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 |
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A2AUM9 | CE152_MOUSE | MSLEFGSVALQTQNEDEEFDKEDFEREKELQQLLTDLPHDMLDDELSSPERHDSDCSMDGRAAEPHPSEHLERKWIERDILPKPHSMNCGNGWEENRSKTEDQHLGYHPGEGGDEGGSGYSPPGKREQADLYRLPEDFRPYTGGSKQAASVITFSDPQRDNFQQFGLSRGPSCGALEPYKAVYKPYRNSSVQKNSSPAQEVAASDMFEGLQQQFLGANETDSAENIHIIQLQVLNKAKERQLDSLVEKLKDSERQVRYLSHQLLIVQDEKDGLALSLRESQQLFQNGKEREMQLEAQIAALEAQVEAFRVSEEKLTKKLR... | null | null | cell projection organization [GO:0030030]; centriole replication [GO:0007099]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535] | centriole [GO:0005814]; centrosome [GO:0005813]; deuterosome [GO:0098536]; nucleoplasm [GO:0005654]; pericentriolar material [GO:0000242]; procentriole [GO:0120098]; procentriole replication complex [GO:0120099] | protein kinase binding [GO:0019901] | null | null | CEP152 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O94986}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O94986}. Note=Colocalizes with CDK5RAP2, WDR62 and CEP63 in a discrete ring around the proximal en... | null | null | null | null | null | FUNCTION: Necessary for centrosome duplication; the function seems also to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (By similarity). Acts as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, 2 molecu... | Mus musculus (Mouse) |
A2AUU0 | METL8_MOUSE | MNVIWRSCICRLRQGKVPHRCQSGVHPVAPLGSRILTDPAKVFEHNMWDHMQWSKEEEDAARKKVEENSATRVAPEEQVKFESDANKYWDIFYQTHKNKFFKNRNWLLREFPEILPVNQNTKEKVGESSWDQVGSSISRTQGTETHCQESFVSPEPGSRGRSAPDPDLEEYSKGPGKTEPFPGSNATFRILEVGCGAGNSVFPILNTLQNIPGSFLYCCDFASEAVELVKSHESYSEAQCSAFIHDVCDDGLAYPFPDGILDVVLLVFVLSSIHPDRALFI | 2.1.1.- | null | fat cell differentiation [GO:0045444]; mRNA methylation [GO:0080009]; positive regulation of mitochondrial translation [GO:0070131]; skeletal muscle tissue development [GO:0007519]; tRNA C3-cytosine methylation [GO:0106217] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | histone acetyltransferase activity [GO:0004402]; mRNA methyltransferase activity [GO:0008174]; tRNA (cytidine-3-)-methyltransferase activity [GO:0052735] | PF08242; | 3.40.50.150; | Methyltransferase superfamily, METL family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H825}. Cytoplasm {ECO:0000305|PubMed:15992539}. Nucleus {ECO:0000305|PubMed:15992539}. Note=Mitochondrial protein (By similarity). The cytoplasmic or nuclear localization observed by some groups is either the result of an incorrect localization caused by N-te... | CATALYTIC ACTIVITY: Reaction=cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50956, Rhea:RHEA-COMP:12849, Rhea:RHEA-COMP:12851, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; Evi... | null | null | null | null | FUNCTION: Mitochondrial S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of mitochondrial tRNA(Ser)(UCN) and tRNA(Thr) (By similarity). N(3)-methylcytidine methylation modification regulates mitochondrial translation efficiency a... | Mus musculus (Mouse) |
A2AVA0 | SVEP1_MOUSE | MWSRLAFCCWALALVSGWTNFQPVAPSLNFSFRLFPEASPGALGRLAVPPASSEEEAAGSKVERLGRAFRSRVRRLRELSGSLELVFLVDESSSVGQTNFLNELKFVRKLLSDFPVVSTATRVAIVTFSSKNNVVARVDYISTSRAHQHKCALLSREIPAITYRGGGTYTKGAFQQAAQILRHSRENSTKVIFLITDGYSNGGDPRPIAASLRDFGVEIFTFGIWQGNIRELNDMASTPKEEHCYLLHSFEEFEALARRALHEDLPSGSFIQEDMARCSYLCEAGKDCCDRMASCKCGTHTGQFECICEKGYYGKGLQHE... | null | null | cell migration [GO:0016477]; epidermis development [GO:0008544]; epithelial cell-cell adhesion [GO:0090136]; gene expression [GO:0010467]; lymph circulation [GO:0003017]; lymph vessel development [GO:0001945]; lymph vessel morphogenesis [GO:0036303]; negative regulation of complement activation, classical pathway [GO:0... | cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; chromatin binding [GO:0003682]; integrin binding [GO:0005178]; integrin binding involved in cell-matrix adhesion [GO:0098640] | PF00008;PF12947;PF07645;PF07699;PF12661;PF02494;PF00354;PF00084;PF00092; | 2.60.120.200;2.10.70.10;2.60.40.10;2.10.25.10;2.10.50.10;3.40.50.410; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22654117}. Nucleus {ECO:0000250|UniProtKB:Q4LDE5}. Cytoplasm {ECO:0000250|UniProtKB:Q4LDE5}. Membrane {ECO:0000250|UniProtKB:Q4LDE5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4LDE5}. | null | null | null | null | null | FUNCTION: Required for morphological development, cell alignment and migration of lymphatic endothelial cells during embryonic development, potentially via modulation of ANGPT2-TIE1 signaling and subsequent activation of FOXC2 transcription (PubMed:28179430). Required for embryonic lymphatic vascular development, via m... | Mus musculus (Mouse) |
A2AVJ5 | PRR5L_MOUSE | MTRGLAPLLPIEFHKMGSFRRPRPRFMSSPVLSELPRFQAARQALQLSSNSAWNSVQTAVINVFKGGGLQSNELYALNESIRRLLKSELGSFITDYFQNQLLAKGLSFVEEKIKLCEGDNRIEVLAEVWDHFFTETLPTLQAIFYPVQGQELTIRQISLLGFRDLVLLKVKLGDVLLLAQSKLPSSVIQMLLILQSVHEPTGPSEGYLQLEELVKQVVSPFLSISGDRSCSGPTYSLARRHSRVRPKVTVLNYASLMTTVGRPLNEMVLTPLTEQEGEAYLEKCGSVRRHTVANAHSDIQLLAMATMMHSGLGEEAGGED... | null | null | cellular response to oxidative stress [GO:0034599]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of signal transduction [GO:0009968]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of intracellular protein transport [GO:0090316]; ... | mitochondrion [GO:0005739]; TORC2 complex [GO:0031932] | ubiquitin protein ligase binding [GO:0031625] | PF08539; | null | PROTOR family | PTM: Ubiquitinated. Ubiquitination by RFFL promotes proteasomal degradation of PRR5L thereby modifying the substrate-specific activity of the mTORC2 complex. Ubiquitination by RFFL is stimulated by LPA/lysophosphatidic acid (By similarity). {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Associates with the mTORC2 complex that regulates cellular processes including survival and organization of the cytoskeleton (By similarity). Regulates the activity of the mTORC2 complex in a substrate-specific manner preventing for instance the specific phosphorylation of PKCs and thereby controlling cell mi... | Mus musculus (Mouse) |
A2AVZ9 | S43A3_MOUSE | MASKGLPLYLATLLTGLLECIGFAGVLFGWTSLLFVFKAENYFSEPCEQDCLLQSNVTGPSDLKAQDEKFSLIFTLASFMNNFMTFPTGYIFDRFKTTVARLIAIFFYTCATIIIAFTSANTAMLLFLAMPMLAVGGILFLITNLQIGNLFGKHRSTIITLYNGAFDSSSAVFLVIKLLYEQGISLRSSFIFMSVCSVWHIARTFLLMPKGHIPYPLPPNYSYGLCSRFGASKKENKAAEHETKELRSKECLPPKEENSGPEQQQQQEQQQQQQQQQEQHEQHSFRRCALSRRFILHVVWLSIIQLWHYLFIGTLNSLLT... | null | null | hypoxanthine transport [GO:0035344] | basolateral plasma membrane [GO:0016323] | adenine transmembrane transporter activity [GO:0015207]; fatty acid transmembrane transporter activity [GO:0015245]; guanine transmembrane transporter activity [GO:0015208]; xenobiotic transmembrane transporter activity [GO:0042910] | PF07690; | 1.20.1250.20; | SLC43A transporter (TC 2.A.1.44) family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q8NBI5}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=adenine(out) = adenine(in); Xref=Rhea:RHEA:71523, ChEBI:CHEBI:16708; Evidence={ECO:0000250|UniProtKB:Q8NBI5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71524; Evidence={ECO:0000250|UniProtKB:Q8NBI5}; CATALYTIC ACTIVITY: Reaction=guanine(out) = guanine(in); Xref=Rhea:RHEA:71531, C... | null | null | null | null | FUNCTION: Sodium-independent purine-selective nucleobase transporter which mediates the equilibrative transport of extracellular purine nucleobases such as adenine, guanine and hypoxanthine (By similarity). May regulate fatty acid (FA) transport in adipocytes, acting as a positive regulator of FA efflux and as a negati... | Mus musculus (Mouse) |
A2AWL7 | MGAP_MOUSE | MEEKQQIILANQDGGTVTGGAPTFFVILKQPGNGKTDQGILVTNRDARALLSRESSPGKSKEKICLPADCTVGKITVTLDNNSMWNEFHNRSTEMILTKQGRRMFPYCRYWITGLDSNLKYILVMDISPVDSHRYKWNGRWWEPSGKAEPHILGRVFIHPESPSTGHYWMHQPVSFYKLKLTNNTLDQEGHIILHSMHRYLPRLHLVPAEKATEVIQLNGPGVHTFTFPQTEFFAVTAYQNIQITQLKIDYNPFAKGFRDDGLSSKPQREGKQRNSSDQEGNSVSSSPAHRVRLTEGEGSEIHSGDFDPVLRGHEASSLS... | null | null | cell fate specification [GO:0001708]; cellular response to leukemia inhibitory factor [GO:1990830]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; MLL1 complex [GO:0071339]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-... | PF00010;PF16059;PF00907; | 4.10.280.10;2.60.40.820; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Functions as a dual-specificity transcription factor, regulating the expression of both MAX-network and T-box family target genes. Functions as a repressor or an activator. Binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX target genes. Suppresses transcriptional activation b... | Mus musculus (Mouse) |
A2AWP0 | BIRC7_MOUSE | MFSPADLFRAAVFSMGPESRARDSVRGPELSHREDGSGRTQEQDKPHCPCNHVLGQDCLDGQILGQLRPLSEEEESSGAAFLGEPAFPEMDSEDLRLASFYDWPSTAGIQPEPLAAAGFFHTGQQDKVRCFFCYGGLQSWERGDDPWTEHARWFPRCQFLLRSKGRDFVERIQTYTPLLGSWDQREEPEDAVSATPSAPAHGSPELLRSRRETQPEDVSEPGAKDVQEQLRQLQEERRCKVCLDRAVSIVFVPCGHFVCTECAPNLQLCPICRVPICSCVRTFLS | 2.3.2.27 | null | apoptotic process [GO:0006915]; lens development in camera-type eye [GO:0002088]; negative regulation of apoptotic process [GO:0043066]; negative regulation of necroptotic process [GO:0060546]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; positive regulation of JNK cascade [GO:0... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00653;PF13920; | 3.30.40.10; | IAP family | PTM: Autoubiquitinated and undergoes proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q96CA5}.; PTM: The truncated protein (tLivin) not only loses its anti-apoptotic effect but also acquires a pro-apoptotic effect. {ECO:0000250|UniProtKB:Q96CA5}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96CA5}. Cytoplasm {ECO:0000250|UniProtKB:Q96CA5}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CA5}. Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively cytoplasm, whereas the truncated form (tLivin) is found i... | 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:0000250|UniProtKB:Q96CA5}; | null | null | null | null | FUNCTION: Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity.... | Mus musculus (Mouse) |
A2AX52 | CO6A4_MOUSE | MGTWKTFWLIISLAAGLGFVKSQRIVCREASVGDIVFLVHNSINPQHAHSVRNFLYILANSLQVGRDNIRVGLAQYSDTPTSEFLLSVYHRKGDVLKHIRGLQFKPGGNRMGQALQFILEHHFREGAGSRASQGVPQVAVVVSSGLTEDHIREPAEALRRAGILVYAIGVKDASQAELREISSSPKDNFTFFVPNFPGLPGLAQKLRPELCSTLGKAAQYTERESPACSEASPADIVFLVDSSTSIGLQNFQKVKHFLHSVVSGLDVRSDQVQVGLVQYSDNIYPAFPLKQSSLKSAVLDRIRNLPYSMGGTSTGSALEF... | null | null | cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; protein-containing complex [GO:0032991] | collagen binding [GO:0005518] | PF01391;PF00092; | 3.40.50.410; | Type VI collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}. | Mus musculus (Mouse) |
A2BD05 | NEK6_PIG | MAGQPSHMPHGGSPNNLCHTPGPAHPPDPQRHPNALSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGIVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCIYPDPNQRPDIGYVHQVARQMHVWTSST | 2.7.11.34 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of mitotic metaphase/anaphase transition [GO:0030071] | centriolar satellite [GO:0034451]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; protein-containing complex [GO:0032991]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; kinesin binding [GO:0019894]; magnesium ion binding [GO:0000287]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transcription corepressor binding [G... | PF00069; | 1.10.510.10; | Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily | PTM: Autophosphorylated. Phosphorylation at Ser-206 is required for its activation. Phosphorylated upon IR or UV-induced DNA damage. Phosphorylated by CHEK1 and CHEK2. Interaction with APBB1 down-regulates phosphorylation at Thr-210 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Colocalizes with APBB1 at the nuclear speckles. Colocalizes with PIN1 in the nu... | 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=2.7.11.34; Evidence={ECO:0000250|UniProtKB:Q9HC98}; CATALYT... | null | null | null | null | FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphoryla... | Sus scrofa (Pig) |
A2BDX3 | MOCS3_MOUSE | MAAPEDVAALQAEITRREEELASLKRRLAAALTAEPEPERPLRVPPPPLAPRAALSRDEILRYSRQLLLPELGVRGQLRLAAAAVLVVGCGGLGCPLAQYLAAAGVGRLGLVDHDVVETSNLARQVLHGEAQAGESKARSAAAALRRLNSAVECVAYPRALAEDWALDLVRGYDVVADCCDNVPTRYLVNDACVLAGRPLVSASALRFEGQMTVYHHDGGPCYRCVFPRPPPPETVTNCADGGVLGAVPGVLGCAQALEVLKIAAGLGSSYSGSMLLFDGLGGHFRRIRLRRRRPDCVVCGQQPTVTRLQDYEAFCGSSA... | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; molybdopterin cofactor biosynthetic process [GO:0032324]; protein urmylation [GO:0032447]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; sulfurtransferase activity [GO:0016783]; thios... | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM... | Mus musculus (Mouse) |
A2BGM5 | FOXN4_DANRE | MTVQSKLQGRGKFKKRFFRAGQQVPRPTLELSSVWLSKIFYNPEQHHNKQKMIESGITTRMSGIHENPGQSHHTSAQDYRLLTTDPSQLKDELPGDLQSLSWLTSVDVPRLQQIGGGRPDFTSSAQSSLLERQTAQLNSMTVAGGAGSAIHLQSEMQHSPLAINSMPQFSPGFPCAASVYQTAPQQVLTFTQANQQCSPGGLYGNYNSQNLFPQPRITAHSQDLQPKCFPKPIYSYSCLIAMALKNSKTGSLPVSEIYSFMKEHFPYFKTAPDGWKNSVRHNLSLNKCFEKVENKMSGSSRKGCLWALNPAKIDKMEEEM... | null | null | amacrine cell differentiation [GO:0035881]; atrioventricular canal development [GO:0036302]; heart looping [GO:0001947]; heart valve development [GO:0003170]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templa... | nucleus [GO:0005634] | chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565] | PF00250; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. | null | null | null | null | null | FUNCTION: Transcription factor essential for neural and some non-neural tissues development. Binds to an 11-bp consensus sequence containing the invariant tetranucleotide 5'-ACGC-3'. During development of the central nervous system, required to specify the amacrine and horizontal cell fates from multipotent retinal pro... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A2BH40 | ARI1A_MOUSE | MAAQVAPAAASSLGNPPPPPSELKKAEQQQREEAGGEAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLPEPPGGGGGGGSSSSDGVGAPPHSAAAALPPPAYGFGQAYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPPQAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYGGG... | null | null | androgen receptor signaling pathway [GO:0030521]; cardiac chamber development [GO:0003205]; cardiac muscle cell differentiation [GO:0055007]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; embryo implantation [GO:0007566]; forebrain development [GO:0030900]; formation of primary germ layer [GO:... | bBAF complex [GO:0140092]; brahma complex [GO:0035060]; chromatin [GO:0000785]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nucleoplasm [GO:0005654]; SWI/SNF complex [GO:0016514] | ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; nucleosome binding [GO:0031491] | PF01388;PF12031; | 1.10.150.60;1.25.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}. | null | null | null | null | null | FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome ... | Mus musculus (Mouse) |
A2BIE7 | TAPT1_DANRE | MADSVAAGLGDENETENEDKEREKRLFSGVKKMEKQAAASDVTETLGFYERKAKCKDRKTNVSDLSLVRFISAELTRGYFLEHNEAKYTERRERVYTCLRIPKELEKLMIFGYFLCLDVFLYVFTLLPLRVLLALVRLLTLPCCGLSGSRILQPAQVCDVLKGFIMVLCYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYTLLLIVCLR... | null | null | cartilage development [GO:0051216]; cell projection organization [GO:0030030]; cranial skeletal system development [GO:1904888]; neural crest cell development [GO:0014032]; ossification [GO:0001503]; positive regulation of bone development [GO:1903012]; positive regulation of cartilage development [GO:0061036]; positiv... | centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; membrane [GO:0016020] | null | PF05346; | null | TAPT1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6NXT6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6NXT6}. Membrane {ECO:0000250|UniProtKB:Q6NXT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6NXT6}. | null | null | null | null | null | FUNCTION: Plays a role in primary cilia formation (PubMed:26365339). Involved in cartilage and bone development (PubMed:26365339). May play a role in the differentiation of cranial neural crest cells (PubMed:26365339). May act as a downstream effector of hoxc8 during development (By similarity). {ECO:0000250|UniProtKB:... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A2BIL7 | BAZ1B_DANRE | MAPLLGRKPYPLVKPLSEPPGPGEEVYTIEHTKEAFRNKEEYEARLRRYGERIWTCKSTGSSQLTHKEAWEEEQEVTELLQEEYPVWFEKPVLEIVHHNTVPLDKLVDQVWVEILTKYAVGEKCDLMVGNDKTLSVEVVKIHPLENPPEENAEKKMEGACDSPSSDKENASQENLKKEPQSKEEESRRESLSDRARRSPRKLPTTMKEEKKKWVMPKFLPHKYDVKLVNEDKVISDVPADNLFRTERPPNKEIMRYFIRHYALRLGSGESAPWVVEDELVKKFSLPSKFSDFLLDPHKFLAENPSTKRKSLSSPEGKPRK... | 2.7.10.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | chromatin remodeling [GO:0006338]; DNA damage response [GO:0006974]; phosphorylation [GO:0016310]; post-translational protein modification [GO:0043687] | nucleus [GO:0005634]; WICH complex [GO:0090535] | ATP binding [GO:0005524]; histone binding [GO:0042393]; histone H2AXY142 kinase activity [GO:0140801]; histone kinase activity [GO:0035173]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715] | PF00439;PF00628;PF10537;PF15612;PF15613; | 1.20.920.10;3.30.40.10; | WAL family, BAZ1B subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063, ECO:0000255|PROSITE-ProRule:PRU00475}. Note=Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase (By similarity). Localizes to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; | null | null | null | null | FUNCTION: Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apopt... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A2BIX4 | SPEE1_HYPBU | MELGMFRLNIYQPGGPIGALYPVEKILYHGRSQYQEIMILVLRGFGKTLVLDGLIQSTESDEHIYHETLVHPAMTVHPNPRRVLILGGGEGATLREVLKHNTVEKAVMVDIDGEVVRVAREYLPEWHQGAFDDPRAQVVIMDGFEYIKEAARRGEDFDVIIMDLTDPFGPKIAAKLYTKEAIGLVKSVLRSDGILVTQAGCAALFPEAFEKVYGSVKSLFAHAEEYGVWVPSFMYVNSFVFASDKYRLTDLSMEEVDRRLRERGVETRFYSGLRHYTLIGLGGIRLLEGRGS | 2.5.1.126; 2.5.1.127; 2.5.1.79 | null | polyamine biosynthetic process [GO:0006596]; spermidine biosynthetic process [GO:0008295] | cytoplasm [GO:0005737] | spermidine synthase activity [GO:0004766]; sym-norspermidine synthase activity [GO:0050314]; thermospermine synthase activity [GO:0010487] | PF17284;PF01564; | 2.30.140.10;3.40.50.150; | Spermidine/spermine synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}. | CATALYTIC ACTIVITY: Reaction=norspermine + S-adenosyl 3-(methylsulfanyl)propylamine = caldopentamine + 2 H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:42868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443, ChEBI:CHEBI:58704, ChEBI:CHEBI:82769; EC=2.5.1.127; Evidence={ECO:0000269|PubMed:19822146}; CATALYTIC ... | null | null | null | null | FUNCTION: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine g... | Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5) |
A2CEH0 | POC1B_DANRE | MASVMEDPTLERHFKGHKDVISCADFNPNNKQLATGSCDKSLMIWNLAPKARAFRFVGHTDVITGVNFAPSGSLVASSSRDQTVRLWTPSIKGESTVFKAHTASVRSVHFSRDGQRLVTASDDKSVKVWGVERKKFLYSLNRHTNWVRCARFSPDGRLIASCGDDRTVRLWDTSSHQCINIFTDYGGSATFVDFNSSGTCIASSGADNTIKIWDIRTNKLIQHYKVHNAGVNCFSFHPSGNYLISGSSDSTIKILDLLEGRLIYTLHGHKGPVLTVTFSRDGDLFASGGADSQVLMWKTNFDSLNYRELLSKHSKRVTPD... | null | null | centriole replication [GO:0007099]; cilium assembly [GO:0060271]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; heart development [GO:0007507]; optokinetic behavior [GO:0007634]; renal system process [GO:0003014]; retina homeostasis [GO:0001895]; retina layer formation [GO:0... | centriole [GO:0005814]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; extracellular region [GO:0005576] | null | PF00400; | 2.130.10.10; | WD repeat POC1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8TC44}. | null | null | null | null | null | FUNCTION: Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. {ECO:0000250|UniProtKB:Q8TC44, ECO:0000269|PubMed:20008567}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A2CEI6 | PIWL2_DANRE | MDPKRPTFPSPPGVIRAPWQQSTEDQSQLLDQPSLGRARGLIMPIDEPLPGRGRAFSVPGEMPVRFGRGITQSIAAEPLVGMARGVRLPMEEGGFGRGRGFLLPTPEPTVGIGRGAAIGPVPTLDIQKAEVEEKMPELQAEVAPTVAKVGSPGTGSSLVSMFRGLGIEPGKTWGRGAAPVGRGAAGDMGADLQPKPTIIGASLTPEREEVRSEESISFLGRGFTGFGRAAMPHMTVGRGPIGPLSPSPSVAAPFSLISASSASEDAPVAPGTPPKVEVKIETVKEPLQKIGTKGSPIPIGSNYIPICCKNDAVFQYHVTF... | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9JMB7}; | gamete generation [GO:0007276]; germ-line stem cell population maintenance [GO:0030718]; meiotic cell cycle [GO:0051321]; negative regulation of SMAD protein signal transduction [GO:0060392]; oogenesis [GO:0048477]; piRNA processing [GO:0034587]; positive regulation of gene expression [GO:0010628]; regulation of transl... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; P granule [GO:0043186]; PET complex [GO:1990923]; pi-body [GO:0071546] | metal ion binding [GO:0046872]; piRNA binding [GO:0034584]; RNA endonuclease activity [GO:0004521] | PF08699;PF02170;PF02171; | 3.40.50.2300;2.170.260.10;3.30.420.10; | Argonaute family, Piwi subfamily | PTM: Methylated on arginine residues; required for the interaction with Tudor domain-containing protein and subsequent localization to the meiotic nuage, also named P granule. {ECO:0000250|UniProtKB:Q8CDG1}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18833190}. Nucleus {ECO:0000269|PubMed:18833190}. Note=Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (By similarity). In mitotic and early meiotic cells of ovary, it... | null | null | null | null | null | FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:18833190). Plays an essential role in germ cell differentiation and meiosis, independently of the function in transposa... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A2CG49 | KALRN_MOUSE | MVLSGSFRNDGLKASDVLPILKEKVAFVSGGRDKRGGPILTFPARSNHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGSKWDLIKPLLKTLQEAFPAEIHVALIIKPDNFWQKQKTNFGSSKFIFETSMVSVEGLTKLVDPSQLTEEFDGSLDYNHEEWIELRLSLEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKVLKAPVEELDREGQRLLQCIRCSDGFSGRNCIPGSADFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWISHNKELFLQSHT... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O60229}; | adult locomotory behavior [GO:0008344]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; habituation [GO:0046959]; intracellular signal transduction [GO:0035556]; lactation [GO:0007595]; maternal behavior [GO:0042711]; maternal process involved in parturition [GO:0060137]; memory [GO:0007613]; modification of pos... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density [GO:0014069]; presynapse [GO:0098793] | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13716;PF00041;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: Autophosphorylated. {ECO:0000250|UniProtKB:O60229}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60229, ECO:0000250|UniProtKB:P97924}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O60229, ECO:0000250|UniProtKB:P97924}. | 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; Evidence={ECO:0000250|UniProtKB:O60229}; CATALYTI... | null | null | null | null | FUNCTION: Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity (By similarity). {ECO:000... | Mus musculus (Mouse) |
A2CG63 | ARI4B_MOUSE | MKALDEPPYLTVGTDVSAKYRGAFCEAKIKTAKRLVKVKVTFRHDSSTVEVQDDHIKGPLKVGAIVEVKNLDGAYQEAVINKLTDASWYTVVFDDGDEKTLRRSSLCLKGERHFAESETLDQLPLTNPEHFGTPVIGKKTNRGRRSNHIPEEESSSSSSDDDEEERKQTDELLGKVVCVDYVSLEKKKAMWFPALVVCPDCSDEIAVKKDNILVRSFKDGKFTSVPRKDVHEITSDTVPKPDAVLKQAFDQALEFHKSRAIPANWKTELKEDSSSSEAEEEEEEEDDEKEKEDNSSEEEEEIEPFPEERENFLQQLYKFM... | null | null | chromatin organization [GO:0006325]; establishment of Sertoli cell barrier [GO:0097368]; genomic imprinting [GO:0071514]; negative regulation of cell migration [GO:0030336]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nega... | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | transcription cis-regulatory region binding [GO:0000976] | PF01388;PF08169;PF11717; | 2.30.30.140;1.10.150.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity). Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting cent... | Mus musculus (Mouse) |
A2CI34 | DUSTY_PIMPR | MENPQKAGPLLRDLTRAFSHYNKHNLLLKKNLKETIAFFREIRQNHSNTCSTSGPELDSGQLRCISFPRHDEDHLQKVVGCAPYILILGQDCSARYQLLNCMLGERLLPLGSDAGGACGVEGGACRRRKLCFTHGRQTRLSLALPGQYELVHQLAAHCGRWDTVPREDLEIQECEDPAQRLAELEITLHHALLQEAKIMVLPCRNVQPVEEALEDCRRGILPIILYAVSKATLSADQLSELQKVRETLPYPVCFVRIPTEPAPDPPGQRSALFAQLVSQELIGGAAGNCACGAPAQTPGKMQGILGEDLERLHRVLVPFA... | 2.7.12.1 | null | cellular response to fibroblast growth factor stimulus [GO:0044344]; embryonic organ development [GO:0048568]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast growth factor receptor signalin... | anchoring junction [GO:0070161]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6XUX1}. Cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Cell junction {ECO:0000250|UniProtKB:Q6XUX1}. | 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879}; CATALYTI... | null | null | null | null | FUNCTION: May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. May play a role in the embryonic development. {ECO:0000250|UniProtKB:Q4VSN1, ECO:0000250|UniProtKB:Q6XUX3}. | Pimephales promelas (Fathead minnow) |
A2CI35 | DUSTY_STRPU | MSSRRLGSSRARGRDLAHEVKHFGGLTKHLKKIIFDSNNCLTELKTSDHFEEEVISTLVLPPVADEIVGKVTKNPPALVIFGQTYTSKATLVNKIFREDLFQIVDDSDNNKTWRAVHLKYGSQRNTRLTLTNSFELLNEEPGSPVMRNSWTGIPRVEMLVKEEHQKDACMLSATTEATLNHPLLQCKLQILVTPHNCPGISISQAYNVCTHNVLPVLLYCFDKDQLSEENLRDLQELQNCAGTLPILFVDCREPSEPLVAHRERRLVEDAHEDFDDDSAYDTDERIEGERERHNGLDARLRRRCRPTPNDRPSVIDQLSR... | 2.7.12.1 | null | cellular response to fibroblast growth factor stimulus [GO:0044344]; embryonic organ development [GO:0048568]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast growth factor receptor signalin... | anchoring junction [GO:0070161]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6XUX1}. Cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Cell junction {ECO:0000250|UniProtKB:Q6XUX1}. | 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879}; CATALYTI... | null | null | null | null | FUNCTION: May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. May play a role in the embryonic development. {ECO:0000250|UniProtKB:Q4VSN1, ECO:0000250|UniProtKB:Q6XUX3}. | Strongylocentrotus purpuratus (Purple sea urchin) |
A2D4U1 | OSTCN_ATEGE | MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV | null | null | biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast diffe... | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147] | null | null | Osteocalcin/matrix Gla protein family | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86546}. | null | null | null | null | null | FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly ... | Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey) |
A2D5H2 | SIX1_LAGLA | MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQGNMGHARSSNYSLPGLTASQPSHGLQAHQHQLQDSLLGPLTSSLVDLGS | null | null | apoptotic process [GO:0006915]; branching involved in ureteric bud morphogenesis [GO:0001658]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic skeletal system morphogenesis [GO:0048704]; epithelial cell differentiation [GO:0030855]; generation of neurons [GO:0048699]; inner ear development [GO:0048839]... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF05920;PF16878; | 1.10.10.60; | SIX/Sine oculis homeobox family | PTM: Phosphorylated during interphase; becomes hyperphosphorylated during mitosis. Hyperphosphorylation impairs binding to promoter elements (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the anaphase promoting complex (APC), leading to its proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15475}. Cytoplasm {ECO:0000250|UniProtKB:Q15475}. | null | null | null | null | null | FUNCTION: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development (By similarity). Plays an important role in the development of several organs, including kidney, muscle and inner ear (By similarity). Depending on context, functions as a transcriptional repress... | Lagothrix lagotricha (Brown woolly monkey) (Humboldt's woolly monkey) |
A2D670 | OSTCN_MACMU | MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV | null | null | biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast diffe... | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147] | null | null | Osteocalcin/matrix Gla protein family | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86546}. | null | null | null | null | null | FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly ... | Macaca mulatta (Rhesus macaque) |
A2ICN5 | MEF2A_PIG | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESGTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLADSSMLSPPQATLHRNVSPGAPQRPPSTGSAGGMLSTSDLTVPNGAGSSPVGNGFVNSRASPNLVGTTGANSLGKVMPTESPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQAPQPLATPVVSVTTP... | null | null | apoptotic process [GO:0006915]; cardiac conduction [GO:0061337]; cellular response to calcium ion [GO:0071277]; dendrite morphogenesis [GO:0048813]; ERK5 cascade [GO:0070375]; MAPK cascade [GO:0000165]; mitochondrial genome maintenance [GO:0000002]; mitochondrion distribution [GO:0048311]; negative regulation of transc... | nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; histone acetyltransferase binding [GO:0035035]; histone deacetylase binding [GO:0042826]; protein dimerization activity [GO:0046983]; RNA polymerase ... | PF12347;PF00319; | 3.40.1810.10; | MEF2 family | PTM: Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation. Phosphorylati... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}. | null | null | null | null | null | FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also i... | Sus scrofa (Pig) |
A2IDD5 | CCD78_HUMAN | MEHAATTGPRPGPPSRRVENVVLRAKDWLPGAPGGTAVWATSLEAEVPPDLALNKEQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEELLVAYRAP... | null | null | cell projection organization [GO:0030030]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; skeletal muscle contraction [GO:0003009] | centriole [GO:0005814]; cytoplasm [GO:0005737]; deuterosome [GO:0098536]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529] | null | PF14739; | null | CCDC78 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, perinuclear region. Cell membrane, sarcolemma. Sarcoplasmic reticulum. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in ... | null | null | null | null | null | FUNCTION: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amp... | Homo sapiens (Human) |
A2PYH4 | HFM1_HUMAN | MLKSNDCLFSLENLFFEKPDEVENHPDNEKSLDWFLPPAPLISEIPDTQELEEELESHKLLGQEKRPKMLTSNLKITNEDTNYISLTQKFQFAFPSDKYEQDDLNLEGVGNNDLSHIAGKLTYASQKYKNHIGTEIAPEKSVPDDTKLVNFAEDKGESTSVFRKRLFKISDNIHGSAYSNDNELDSHIGSVKIVQTEMNKGKSRNYSNSKQKFQYSANVFTANNAFSASEIGEGMFKAPSFSVAFQPHDIQEVTENGLGSLKAVTEIPAKFRSIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRL... | 3.6.4.12 | null | resolution of meiotic recombination intermediates [GO:0000712] | nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; nucleic acid binding [GO:0003676] | PF00270;PF00271;PF02889; | 3.40.50.300;1.10.3380.10;1.10.10.10; | Helicase family, SKI2 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=3.6.4.12; | null | null | null | null | FUNCTION: Required for crossover formation and complete synapsis of homologous chromosomes during meiosis. {ECO:0000250|UniProtKB:D3Z4R1}. | Homo sapiens (Human) |
A2PYL6 | HXK2_HORSE | MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLAATTHPTASVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQKVEMENQIYAIPEDIMQGSGTQLFDHIAGCLANFMDKLQIKDKKLPLGFTFSFPCIQTKLDESFLVSWTKGFKSRGVEGRDVVTLIRKAIQRRGDFDIDIVAMVNDTVATMMTCGYDDQNCEIGLIVGMGSNACYMEEMRYIDTVEGDEGRMCINMEWGAFGDDGTLDDIRTEFDQEIDMGSLNPGQQLFEKMISGMYMGELVRLILVKMAKEELLF... | 2.7.1.1 | null | carbohydrate phosphorylation [GO:0046835]; fructose 6-phosphate metabolic process [GO:0006002]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeostasis [GO:0001678] | cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396] | PF00349;PF03727; | 3.30.420.40;3.40.367.20; | Hexokinase family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P52789}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52789}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P52789}. Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane. The interactio... | CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000250|UniProtKB:P52789}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evid... | null | PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000250|UniProtKB:P52789}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000250|UniProtKB:P52789}. | null | null | FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate. Plays a key role in maintaining the in... | Equus caballus (Horse) |
A2PZA5 | FC1_PHOAM | MEFKYSEVVEPSTYYTEGLCEGIDVRKSKFTTLEDRGAIRAHEDWNKHIGPCGEYRGTLGPRFSFISVAVPECIPERLEVISYANEFAFLHDDVTDHVGHDTGEVENDEMMTVFLEAAHTGAIDTSNKVDIRRAGKKRIQSQLFLEMLAIDPECAKTTMKSWARFVEVGSSRQHETRFVELAKYIPYRIMDVGEMFWFGLVTFGLGLHIPDHELELCRELMANAWIAVGLQNDIWSWPKERDAATLHGKDHVVNAIWVLMQEHQTDVDGAMQICRKLIVEYVAKYLEVIEATKNDESISLDLRKYLDAMLYSISGNVVWS... | 2.5.1.29; 4.2.3.43 | null | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386] | null | farnesyltranstransferase activity [GO:0004311]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF00348;PF19086; | 1.10.600.10; | Terpene synthase family; FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate = diphosphate + fusicocca-2,10(14)-diene; Xref=Rhea:RHEA:26245, ChEBI:CHEBI:33019, ChEBI:CHEBI:52463, ChEBI:CHEBI:57533; EC=4.2.3.43; Evidence={ECO:0000269|PubMed:17360612, ECO:0000269|PubMed:26734760}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + i... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.2 uM for GPP {ECO:0000269|PubMed:26734760}; KM=0.14 uM for FPP {ECO:0000269|PubMed:26734760}; KM=0.632 uM for GGPP {ECO:0000269|PubMed:26734760}; | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:17360612, ECO:0000269|PubMed:26734760}. | null | null | FUNCTION: Multifunctional diterpene synthase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constr... | Phomopsis amygdali (Fusicoccum amygdali) |
A2Q0Z0 | EF1A1_HORSE | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV... | 3.6.5.- | null | cellular response to epidermal growth factor stimulus [GO:0071364]; regulation of D-erythro-sphingosine kinase activity [GO:1900022]; translation [GO:0006412]; translational elongation [GO:0006414] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746] | PF00009;PF03144;PF03143; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily | PTM: ISGylated. {ECO:0000250|UniProtKB:P68104}.; PTM: Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2. Phosphorylation by TGFBR1 inhibits translation elongation. {ECO:0000250|UniProtKB:P68104}.; PTM: Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P68104}. Nucleus {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P68104}. Cell membrane {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytopl... | 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; Evidence={ECO:0000250|UniProtKB:P68104}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6810... | null | null | null | null | FUNCTION: Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing ... | Equus caballus (Horse) |
A2Q0Z1 | HSP7C_HORSE | MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKA... | 3.6.4.10 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated autophagy translocation complex disassembly [GO:1904764]; clathrin coat disassembly [GO:0072318]; late endosomal microautophagy [GO:0061738]; mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; pro... | autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic cytosol [GO:0099524]; presynaptic cytosol [GO:0099523]; Prp19 complex [GO:00... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; clathrin-uncoating ATPase activity [GO:1990833]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; protein-macromolecule adaptor activity [GO:0030674] | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P11142}.; PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding. {ECO:0000250|UniProtKB:P11142}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11142}. Melanosome {ECO:0000250|UniProtKB:P11142}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11142}. Cell membrane {ECO:0000250|UniProtKB:P11142}. Lysosome membrane {ECO:0000250|UniProtKB:P11142}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11142}; Cytopl... | 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=3.6.4.10; Evidence={ECO:0000250|UniProtKB:P11142}; | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and... | Equus caballus (Horse) |
A2Q5W1 | ERN1_MEDTR | MEIQFQQPNMQNQKAGISVTNKGGKFKGRNRNSNNTNKFVGVRQRPSGRWVAEIKDTTQKIRMWLGTFETAEEAARAYDEAACLLRGSNTRTNFITHVSLDSPLASRIRNLLNNRKGDKKQEDGAVASAPSNSKTTISNTSTITSNDDNKESTLSTCATRNTELFEDAYKPDLSNCKEVFESGSQSNISCGFGPFFDHFSFTQLLDMAKNDDITDASSLELSEFERMKVERQISASLYAINGVHEYMETVQESNEALWDLPPLCSLFC | null | null | nodulation [GO:0009877]; positive regulation of DNA-templated transcription [GO:0045893] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF00847; | 3.30.730.10; | AP2/ERF transcription factor family, ERF subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:17827349, ECO:0000269|PubMed:23077241}. | null | null | null | null | null | FUNCTION: Transcription factor involved in symbiotic nodule signaling in response to rhizobial Nod factors (NFs) (PubMed:17449807, PubMed:17827349). Binds to the GCC-box (NF-responsive box) of ENOD11 promoter. Acts as a transcriptional activator of NF-responsive box-containing target gene promoters in root hairs (PubMe... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A2QAC0 | LAD_ASPNC | MATATVLEKANIGVFTNTKHDLWVADAKPTLEEVKNGQGLQPGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGQVVAVAPDVTSLKPGDRVAVEPNIICNACEPCLTGRYNGCENVQFLSTPPVDGLLRRYVNHPAIWCHKIGDMSYEDGALLEPLSVSLAGIERSGLRLGDPCLVTGAGPIGLITLLSARAAGASPIVITDIDEGRLEFAKSLVPDVRTYKVQIGLSAEQNAEGIINVFNDGQGSGPGALRPRIAMECTGVESSVASAIWSVKFGGKVFVIGVGKNEMTVPFMRLSTWEIDLQYQYRY... | 1.1.1.12 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:20414651}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:20414651}; | L-arabinose catabolic process to xylulose 5-phosphate [GO:0019569]; sorbitol catabolic process [GO:0006062] | null | L-arabinitol 4-dehydrogenase activity [GO:0050019]; L-iditol 2-dehydrogenase activity [GO:0003939]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-arabinitol + NAD(+) = H(+) + L-xylulose + NADH; Xref=Rhea:RHEA:16381, ChEBI:CHEBI:15378, ChEBI:CHEBI:17399, ChEBI:CHEBI:18403, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.12; Evidence={ECO:0000269|PubMed:16321042}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=89 mM for L-arabinitol (at pH 9.6) {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; KM=5 mM for L-xylulose (at pH 9.6) {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; KM=50 uM for NAD ... | PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route): step 2/5. {ECO:0000269|PubMed:16321042}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4. Active from pH 7 to pH 11. {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; | FUNCTION: Catalyzes the NAD-dependent oxidation of L-arabinitol to L-xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. Not active with NADP as cosubstrate. {ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}. | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2QAN3 | BGALA_ASPNC | MKLSSACAIALLAAQAAGASIKHRINGFTLTEHSDPAKRELLQKYVTWDDKSLFINGERIMIFSGEFHPFRLPVKELQLDIFQKVKALGFNCVSFYVDWALVEGKPGEYRADGIFDLEPFFDAASEAGIYLLARPGPYINAESSGGGFPGWLQRVNGTLRSSDKAYLDATDNYVSHVAATIAKYQITNGGPIILYQPENEYTSGCCGVEFPDPVYMQYVEDQARNAGVVIPLINNDASASGNNAPGTGKGAVDIYGHDSYPLGFDCANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVEFQGGSYDPWGGPGFAACSELLN... | 3.2.1.23 | null | carbohydrate metabolic process [GO:0005975]; lactose catabolic process [GO:0005990]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576]; vacuole [GO:0005773] | beta-galactosidase activity [GO:0004565]; oligosaccharide binding [GO:0070492] | PF13364;PF10435;PF13363;PF01301; | 2.102.20.10;2.60.390.10;2.60.120.260;3.20.20.80; | Glycosyl hydrolase 35 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:28391618}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92.5 mM for lactose {ECO:0000269|PubMed:28391618}; Note=kcat is 214.9 sec(-1). {ECO:0000269|PubMed:28391618}; | null | null | null | FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000269|PubMed:28391618}. | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2QHE5 | FDC1_ASPNC | MSAQPAHLCFRSFVEALKVDNDLVEINTPIDPNLEAAAITRRVCETNDKAPLFNNLIGMKNGLFRILGAPGSLRKSSADRYGRLARHLALPPTASMREILDKMLSASDMPPIPPTIVPTGPCKENSLDDSEFDLTELPVPLIHKSDGGKYIQTYGMHIVQSPDGTWTNWSIARAMVHDKNHLTGLVIPPQHIWQIHQMWKKEGRSDVPWALAFGVPPAAIMASSMPIPDGVTEAGYVGAMTGSSLELVKCDTNDLYVPATSEIVLEGTLSISETGPEGPFGEMHGYIFPGDTHLGAKYKVNRITYRNNAIMPMSSCGRLT... | 4.1.1.102 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754}; COFACTOR: Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746; Evidence={ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083743, ECO:0000269|PubMed:26083754}; Note=Binds 1 prenylated FMN (prenyl-FMN) per su... | aromatic amino acid family catabolic process [GO:0009074]; cinnamic acid catabolic process [GO:0046281]; ferulate metabolic process [GO:0033494]; styrene metabolic process [GO:0018966]; ubiquinone biosynthetic process [GO:0006744] | cytosol [GO:0005829] | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity [GO:0008694]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145] | PF01977;PF20696;PF20695; | 1.20.5.4570;3.40.1670.10; | UbiD family, UbiD-like/FDC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03196}. | CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + H(+) = 4-hydroxystyrene + CO2; Xref=Rhea:RHEA:33227, ChEBI:CHEBI:1883, ChEBI:CHEBI:12876, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; EC=4.1.1.102; Evidence={ECO:0000255|HAMAP-Rule:MF_03196}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + H(+) = CO2 + styrene; Xref=Rhea:RHEA:46920... | null | null | null | null | FUNCTION: Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites. {ECO:0000255|HAMAP-Rule:MF_03196, ECO:00... | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2QIL5 | ATG1_ASPNC | MGLFHHSTLFLPLLRRSNEGPHGEMPIGHYTRLSEIGRGSFAVVYKGVHTRSRTYVAIKSVTMTKLSRKLKENLASEISILKQLHHPHIVALLDCHDTTSNIHLVMEFCALGDLSHFIKGRNTLQDSPYTRELIAKYPNPGEGAGLNEVIVRHFLKQLSSALRFLRDRDLIHRDIKPQNLLLCPAPSSYRSGAADVVPFKSSEDSFSPKTGLESLPMLKLADFGFARSLPATSLAETLCGSPLYMAPEILRYEKYDAKADLWSVGTVLYEMVVGRAPFRAVNHIELIKKIEQNKDQISFPSKNRVSEDIRELIRGLLKQH... | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; axon extension [GO:0048675]; cellular response to oxidative stress [GO:0034599]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO... | autophagosome [GO:0005776]; cytosol [GO:0005829]; phagophore assembly site membrane [GO:0034045] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | 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; Evidence={ECO:0000250|UniProtKB:P53104}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective a... | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2QQ28 | RSP5_ASPNC | MGSNLPAQPNLRVTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPIPNQANGLHRSHAQSSTSSGLVPQVSSASHPSVSPGQAEPSAAASNVSLHPQRVPSTTRPTSTVGPVNGGPAPPPNGPQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEQTQRTQREANMQLERRAHQSRMLPEDRTGANSPNLQESPQPQPQQAHTPPAG... | 2.3.2.26 | null | chromatin organization [GO:0006325]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; mitochondrion organization [GO:0007005]; nonfunctional rRNA decay [GO:0070651]; poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of fatty acid biosynthetic process [GO:0045723]; po... | cellular bud tip [GO:0005934]; cytosolic ribosome [GO:0022626]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; RSP5-BUL ubiquitin ligase complex [GO:1990306]; ubiquitin ligase complex [GO:0000151] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00168;PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | RSP5/NEDD4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39940}. | 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=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. {ECO:0000250|UniProtKB:Q5BDP1}. | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2QTW5 | BPHA_ASPNC | MLALLLSPYGAYLGLALLVLYYLLPYLKRAHLRDIPAPGLAAFTNFWLLLQTRRGHRFVVVDNAHKKYGKLVRIAPRHTSIADDGAIQAVYGHGNGFLKSDFYDAFVSIHRGLFNTRDRAEHTRKRKTVSHTFSMKSIGQFEQYIHGNIELFVKQWNRMADTQRNPKTGFASLDALNWFNYLAFDIIGDLAFGAPFGMLDKGKDFAEMRKTPDSPPSYVQAVEVLNRRGEVSATLGCYPALKPFAKYLPDSFFRDGIQAVEDLAGIAVARVNERLRPEVMANNTRVDLLARLMEGKDSNGEKLGRAELTAEALTQLIAGS... | 1.14.14.92 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | benzoate catabolic process [GO:0043639] | intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | benzoate 4-monooxygenase activity [GO:0018664]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=benzoate + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxybenzoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:18033, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16150, ChEBI:CHEBI:17879,... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.083 mM for benzoate {ECO:0000269|PubMed:11594739}; KM=0.097 mM for 2-fluorobenzoate {ECO:0000269|PubMed:11594739}; KM=0.31 mM for 2-chlorobenzoate {ECO:0000269|PubMed:11594739}; KM=0.28 mM for 2-hydroxybenzoate {ECO:0000269|PubMed:11594739}; KM=1.6 mM for 2-methy... | null | null | null | FUNCTION: Cytochrome P450 monooxygenase; part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway (PubMed:11594739, Ref.5). Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its... | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2R2V4 | OTASE_ASPNC | MVRRIASATPMVQSPMSPLGTTYCVRPNPVSLNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMK... | 3.4.17.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24947135}; | ochratoxin A catabolic process [GO:1900817]; proteolysis [GO:0006508] | extracellular region [GO:0005576] | carboxypeptidase activity [GO:0004180]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237] | PF01979; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Ochratoxinase amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}. | CATALYTIC ACTIVITY: Reaction=H2O + ochratoxin A = L-phenylalanine + ochratoxin alpha; Xref=Rhea:RHEA:72751, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:166829, ChEBI:CHEBI:192527; Evidence={ECO:0000269|PubMed:24947135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72752; Evidence={ECO:0000269|PubMed:24947... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:24947135}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 66 degrees Celsius. {ECO:0000269|PubMed:24947135}; | FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by As... | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2R3H4 | UBA4_ASPNC | MNGVEQTCASLRTQIAATEAKLADLKRELEIAEQAAASHKQNAADAEGGSERRWPLLDEEYRRYGRQMIVPQLGIQGQLKLRSAKVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDAVESSNLHRQVLHRTRNIGKLKVDSAIEYLKELNPHSKYIAHREHLAPEAAPEIFSNYDLILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNNPPRPAGDKTGGPCYRCVFPKPPPANTVTSCADGGIVGPVVGTMGVLQALEAIKVITADETTTPPPPSLHIFSAYSTPLFRTIKLRSRRPNCAVCSAEASVTV... | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiola... | cytosol [GO:0005829] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtr... | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm... | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2R6H1 | OTAA_ASPNC | MSSAPIPQSEPLAIIGLACKYANGIDSPEALYEQVMAARCMHGAMPSNRMDASFYYHPTSEATGTSYSKGGYFLNCDLNAFDSPFFQLSEIDVMAMDPQQKMLLENVYHALENAGIPLKNAISSPTSVFVGCSNNDHLALANSDLLLSLKGKGTGTSPSILANRVSWFYDFQGTSQTIDTACSSSLVAFHQGCMDVRAGKSAMSIISGINLIEHPGPTLYLSSLGVLSPDGKSMSFDARANGYGRGEGVGTVIVKPLQAALRDGNRIRAIVRSTGSNQDGRTPGITVPNPSAQERLIHDVYRVADLDPRRTGYVEAHGTG... | 2.3.1.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000255}; | fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; ochratoxin A biosynthetic process [GO:1900818]; secondary metabolic process [GO:0019748] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; catalytic activity [GO:0003824]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF08240;PF16197;PF00109;PF02801;PF08659;PF08242;PF21089;PF00550;PF14765; | 3.40.47.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150; | null | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 9 H(+) + 4 malonyl-CoA + 5 NADPH = 7-methylmellein + 3 CO2 + 5 CoA + 4 H2O + 5 NADP(+); Xref=Rhea:RHEA:72767, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:1925... | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27959549}. | null | null | FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratog... | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A2RH77 | ADDA_LACLM | MSEVKLTPEQNEAIHSSGKNILVSASAGSGKTFVMAQRIVEKVKQGIEIDRLFISTFTKKAASELRMRLERDLKKARQESSDDEEAHRLTLALQNLSNADIGTMDSFTQKLTKANFNRVNIDPNFRILADQTESDLIRQEVFEQLVESYLSADESLNISKDKFEKLIKNFSKDRNILGFQKVVYTIYRFASATENPISWLENQFLKGFETYKSLTDLSEDFTVNVKENLLTFFELLENSLTNGVIAKKGAGRDKANLILDNKNELLEAISKKDFVTCTALFLSIDTDIRVGSSKDEALSALKKDFSAQKQDLVGSKSKPG... | 3.1.-.-; 5.6.2.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01451}; | double-strand break repair via homologous recombination [GO:0000724] | cytosol [GO:0005829]; DNA helicase complex [GO:0033202] | 3'-5' DNA helicase activity [GO:0043138]; 3'-5' exonuclease activity [GO:0008408]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded DNA binding [GO:0003690]; isomerase activity [GO:0016853] | PF00580;PF13361; | 1.10.10.160;3.90.320.10;3.40.50.300; | Helicase family, AddA subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01451}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:... | null | null | null | null | FUNCTION: The heterodimer acts both as an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the L.lactis chi site (5'-GCGCGTG-3'), which stimulates homologous recombination. The RexA (AddA) nuclease domain is required for chi fragment generation; this subunit has 3'... | Lactococcus lactis subsp. cremoris (strain MG1363) |
A2RJT9 | PYRDA_LACLM | MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLDYVLKNQKENAQEGPIFFSIAGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIADFHGKLKSL | 1.3.98.1 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205] | cytoplasm [GO:0005737] | dihydroorotate dehydrogenase (fumarate) activity [GO:1990663] | PF01180; | 3.20.20.70;2.30.26.10; | Dihydroorotate dehydrogenase family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + fumarate = orotate + succinate; Xref=Rhea:RHEA:30059, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864; EC=1.3.98.1; Evidence={ECO:0000269|PubMed:8021180}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for dihydroorotate {ECO:0000269|PubMed:12732650}; KM=250 uM for fumarate {ECO:0000269|PubMed:12732650}; Vmax=18.6 umol/min/mg enzyme {ECO:0000269|PubMed:12732650}; | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway. | null | null | FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro, but cannot use NAD(+) as an electron acceptor. {ECO:0000269|PubMed:8021180}. | Lactococcus lactis subsp. cremoris (strain MG1363) |
A2RRP1 | NBAS_HUMAN | MAAPESGPALSPGTAEGEEETILYDLLVNTEWPPETEVQPRGNQKHGASFIITKAIRDRLLFLRQYIWYSPAPFLLPDGLVRLVNKQINWHLVLASNGKLLAAVQDQCVEIRSAKDDFTSIIGKCQVPKDPKPQWRRVAWSYDCTLLAYAESTGTVRVFDLMGSELFVISPASSFIGDLSYAIAGLIFLEYKASAQWSAELLVINYRGELRSYLVSVGTNQSYQESHCFSFSSHYPHGINTAIYHPGHRLLLVGGCETAEVGMSKASSCGLSAWRVLSGSPYYKQVTNGGDGVTAVPKTLGLLRMLSVKFYSRQGQEQDG... | null | null | negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000623]; nuclear-transcribed mRNA catabolic process [GO:0000956]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890] | cytosol [GO:0005829]; Dsl1/NZR complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | SNARE binding [GO:0000149] | PF15492;PF08314; | 2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20577004}. Endoplasmic reticulum {ECO:0000269|PubMed:19369418}. Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in Golgi-to-endoplasmic reticulum (ER) retrograde transport; the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:19369418). Required for normal embryonic development (By similarity). May play a role in the nonse... | Homo sapiens (Human) |
A2RRU4 | SCAP_RAT | MTLTERLREKISQAFYNHGLLCASYPIPIILFTGLCILACCYPLLKLPLPGTGPVEFSTPVKGYSPPPADSDHKQGEPSEQPEWYVGAPVAYIQQIFVKSSVSPWHRNLLAVDVFRSPLSRAFQLVEEIRNHVLRDSSGTKSLEEVCLQVTDLLPGLRKLRSLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRMVSYTITLVFQRYHAKFLSSLRARLMLLHPSPNCSLRAENLVHVHFKEEIGIAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAV... | null | null | cellular lipid metabolic process [GO:0044255]; cholesterol metabolic process [GO:0008203]; COPII-coated vesicle cargo loading [GO:0090110]; immune response [GO:0006955]; positive regulation of cholesterol biosynthetic process [GO:0045542]; regulation of cholesterol biosynthetic process [GO:0045540]; regulation of fatty... | endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; protein-containing complex [GO:0032991]; SREBP-SCAP complex [GO:0032936] | protein-containing complex binding [GO:0044877]; sterol binding [GO:0032934] | PF12349;PF00400; | 2.130.10.10; | WD repeat SCAP family | PTM: Ubiquitinated at Lys-454 and Lys-466. RNF145 triggers ubiquitination of SCAP, likely inhibiting SCAP-SREBP complex transport to the Golgi apparatus and the subsequent processing/maturation of SREBF2/SREBP2. {ECO:0000250|UniProtKB:Q6GQT6}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P97260}; Multi-pas... | null | null | null | null | null | FUNCTION: Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. At high s... | Rattus norvegicus (Rat) |
A2RST1 | MGST2_MOUSE | MAGDSSLLAAVSLLSACQQSYFAWRVGRARLKHKIAPPAVTGPLEFERIFRAQQNSLEFYPVFIVMLWMAGWYFNQVFAACLGLLYIYARHKYFWGYAEAAEKRITGFRLSLGILTLLPVLAVLGVASRFLNEYLDFHVAKKLRKPF | 1.11.1.-; 2.5.1.18; 4.4.1.20 | null | glutathione biosynthetic process [GO:0006750]; leukotriene biosynthetic process [GO:0019370]; lipid metabolic process [GO:0006629]; membrane lipid catabolic process [GO:0046466]; response to lipopolysaccharide [GO:0032496]; response to organonitrogen compound [GO:0010243] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886] | enzyme activator activity [GO:0008047]; glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; leukotriene-C4 synthase activity [GO:0004464] | PF01124; | 1.20.120.550; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99735}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q99735}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:Q99735}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinit... | null | null | null | null | FUNCTION: Catalyzes several different glutathione-dependent reactions. Catalyzes the glutathione-dependent reduction of lipid hydroperoxides, such as 5-HPETE. Has glutathione transferase activity, toward xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB). Catalyzes also the conjugation of leukotriene... | Mus musculus (Mouse) |
A2RSY6 | TRM1L_MOUSE | MENMAEEELLPQEKEEAQVRVPTPAPDSAPVPAPAADTALDSAPTPDSDPAPALAPAPAPALSPSLASVPEEAESKRHISIQRRLADLEKLAFGTEGDVDSASSLNSDNPGTENSQTCPLCPKEKFRAYSSHKLRRHLQNLHWKISVEFEGYRMCICHLACRPVKPTIVGEQISSKLGAHYHCIICSATITRRTDMLGHVKRHVNKGETKSRYIAASTAKSSNEILKETDTDIQVFPNYSIPQKTDSYFNPKMKLNRQIIFCTLAALAKERKPLECLDAFGATGIMGLQWAKHLGNAVKVTINDLNENSVTLIQKNCHLN... | 2.1.1.- | null | adult behavior [GO:0030534]; adult locomotory behavior [GO:0008344]; tRNA N2-guanine methylation [GO:0002940] | nucleus [GO:0005634] | metal ion binding [GO:0046872]; tRNA (guanine(10)-N2)-methyltransferase activity [GO:0160102]; tRNA binding [GO:0000049] | PF02005; | 3.30.56.70;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Trm1 family | null | null | null | null | null | null | null | FUNCTION: May play a role in motor coordination and exploratory behavior. {ECO:0000269|PubMed:17198746}. | Mus musculus (Mouse) |
A2RT67 | DEND3_MOUSE | MAEPAARHLSLPSGLLELCALLGASQDSLRGLEQIAQKRGVKSASSLVPEVLSVFVPPFTTKEDGQVPGASCALGKGRRRSFRKKREKPRMEPWKSHPGDSKGPDSEDVTIPGGVDLLALPQLCFPGCVCVASEPKEDYIHFLVLTDVCGNRTYGVVAQYYRPLHDEYCFYNGKSHWEPSVISARCFVPFAVCVVSRFPYYNSLKDCLSCLLTHLKLCKDFEVDNHIKDFAARLSLIPSPPPGPLHLIFNMKPLQVVFPSRADPESPIVDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLMAECFVAYLH... | null | null | endosome to lysosome transport [GO:0008333]; protein catabolic process [GO:0030163]; regulation of Rab protein signal transduction [GO:0032483] | cytoplasmic vesicle [GO:0031410] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF02141; | 3.30.450.200;3.40.50.11500;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28249939}. Note=Transiently recruited to membranes to activate Rab12. {ECO:0000269|PubMed:28249939}. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor (GEF) activating Rab12. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab12 into its active GTP-bound form. Regulates autophagy in response to starvation through Rab12 activation (PubMed:24719330, PubMed:25925668, PubMed:28249939). Starvation leads to UL... | Mus musculus (Mouse) |
A2RTF1 | CTSRB_MOUSE | MESPLIYVMLVLLNVFVFSSGVIHNKGKERTYFSCSGEGILTGLHTIKLFLTMDNLKVRCFFRNENQSPSKEILGLFTSGGLAPNMIITNSTFYGGYYFKLTPFSNRLEWLIDIPRQNITVNTDIAAVEQWMIKITMHEGLNIYDTEGTLLDLVREPILQWNLGRVLTEMEVRDLYPEVNDIKVTKSPCANDVALIGFMMKPSSNGVFIGKTISGFWTYKECIWHDLTEIIYAELKDEHQGLTVIDLVLTNHFLVILTSLGLYVSSDLRYPTTSQIKLSRAEFCGFERVDYIRGNLWYNEKCFANRESFEVDYVTITFNR... | null | null | sperm capacitation [GO:0048240] | CatSper complex [GO:0036128]; cilium [GO:0005929]; monoatomic ion channel complex [GO:0034702]; sperm principal piece [GO:0097228] | null | PF15149;PF21541;PF21548; | null | null | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:34225353}; Single-pass membrane protein {ECO:0000269|PubMed:34225353}. Note=Predominantly located in the principal piece of the sperm tail. {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:34225353}. | null | null | null | null | null | FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:17478420, PubMed:34225353). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:17478420). {ECO:0000269|PubMed:17478420, ECO:00... | Mus musculus (Mouse) |
A2RTX5 | SYTC2_HUMAN | MAAEALAAEAVASRLERQEEDIRWLWSEVERLRDEQLNAPYSCQAEGPCLTREVAQLRAENCDLRHRLCSLRLCLAEERSRQATLESAELEAAQEAGAQPPPSQSQDKDMKKKKMKESEADSEVKHQPIFIKERLKLFEILKKDHQLLLAIYGKKGDTSNIITVRVADGQTVQGEVWKTTPYQVAAEISQELAESTVIAKVNGELWDLDRPLEGDSSLELLTFDNEEAQAVYWHSSAHILGEAMELYYGGHLCYGPPIENGFYYDMFIEDRAVSSTELSALENICKAIIKEKQPFERLEVSKEILLEMFKYNKFKCRILN... | 6.1.1.3 | null | threonyl-tRNA aminoacylation [GO:0006435] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; threonine-tRNA ligase activity [GO:0004829] | PF03129;PF02824;PF00587;PF07973; | 3.10.20.30;3.40.50.800; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BLY2}. Nucleus {ECO:0000250|UniProtKB:Q8BLY2}. Note=Primarily cytoplasmic. Also detected at lower levels in the nucleus. {ECO:0000250|UniProtKB:Q8BLY2}. | CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; ... | null | null | null | null | FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage. {ECO:0000250|UniProtKB:Q8BLY2}. | Homo sapiens (Human) |
A2RU14 | TM218_HUMAN | MAGTVLGVGAGVFILALLWVAVLLLCVLLSRASGAARFSVIFLFFGAVIITSVLLLFPRAGEFPAPEVEVKIVDDFFIGRYVLLAFLSAIFLGGLFLVLIHYVLEPIYAKPLHSY | null | null | null | cilium [GO:0005929]; membrane [GO:0016020] | null | null | null | TMEM218 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9CQ44}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000250|UniProtKB:Q9CQ44}. | null | null | null | null | null | FUNCTION: May be involved in ciliary biogenesis or function. {ECO:0000250|UniProtKB:Q9CQ44}. | Homo sapiens (Human) |
A2RU30 | TESP1_HUMAN | MEASVLSPTSWEKRRAWLRQSRNWQTQVLEEEAAAALQDVPDPEPSSLDDVFQEGNPINKIEDWLQDCGYSEEGFSEEAGQFIYNGFCSHGTSFEDDLTLGAEATLLAANGKLFSRSFLETARPCQLLDLGCSLASSSMTGGTNKTSSSISEILDKVQEDAEDVLFSLGFGQEDHKDTSRIPARFFTTPSQAKGIDFQLFLKSQVRRIEMEDPCLMLASRFKQVQTLAVTADAFFCLYSYVSKTPVQKFTPSHMFWNCNHPTDVPSIRILSREPEPQSPRDRLRKAISKMCLYTCPRDRPPPPHNTPKRNSLDQVVLEVM... | null | null | COP9 signalosome assembly [GO:0010387]; positive regulation of T cell differentiation in thymus [GO:0033089]; positive regulation of T cell receptor signaling pathway [GO:0050862]; protein localization [GO:0008104]; T cell differentiation in thymus [GO:0033077]; TCR signalosome assembly [GO:0036399] | COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; TCR signalosome [GO:0036398] | phospholipase binding [GO:0043274]; signaling receptor binding [GO:0005102] | PF14722; | null | null | PTM: May be phosphorylated in response to store-operated Ca(+2) entry. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:23501103}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23501103}. Note=May localize to mitochondria-associated endoplasmic reticulum membrane (MAM). {ECO:0000269|PubMed:23501103}. | null | null | null | null | null | FUNCTION: Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promote... | Homo sapiens (Human) |
A2RU49 | HYKK_HUMAN | MSSGNYQQSEALSKPTFSEEQASALVESVFGLKVSKVRPLPSYDDQNFHVYVSKTKDGPTEYVLKISNTKASKNPDLIEVQNHIIMFLKAAGFPTASVCHTKGDNTASLVSVDSGSEIKSYLVRLLTYLPGRPIAELPVSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHRENFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILIESSKSASGNAEYQVSGILDFGDMSYGYYVFEVAITIMYMMIESKSPIQVGGHVLAGFESITPLTAVEKGALFLLVCSRFCQSLVMA... | 2.7.1.81 | null | lysine catabolic process [GO:0006554]; phosphorylation [GO:0016310] | mitochondrial matrix [GO:0005759] | amino acid kinase activity [GO:0019202]; hydroxylysine kinase activity [GO:0047992] | PF01636; | 3.90.1200.10; | Aminoglycoside phosphotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(5R)-5-hydroxy-L-lysine + GTP = (5R)-5-phosphooxy-L-lysine + GDP + H(+); Xref=Rhea:RHEA:19049, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:57882, ChEBI:CHEBI:58189, ChEBI:CHEBI:58357; EC=2.7.1.81; Evidence={ECO:0000269|PubMed:22241472}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=280 uM for (5R)-5-hydroxy-L-lysine (in the presence of 2 mM ATP) {ECO:0000269|PubMed:22241472}; KM=7.6 uM for (5R)-5-hydroxy-L-lysine (in the presence of 0.2 mM GTP) {ECO:0000269|PubMed:22241472}; KM=810 uM for ATP (in the presence of 0.5 mM (5R)-5-hydroxy-L-lysine... | null | null | null | FUNCTION: Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-lysine. {ECO:0000269|PubMed:22241472}. | Homo sapiens (Human) |
A2RUB1 | MEIOC_HUMAN | MEVRRGDTCPRPHPSGLREEGLEPKVAFPGGANRCWNLGADAGSRLTDVFGSVMLTGSASFYDCYTSQSEDNVDLRQTYTPFSSTEYSSSVDSSLFCAPWSTYGDDIKQPSNSQISIKNRIQTERNDYGSETDLYGLVSNILEEQDKSQPYFAEGTCSSNLKSVWPMNTSRFADHHDLLTETKRPIDTVISQQAFYSDESVSAMEKQYLRNSNLTPQQKIDELHHGFTGLDLEEQWMYPSRSDHSNCHNIQTNDTAKTTFQEYPLIKNCFTPQTGLSDIMKESGVDIYHYGRDRICTKGLEAPLQQKRAEMFLSQFNRYN... | null | null | chromosome organization involved in meiotic cell cycle [GO:0070192]; double-strand break repair [GO:0006302]; female meiosis I [GO:0007144]; germline cell cycle switching, mitotic to meiotic cell cycle [GO:0051729]; male meiosis I [GO:0007141]; metaphase chromosome alignment [GO:0051310]; mRNA stabilization [GO:0048255... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF15189; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2AG06}. Nucleus {ECO:0000250|UniProtKB:A2AG06}. Note=at late pachytene a fraction is nuclear. {ECO:0000250|UniProtKB:A2AG06}. | null | null | null | null | null | FUNCTION: Is required for meiosis completion in both male and female germ cells. Confers stability to numerous meiotic mRNAs in gonads allowing proper initiation and progression into meiosis prophase I. The function may involve YTHDC2 and is independent of induction by retinoic acid (RA). Maintains an extended meiotic ... | Homo sapiens (Human) |
A2RUB6 | CCD66_HUMAN | MNLGDGLKLETELLDGKTKLILSPYEHKSKISVKMGNKAKIAKCPLRTKTGHILKSTQDTCIGSEKLLQKKPVGSETSQAKGEKNGMTFSSTKDLCKQCIDKDCLHIQKEISPATPNMQKTRNTVNTSLVGKQKPHKKHITAENMKSSLVCLTQDQLQQILMTVNQGNRSLSLTENGKEAKSQYSLYLNSISNQPKDENIMGLFKKTEMVSSVPAENKSVLNEHQETSKQCEQKIAIENEWKPADIFSTLGERECDRSSLEAKKAQWRKELDEQVALKKKEKEVSEKWNDPWKKSESDKIIWEKHQILDQSRETVLLEHP... | null | null | cilium assembly [GO:0060271]; detection of light stimulus involved in visual perception [GO:0050908]; microtubule bundle formation [GO:0001578]; regulation of protein localization to cilium [GO:1903564]; retina homeostasis [GO:0001895] | cell junction [GO:0030054]; centriolar satellite [GO:0034451]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytosol [GO:0005829]; Flemming body [GO:0090543]; microtubule [GO:0005874]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803] | PF15236; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:28235840}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:28235840}. Cell projection, cilium {ECO:0000269|PubMed:28235840}. Cytoplasm, cytoskeleton, ... | null | null | null | null | null | FUNCTION: Microtubule-binding protein required for ciliogenesis (PubMed:28235840). May function in ciliogenesis by mediating the transport of proteins like BBS4 to the cilium, but also through the organization of the centriolar satellites (PubMed:28235840). Plays a role in retina morphogenesis and/or homeostasis (By si... | Homo sapiens (Human) |
A2RUC4 | TYW5_HUMAN | MAGQHLPVPRLEGVSREQFMQHLYPQRKPLVLEGIDLGPCTSKWTVDYLSQVGGKKEVKIHVAAVAQMDFISKNFVYRTLPFDQLVQRAAEEKHKEFFVSEDEKYYLRSLGEDPRKDVADIRKQFPLLKGDIKFPEFFKEEQFFSSVFRISSPGLQLWTHYDVMDNLLIQVTGKKRVVLFSPRDAQYLYLKGTKSEVLNIDNPDLAKYPLFSKARRYECSLEAGDVLFIPALWFHNVISEEFGVGVNIFWKHLPSECYDKTDTYGNKDPTAASRAAQILDRALKTLAELPEEYRDFYARRMVLHIQDKAYSKNSE | 1.14.11.42 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:20972222}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:20972222}; | wybutosine biosynthetic process [GO:0031591] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone H3K36 demethylase activity [GO:0051864]; iron ion binding [GO:0005506]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049]; tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase activity [GO:0102524] | PF13621; | 6.10.140.1470;2.60.120.650; | TYW5 family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + O2 = 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine(37) in tRNA(Phe) + CO2 + succinate; Xref=Rhea:RHEA:37899, Rhea:RHEA-COMP:10379, Rhea:RHEA-COMP:11848, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:... | null | PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis. {ECO:0000269|PubMed:20739293, ECO:0000269|PubMed:20972222}. | null | null | FUNCTION: tRNA hydroxylase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into u... | Homo sapiens (Human) |
A2RUH7 | MBPHL_HUMAN | MEAATAPEVAAGSKLKVKEASPADAEPPQASPGQGAGSPTPQLLPPIEEHPKIWLPRALRQTYIRKVGDTVNLLIPFQGKPKPQAIWTHDGCALDTRRVSVRNGEQDSILFIREAQRADSGRYQLRVQLGGLEATATIDILVIERPGPPQSIKLVDVWGFSATLEWTPPQDTGNTALLGYTVQKADTKSGLWFTVLEHYHRTSCIVSDLIIGNSYAFRVFAENQCGLSETAPITTDLAHIQKAATVYKTKGFAQRDFSEAPKFTQPLADCTTVTGYNTQLFCCVRASPRPKIIWLKNKMDIQGNPKYRALTHLGICSLEI... | null | null | in utero embryonic development [GO:0001701] | myofilament [GO:0036379]; sarcomere [GO:0030017] | null | PF00041;PF07679; | 2.60.40.10; | Immunoglobulin superfamily, MyBP family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000305|PubMed:28778945}. | null | null | null | null | null | FUNCTION: Myosin-binding protein which plays a role in cardiac function (PubMed:28778945). Seems to regulate conduction in the atria and ventricular conduction systems (PubMed:28778945). {ECO:0000269|PubMed:28778945}. | Homo sapiens (Human) |
A2RUV0 | NOTC1_XENTR | MYRIGLLVLIWSLLGLAQGLRCTQTAEMCLNGGRCEMTPGGTGVCLCSSSYFGERCQYPNPCALKNQCMNFGTCEPVLLGNAIDFTCHCPVGFTDKVCLTPVDNACVNNPCRNGGTCELLSSVSDYRCRCPPGWTGDSCQQADPCASNPCANGGKCLPFETQYICKCPSGFHGATCKQDINECSQNPCRNGGQCLNEFGSYRCNCQNRFTGRNCEEPYVPCNPSPCLNGGTCRQTDDTSYECTCLPGFSGQNCEENIDDCPSNNCRNGGTCVDGVNTYNCQCPPDWTGQYCTEDVDECQLMPNACQNGGTCHNTYGGYNC... | null | null | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; cilium assembly [GO:0060271]; Notch signaling involved in heart development [GO:0061314]; regulation of developmental process [GO:0050793]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; Notch binding [GO:0005112]; signaling receptor activity [GO:0038023] | PF12796;PF00008;PF07645;PF12661;PF06816;PF07684;PF00066; | 3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10; | NOTCH family | PTM: O-glycosylated on the EGF-like domains. Contains both O-linked fucose and O-linked glucose. O-linked glycosylation by galnt11 is involved in determination of left/right symmetry: glycosylation promotes activation of notch1, possibly by promoting cleavage by adam17, modulating the balance between motile and immotil... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01705}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q01705}.; SUBCELLULAR LOCATION: [Notch 1 intracellular domain]: Nucleus {ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical processing NICD is translocated to the nucleus. {ECO:0000250... | null | null | null | null | null | FUNCTION: Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enh... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A2RUV9 | AEBP1_RAT | MAAVRTASLLCGLLALLALCPEGSPQTVLTDDEIQEFLEGFLSEFETQSPPREDDVEAQPLPEPTQRARKSKAGGKPRADAEAPPEKNKDKEKKGKKDKGPKAAKHLEGSTRPTKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKRPSAGKRFSTVAPLETPERSLTSPSNPGTRELPEERGRTSLNTWQGQGEETQVEARQHRPEPEEETEMPTLDYNDQIEREDYEDFEYIRRQKQPRPTPSRKRIWPEPPEEKTQEPEERKEVDPPLKPLLPPDYGDGYLIPNYDDLDYYFPHPPPQKPDVGQ... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; peptide metabolic process [GO:0006518]; protein processing [GO:0016485]; regulation of collagen fibril organization [GO:1904026]; regulation of DNA-templated transcription [GO:0006355] | extracellular space [GO:0005615] | calmodulin binding [GO:0005516]; carboxypeptidase activity [GO:0004180]; collagen binding [GO:0005518]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metallocarboxypeptidase activity [GO:0004181]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [G... | PF13620;PF00754;PF00246; | 2.60.40.1120;2.60.120.260;3.40.630.10; | Peptidase M14 family | PTM: Phosphorylated by MAPK1 in vitro. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q640N1}. | null | null | null | null | null | FUNCTION: As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellular matrix (By similarity). May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also po... | Rattus norvegicus (Rat) |
A2RUW1 | TOLIP_RAT | MATTVSTQRGPVYIGELPQDFLRITPTQQQQQIQLDAQAAQQLQYGGAVGTVGRLSITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRWNKVIQCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLKQGQVEDEWYSLSGRQGDDKEGMINLVMSYTSLPAAMMMPPQPVVLMPTVYQQGVGYVPIAGMPAVCSPGMVPMAMPPPAVAPQPRCNEEDLKAIQDMFPNMDREVIRSVLEAQRGNKDAAINSLLQMGEES | null | null | autophagy [GO:0006914]; epithelial cell differentiation [GO:0030855]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; interleukin-1-mediated signaling pathway [GO:0070498]; phosphorylation [GO:0016310]; positive regulation of protein sumoylation [GO:0033235]; protein localization to endosome [G... | cytoplasm [GO:0005737]; early endosome [GO:0005769]; nuclear body [GO:0016604]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991] | interleukin-1, type I receptor binding [GO:0005150]; kinase binding [GO:0019900]; molecular adaptor activity [GO:0060090]; SUMO binding [GO:0032183]; Toll-like receptor binding [GO:0035325]; ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase binding [GO:0031625] | PF00168;PF02845; | 2.60.40.150;1.10.8.10; | Tollip family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H0E2}. Endosome {ECO:0000250|UniProtKB:Q9H0E2}. Early endosome {ECO:0000250|UniProtKB:Q9H0E2}. Note=Localized to endo/exosomal vesicles. {ECO:0000250|UniProtKB:Q9H0E2}. | null | null | null | null | null | FUNCTION: Component of the signaling pathway of IL-1 and Toll-like receptors (By similarity). Inhibits cell activation by microbial products (By similarity). Recruits IRAK1 to the IL-1 receptor complex (By similarity). Inhibits IRAK1 phosphorylation and kinase activity. Connects the ubiquitin pathway to autophagy by fu... | Rattus norvegicus (Rat) |
A2RVJ8 | HIT4_ARATH | MKKGAKRKGVSKAGRKAAVAETQNDEVIEETTKTTQEESQQHEEEVVDEVKENGEEEEAKGDQEEEEDAKPDSLEEDEENQEDEVKAEEVKEEVEKKPVARRGGKRKRATKKDTEIKDEKKPVPKAKKPRAAKVKEEPVYFEEKRSLEDLWKVAFPVGTEWDQLDALYEFNWDFQNLEEALEEGGKLYGKKVYVFGCTEPQLVPYKGANKIVHVPAVVVIESPFPPSDKIGITSVQREVEEIIPMKKMKMDWLPYIPIEKRDRQVDKMNSQIFTLGCTQRRSALRHMKEDQLKKFEYCLPYFYQPFKEDELEQSTEVQIM... | null | null | heat acclimation [GO:0010286]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of heterochromatin formation [GO:0031452]; regulation of cellular response to heat [GO:1900034]; response to heat [GO:0009408] | chromocenter [GO:0010369]; nucleolus [GO:0005730] | null | null | 6.10.250.2770; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:23408827, ECO:0000269|PubMed:25329561}. Nucleus, nucleolus {ECO:0000269|PubMed:25329561}. Note=Localizes to the chromocentre at 23 degrees Celsius, a condensed heterochromatin domain that harbors repetitive elements for which transc... | null | null | null | null | null | FUNCTION: Essential protein required for basal thermotolerance, especially during heat-induced chromocentre decondensation, thus regulating transcriptional gene silencing (TGS). {ECO:0000269|PubMed:23408827, ECO:0000269|PubMed:25329561}. | Arabidopsis thaliana (Mouse-ear cress) |
A2RVK7 | RP41L_ARATH | MAAKPGAATPTYSPKIVGRSRLPIFKDSDLDWSRPDGRGFHQCRPALLQTGAVSSASGSAYAEFGNTKVIVSVFGPRESKKAMVYSDVGRLNCNVSYTNFASPTLGQGTDHKEYSSMLHKALEGVIMMETFPKTTVDVFALVLESGGSDLSVLISCASLALADAGIMMYDLITAVSVSCIGKSLMIDPVTEEEGCEDGSFMMTCMPSRYEITQLTITGEWTTPNINEAMQLCLDASSKLGEIMRDCLKQSASASDE | null | null | nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; seed germination [GO:0009845]; seedling development [GO:0090351]; U4... | cytoplasm [GO:0005737]; cytoplasmic exosome (RNase complex) [GO:0000177]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634] | 3'-5' exonuclease activity [GO:0008408]; RNA binding [GO:0003723] | PF01138;PF03725; | 3.30.230.70; | RNase PH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23132787}. Nucleus {ECO:0000269|PubMed:23132787}. | null | null | null | null | null | FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing, maturation and degradation events. In vitro, is a processive phosphorolytic exonuclease and requires a single-stranded poly(A) tail on the substrate RNA for ... | Arabidopsis thaliana (Mouse-ear cress) |
A2RVM0 | TIC32_ARATH | MWFFGSKGASGFSSRSTAEEVTHGVDGTGLTAIVTGASSGIGVETARVLSLRGVHVVMAVRNTDSGAKVKEDIVKQVPGAKLDVMELDLSSMQSVRKFASEYKSTGLPLNLLINNAGIMACPFMLSKDNIELQFATNHLGHFLLTKLLLDTMKSTSRESKREGRIVNLSSEAHRFSYPEGVRFDKINDKSSYSSMRAYGQSKLCNVLHANELTKQLKEDGVNITANSLHPGAIMTNLGRYFNPYLAVAVGAVAKYILKSVPQGAATTCYVALNPQVAGVSGEYFQDSNIAKPLPLVKDTELAKKVWDFSTKLTDSQSGES... | 1.1.1.- | null | protein transport [GO:0015031] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast inner membrane [GO:0009706]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | oxidoreductase activity [GO:0016491] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in protein precursor import into chloroplasts. Part of the redox regulon consisting of TIC32, TIC 55 and TIC62. {ECO:0000269|PubMed:15180984}. | Arabidopsis thaliana (Mouse-ear cress) |
A2RVQ5 | AGL16_ARATH | MGRGKIAIKRINNSTSRQVTFSKRRNGLLKKAKELAILCDAEVGVIIFSSTGRLYDFSSSSMKSVIERYSDAKGETSSENDPASEIQFWQKEAAILKRQLHNLQENHRQMMGEELSGLSVEALQNLENQLELSLRGVRMKKDQMLIEEIQVLNREGNLVHQENLDLHKKVNLMHQQNMELHEKVSEVEGVKIANKNSLLTNGLDMRDTSNEHVHLQLSQPQHDHETHSKAIQLNYFSFIA | null | null | flower development [GO:0009908]; positive regulation of transcription by RNA polymerase II [GO:0045944]; stomatal lineage progression [GO:0010440] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:... | PF01486;PF00319; | 3.40.1810.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}. | null | null | null | null | null | FUNCTION: Probable transcription factor involved in the regulation of flowering time in long-day photoperiod. Participates in the repression of FT expression and floral transition, by interacting closely with the FLC-SVP pathways (PubMed:24876250). Functions in the satellite meristemoid lineage of stomatal development ... | Arabidopsis thaliana (Mouse-ear cress) |
A2RVU1 | MWL1_ARATH | MFIFLFGLAAFFLCLSAEFQKAKALLRAQVFLKGKDLKWDGESCYLPENRAFGLGIAALVCVSVAQIVGNVVICRGFTKTDKTRTTIFCIILLLFSWVNFAVAVTLISVGASMNREQIYGKGWLNRECYLVKDGVFAASGFLSVTTMAAILGAFAFKVKPSLQVENHDKRHTQNV | null | null | lignin biosynthetic process [GO:0009809]; lignin metabolic process [GO:0009808] | membrane [GO:0016020]; plasma membrane [GO:0005886] | null | PF06749; | null | DESIGUAL family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26930070}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Together with MWL2, contributes to secondary cell wall biology, specifically lignin biosynthesis. {ECO:0000269|PubMed:26930070}. | Arabidopsis thaliana (Mouse-ear cress) |
A2SW69 | ANXA2_SHEEP | MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIVSDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKKKYGKSLYYYIQ... | null | null | null | basement membrane [GO:0005604]; cytoplasm [GO:0005737]; endosome [GO:0005768]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | 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]; cytoskeletal protein binding [GO:0008092]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [G... | PF00191; | 1.10.220.10; | Annexin family | PTM: ISGylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=In the lamina beneath the plasma membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechani... | Ovis aries (Sheep) |
A2SWM2 | SPNS2_DANRE | MCVESDGCEIEGCSSSDEVHTLSGSMSPALKSRDLHHCRPGQKFHAALLRCRTPLVAAGILSFGNVLNYMDRYTVAGVLLDIQKQFKVGDSSAGLLQTVFICSFMVAAPIFGYLGDRFNRKIILSCGIFFWSAVTLLSSFITKEYYWLLVLSRCLVGIGESSYSSISPTIIGDLFTNNKRTVMLSVFYLAIPLGSGLGYILGSIAKDAGGHWYWALRVSPMLGLTAGTLILIFVSEPKRGSADQPGGRLKTRTSWVCDMKALAKNRSYVFSSLASAAVSFATGAFGIWIPQYLVRAQVVQKSAESCTYQPCSSRDSLIFG... | null | null | branching involved in blood vessel morphogenesis [GO:0001569]; cardioblast migration to the midline involved in heart rudiment formation [GO:0003319]; embryonic heart tube morphogenesis [GO:0003143]; embryonic viscerocranium morphogenesis [GO:0048703]; lipid transport [GO:0006869]; regulation of cartilage development [... | endosome membrane [GO:0010008]; membrane [GO:0016020]; plasma membrane [GO:0005886] | sphingolipid transporter activity [GO:0046624]; transmembrane transporter activity [GO:0022857] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Spinster (TC 2.A.1.49) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19074308}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:19074308}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38667, ChEBI:CHEBI:60119; Evidence={ECO:0000250|UniProtKB:Q8IVW8}; CATALYTIC ACTIVITY: Reaction=sphinganine 1-phosphate(in) = sphinganine 1-phosphate(out); Xref=Rhea:RHEA:38671, ChEBI:CHEBI:57939; Evidence={ECO... | null | null | null | null | FUNCTION: Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate, which play critical roles in regulating heart development (PubMed:19062281, PubMed:19074308). Mediates the export of S1P from cells in the extraembryonic yolk syncytial... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A2SZS3 | L_RVFV | MDSILSKQLVDKTGFVRVPIKHFDCTMLTLALPTFDVSKMVDRITIDFNLDDIQGASEIGSTLLPSMSIDVEDMANFVHDFTFGHLADKTDRLLMREFPMMNDGFDHLSPDMIIKTTSGMYNIVEFTTFRGDERGAFQAAMTKLAKYEVPCENRSQGRTVVLYVVSAYRHGVWSNLELEDSEAEEMVYRYRLALSVMDELRTLFPELSSTDEELGKTERELLAMVSSIQINWSVTESVFPPFSREMFDRFRSSPPDSEYITRIVSRCLINSQEKLINSSFFAEGNDKALRFSKNAEECSLAVERALNQYRAEDNLRDLND... | 2.7.7.48; 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A5HC98}; Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site (By similarity). The divalent metal ions are crucial for catalytic activity (PubMed:31948728). {ECO:0000250|UniProtKB:A5HC98, ECO:0000269|PubMed:31948728}; COFAC... | DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694] | host cell endoplasmic reticulum [GO:0044165]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; virion component [GO:0044423] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleoside binding [GO:0001882]; RNA-dependent RNA polymerase activity [GO:0003968] | PF04196;PF12603;PF15518; | null | Bunyavirales RNA polymerase family | null | SUBCELLULAR LOCATION: Host Golgi apparatus {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:I0DF35}. Virion {ECO:0000250|UniProtKB:P20470}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; | null | null | null | null | FUNCTION: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activi... | Rift valley fever virus (RVFV) |
A2T1U1 | ORANG_BRAOB | MSCLGRILSVSYPPDPYGSRLSVSKLSSPGRNRRLRWRFTALDSDSSSLDSDSSDKFAAGFCIIEGPETVQDFAKMQLQEIQDNIRSRRNKIFLHMEEVRRLRIQQRIRNTELGIIDEEQEHELPNFPSFIPFLPPLTAANLRVYYATCFSLIAGIILFGGLLAPTLELKLGIGGTSYKDFIQSLHLPMQLSQVDPIVASFSGGAVGVISALMVVEVNNVKQQEHKRCKYCLGTGYLACARCSSTGSLIISEPVSAIAGGNHSVSTSKTERCSNCSGAGKVMCPTCLCTGMAMASEHDPRIDPFL | null | null | chromoplast organization [GO:0009661]; positive regulation of carotenoid biosynthetic process [GO:1904143]; unidimensional cell growth [GO:0009826] | chloroplast membrane [GO:0031969]; nucleus [GO:0005634] | null | null | null | Orange-like family | null | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305}. Plastid {ECO:0000269|PubMed:17172359}. Nucleus {ECO:0000269|PubMed:21175633}. Note=Targeted to non-green plastids. {ECO:0000269|PubMed:17172359}. | null | null | null | null | null | FUNCTION: Involved in chromoplast differentiation. Is associated with a cellular process that triggers the differentiation of pro-plastids or other non-colored plastids into chromoplasts for carotenoid accumulation (PubMed:17172359, PubMed:18256051). Associated with carotenoid accumulation in de-etiolated cotyledons (P... | Brassica oleracea var. botrytis (Cauliflower) |
A2T2X4 | IFT46_CHLRE | MDDSMDYPDRDGDDLDQFQGTARSQVVQNQPHDEEVNLSESESFAGADEPPAAPRDASLIESHDMDEGPAAPARTLSPTGYEAGKHAPGGIANSDEAPPGAYNAQEYKHLNVGEDVRELFSYIGRYKPQTVELDTRIKPFIPDYIPAVGGIDEFIKVPRPDTKPDYLGLKVLDEPAAKQSDPTVLTLQLRQLSKEAPGAKADMVGRLEHTDENKAKKIQQWIASINDIHKAKPAATVNYSKRMPEIEALMQEWPPEVETFLKTMHMPSGDVELDIKTYARLVCTLLDIPVYDDPVESLHVLFTLYLEFKNNPIFRQHMEM... | null | null | axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; cilium organization [GO:0044782]; cilium-dependent cell motility [GO:0060285]; intraciliary transport [GO:0042073]; outer dynein arm assembly [GO:0036158]; protein stabilization [GO:0050821]; protein transport [GO:0015031]; regulation of cilium assembly [GO:1... | ciliary base [GO:0097546]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514] | null | PF12317; | null | IFT46 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199, ECO:0000269|PubMed:19412537}. Cell projection, cilium {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:188522... | null | null | null | null | null | FUNCTION: Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Plays a role in maintaining IFT complex B stability. {ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:20435895}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A2T3P0 | NSP2_ROTSH | MAELACFCYPHLENDSYKFIPFNNLAIKAMLTAKVDKKDMDKFYDSIIYGIAPPPQFKKRYNTNDNSRGMNFETIMFTKVAMLICEALNSLKVTQANVSNVLSRVVSIRHLENLVIRKENPQDILFHSKDLLLKSTLIAIGQSKEIETTITAEGGEIVFQNAAFTMWKLTYLEHQLMPILDQNFIEYKVTLNEDKPISDVHVKELVAELRWQYNKFAVITHGKGHYRIVKYSSVANHADRVYATFKSNVKTGVNNDFNLLDQRIIWQNWYAFTSSMKQGNTLDVCKRLLFQKMKPEKNPFKGLSTDRKMDEVSQVGV | 3.6.4.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04089}; | viral genome replication [GO:0019079] | host cell cytoplasm [GO:0030430] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723] | PF02509;PF21067; | 3.30.428.20;3.90.1400.10; | Rotavirus NSP2 family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04089}. Note=Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04089}. | null | null | null | null | null | FUNCTION: Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA bindin... | Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58)) |
A2T3P5 | VP7_ROTSH | MYGIEYTTVLTFLISIILLNYILKSLTRIMDFIIYRFLFIIVILSPFLRAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTNIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDATTFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDILDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVDQIIQVMSKRSRSLNSA... | null | null | receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum lumen [GO:0044166]; T=13 icosahedral viral capsid [GO:0039621]; viral outer capsid [GO:0039624] | metal ion binding [GO:0046872] | PF00434; | 3.40.50.11130;2.60.120.800; | Rotavirus VP7 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131}.; PTM: The N-terminus is blocked possibly by pyroglutamic acid. {ECO:0000255|HAMAP-Rule:MF_04131}. | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:1649333, ECO:0000269|PubMed:19036817}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytopla... | null | null | null | null | null | FUNCTION: Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (PubMed:10590110, Pu... | Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58)) |
A2T3Q9 | NSP5_ROTSH | MSLSIDVTSLPSIPSTIYKNESSSTTSTLSGKSIGRSEQYISPDAEAFNKYMLSKSPEDIGPSDSASNDPLTSFSIRSNAVKTNADAGVSMDSSAQSRPSSNVGCDQVDFSLNKGLKVKANLDSSISISTDTKKEKSKQNHKSRKHYPRIEAESDSDDYVLDDSDSDDGKCKNCKYKKKYFALRMRMKQVAMQLIEDL | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04092}; | viral genome replication [GO:0019079] | host cell cytoplasm [GO:0030430] | ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723] | PF01525; | null | Rotavirus NSP5 family | PTM: O-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04092}.; PTM: Hyperphosphorylated on serine residues, when in dimeric form. Phosphorylation by host CK1 is required for the hyperphosphorylation of NSP5 dimer. {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:15520389, ECO:0000269|PubMed:1... | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:14993647, ECO:0000269|PubMed:17182692}. Note=Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {E... | null | null | null | null | null | FUNCTION: Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of vir... | Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58)) |
A2T3S5 | VP3_ROTSH | MKVLALRHSVAQVYADTQVYVHDDTKDSYENAFLISNLTTHNILYLNYSIKTLEILNKSGIAAIALQSLEELFTLIRCNFTYDYELDIIYLHDYSYYTNNEIRTDQHWITKTNIEEYLLPGWKLTYVGYNGSETRGHYNFSFKCQNAATDDDLIIEYIYSEALDFQNFMLKKIKERMTTSLPIARLSNRVFRDKLFPSLLKEHKNVVNVGPRNESMFTFLNYPTIKQFSNGAYLVKDTIKLKQERWLGKRISQFDIGQYKNMLNVLTAIYYYYNLYKSKPIIYMIGSAPSYWIYDVRHYSDFFFETWDPLDTPYSSIHHK... | 2.1.1.56; 2.7.7.50; 3.1.4.- | null | RNA 5'-cap (guanine-N7)-methylation [GO:0106005]; virus-mediated perturbation of host defense response [GO:0019049] | viral nucleocapsid [GO:0019013] | GTP binding [GO:0005525]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; mRNA guanylyltransferase activity [GO:0004484]; phosphoric diester hydrolase activity [GO:0008081]; RNA binding [GO:0003723] | PF05213;PF06929; | null | Rotavirus VP3 family | null | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04128}. Note=Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04128}. | CATALYTIC ACTIVITY: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617;... | null | null | null | null | FUNCTION: Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and cap... | Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58)) |
A2T3T2 | VP4_ROTSH | MASLIYRQLLTNSYTVDLSDEIQEIGSTKSQNVTINPGPFAQTGYAPVNWGPGEINDSTTVEPLLDGPYQPTTFNPPVDYWMLLAPTTPGVIVEGTNNTDRWLATILIEPNVQSENRTYTIFGIQEQLTVSNTSQDQWKFIDVVKTTANGSIGQYGPLLSSPKLYAVMKHNEKLYTYEGQTPNARTAHYSTTNYDSVNMTAFCDFYIIPRSEESKCTEYINNGLPPIQNTRNVVPLSLTARDVIHYRAQANEDIVISKTSLWKEMQYNRDITIRFKFANTIIKSGGLGYKWSEISFKPANYQYTYTRDGEEVTAHTTCSV... | null | null | permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell plasma membrane [GO:0020002]; host cell rough endoplasmic reticulum [GO:0044168]; host cytoskeleton [GO:0044163]; membrane [GO:0016020]; viral outer capsid [GO:0039624] | null | PF17477;PF00426;PF17478; | 1.20.5.170;2.60.120.200; | Rotavirus VP4 family | PTM: [Outer capsid protein VP4]: Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion. Cleavage of VP4 by tryps... | SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:1649333}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04132}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04132}. Host cytoplasm, host cytoskeleton {ECO:0000255|HAMAP-Rule:MF_04132}. Host endo... | null | null | null | null | null | FUNCTION: [Outer capsid protein VP4]: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence (PubMed:1649333). Rotavirus attachment and entry into the host cell probably involves multip... | Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58)) |
A2T6K4 | OSTCN_MACNE | MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV | null | null | biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast diffe... | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147] | null | null | Osteocalcin/matrix Gla protein family | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86546}. | null | null | null | null | null | FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly ... | Macaca nemestrina (Pig-tailed macaque) |
A2T6Y4 | APEX1_PANTR | MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL | 3.1.11.2; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695}; | base-excision repair [GO:0006284]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; damaged DNA binding [GO:0003684]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded ... | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to... | SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocaliz... | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695}; | null | null | null | null | FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DN... | Pan troglodytes (Chimpanzee) |
A2T756 | PDX1_PANTR | MNGEEQYYAATQLYKDSCAFQRGPAPEFSAGPPACLYMGRQPPPPPPHPFPGALGALEQGSPPDISPYEVPPLADDPAVAHLHHHLPAQLALPHPPAGPFPEGAEPGVLEEPNRVQLPFPWMKSTKAHAWKGQWAGGAYAAEPEENKRTRTAYTRAQLLELEKEFLFNKYISRPRRVELAVMLNLTERHIKIWFQNRRMKWKKEEDKKRGGGTAVGGGGVAEPEQDCAVTSGEELLALPPPPPPGGAVPPAAPVAAREGRLPPGLSASPQPSSVAPRRPQEPR | null | null | digestive tract development [GO:0048565]; exocrine pancreas development [GO:0031017]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin secretion [GO:0030073]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; liver development [GO:0001889]; ... | cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family, IPF1/XlHbox-8 subfamily | PTM: Phosphorylated by the SAPK2 pathway at high intracellular glucose concentration. Phosphorylated by HIPK2 on Ser-268 upon glucose accumulation. This phosphorylation mediates subnuclear localization shifting. Phosphorylation by PASK may lead to translocation into the cytosol (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, cytosol {ECO:0000250}. | null | null | null | null | null | FUNCTION: Activates insulin and somatostatin gene transcription. Key regulator of islet peptide hormone expression but also responsible for the development of the pancreas, most probably by determining maturation and differentiation of common pancreatic precursor cells in the developing gut. As part of a PDX1:PBX1b:MEI... | Pan troglodytes (Chimpanzee) |
A2T7I6 | APEX1_PONPY | MPKRGKKGAVAEDGDELKTEPEAKKSKTTAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRRFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLTALCDSKIRSKALGSDHCPITLYLAL | 3.1.11.2; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695}; | base-excision repair [GO:0006284]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; damaged DNA binding [GO:0003684]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded ... | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to... | SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocaliz... | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695}; | null | null | null | null | FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DN... | Pongo pygmaeus (Bornean orangutan) |
A2T7L5 | MYC_PONPY | MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSPRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSLPKSCTSPDSSAFSPSSDSLLSSTESSPQASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHIKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYP... | null | null | chromatin remodeling [GO:0006338]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; G1/S transition of mitotic cell cycle [GO:0000082]; intracellular iron ion homeostasis [GO:0006879]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell di... | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; protein-containing complex binding [GO:0044877] | PF00010;PF02344;PF01056; | 4.10.280.10; | null | PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphoryla... | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}. | null | null | null | null | null | FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogrammi... | Pongo pygmaeus (Bornean orangutan) |
A2T928 | RARGB_DANRE | MRDVFREATPMTCRSPLPDLRDMMEKLTVFEPTIDSTVETQSTSSEEMIPSSPSPPPPPRVYKPCFVCQDKSSGYHYGVSSCEGCKGFFRRSIQKNMVYTCHRDKNCQINKVTRNRCQYCRLRKCFEVGMSKEAVRNDRNKKKKDVKEEVVLPESYELSGELEELVNKVSKAHRETFPSLCQLGKYTTNSSADHRVQLDLGLWDKFSELSTKCIIKIVEFAKRLPGFTSLTIADQITLLKSACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFAGQLLPLEMDDTETGLLSAICLICGDRMDL... | null | null | cell differentiation [GO:0030154]; cellular response to corticotropin-releasing hormone stimulus [GO:0071376]; determination of digestive tract left/right asymmetry [GO:0071907]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; determinati... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | nuclear glucocorticoid receptor binding [GO:0035259]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) c... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A2TGX5 | CLM8_RAT | MTQLASAVWPPTLLLLLLFWVPGCVPLRGPSSVTGTVGESLNVTCQYEERFKMNKKYWCRGSLVLLCKDIVRTGGSEEARNGRVSIRDDRDNLTFTVTLQNLTLEDAGTYMCAVDIPLIDHSFKVELSVVPGNIPVSSPGTTRETTVVPTSFSTKGPTQGSIPEGHHEHYEPQGLSLPVLLSVLALLLLLLVGTSLLAWRMFQKRSVKADKHPEMSQNLRQAEEQSESQYVNLQLHTLPLREEPVPPSQVEVEYSTLALPQEELHYTSVVFDSQRQNSHANGDPPCQSPDQKTEYSEIRKPREGLSDPHP | null | null | establishment of localization in cell [GO:0051649]; mast cell degranulation [GO:0043303]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of B cell receptor signaling pathway [GO:0050859]; negative regulation of eosinophil activation [GO:1902567]; negative regulation of eosinophil migratio... | membrane [GO:0016020]; plasma membrane [GO:0005886] | phosphatase binding [GO:0019902]; phosphatidylethanolamine binding [GO:0008429]; phosphatidylserine binding [GO:0001786]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888] | PF15330;PF07686; | 2.60.40.10; | CD300 family | PTM: Phosphorylated on tyrosine. {ECO:0000250|UniProtKB:Q6SJQ0}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6SJQ0}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6SJQ0}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6SJQ0}. | null | null | null | null | null | FUNCTION: Inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation. Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 but not TRIF through activation of PTPN6. {ECO:0000250|UniPro... | Rattus norvegicus (Rat) |
A2TJ54 | CLN5_SHEEP | MAQAGGAGAGAWGRRGAGAGAGPERAPWRWAPALLWLAAATAAAAAAGDPSRRQWPVPYKRFSFRPEPDPYCQAKYTFCPTGSPIPVMKDDDVIEVFRLQAPVWEFKYGDLLGHLKIMHDAIGFRSTLTEKNYTMEWYELFQLGNCTFPHLRPEMNAPFWCNQGAACFFEGIDDNHWKENGTLVLVATISGGMFNKMAKWVKQDNETGIYYETWTVQASPKKEAEKWFESYDCSKFVLRTYEKLAELGADFKKIETNYTRIFLYSGEPTYLGNETSVFGPTGNKTLALAIKKFYYPFKPHLSTKEFLLSLLQIFDAVVIH... | 2.3.1.-; 3.1.2.22 | null | glycosylation [GO:0070085]; lysosome organization [GO:0007040]; positive regulation of GTP binding [GO:1904426]; retrograde transport, endosome to Golgi [GO:0042147]; signal peptide processing [GO:0006465] | cytosol [GO:0005829]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764] | hydrolase activity, acting on glycosyl bonds [GO:0016798]; mannose binding [GO:0005537]; transferase activity [GO:0016740] | PF15014; | null | CLN5 family | PTM: N-glycosylated with both high mannose and complex type sugars. Glycosylation is important for proper folding and trafficking to the lysosomes. {ECO:0000250|UniProtKB:O75503}.; PTM: [Bis(monoacylglycero)phosphate synthase CLN5]: The type II membrane signal anchor is proteolytically cleaved to produce a mature form ... | SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Lysosome {ECO:0000250|UniProtKB:O75503}.; SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5]: Membrane {ECO:0000250|UniProtKB:O75503}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O75503}. Note=An amphipa... | CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000250|UniPr... | null | null | null | null | FUNCTION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Catalyzes the synthesis of bis(monoacylglycero)phosphate (BMP) via transacylation of 2 molecules of lysophosphatidylglycerol (LPG). BMP also known as lysobisphosphatidic acid plays a key role in the formation of intraluminal vesicles and in maintai... | Ovis aries (Sheep) |
A2TK72 | VM3A2_DEIAC | KREAEANRTPEQQIYDPYKYVETVFVVDKAMVTKYNGDLDKIKTRMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTYLLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCIMGPSISPEPSKFFSNCSYIQCWDFIMNHNPECIDNEPLGTDIISPPLCGNELLEA | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9PW35}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9PW35}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF01421; | 3.40.390.10; | Venom metalloproteinase (M12B) family, P-III subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9W6M5}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=538.2 uM for N-(p-Tosyl)-Gly-Pro-Lys-pNA {ECO:0000269|PubMed:19013210}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-10.5. {ECO:0000269|PubMed:19013210}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-50 degrees Celsius. {ECO:0000269|PubMed:19013210}; | FUNCTION: Snake venom zinc metalloprotease that acts at several levels. It has direct fibrino(geno)lytic activity (Aalpha chain of fibrinogen is cleaved quickly, Bbeta chain slowly, and gamma chain even more slowly) and degradation of TNF-alpha. These activities permit to protect against sepsis and disseminated intrava... | Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
A2V9Y8 | OXDA_MACFA | MRVVVIGAGVIGLSTALCIHECYHSVLQPLDIKVYADRFTPLTTTDVAAGFWQPYLSDPSNPKEADWSQQTFDYLLSHIHSPNAEKLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPRELDIFPDYSYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVNCTGVWAGVLQPDPLLQPGRGQIIKVDAPWIKHFILTHEPESGIYNSPYIIPGTQTVTLGGIFQLGNWNELNNIQDHNTIWEGCCRLEPTLKNARIVDERTGFRPVRPKIRLEREQLRVGPSNTEVIHNYGHGGYGLTIHW... | 1.4.3.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P18894}; | D-alanine catabolic process [GO:0055130]; D-serine catabolic process [GO:0036088]; digestion [GO:0007586]; dopamine biosynthetic process [GO:0042416]; neutrophil-mediated killing of gram-negative bacterium [GO:0070945]; proline catabolic process [GO:0006562] | peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]; presynaptic active zone [GO:0048786] | D-amino-acid oxidase activity [GO:0003884]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | PTM: Phosphorylated in the cerebellum; probably not by PRKACA, PRKCA or PRKCE. {ECO:0000250|UniProtKB:P14920}.; PTM: May be S-nitrosylated, which partially inactivates the enzyme. {ECO:0000250|UniProtKB:P14920}. | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P18894}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14920}. Presynaptic active zone {ECO:0000250|UniProtKB:O35078}. Secreted {ECO:0000250|UniProtKB:P18894}. Note=Transiently present in the cytosol before being delivered to the peroxisomes (By similarity). I... | CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000250|UniProtKB:P18894}; PhysiologicalDirection=left-to-r... | null | null | null | null | FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Required to catabolize D-amino acids synthesized endogenously, of gastrointestinal bacterial origin or obtained from the diet, and to use these as nutrients. Regulates the level of D-amino acid neurotransmitters in the brai... | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
A2VBC4 | PA1_POLPI | MNFKYSILFICFGTLDRGLIPECPFNEYDILFFVYTRQQRDGIVLTEETLQNYDLFKKSTISRQVVFIDHGFLSNGNNENFIAMAKALIEKDNFLVISVDWKKGACNAFASTLDYLGYSTAVGNTRHVGKYVADFTKLLVEQYKVSMSNIRLIGHSLGAHTSGFAGKEVQELKLNKYSNIDGLDPAGPSFDSNDCPERLCETDAEYVQIIHTSNILGVYSKIGTVDFYMNYGSHQPGCGRFFSPSCSHTKAVKYLTECIKHECCLIGTPWKKYFSTPKPISQCTKDTCVCVGLNAKSYPARGSFYVPVEATAPYCHNEGI... | 3.1.1.32 | null | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970] | PF00151; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | PTM: Contains six disulfide bonds. {ECO:0000269|PubMed:17761205}.; PTM: Is not glycosylated. {ECO:0000269|PubMed:17761205}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17761205}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:17761205}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (PubMed:17761205). Shows hemolytic activity (PubMed:17761205). Acts as an allergen (PubMed:17761205). {ECO:0000269|PubMed:17761205}. | Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp) |
A2VCW5 | S38A5_RAT | MAISCAVGMEMQEPKMNGTLSTGAAAGYRQEREGFLPTTHGPAPGRKPVQFLDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMAHTGVIFFLALLLCIALLSSYSIHLLLTCASVVGIRAYEQLGQRAFGPAGKVVVAIIICLHNVGAMSSYLFIIKSELPLVIGTFLHMDPEGDWFLKGNLLIILVSLLIILPLALMKHLGYLGYTSSLSLTCMLFFLISVIYKKFQLGCVVSHNDTVVESEPAPLQAFNSSCEAKLFTVDSQMSYTVPIMAFAFVCHPEVLPIYTELCCPTQRRMQAVANMSIGAMFIMYGLTATFGY... | null | null | amino acid export across plasma membrane [GO:0032973]; amino acid import across plasma membrane [GO:0089718]; asparagine transmembrane transport [GO:1903713]; glutamine transport [GO:0006868]; glycine transport [GO:0015816]; L-alanine transmembrane transport [GO:1904557]; L-glutamine import across plasma membrane [GO:1... | plasma membrane [GO:0005886] | alanine transmembrane transporter activity [GO:0022858]; amino acid transmembrane transporter activity [GO:0015171]; glycine transmembrane transporter activity [GO:0015187]; L-asparagine transmembrane transporter activity [GO:0015182]; L-glutamine transmembrane transporter activity [GO:0015186]; L-glutamine, sodium:pro... | PF01490; | null | Amino acid/polyamine transporter 2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15390093, ECO:0000269|PubMed:22821889}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at astroglial membrane. {ECO:0000269|PubMed:22821889}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-serine(out) + Na(+)(out) = H(+)(out) + L-serine(in) + Na(+)(in); Xref=Rhea:RHEA:71159, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:16629640, ECO:0000269|PubMed:22821889}; Physiol... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.92 mM for L-serine (at pH 8.0) {ECO:0000269|PubMed:16629640}; KM=0.99 mM for L-glutamine influx (at pH 8.0) {ECO:0000269|PubMed:15218073}; KM=0.73 mM for L-serine (at pH 8.0) {ECO:0000269|PubMed:15218073}; KM=0.21 mM for L-histidine (at pH 8.0) {ECO:0000269|PubMe... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:16249471}; | null | FUNCTION: Symporter that cotransports neutral amino acids and sodium ions, coupled to an H(+) antiporter activity (PubMed:11698233, PubMed:15218073, PubMed:16249471, PubMed:16629640, PubMed:22821889). Releases L-glutamine and glycine from astroglial cells and may participate in the glutamate/GABA-glutamine cycle and th... | Rattus norvegicus (Rat) |
A2VD12 | PBIP1_RAT | MASCPDSDNSWVLAGSETLPVETLGPESRVDPESEEAPQALQDSSKADGKESAGTLNGEEMLFQTESSQGEGAALPEESEAKGALGGDDGHGTKRPGDTAVQEDLQETPMVTSLGPDTQDLERNIHPQNLPSSPRAVWKEHGCSSSDDDTDVDVEGLRRRRGREPSPPQPTAAVDGEDQAKGEGIGELGISLNMCFLGALVLLGLGILLFSGALLEPETEPVEEAELQVFPETELVQTVGNRQDEVEQLQASVPPDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSH... | null | null | articular cartilage development [GO:0061975]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; extracellular matrix disassembly [GO:0022617]; gene expression [GO:0010467]; gene expression involved in extracellular matrix organization [GO:1901148]; hemopoiesis [GO:0030097]; negative regulation of DNA-templated t... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule [GO:0005874]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor binding [GO:0140297]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714] | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96AQ6}. Nucleus {ECO:0000250|UniProtKB:Q96AQ6}. Note=Shuttles between the nucleus and the cytosol. Mainly localized in the cytoplasm, associated with microtubules. Detected in small amounts in the nucleus. {ECO:0000250|UniProtKB:Q96AQ6}. | null | null | null | null | null | FUNCTION: Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling (By similarity). {... | Rattus norvegicus (Rat) |
A2VD92 | DDX1_XENLA | MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEGKKGKASVKTGSTVLNKWQMNPYDRGSAFAIGSDGLCCQSREIKEWHGCRSTRGVNKGKYYYEVSCHDQGLCRVGWSTLSASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDNSIVKFSKNGKDLGLAFQIPSHMKNQAFFTSCVLKNAELKFNFGEEDFKFPPKDGFVALSKAPDGHVVKSQNTGSAQVSQTKSLPNAPKALIIEPSRELAEQTLNNVKQFKKYVDNPKLRE... | 3.6.4.13 | null | DNA duplex unwinding [GO:0032508]; double-strand break repair [GO:0006302]; mRNA processing [GO:0006397]; rRNA processing [GO:0006364]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; tRNA-splicing ligase complex [GO:0072669] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA/RNA helicase activity [GO:0033677]; exonuclease activity [GO:0004527]; nuclease activity [GO:0004518]; poly(A) binding [GO:0008143]; RNA helicase activity [GO:0003724]; transcription coregulator... | PF00270;PF00271;PF00622; | 2.60.120.920;3.40.50.300; | DEAD box helicase family, DDX1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92499}. Cytoplasm {ECO:0000250|UniProtKB:Q92499}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q92499}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91VR5}. Mitochondrion {ECO:0000250|UniProtKB:Q91VR5}. | 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: Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Acts as a positive regulator of transcription. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Binds DNA and RNA. Component of the tRNA-spl... | Xenopus laevis (African clawed frog) |
A2VDJ0 | T131L_HUMAN | MAGLRRPQPGCYCRTAAAVNLLLGVFQVLLPCCRPGGAQGQAIEPLPNVVELWQAEEGELLLPTQGDSEEGLEEPSQEQSFSDKLFSGKGLHFQPSVLDFGIQFLGHPVAKILHAYNPSRDSEVVVNSVFAAAGHFHVPPVPCRVIPAMGKTSFRIIFLPTEEGSIESSLFINTSSYGVLSYHVSGIGTRRISTEGSAKQLPNAYFLLPKVQSIQLSQMQAETTNTSLLQVQLECSLHNKVCQQLKGCYLESDDVLRLQMSIMVTMENFSKEFEENTQHLLDHLSIVYVATDESETSDDSAVNMYILHSGNSLIWIQDIR... | null | null | negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of immature T cell proliferation in thymus [GO:0033088]; Wnt signaling pathway [GO:0016055] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886] | null | PF19532;PF12371; | 2.60.40.10; | TMEM131 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23690469}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:23690469}. Note=During intrathymic development, resides in punctate cytoplasmic structures in DN1 and DN2 cells. In DN3 cells, found in large crescent-shaped membrane struc... | null | null | null | null | null | FUNCTION: [Isoform 1]: Membrane-associated form that antagonizes canonical Wnt signaling by triggering lysosome-dependent degradation of Wnt-activated LRP6. Regulates thymocyte proliferation. {ECO:0000269|PubMed:23690469}. | Homo sapiens (Human) |
A2VDL6 | AT1A2_BOVIN | MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAFGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVVREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVI... | 7.2.2.13 | null | intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; potassium ion import across plasma membrane [GO:1990573]; proton transmembrane transport [GO:1902600]; sodium ion export across plasma membrane [GO:0036376] | cell projection [GO:0042995]; plasma membrane [GO:0005886]; sodium:potassium-exchanging ATPase complex [GO:0005890] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type sodium:potassium-exchanging transporter activity [GO:0005391] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrient... | Bos taurus (Bovine) |
A2VDN5 | SPAST_BOVIN | MNSPGGRGKKKGSGGPSSPVPPRPPPPCQARSRPAPKPAPPPQSPHKRNLYYFSYPLFLGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPASASPPAPVPGGEAERVRAFHKQAFEYISVALRIDEDEKVGQKDQAVEWYKKGIEELEKGIAVVVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKLQPSLQFSKSQTDVYNDSTNLTCRNGHLQSESGAVPKRKDPLTHASNSLPRSKTVMKTGPTGLSGHHRAPSCSGLSMVSGVRQGPGSAAATHKSTPKTNRTNKPSTPTTAARKKKDLKNFRNVDS... | 5.6.1.1 | null | anterograde axonal transport [GO:0008089]; axonal transport of mitochondrion [GO:0019896]; axonogenesis [GO:0007409]; cytokinetic process [GO:0032506]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; exit from mitosis [GO:0010458]; membrane fission [GO:0090148]; metabolic process [GO:0008152]; m... | axon [GO:0030424]; axon cytoplasm [GO:1904115]; centrosome [GO:0005813]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sp... | alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; beta-tubulin binding [GO:0048487]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568] | PF00004;PF17862;PF09336; | 1.10.8.60;3.40.50.300;1.20.58.80; | AAA ATPase family, Spastin subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:... | CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021}; | null | null | null | null | FUNCTION: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but... | Bos taurus (Bovine) |
A2VDP1 | BRE1A_BOVIN | MSGIGSKRAAGEPGTSVPPEKKTAVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDSLMVEEAVQELNSFLAQENTRLQELTDLLQEKHCTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITI... | 2.3.2.27 | null | chromatin organization [GO:0006325]; negative regulation of cell migration [GO:0030336]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein polyubiquitination [GO:0000209]; regulation of DNA-templated transcription [GO:0006355... | HULC complex [GO:0033503]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | histone binding [GO:0042393]; metal ion binding [GO:0046872]; p53 binding [GO:0002039]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625] | PF00097; | 1.20.1170.10;3.30.40.10; | BRE1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VTR2}. | 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:0000250|UniProtKB:Q5VTR2}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respe... | Bos taurus (Bovine) |
A2VDU3 | M3K7_BOVIN | MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFM... | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O43318}; | apoptotic process [GO:0006915]; I-kappaB phosphorylation [GO:0007252]; immune response [GO:0006955]; JNK cascade [GO:0007254]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of JUN kinase activity [GO:0043507] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310] | PF07714; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane. {ECO... | 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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43318}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming ... | Bos taurus (Bovine) |
A2VDZ3 | MEF2A_BOVIN | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPSALSYTNPGSSLVSPSLAASSALADTSMLSPPQATLHRNVSPGAPQRPPSTGSAGGMLSTSDLTVPNGAGSSPVGNGFVNSRASPNLIGTTGANSLGKVMPTKSPPPPGGGSLGMNSRKPDLRVVIPPSSKGMMPPLNTQRISSSQATQPLATPVVSVTTPSLPPQGLV... | null | null | apoptotic process [GO:0006915]; cardiac conduction [GO:0061337]; cellular response to calcium ion [GO:0071277]; dendrite morphogenesis [GO:0048813]; DNA-templated transcription [GO:0006351]; ERK5 cascade [GO:0070375]; MAPK cascade [GO:0000165]; mitochondrial genome maintenance [GO:0000002]; mitochondrion distribution [... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; histone acetyltransferase binding [GO:0035035]; histone deacet... | PF12347;PF00319; | 3.40.1810.10; | null | PTM: Constitutive phosphorylation on Ser-400 promotes Lys-395 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-400 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-395 leading to inhibition of dendrite claw differentiation. Phosphorylati... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}. | null | null | null | null | null | FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also i... | Bos taurus (Bovine) |
A2VDZ4 | PLK4_BOVIN | MATCIGEKIEDFRVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRRKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLAAQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPTFLSREAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSKKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDRRRLLIEQPLPN... | 2.7.11.21 | null | centriole replication [GO:0007099]; cilium assembly [GO:0060271]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; mitotic spindle organization [GO:0007052]; positive regulation of centriole replication [GO:0046601]; protein phosphorylation [GO:0006468]; trophoblast gi... | centriole [GO:0005814]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; deuterosome [GO:0098536]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF18190;PF18409; | 2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Ubiquitinated; leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Tyrosine-phosphorylated by TEC. {ECO:0000250}.; PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting the kinase to an inactive conformation. {ECO:0000250|UniProtKB:O00444}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q64702}. Cleavage furrow {ECO:0000250|UniProtKB:Q64702}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB... | 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=2.7.11.21; Evidence={ECO:0000250|UniProtKB:O00444}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpres... | Bos taurus (Bovine) |
A2VE31 | S38A2_BOVIN | MKKAEMGRFNISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETDFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGHKAFGMVGKLTASGSITMQNIGAMSSYLFIVKYELPLVIQALMNIEDTNGLWYLNGDYLVLLVSLVLILPLSLLRNLGYLGYTSGLSLLCMMFFLIVVIFKKFQISCPAEIAFLVNETVNSSLTQPATFLPDMGFNRTESDSCQPRYFIFNSQTVYAVPILTFSFVCHPAILPIYEELKGRS... | null | null | alanine transport [GO:0032328]; amino acid import [GO:0043090]; amino acid transmembrane transport [GO:0003333]; amino acid transport [GO:0006865]; glutamine transport [GO:0006868]; L-glutamine import across plasma membrane [GO:1903803]; L-proline import across plasma membrane [GO:1904271]; L-serine import across plasm... | plasma membrane [GO:0005886] | acidic amino acid transmembrane transporter activity [GO:0015172]; alanine:sodium symporter activity [GO:0015655]; amino acid transmembrane transporter activity [GO:0015171]; amino acid:sodium symporter activity [GO:0005283]; L-glutamine transmembrane transporter activity [GO:0015186]; neutral L-amino acid transmembran... | PF01490; | null | Amino acid/polyamine transporter 2 family | PTM: Polyubiquitination by NEDD4L regulates the degradation and the activity of SLC38A2. {ECO:0000250|UniProtKB:Q8CFE6}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JHE5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9JHE5}. Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes. Enriched in the somatodendritic compartment of neurons, it is also detec... | CATALYTIC ACTIVITY: Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out); Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29285; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=gly... | null | null | null | null | FUNCTION: Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane. The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoi... | Bos taurus (Bovine) |
A2VE79 | NUDT3_BOVIN | MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPGTAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVSIGRKREWFKIEDAINVLQCHKPVQASYFETLRQGYSANNGTPLVAPTYSVSAQSSMPGIR | 3.6.1.10; 3.6.1.52; 3.6.1.59; 3.6.1.61; 3.6.1.62 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O95989}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O95989}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O95989}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:O95989}; | adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diphosphoinositol polyphosphate catabolic process [GO:0071544]; diphosphoinositol polyphosphate metabolic process [GO:0071543]; ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity [GO:0140932]; 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphata... | PF00293; | 3.90.79.10; | Nudix hydrolase family, DIPP subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95989}. Nucleus {ECO:0000250|UniProtKB:O95989}. | CATALYTIC ACTIVITY: Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.; EC=3.6.1.52; Evidence={ECO:0000250|UniProtKB:O95989}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O = 1D-myo-inositol hexakisphosphate + H(+) + phosphate; Xref=... | null | null | null | null | FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (By similarity). InsP6 (inositol hexakisphosphate) is not a substrate (By similarity). Also... | Bos taurus (Bovine) |
A2VEA3 | ARI1_BOVIN | MDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDNLDLGEVELVEPGLGVGGERDGLLCGETGGGGGSALGPGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKK... | 2.3.2.31 | null | positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | Cajal body [GO:0015030]; cytoplasm [GO:0005737]; Lewy body [GO:0097413]; nuclear body [GO:0016604]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF21235;PF19422;PF01485;PF00097; | 1.20.120.1750;3.30.40.10; | RBR family, Ariadne subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9Y4X5}. Note=Mainly cytoplasmic. Present in Lewy body. {ECO:0000250|UniProtKB:Q9Y4X5}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates... | Bos taurus (Bovine) |
A2VEC9 | SSPO_HUMAN | MLLPALLFGMAWALADGRWCEWTETIRVEEEVAPRQEDLVPCASLDHYSRLGWRLDLPWSGRSGLTRSPAPGLCPIYKPPETRPAKWNRTVRTCCPGWGGAHCTEALAKASPEGHCFAMWQCQLQAGSANASAGSLEECCARPWGQSWWDGSSQACRSCSSRHLPGSASSPALLQPLAGAVGQLWSQHQRPSATCASWSGFHYRTFDGRHYHFLGRCTYLLAGAADSTWAVHLTPGDRCPQPGHCQRVTMGPEEVLIQAGNVSVKGQLVPEGQSWLLHGLSLQWLGDWLVLSGGLGVVVRLDRTGSISISVDHELWGQTQ... | null | null | cell adhesion [GO:0007155] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane protein complex [GO:0098797] | peptidase inhibitor activity [GO:0030414] | PF08742;PF00754;PF00057;PF01826;PF00090;PF00094; | 2.10.70.10;2.60.120.260;2.10.25.10;4.10.400.10;2.20.100.10; | Thrombospondin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:P98167}. | null | null | null | null | null | FUNCTION: Involved in the modulation of neuronal aggregation (By similarity). May be involved in developmental events during the formation of the central nervous system (By similarity). {ECO:0000250|UniProtKB:P98167}. | Homo sapiens (Human) |
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