segmental determination. Can act as a modifier of position effect variegation (PEV). {ECO:0000269|PubMed:9310333}.
|
Drosophila melanogaster (Fruit fly)
|
O76908
|
VILYA_DROME
|
MAKSQAGQTVEPEASKLWIHCNSCCALFCDKKHTFFLLACHHVFCERCVKVSAGRTPSDAPIFECSTCRRSVRGRQLTNSMPNHFKQLFHPEPFTIGNDFVETFQRGNHRHFDKYKERKELEMDKLFKDIEVAKSVCQKRFLEAQMLRVERKKLMQRSRYIKAEVANRKAEMHRMAQAYRSRSLTSQSSSSAQRSARGRPRGRGTATQSSSRRRSTESAKRQQITSFIHPPNNSFDL
| null | null |
female meiotic nuclear division [GO:0007143]; homologous chromosome pairing at meiosis [GO:0007129]; positive regulation of meiotic DNA double-strand break formation [GO:1903343]; protein sumoylation [GO:0016925]; reciprocal meiotic recombination [GO:0007131]
|
central element [GO:0000801]; chromosome [GO:0005694]; recombination nodule [GO:0005713]; site of double-strand break [GO:0035861]; synaptonemal complex [GO:0000795]
|
metal ion binding [GO:0046872]; SUMO transferase activity [GO:0019789]
|
PF14634;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:26452093, ECO:0000269|PubMed:30615609}. Note=During early pachytene, colocalizes with narya to the central region of the synaptonemal complex (SC) in both linear stretches and discrete foci which correspond to recombination nodules. As pachytene progresses, found mainly at recombination nodules. Double-strand break formation is required for recruitment to recombination nodules but not for linear localization to the central region of the SC. {ECO:0000269|PubMed:26452093, ECO:0000269|PubMed:30615609}.
| null | null | null | null | null |
FUNCTION: Required for the formation of DNA double-strand breaks during meiosis together with narya and nenya. {ECO:0000269|PubMed:26452093, ECO:0000269|PubMed:30615609}.
|
Drosophila melanogaster (Fruit fly)
|
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