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
MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNK...
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 develo...
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}...
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:...
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...
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
MEIAPQEAPPVPGADGDIEEAPAEAGSPSPASPPADGRLKAAAKRVTFPSDEDIVSGAVEPKDPWRHAQNVTVDEVIGAYKQACQKLNCRQIPKLLRQLQEFTDLGHRLDCLDLKGEKLDYKTCEALEEVFKRLQFKVVDLEQTNLDEDGASALFDMIEYYESATHLNISFNKHIGTRGWQAAAHMMRKTSCLQYLDARNTPLLDHSAPFVARALRIRSSLAVLHLENASLSGRPLMLLATALKMNMNLRELYLADNKLNGLQDSAQLGNLLKFNCSLQILDLRNNHVLDSGLAYICEGLKEQRKGLVTLVLWNNQLTHT...
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
MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQ...
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 pho...
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-...
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:1...
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...
Homo sapiens (Human)
O75879
GATB_HUMAN
MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGEHKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQINELENGGEILNETRSFHHKL...
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, C...
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:15...
Homo sapiens (Human)
O75881
CP7B1_HUMAN
MAGEVSAATGRFSLERLGLPGLALAAALLLLALCLLVRRTRRPGEPPLIKGWLPYLGVVLNLRKDPLRFMKTLQKQHGDTFTVLLGGKYITFILDPFQYQLVIKNHKQLSFRVFSNKLLEKAFSISQLQKNHDMNDELHLCYQFLQGKSLDILLESMMQNLKQVFEPQLLKTTSWDTAELYPFCSSIIFEITFTTIYGKVIVCDNNKFISELRDDFLKFDDKFAYLVSNIPIELLGNVKSIREKIIKCFSSEKLAKMQGWSEVFQSRQDVLEKYYVHEDLEIGAHHLGFLWASVANTIPTMFWAMYYLLRHPEAMAAVRD...
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 recepto...
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...
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 elect...
Homo sapiens (Human)
O75882
ATRN_HUMAN
MVAAAAATEARLRRRTAATAALAGRSGGPHWDWDVTRAGRPGLGAGLRLPRLLSPPLRPRLLLLLLLLSPPLLLLLLPCEAEAAAAAAAVSGSAAAEAKECDRPCVNGGRCNPGTGQCVCPAGWVGEQCQHCGGRFRLTGSSGFVTDGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATECSWDHLYVYDGDSIYAPLVAAFSGLIVPERDGNETVPEVVATSGYALLHFFSDAAYNLTGFNITYSFDMCPNNCSGRGECKISNSSDTVECECSENWKGEACDIPHCTDNCGFPHRGICNSSDVRGCSCFSDWQGPGCSV...
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 m...
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 ...
Homo sapiens (Human)
O75886
STAM2_HUMAN
MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDKVGSTPNGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRAVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGITFPPAGSQTVSAAAKNGTSSNKNKEDEDIAKAIELSLQEQKQQHTETKSLYPSSEIQLNNKVARKVRALYDFEAVEDNELTFKHGEIIIVLDDSDANWWKGENHRGIGLFPSNFVTTNLNIETEAAAVDKLNVIDDDVEEIKKSEPEPVYIDEDKMDRALQVLQSIDPTDSKPDSQDLL...
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 multivesicu...
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
MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAASSVLELTEAE...
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|...
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, propi...
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 ...
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...
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...
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 1...
Homo sapiens (Human)
O75899
GABR2_HUMAN
MASPRSSGQPGPPPPPPPPPARLLLLLLLPLLLPLAPGAWGWARGAPRPPPSSPPLSIMGLMPLTKEVAKGSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFSNDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEPSWWEQVHTEANSSRCLRKNLLAAMEGYIGVDFE...
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-g...
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 ...
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 pr...
Homo sapiens (Human)
O75900
MMP23_HUMAN
MGRGARVPSEAPGAGVERRWLGAALVALCLLPALVLLARLGAPAVPAWSAAQGDVAALGLSAVPPTRVPGPLAPRRRRYTLTPARLRWDHFNLTYRILSFPRNLLSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKALSQDELWGLHRLYGCLDRLFVCASWARRGFCDARRRLMKRLCPSSCDFCYEFPFPTVATTPPPPRTKTRLVPEGRNVTFR...
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
MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVGSGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPAAVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRII...
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-...
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}; Physiologica...
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 hex...
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 activi...
Homo sapiens (Human)
O75908
SOAT2_HUMAN
MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQLRELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHFRTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLAPYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFLMKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKNFAQALGCVLYACFILGRLCV...
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-lo...
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 th...
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:...
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,...
Homo sapiens (Human)
O75909
CCNK_HUMAN
MKENKENSSPSVTSANLDHTKPCWYWDKKDLAHTPSQLEGLDPATEARYRREGARFIFDVGTRLGLHYDTLATGIIYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFGQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLKYAKQLKGDKNKIQKLVQMAWTFVNDSLCTTLSLQWEPEIIAVAVMYLAGRLCKFEIQEWTSKPMYRRWWEQFVQDVPVDVLEDICHQILDLYSQGKQQMPHHTPHQLQQPPSLQPTPQVPQVQQSQPSQSSEPSQPQQKDPQQPAQQQQPAQQP...
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]; reg...
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|PubM...
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 metab...
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
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAGEEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEEKLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVP...
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:...
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}; Physiolo...
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 differe...
Homo sapiens (Human)
O75914
PAK3_HUMAN
MSDGLDNEEKPPAPPLRMNSNNRDSSALNHSSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLYGSQMCPGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHPSSTKTASEPPLAPPVSEEEDEEEEEEEDENEPPPVIAPRPEHTKSIYTRSVVESIASPAVPNKEVTPPSAENANSSTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQP...
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 cytoskele...
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-[pr...
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 GTPas...
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...
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=...
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...
Homo sapiens (Human)
O75916
RGS9_HUMAN
MTIRHQGQQYRPRMAFLQKIEALVKDMQNPETGVRMQNQRVLVTSVPHAMTGSDVLQWIVQRLWISSLEAQNLGNFIVRYGYIYPLQDPKNLILKPDGSLYRFQTPYFWPTQQWPAEDTDYAIYLAKRNIKKKGILEEYEKENYNFLNQKMNYKWDFVIMQAKEQYRAGKERNKADRYALDCQEKAYWLVHRCPPGMDNVLDYGLDRVTNPNEVKVNQKQTVVAVKKEIMYYQQALMRSTVKSSVSLGGIVKYSEQFSSNDAIMSGCLPSNPWITDDTQFWDLNAKLVEIPTKMRVERWAFNFSELIRDPKGRQSFQYFL...
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]; regula...
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...
Homo sapiens (Human)
O75923
DYSF_HUMAN
MLRVFILYAENVHTPDTDISDAYCSAVFAGVKKRTKVIKNSVNPVWNEGFEWDLKGIPLDQGSELHVVVKDHETMGRNRFLGEAKVPLREVLATPSLSASFNAPLLDTKKQPTGASLVLQVSYTPLPGAVPLFPPPTPLEPSPTLPDLDVVADTGGEEDTEDQGLTGDEAEPFLDQSGGPGAPTTPRKLPSRPPPHYPGIKRKRSAPTSRKLLSDKPQDFQIRVQVIEGRQLPGVNIKPVVKVTAAGQTKRTRIHKGNSPLFNETLFFNLFDSPGELFDEPIFITVVDSRSLRTDALLGEFRMDVGTIYREPRHAYLRKW...
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 [...
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];...
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...
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
MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRNYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADP...
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 ub...
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]; transcri...
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 cyto...
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, MRE1...
Homo sapiens (Human)
O75928
PIAS2_HUMAN
MADFEELRNMVSSFRVSELQVLLGFAGRNKSGRKHDLLMRALHLLKSGCSPAVQIKIRELYRRRYPRTLEGLSDLSTIKSSVFSLDGGSSPVEPDLAVAGIHSLPSTSVTPHSPSSPVGSVLLQDTKPTFEMQQPSPPIPPVHPDVQLKNLPFYDVLDVLIKPTSLVQSSIQRFQEKFFIFALTPQQVREICISRDFLPGGRRDYTVQVQLRLCLAETSCPQEDNYPNSLCIKVNGKLFPLPGYAPPPKNGIEQKRPGRPLNITSLVRLSSAVPNQISISWASEIGKNYSMSVYLVRQLTSAMLLQRLKMKGIRNPDHSR...
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:2240662...
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 horm...
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 scaff...
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|Pub...
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
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIFDVPVERVQPFYAALKEFVDL...
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
MSKTFLRPKVSSTKVTDWVDPSFDDFLECSGVSTITATSLGVNNSSHRRKNGPSTLESSRFPARKRGNLSSLEQIYGLENSKEYLSENEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKQGGSILLITGPPGCGKTTTLKILSKEHGIQVQEWINPVLPDFQKDDFKGMFNTESSFHMFPYQSQIAVFKEFLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLRKYVRIGRCPLIFIISDSLSGDNNQRLLFPKEIQEECSISNISFNPVAPTIMMKFLNRIVTIEANKNGGKITVPDKT...
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:...
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 upo...
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 ...
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 chromat...
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 physiologi...
Homo sapiens (Human)
O75952
CABYR_HUMAN
MISSKPRLVVPYGLKTLLEGISRAVLKTNPSNINQFAAAYFQELTMYRGNTTMDIKDLVKQFHQIKVEKWSEGTTPQKKLECLKEPGKTSVESKVPTQMEKSTDTDEDNVTRTEYSDKTTQFPSVYAVPGTEQTEAVGGLSSKPATPKTTTPPSSPPPTAVSPEFAYVPADPAQLAAQMLGKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVAAPLVCSGKVLEVQVVNQTSVHVDLGSQPKENEAEPSTASSVPLQDEQEPPAYDQAPEVTLQADIEVMSTVHISSVYNDVPVTEGVVYIEQLPEQIVIPF...
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=Accord...
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
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRG...
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:004312...
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]...
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|PubMe...
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 enr...
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)...
Homo sapiens (Human)
O75962
TRIO_HUMAN
MSGSSGGAAAPAASSGPAAAASAAGSGCGGGAGEGAEEAAKDLADIAAFFRSGFRKNDEMKAMDVLPILKEKVAYLSGGRDKRGGPILTFPARSNHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDSIKPLLKILQESFPCCIHVALIIKPDNFWQKQRTNFGSSKFEFETNMVSLEGLTKVVDPSQLTPEFDGCLEYNHEEWIEIRVAFEDYISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKKKVIKAPIEDLDLEGQKLLQRIQSSESFPKKNSGSGNADLQNLLPKVSTMLDRLHS...
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]; transmembran...
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-[pr...
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 lam...
Homo sapiens (Human)
O75969
AKAP3_HUMAN
MSEKVDWLQSQNGVCKVDVYSPGDNQAQDWKMDTSTDPVRVLSWLRRDLEKSTAEFQDVRFKPGESFGGETSNSGDPHKGFSVDYYNTTTKGTPERLHFEMTHKEIPCQGPRAQLGNGSSVDEVSFYANRLTNLVIAMARKEINEKIDGSENKCVYQSLYMGNEPTPTKSLSKIASELVNETVSACSRNAAPDKAPGSGDRVSGSSQSPPNLKYKSTLKIKESTKERQGPDDKPPSKKSFFYKEVFESRNGDYAREGGRFFPRERKRFRGQERPDDFTASVSEGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKK...
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
MLEAIDKNRALHAAERLQTKLRERGDVANEDKLSLLKSVLQSPLFSQILSLQTSVQQLKDQVNIATSATSNIEYAHVPHLSPAVIPTLQNESFLLSPNNGNLEALTGPGIPHINGKPACDEFDQLIKNMAQGRHVEVFELLKPPSGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQALDQTITHQQAISILQKAKDTVQLVIARGSLPQLVSPIVSRSPSAASTISAHSNPVHWQHMETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQ...
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 ep...
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:00002...
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
MASGRDERPPWRLGRLLLLMCLLLLGSSARAAHIKKAEATTTTTSAGAEAAEGQFDRYYHEEELESALREAAAAGLPGLARLFSIGRSVEGRPLWVLRLTAGLGSLIPEGDAGPDAAGPDAAGPLLPGRPQVKLVGNMHGDETVSRQVLIYLARELAAGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGFGDGGPSGASGRDNSRGRDLNRSFPDQFSTGEPPALDEVPEVRALIEWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKATGIYSKTSDDEVFKYLAKAYASNHPIMKTGEPHCPGDEDETFKDG...
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
MLRRKPSNASEKEPTQKKKLSLQRSSSFKDFAKSKPSSPVVSEKEFNLDDNIPEDDSGVPTPEDAGKSGKKLGKKWRAVISRTMNRKMGKMMVKALSEEMADTLEEGSASPTSPDYSLDSPGPEKMALAFSEQEEHELPVLSRQASTGSELCSPSPGSGSFGEEPPAPQYTGPFCGRARVHTDFTPSPYDHDSLKLQKGDVIQIIEKPPVGTWLGLLNGKVGSFKFIYVDVLPEEAVGHARPSRRQSKGKRPKPKTLHELLERIGLEEHTSTLLLNGYQTLEDFKELRETHLNELNIMDPQHRAKLLTAAELLLDYDTGS...
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 ...
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
MAAGAAEAAVAAVEEVGSAGQFEELLRLKAKSLLVVHFWAPWAPQCAQMNEVMAELAKELPQVSFVKLEAEGVPEVSEKYEISSVPTFLFFKNSQKIDRLDGAHAPELTKKVQRHASSGSFLPSANEHLKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKAYSSWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIVKE...
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 forc...
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 ext...
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...
Homo sapiens (Human)
O76011
KRT34_HUMAN
MSYSCCLPSLGCRTSCSSRPCVPPSCHGYTLPGACNIPANVSNCNWFCEGSFNGSEKETMQFLNDRLASYLEKVRQLERDNAELEKLIQERSQQQEPLLCPSYQSYFKTIEELQQKILCAKAENARLVVNIDNAKLASDDFRSKYQTEQSLRLLVESDINSIRRILDELTLCKSDLESQVESLREELICLKKNHEEEVNTLRSQLGDRLNVEVDTAPTVDLNQVLNETRSQYEALVEINRREVEQWFATQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEAHYSSQLSQVQSLITN...
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
MATQTCTPTFSTGSIKGLCGTAGGISRVSSIRSVGSCRVPSLAGAAGYISSARSGLSGLGSCLPGSYLSSECHTSGFVGSGGWFCEGSFNGSEKETMQFLNDRLANYLEKVRQLERENAELESRIQEWYEFQIPYICPDYQSYFKTIEDFQQKILLTKSENARLVLQIDNAKLAADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELMCLKKNHEEEVSVLRCQLGDRLNVEVDAAPPVDLNKILEDMRCQYEALVENNRRDVEAWFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALE...
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
MTSFYSTSSCPLGCTMAPGARNVFVSPIDVGCQPVAEANAASMCLLANVAHANRVRVGSTPLGRPSLCLPPTSHTACPLPGTCHIPGNIGICGAYGKNTLNGHEKETMKFLNDRLANYLEKVRQLEQENAELETTLLERSKCHESTVCPDYQSYFRTIEELQQKILCSKAENARLIVQIDNAKLAADDFRIKLESERSLHQLVEADKCGTQKLLDDATLAKADLEAQQESLKEEQLSLKSNHEQEVKILRSQLGEKFRIELDIEPTIDLNRVLGEMRAQYEAMVETNHQDVEQWFQAQSEGISLQAMSCSEELQCCQSEI...
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
MTSSYSSSSCPLGCTMAPGARNVSVSPIDIGCQPGAEANIAPMCLLANVAHANRVRVGSTPLGRPSLCLPPTCHTACPLPGTCHIPGNIGICGAYGENTLNGHEKETMQFLNDRLANYLEKVRQLEQENAELEATLLERSKCHESTVCPDYQSYFHTIEELQQKILCSKAENARLIVQIDNAKLAADDFRIKLESERSLRQLVEADKCGTQKLLDDATLAKADLEAQQESLKEEQLSLKSNHEQEVKILRSQLGEKLRIELDIEPTIDLNRVLGEMRAQYEAMLETNRQDVEQWFQAQSEGISLQDMSCSEELQCCQSEI...
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
MEDSASASLSSAAATGTSTSTPAAPTARKQLDKEQVRKAVDALLTHCKSRKNNYGLLLNENESLFLMVVLWKIPSKELRVRLTLPHSIRSDSEDICLFTKDEPNSTPEKTEQFYRKLLNKHGIKTVSQIISLQTLKKEYKSYEAKLRLLSSFDFFLTDARIRRLLPSLIGRHFYQRKKVPVSVNLLSKNLSREINDCIGGTVLNISKSGSCSAIRIGHVGMQIEHIIENIVAVTKGLSEKLPEKWESVKLLFVKTEKSAALPIFSSFVSNWDEATKRSLLNKKKKEARRKRRERNFEKQKERKKKRQQARKTASVLSKDD...
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
MDSNTAPLGPSCPQPPPAPQPQARSRLNATASLEQERSERPRAPGPQAGPGPGVRDAAAPAEPQAQHTRSRERADGTGPTKGDMEIPFEEVLERAKAGDPKAQTEVGKHYLQLAGDTDEELNSCTAVDWLVLAAKQGRREAVKLLRRCLADRRGITSENEREVRQLSSETDLERAVRKAALVMYWKLNPKKKKQVAVAELLENVGQVNEHDGGAQPGPVPKSLQKQRRMLERLVSSESKNYIALDDFVEITKKYAKGVIPSSLFLQDDEDDDELAGKSPEDLPLRLKVVKYPLHAIMEIKEYLIDMASRAGMHWLSTIIP...
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 apoptoti...
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 ...
Homo sapiens (Human)
O76027
ANXA9_HUMAN
MSVTGGKMAPSLTQEILSHLGLASKTAAWGTLGTLRTFLNFSVDKDAQRLLRAITGQGVDRSAIVDVLTNRSREQRQLISRNFQERTQQDLMKSLQAALSGNLERIVMALLQPTAQFDAQELRTALKASDSAVDVAIEILATRTPPQLQECLAVYKHNFQVEAVDDITSETSGILQDLLLALAKGGRDSYSGIIDYNLAEQDVQALQRAEGPSREETWVPVFTQRNPEHLIRVFDQYQRSTGQELEEAVQNRFHGDAQVALLGLASVIKNTPLYFADKLHQALQETEPNYQVLIRILISRCETDLLSIRAEFRKKFGKSL...
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...
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
MPSCGACTCGAAAVRLITSSLASAQRGISGGRIHMSVLGRLGTFETQILQRAPLRSFTETPAYFASKDGISKDGSGDGNKKSASEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEVEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQIPQEKRGGEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCT...
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 require...
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
MKIPNIGNVMNKFEILGVVGEGAYGVVLKCRHKETHEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLELLEEMPNGVPPEKVKSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGNNANYTEYVATRWYRSPELLLGAPYGKSVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPSEQMKLFYSNPRFHGLRFPAVNHPQSLERRYLGILNSVLLDLMKNLLKLDPADRYLTEQCLNHPTFQTQRLLDRSPSRSAKRKPYHVES...
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]; ...
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 c...
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-[p...
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
MRVPVFEDIKDETEEEKIGEEENEEDQVFYKPVIEDLSMELARKCTELISDIRYKEEFKKSKDKCTFVTDSPMLNHVKNIGAFISEAKYKGTIKADLSNSLYKRMPATIDSVFAGEVTQLQSEVAYKQKHDAAKGFSDYAHMKEPPEVKHAMEVNKHQSNISYRKDVQDTHTYSAELDRPDIKMATQISKIISNAEYKKGQGIMNKEPAVIGRPDFEHAVEASKLSSQIKYKEKFDNEMKDKKHHYNPLESASFRQNQLAATLASNVKYKKDIQNMHDPVSDLPNLLFLDHVLKASKMLSGREYKKLFEENKGMYHFDAD...
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,...
Homo sapiens (Human)
O76050
NEUL1_HUMAN
MGNNFSSIPSLPRGNPSRAPRGHPQNLKDSIGGPFPVTSHRCHHKQKHCPAVLPSGGLPATPLLFHPHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFHRINDSAVMLFFSGVRTADPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLRREADDARLSVSLCDLNVPGADGDEAAPAAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARVEHGR...
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 p...
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...
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 CP...
Homo sapiens (Human)
O76054
S14L2_HUMAN
MSGRVGDLSPRQKEALAKFRENVQDVLPALPNPDDYFLLRWLRARSFDLQKSEAMLRKHVEFRKQKDIDNIISWQPPEVIQQYLSGGMCGYDLDGCPVWYDIIGPLDAKGLLFSASKQDLLRTKMRECELLLQECAHQTTKLGRKVETITIIYDCEGLGLKHLWKPAVEAYGEFLCMFEENYPETLKRLFVVKAPKLFPVAYNLIKPFLSEDTRKKIMVLGANWKEVLLKHISPDQVPVEYGGTMTDPDGNPKCKSKINYGGDIPRKYYVRDQVKQQYEHSVQISRGSSHQVEYEILFPGCVLRWQFMSDGADVGFGIFL...
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 wi...
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 ...
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
MAPTQGPRAPLEFGGPLGAAALLLLLPATMFHLLLAARSGPARLLGPPASLPGLEVLWSPRALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAGLPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSGNPIYDFFLGRELNPRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWHEEAVLTTMDITHDGFGFMLAFGDMAWVPFTYSLQAQFLLHHPQPLGLPMASVICLINATGYYIFRGANSQKNTFRKNPSD...
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:Q...
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
MGEPGFFVTGDRAGGRSWCLRRVGMSAGWLLLEDGCEVTVGRGFGVTYQLVSKICPLMISRNHCVLKQNPEGQWTIMDNKSLNGVWLNRARLEPLRVYSIHQGDYIQLGVPLENKENAEYEYEVTEEDWETIYPCLSPKNDQMIEKNKELRTKRKFSLDELAGPGAEGPSNLKSKINKVSCESGQPVKSQGKGEVASTPSDNLDPKLTALEPSKTTGAPIYPGFPKVTEVHHEQKASNSSASQRSLQMFKVTMSRILRLKIQMQEKHEAVMNVKKQTQKGNSKKVVQMEQELQDLQSQLCAEQAQQQARVEQLEKTFQEE...
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]; interstran...
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_030...
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 t...
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 ce...
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. Activat...
Homo sapiens (Human)
O76071
CIAO1_HUMAN
MKDSLVLLGRVPAHPDSRCWFLAWNPAGTLLASCGGDRRIRIWGTEGDSWICKSVLSEGHQRTVRKVAWSPCGNYLASASFDATTCIWKKNQDDFECVTTLEGHENEVKSVAWAPSGNLLATCSRDKSVWVWEVDEEDEYECVSVLNSHTQDVKHVVWHPSQELLASASYDDTVKLYREEEDDWVCCATLEGHESTVWSLAFDPSGQRLASCSDDRTVRIWRQYLPGNEQGVACSGSDPSWKCICTLSGFHSRTIYDIAWCQLTGALATACGDDAIRVFQEDPNSDPQQPTFSLTAHLHQAHSQDVNCVAWNPKEPGLLA...
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 ...
Homo sapiens (Human)
O76074
PDE5A_HUMAN
MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLY...
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:1295...
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 ooc...
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:0...
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:15489...
Homo sapiens (Human)
O76075
DFFB_HUMAN
MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSR...
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]; vascu...
cytoplasm [GO:0005737]
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 activatio...
Homo sapiens (Human)
O76081
RGS20_HUMAN
MPQLSQDNQECLQKHFSRPSIWTQFLPLFRAQRYNTDIHQITENEGDLRAVPDIKSFPPAQLPDSPAAPKLFGLLSSPLSSLARFFSHLLRRPPPEAPRRRLDFSPLLPALPAARLSRGHEELPGRLSLLLGAALALPGRPSGGRPLRPPHPVAKPREEDATAGQSSPMPQMGSERMEMRKRQMPAAQDTPGAAPGQPGAGSRGSNACCFCWCCCCSCSCLTVRNQEDQRPTIASHELRADLPTWEESPAPTLEEVNAWAQSFDKLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKNIIEEKARIIYEDYIS...
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 ...
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 i...
Homo sapiens (Human)
O76082
S22A5_HUMAN
MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQD...
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 symbi...
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:001565...
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 m...
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...
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 {...
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 ...
Homo sapiens (Human)
O76083
PDE9A_HUMAN
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCV...
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 ...
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]; si...
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}...
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}; ...
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:96241...
Homo sapiens (Human)
O76090
BEST1_HUMAN
MTITYTSQVANARLGSFSRLLLCWRGSIYKLLYGEFLIFLLCYYIIRFIYRLALTEEQQLMFEKLTLYCDSYIQLIPISFVLGFYVTLVVTRWWNQYENLPWPDRLMSLVSGFVEGKDEQGRLLRRTLIRYANLGNVLILRSVSTAVYKRFPSAQHLVQAGFMTPAEHKQLEKLSLPHNMFWVPWVWFANLSMKAWLGGRIRDPILLQSLLNEMNTLRTQCGHLYAYDWISIPLVYTQVVTVAVYSFFLTCLVGRQFLNPAKAYPGHELDLVVPVFTFLQFFFYVGWLKVAEQLINPFGEDDDDFETNWIVDRNLQVSLL...
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 c...
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:17...
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:000...
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 hy...
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 ERK...
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
MASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGSFKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLYRLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEKVVPENLGLQEGTHELCYNTACALIGQGQLNQAMKILQKAEDLCRRSLSEDTDGTEEDPQAELAIIHGQMAYILQLQGRTEEALQLYNQIIKLKPTDVGLLAVIANNIITINKDQNVFDSKKKVKLTNAEGVEFKLSKKQLQAIEFNKALLAMYTNQA...
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 prote...
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 meta...
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 align...
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:0008...
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....
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|Uni...
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
MELRVGNKYRLGRKIGSGSFGDIYLGTTINTGEEVAIKLECIRTKHPQLHIESKFYKTMQGGIGIPRIIWCGSEGDYNVMVMELLGPSLEDLFNFCSRRFSLKTVLLLADQMISRIDYIHSRDFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKFRDARSLKHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGALPWQGLKAANKRQKYERISEKKLSTSIVVLCKGFPSEFVNYLNFCRQMHFDQRPDYCHLRKLFRNLFHRLGFTYDYVFDWNLLKFGGPRNPQAIQQAQDGADGQAGHDAV...
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 regul...
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-[pr...
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 ...
Drosophila melanogaster (Fruit fly)
O76329
ACTNB_DICDI
MEHSTPLNEEIVHKKNDENWVIAQKKVFTNWCNIFLNQRSQKIEDLETDLYDGILLGSLLEILSGKNVILSKCKQLKTRLHYINNLNFSLKFIGDEGLRLVGVASEDITDGNLKLILGLVWTLILRYQIQSMQNSKSSQQNLHSSTKPSELMLNWVKSQISDYGHHIKDLTTSFQNGLLFCALVHKLVPEKLDYKSLSESDSLGNLTLAFEVANKELGIPSILDPHDIITTPDELSILTYISLFPKVYQQTLEPLNNNNNISPSLSSSSSSLLNTPNKRNSIQLSKSTSFEQQNQQQQQQNLLSPNSYRNSISFSKSPSF...
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]; nuc...
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 i...
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
MAKDIYKTFKRSVSGIVGGNNINGEGSSSPSTSAPQVKYRGGTGRTWIHPPDYLINGHVEYVARFLGCVETPKANGSDVAREAIHAIRFQRDLKRSEQTRETAKLQKVEIRISIDNVIIADIKTKAPMYTFPLGRISFCADDKDDKRMFSFIARAEGASGKPSCYAFTSEKLAEDITLTIGEAFDLAYKRFLDKNRTSLENQKQIYILKKKIVELETENQVLIERLAEALRANSKADYENTGPPIYPGLGPPALPLSPMPQGPPPNIPPSSIYSMPRANDLPPTEMAPTLPQISTSSNGASPSVSPASTSPSGPAPSIPP...
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 ...
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 ne...
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 c...
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
MSSGSRPSSGGGGGGGGASGGAGGGAPGGGGGGIRGFFSKLRKPSDQPNGNQVQVGTRTFEAHELQKLIPQLEEAISRKDAQLRQQQTIVEGHIKRISELEGEVTTLQRECDKLRSVLEQKAQSAASPGGQPPSPSPRTDQLGNDLQQKAVLPADGVQRAKKIAVSAEPTNFENKPATLQHYNKTVGAKQMIRDAVQKNDFLKQLAKEQIIELVNCMYEMRARAGQWVIQEGEPGDRLFVVAEGELQVSREGALLGKMRAGTVMGELAILYNCTRTASVQALTDVQLWVLDRSVFQMITQRLGMERHSQLMNFLTKVSIF...
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 ...
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|PubM...
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:00002...
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 sae...
Caenorhabditis elegans
O76365
CTU1_CAEEL
MEKRRGPPPCQSGSGCSNPAKIRKAKDGAQLCGPCFSRNFEDDVHEAIVNNKLFKRGERVAIGASGGKDSTVLAYVMKTLNDRHDYGLDLQLLSIDEGIKGYRDDSLLAVEKNRVEYGLPLTILSYRDLYGWTMDDIVAKIGKKNNCTFCGVFRRQALDRGAFKIGATKLVTGHNADDMAETLLMNVLRGDIARLERCTNIVTGEEGDLPRAKPLKYCFERDIVMYARTNQLEYFYTECIYAPNAYRGYARKYVRDLEKVHPRAILDLIRSGEKVSVKKEVEMPTLKICERCGYMTSQKLCKACLLIEGLNTGNTDLGVR...
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...
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 f...
Caenorhabditis elegans
O76373
CBPC1_CAEEL
MPSDSDDVAAVKQPWSQLIVDISNFLSEHPQSKTSQALLPSCNGVWSDEEKLELIEAFGHKKQSHLTKSGVKAVLAAFEGDRTQPDVIFLCRLLHLIFSHFSSENDRKKEKYIVKCDVIATLTRITRKRIIMTLDVTDESSIDHNLDEVLWKLLHKIGLKDPRVSLKVRMGGLISPMCKLFIQKDTLPELFLPFFIKISRSPRNGQAIGRYEGFMTRLLVKIKALDASDQTSQVLLLDKHLQLLFFTMKNKRTRTQLLRENICKYLLEVLRRHLASSSNSRPTRLLSSLFGTFDKSLSAAHTEVVIGTIAILRLLSNFKK...
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 (Pub...
Caenorhabditis elegans
O76411
SCD2_CAEEL
MRKRRLWWFVVLFRVTLVGAILPNETFDVRRYYADRFLIEDEENGSSRSYYISAESKAKAAEQFALLAPNCSLTSDIQENTCNETSSFCDHRVDSTYKTYHYEQEKCNCFIETCDEETNSTELMVLYPDCYCGKREKHCDLSKEKCHWTPDSDHDDLKFEVFESSNKVLFDYMLQAGSEKANLKMNKVSMVSKFFRQSGFNCSLRFMHHFTHQSSTSRLVVRSILQSGEKKNLYEHWLKPASVFWVPVQVAIGSYAEPFKISIDCETGFPPKKKKNKPFTCSIADIYFENCGEIRDPIEQCSRGDQFLCSISANTRCLQN...
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...
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 interneuron...
Caenorhabditis elegans
O76460
RAD54_DROME
MRRSLAPSQRGPLRPESRHSFTPPLLKKNKRSCQQELEREQELDRRRLGALRDASNTSELPLPIRFTANSEYELAIAKVLARKFKVPMDNYVPDYGGKRVLGVRRCISRRPLHDPMACNALVLFHPPAYTEHERMGMDPTKVLVHVVVDPLLSNILRPHQREGVRFMYECVEGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMGLKTKR...
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-st...
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. ...
Drosophila melanogaster (Fruit fly)
O76512
RENT1_CAEEL
MDDSDDEYSRSHGETLTFVDPEDDGVSIGNTQDSQFAYEQFSVPTQSSQATDLLPGGTDGTTNDLPFHDVEDDESDSEKSLTEEQHEQKLPEHACRYCGISDPLCVAKCTVCRKWFCNSNDGTSGGHIVHHMVRSQHKEAYTHKDSPCGDTQLECYRCGSKNVFNLGFIPGKKDQVVVIICRTPCASIAFQNDDNWSPEDWKSVIAEKQLLSWIVNVPSEEQVARARKITATQAVRMEELWRDHPEATVDDLNKPGLDREPDHVQLRYVDAHHYSKVFRPLVAIEAEYDRRVKESASQAVGTVRWEQGLRQSVLAFFHLP...
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 silencin...
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|U...
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 appear...
Caenorhabditis elegans
O76584
GPA11_CAEEL
MSAADMARKNSLINRQLEKEKIDSKKMLKILLLGGPECGKSTIFKQMKIIHMNGFSDLDYVNFRYLIYSNIMQSMDQLLEAAEFFHFPPDDSPSIRRALNHYKSYKVRYSTSEVELNRELADSLSKLYNAEFIKSVLNRKNELKLLDSAVYFLDDIDRISAHEYKPTEMDVLRARVPTTGITEIEFPFKQASLRMVDVGGQRSEQRKWIHCFDNVNGVLFIAAISGYNLYDEDEENRKDDGTPTKTNRLRYSMELFKRIANHQCFSKKTAMILFLNKIDIFKEKIGKYPLTTCFKNYKGVNAFEPACKYVTDRFSRLVSG...
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:00002...
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...
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 p...
Caenorhabditis elegans
O76689
SNF6_CAEEL
MSVSSNDPEQRNGRGMASGNNVDMSLYPPFIKQLDAKLPDYTREGDIEYPFEEITGVGDENRIRGNWSNKSDYLLAVIGFTAGVGSFWKFPFLVFQHGGAAFLVPYLCMLCLASLPMFFMEMVLGQFSSSAAISVWKVVPLFKGIGFAQVTISGFFAVFFNIISAWTLFYLINSFSFSIPWSNCANSWSGENCTLGTRIQCKEMNGTLLVNGSCIVEHASSNETTVIPLHDLGSIPSLKYFHNDVLMLSKGVDDFGTLNWYLGLCVLACWIAVFLCLFQGVKSSGKVVYVAVIVPFIILTVLLTRLLTLDGSLAAVFYFL...
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 mainten...
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 up...
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...
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...
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 me...
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|Uni...
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 p...
Drosophila melanogaster (Fruit fly)
O76743
GLH4_CAEEL
MSFSDDGWGAEAEVKVAEDVPEKNVPPPVEPPRAPQSTAIKTEPERNSDEPSAGFGIDPITTSKTFGSQTTPKTEFGGAPSLSGFGGNAAAAAANKTSFDQQGNGFGGAAKHGFGGVGGAPSSFGANVIPVNKPSLGHKTTGFGGEPKHVSGGAFSSANNFDQQDKGFGGAASSGFGNGSMLTNQKVGLENQTTGVGASEVPTSKPSSFGQQPAVVSGFGGAAKMGFGGSSSSGFGGQKAGATESSGFPTKETSTSQPGFGGDSSTGFGSGLKAGFGGHGAGAAENSGLPTETTGFGGKLPSAGFGASSSNESAFGQQSK...
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:000026...
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 ...
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
MRLLLFSAALLLCSVPTWAFSLSSFFGSDVAQKPYLHPNSPPERDPASSRMKRQAYQVYVDGDVSVTVDKSGQKETGNWGPWVPENECSRSCGGGVQLEKRQCSGDCTGASVRYISCNLNACESGTDFRAEQCSKFNDEALDGNYHKWTPYKGKNKCELVCKPESGNFYYKWADKVVDGTKCDSKSNDICVDGECLPVGCDGKLGSSLKFDKCGKCDGDGSTCKTIEGRFDERNLSPGYHDIIKLPEGATNIKIQEARKSTNNLALKNGSDHFYLNGNGLIQVEKEVEVGGTIFVYDDAEPETLSAQGPLSEELTVALLF...
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:0000...
Caenorhabditis elegans
O76856
CATD_DICDI
MKLLILTLFLATIVLAQALTVPLNFHQASRESRRRVPQKWSNRLSALNAGTTIPISDFEDAQYYGAITIGTPGQAFKVVFDTGSSNLWIPSKKCPITVVACDLHNKYNSGASSTYVANGTDFTIQYGSGAMSGFVSQDSVTVGSLTVKDQLFAEATAEPGIAFDFAKFDGILGLAFQSISVNSIPPVFYNMLSQGLVSSTLFSFWLSRTPGANGGELSFGSIDNTKYTGDITYVPLTNETYWEFVMDDFAIDGQSAGFCGTTCHAICDSGTSLIAGPMADITALNEKLGAVILNGEGVFSDCSVINTLPNVTITVAGREF...
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...
Drosophila melanogaster (Fruit fly)
O76906
CRM_DROME
MEELSKQPPPPPLTQPPPPSSSVSIEEPLPNGKGGGAVVVNSIAKLPEEELLGSVTMHNCPGTRASARVIQKMKQDQTRPMTPPPSEREPNKKEEKAAQKTPSQLKTGSGKTTWTNVERNCFFDALNEFGKDFEAVANCINAKLKRRNANSDYSFKTKDQVRQHYYQTHHKICKYVRFSEELKKPAQELYTLINYGEMRRKLQFLTEKHFMKLKQLVYQGQITVRCKGKNIRIKTPSCKALRRLNQLDDSLEDIRLPSKVEVLVTPANMEAFGRVQSLAQNPRGRIIVPLHKKLISFIKTFEYKWRSANQRLHEEKSAYF...
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 mai...
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)