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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A5GZW8 | DHSD_PIG | MATLWRLSVLCGARGGGALVLRTSVVRPAHVSAFLQDRHTPGWCGVQHIHLSPSHQASSKAASLHWTGERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGIGQVVTDYVRGDALQKVAKAGLLALSAFTFAGLCYFNYHDVGICKAVAMLWKL | null | null | mitochondrial electron transport, succinate to ubiquinone [GO:0006121]; protein insertion into mitochondrial inner membrane [GO:0045039]; tricarboxylic acid cycle [GO:0006099] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; TIM22 mitochondrial import inner membrane insertion complex [GO:0042721] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein transmembrane transporter activity [GO:0008320]; succinate dehydrogenase (quinone) activity [GO:0008177]; ubiquinone binding [GO:0048039] | PF05328; | 1.20.1300.10; | CybS family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. | null | null | FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). | Sus scrofa (Pig) |
A5H2P4 | ARO12_LODEL | MSIEKVSILGKESIHVGYGIQSHIVEETIKCLASSTYVIISDTNMSKTPTYEKLQDSFQKELAKQRPQSRLLTYLIPPGENHKNRETKAEVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLSMVDSSVGGKTAIDTELGKNFIGAFHQPEFVFCDVSFLQTLPKRQLINGMAEVVKTAAIWDETEFTRLEGFAKRFLAEISAPTPNLESIKDELIKTVLGSVRVKAFVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPSAVARLSKCLAAYGLPI... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
A5H2Q8 | ARO11_LODEL | MSIEKVSILGKESIHVGYGIQSHIVEETIKCLASSTYVIISDTNMSKTPTYEKLQDSFQKELAKQRPQSRLLTYLIPPGENHKNRETKAEVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLSMVDSSVGGKTAIDTELGKNFIGAFHQPEFVFCDVSFLQTLPKRQLINGMAEVVKTAAIWDETEFTRLESFAKRFLAEISAPTPNLESIKDELIKTVLGSVRVKAFVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPSAVARLSKCLAAYGLPI... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
A5H447 | ZYX_XENLA | MDPAAPATRMTSSFTINISTPSFYNPPKKFAPVVPPKPKINPFKAPEEPQSLVPQENSAGPGLHQAFVGKVGEMPPGVDHDDFVLPPPPPSEESISPPSSSFPPPPPSFGDEGLGSPSGGSFPPPPPPEFSEPFPPPIEEFFPSPPPLEECVSDTQDLPVPVPPPPPPPLPSPPAAPPPKPSAPCEAPKPAPVFPKSSPPPAFPKPEPPSVAPKAASSIFIPKPSAPMAVAPKPLAPPPVAAKPSGPVSFAPPSPAPHTFSPDPSAPAHTFSPKTVTFSPKSAPHTFMPKPSAPVTYPQKTTEPPAEASQSSPKVTPAAK... | null | null | cell adhesion [GO:0007155]; integrin-mediated signaling pathway [GO:0007229]; regulation of transcription by RNA polymerase II [GO:0006357]; transforming growth factor beta receptor signaling pathway [GO:0007179] | cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; stress fiber [GO:0001725] | DNA-binding transcription factor binding [GO:0140297]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712] | PF00412; | 2.10.110.10; | Zyxin/ajuba family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}. Cell junction, focal adhesion {ECO:0000250}. Note=Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in th... | null | null | null | null | null | FUNCTION: Adhesion plaque protein. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity). Suppresses the transcription-repressing activity of hesx1/anf1. {ECO:0000250|UniProtKB:Q04584, ECO:0000269|PubMed:18297730}. | Xenopus laevis (African clawed frog) |
A5H8G4 | PER1_MAIZE | MAKESKLTAGVAAALTVVAACALCLLLPATARAQLRVGFYDTSCPNAEALVRQAVAAAFAKDAGIAAGLIRLHFHDCFVRGCDGSVLLTVNPGGGQTERDALPNNPSLRGFDVIDAAKTAVEQSCPRTVSCADIVAFAARDSISLTGSVSYQVPAGRRDGRVSNATETVDLPPPTSTAQSLTDLFKAKELSVEDMVVLSGAHTVGRSFCASFFKRVWNTSTNPATAIVDAGLSPSYAQLLRALCPSNTTQTTPITTAMDPGTPNVLDNNYYKLLPRGMGLFFSDNQLRVNPQMAALVSSFASNETLWKEKFAAAMVKMGR... | 1.11.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 2 calcium... | hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]; vacuole [GO:0005773] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Classical plant (class III) peroxidase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=61.9 umol/min/mg enzyme with guaiacol as substrate {ECO:0000269|PubMed:18603027}; Note=In the presence of H(2)O(2).; | null | null | null | FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. {ECO:0000255|P... | Zea mays (Maize) |
A5HAK0 | RNSL3_DANRE | MGIHQCTAVVLLLLCASLSTYGQPAEIRRRYEHFLTQHVYGGITEQTCDRVMRQRRITRFPTGNDCKEVNTFIQANGNHVRTVCTGGGTRQTDNRDLYMSNNQFTVITCTLRSGERHPNCRYRGKESSRKIVVACEGEWPTHYEKGVIV | 3.1.27.- | null | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; immune system process [GO:0002376] | extracellular region [GO:0005576] | endonuclease activity [GO:0004519]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | PTM: Cleavage between Arg-55 and Arg-56 is catalyzed by a membrane-localized Gram-negative bacterium protease (OmpT in E.coli). The excised fragment is then transported to the bacterium cytosol for cleavage of the disulfide bridge linking Cys-48 and Cys-109, thus separating the N-terminal and LF-ZF3. LF-ZF3 but not the... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P34096}. | null | null | null | null | null | FUNCTION: Ribonuclease. Angiogenic. Plays a role in host defense. Exhibits strong antibacterial activity against Gram-negative bacteria but mild antibacterial activity against Gram-positive bacteria. The RNase activity is not required for the bactericidal activity. {ECO:0000269|PubMed:16861230, ECO:0000269|PubMed:17347... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5HBE1 | VP2_POVWU | MGILLAVPEIIAASVAGGAEALSIAGSGAAIATGEGLAALGGLTESAALLGETVEISEAAATVLTKVPELVTVTQGVTAAVQGGAGLVGGIYTALAADRPGDLPASTPTGSPSGLHPPAGYNPQGGGLNIQSIHKPLHAPYPGMALAPIPEYNLETGIPGVPDWVFNFIASHLPELPSLQDVFNRIAYGIWTSYYNTGRTVVNRAVSEELQRLLGDLEYGFRTALATIGESDPVNAIVEQVRSFVSGGRQRELLQIAAGQPVDISEGVSRGTATISNAVEAVRDATQRLSQATYNFVYDASTLPRDGFNALSDGVHRLGQ... | null | null | symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028] | DNA binding [GO:0003677] | null | null | Polyomaviruses capsid protein VP2 family | null | SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic ret... | WU polyomavirus (WUPyV) |
A5HBG1 | LT_POVWU | MDKTLSRNEAKELMQLLGLDMTCWGNLPLMRTKYLSKCKEFHPDKGGNEEKMKKLNSLYLKLQECVSTVHQLNEEEDEVWSSSQIPTYGTPDWDYWWSQFNSYWEEELRCNEEMPKSPGETPTKRTREDDEEPQCSQATPPKKKKDNATDASLSFPKELEEFVSQAVFSNRTLTAFVIHTTKEKAETLYKKLLSKFKCNFASRHSYYNTALVFILTPFRHRVSAVNNFCKGYCTISFLFCKGVNNAYGLYSRMTRDPFTLCEENIPGGLKENDFKAEDLYGEFKDQLNWKALSEFALELGIDDVYLLLGLYLQLSIKVEE... | 3.6.4.- | null | DNA replication [GO:0006260]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of JAK1 activity [GO:0039576]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; v... | host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; DNA replication origin binding [GO:0003688]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF06431;PF02217; | 3.40.1310.20;1.10.287.110;1.20.1050.70;3.40.50.300;1.10.10.510; | null | PTM: Phosphorylated on both serine and threonine residues. Small t antigen inhibits the dephosphorylation by the AC form of PP2A. {ECO:0000250|UniProtKB:P03070}.; PTM: O-Glycosylated near the C-terminal region. {ECO:0000250|UniProtKB:P03070}.; PTM: Acetylated by CBP in a TP53-dependent manner. {ECO:0000250|UniProtKB:P0... | SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03070}. | null | null | null | null | null | FUNCTION: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic ... | WU polyomavirus (WUPyV) |
A5HC98 | L_BUNLC | MDYQEYQQFLARINTARDACVAKDIDVDLLMARHDYFGRELCKSLNIEYRNDVPFIDIILDIRPEVDPLTIDAPHITPDNYLYINNVLYIIDYKVSVSNESSVITYDKYYELTRDISDRLSIPIEIVIIRIDPVSRDLHINSDRFKELYPTIVVDINFNQFFDLKQLLYEKFGDDEEFLLKVAHGDFTLTAPWCKTGCPEFWKHPIYKEFKMSMPVPERRLFEESVKFNAYESERWNTNLVKIREYTKKDYSEHISKSAKNIFLASGFYKQPNKNEISEGWTLMVERVQDQREISKSLHDQKPSIHFIWGAHNPGNSNNA... | 2.7.7.48; 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20862319}; Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site (PubMed:20862319). The divalent metal ions are crucial for catalytic activity (PubMed:31948728). {ECO:0000269|PubMed:20862319, 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]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF04196;PF15518;PF21561; | 3.40.91.60; | 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:0000250|UniProtKB:P20470}; | 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 (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease a... | Bunyavirus La Crosse |
A5HEH4 | GIF1_MAIZE | MQQQHLMQMNQNMMGGYTSPAAVTTDLIQQYLDENKQLILAILDNQNNGKAEECERHQAKLQHNLMYLAAIADSQPPQTAPLSQYPSNLMMQPGPRYMPPQSGQMMNPQSLMAARSSMMYAHPSLSPLQQQQAAHGQLGMAPGGGGGGTTSGFSILHGEASMGGGGAGAGAGNNMMNAGMFSGFGRSGSGAKEGSTSLSVDVRGGTSSGAQSGDGEYLKVGTEEEGS | null | null | adaxial/abaxial pattern specification [GO:0009955]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; cotyledon development [GO:0048825]; floral meristem determinacy [GO:0010582]; leaf development [GO:0048366]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | transcription coactivator activity [GO:0003713] | PF05030; | null | SS18 family | null | null | null | null | null | null | null | FUNCTION: Transcription coactivator that plays a role in the regulation of meristematic function in leaves, stems and inflorescences (PubMed:29437990). Regulates shoot architecture and meristem determinacy (PubMed:29437990). Binds to the inflorescence architecture gene UB3 (unbranched3) (PubMed:29437990). Regulates the... | Zea mays (Maize) |
A5HEI1 | SCC2_ARATH | MSNPSSSGLGSSSGLTHFGIGLANTVQSEVTPYLPLPSLPIFCGAAEPGEFKLFDEVGQGSGYRSLDRSEILAQSSRIANMLHETDVSYLDLRNEARAPDCNSGEHFQLYDLVLRCNPGAFEYVTPGPTCDPLFTNEGPQKIISEPSVPVKMQRQTDTHLARSIEPEPVKRVLRPNHVEDHSWQHETLTNQSPKDVTAYDSRPETITMNELSASKKPKGKKKRKDDLSSVQPDPSVLQESIVQNFCEMLEDFCGRAEVPGDDRDEAEWSSVPVDEVRVLINELMTIRSKMLLHMVPVDILSRLLRTLDHQIHRAEGLSIY... | null | null | brain development [GO:0007420]; cell division [GO:0051301]; centromere complex assembly [GO:0034508]; chromosome segregation [GO:0007059]; digestive tract development [GO:0048565]; embryo development ending in seed dormancy [GO:0009793]; establishment of protein localization to chromatin [GO:0071169]; heart morphogenes... | chromosome, centromeric region [GO:0000775]; Scc2-Scc4 cohesin loading complex [GO:0090694] | chromatin binding [GO:0003682]; metal ion binding [GO:0046872] | PF12765;PF12830;PF00628; | 1.25.10.10;3.30.40.10; | SCC2/Nipped-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04002}. Chromosome, centromere {ECO:0000250|UniProtKB:Q04002}. Note=Associates with chromatin. {ECO:0000250|UniProtKB:Q04002}. | null | null | null | null | null | FUNCTION: Essential protein required for cell fate determination during embryogenesis (PubMed:15266054, PubMed:19228337, PubMed:28137757). Involved in sister chromatid cohesion during meiosis and mitosis (PubMed:19228337, PubMed:19533160). Forms a complex with SCC4, which is required for the association of the cohesin ... | Arabidopsis thaliana (Mouse-ear cress) |
A5HNF6 | MYD88_CHICK | MATVPVGAGSAPGPEPADLHSVPMVALNYGVRRRLGLYLNPRAATAADWTALAEKLGHDYLEIRRLEALPDPTAALLEEWQSRCPGGATVGQLLELLRQLGRHDVLLELGGSVEEDCKKYLRRKQQEAEQPLQVPAVDSSVPKTSELMGITTRDDPYGHGTEMFDAFICYCQKDLQFVQEMIRELEQTEFKLKLCVFDRDVLPGTCVWSISGELIERRCRRMVVVISDDYLESDECDFQTKFALSLSPGARLKRLIPVKCKTMKNEFPSILRFITICDYTNPCTKKWFWTRLAKSLLLP | null | null | defense response to Gram-positive bacterium [GO:0050830]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of non-canonical NF-kappa... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | TIR domain binding [GO:0070976]; Toll-like receptor binding [GO:0035325] | PF00531;PF13676; | 1.10.533.10;3.40.50.10140; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18582498}. Nucleus {ECO:0000269|PubMed:18582498}. Note=Predominantly cytoplasmic, with some expression in the nucleus. | null | null | null | null | null | FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. {ECO:0000250, ECO:0000269|PubMed:18582498}. | Gallus gallus (Chicken) |
A5HNV6 | DCAMP_TRYBB | MSVTRINQQTECPSSVHDLVSCWGGCTQSKTSTDSGLEKRFELNFAQPVDIGTVTVKQLASVMERAGESLRQNSAELGIHTLKFDRSLLVFTAKQIVVRSSVSVMLHEAVHPMLELMRSHNIIVDWASFMRVNYGSPWDMTSETSDIMAHEYAELKSAFPTGHPYLAGPVDRDHCFYFVYDGIDRDPSSCRRENDVQINVYMYNVQADDEYDLDGNTKEQQLLVSHCAGEYETLRVSTYGSTHPFASFETNAVSAASDITKIVNGLLKKFYPERVLLVLLQDRDAQGTTACGVMDRLEGFTVVHRGANHFGGGYVFHQAT... | null | null | positive regulation of catalytic activity [GO:0043085]; positive regulation of spermidine biosynthetic process [GO:1901307]; S-adenosylmethionine metabolic process [GO:0046500]; spermidine biosynthetic process [GO:0008295]; spermine biosynthetic process [GO:0006597]; trypanothione biosynthetic process [GO:0019342] | catalytic complex [GO:1902494]; cytosol [GO:0005829] | adenosylmethionine decarboxylase activity [GO:0004014]; enzyme activator activity [GO:0008047]; enzyme binding [GO:0019899]; protein heterodimerization activity [GO:0046982] | PF01536; | 3.60.90.10; | Eukaryotic AdoMetDC family | null | null | null | null | PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. {ECO:0000269|PubMed:17485680, ECO:0000269|PubMed:18949025}. | null | null | FUNCTION: Probably has no catalytic activity due to the loss of several residues required for processing and catalysis (PubMed:17485680). Forms a complex with S-adenosylmethionine decarboxylase AdoMetDC which is essential to activate AdoMetDC (PubMed:17485680, PubMed:18949025). Required for the biosynthesis of the poly... | Trypanosoma brucei brucei |
A5HUI5 | AMPE_GLOBR | MDIEDKSSKMHCMKGKHVAIICGVVIAVGLILGLGLGLGLKPEACNPPEDNGLLSTKPPTTSTPNVTNPSGSSVFCSAKNDENGAWTNFRLPNYVQPVHYDLDLTPEMEAEVYTGMVNISIRLEEQTTRHLWLHLRETKITEMPQLRTSSGQVIEIKRCFGYEPQEYVVIEAEEDLRPGNYFLSMKFKGYLNGSLVGFYSTTYGENGKTKYIAATDHEPTDARKSFPCFDEPNKKATYTISITHEHDYEAISNMPVEKTISLDNKWTKTIFKKSVPMSTYLVAWAVHQFKYEERISSRGIPLRVYAQPQQINTTIYAANV... | 3.4.11.7 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q07075}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q07075}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]; regulation of blood pressure [GO:0008217] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07075}; Single-pass type II membrane protein {ECO:0000255}. Note=Found in the venom as transmembrane proteins in exosome-like vesicles. {ECO:0000250|UniProtKB:P0DQU2}. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.; EC=3.4.11.7; Evidence={ECO:0000269|PubMed:17383704}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4 (measured only for partially purified enzyme). {ECO:0000269|PubMed:17383704}; | null | FUNCTION: Venom protein that cleaves N-terminal acidic residues from peptides with high potency in presence of calcium (PubMed:17383704). It may have several roles in venom including alteration of blood pressure by cleaving circulating angiotensin-2, general degradation of host tissue, increase of permeability to other... | Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys brevicaudus) |
A5IQA5 | HCHA_STAA9 | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Staphylococcus aureus (strain JH9) |
A5JTM5 | CBADH_PSEUC | MYEAIGHRVEDGVAEITIKLPRHRNALSVKAMQEVTDALNRAEEDDSVGAVMITGAEDAFCAGFYLREIPLDKGVAGVRDHFRIGALWWHQMIHKIIRVKRPVLAAINGVAAGGGLGISLASDMAICADSAKFVCAWHTIGIGNDTATSYSLARIVGMRRAMELMLTNRTLYPEEAKDWGLVSRVYPKDDFREVAWKVARELAAAPTHLQVMAKERFHAGWMQPVEECTEFEIQNVIASVTHPHFMPCLTEFLDGHRADRPQVELPAGV | 3.8.1.7 | null | coenzyme A metabolic process [GO:0015936] | null | 4-chlorobenzoyl-CoA dehalogenase activity [GO:0018787] | PF00378; | 1.10.12.10; | Enoyl-CoA hydratase/isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + chloride + H(+); Xref=Rhea:RHEA:14853, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:57354, ChEBI:CHEBI:57356; EC=3.8.1.7; Evidence={ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:7579994}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 uM for 4-chlorobenzoyl-CoA {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; KM=4... | PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-hydroxybenzoate from 4-chlorobenzoate: step 2/3. {ECO:0000269|PubMed:1610806}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.0. Half maximum activity remains at pH 9.0 and 11.5. Stable from pH 6.5 to 11.0, activity is lost following 10 minutes incubation at pH 4.5 or 12.0. {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. Retains 60% of maximum activity at 30 degrees Celsius and 65 degrees Celsius. After 15 minutes preincubation at 60 degrees Celsius 70% of the initial activity remains, 15 minutes preincubation at 65 degrees Celsius result... | FUNCTION: Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and 4-bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-CoA. {ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:7579994}. | Pseudomonas sp. (strain CBS-3) |
A5JTM6 | CBACL_PSEUC | MQTVHEMLRRAVSRVPHRWAIVDAARSTFDICRTGETSRNEGSATARLWPQPARPLAVVSGNSVEAVIAVLALHRLQAVPALMNPRLKPAEISELVARGEMARAVVANDAGVMEAIRTRVPSVCVLALDDLVSGSRVPEVAGKSLPPPPCEPEQAGFVFYTSGTTGLPKGAVIPQRAAESRVLFMATQAGLRHGSHNVVLGLMPLYHTIGFFAVLVAAMAFDGTYVVVEEFDAGNVLKLIERERVTAMFATPTHLDALTTAVEQAGARLESLEHVTFAGATMPDTVLERVNRFIPGEKVNIYGTTEAMNSLYMRAVRIAG... | 6.2.1.33 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806}; | fatty acid metabolic process [GO:0006631] | null | 4-chlorobenzoate-CoA ligase activity [GO:0018861]; ATP binding [GO:0005524]; medium-chain fatty acid-CoA ligase activity [GO:0031956] | PF00501;PF13193; | 3.30.300.30;3.40.50.980; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=4-chlorobenzoate + ATP + CoA = 4-chlorobenzoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23220, ChEBI:CHEBI:17861, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57354, ChEBI:CHEBI:456215; EC=6.2.1.33; Evidence={ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.5 uM for 4-chlorobenzoate {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=70 uM for CoA {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=104 uM for ATP (with magnesium as cofactor) {... | PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-hydroxybenzoate from 4-chlorobenzoate: step 2/3. {ECO:0000269|PubMed:1610806}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.4. 85% of activity remains at pH 9.0, 54% of activity remains at pH 7.0. {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; | FUNCTION: Catalyzes the formation of chlorobenzoyl-CoA via a 2 step reaction. First 4-chlorobenzoyl is adenylated by ATP, followed by acyl transfer from the 4-chlorobenzoyl-AMP intermediate to CoA. Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-methylbenzoate also act as substrates. Inactive towards 4-aminobenzoate, 4... | Pseudomonas sp. (strain CBS-3) |
A5JUY8 | PERL_BUBBU | MWVCLQLPVFLASVTLFEVAASDTIAQAASTTTISDAVSKVKIQVNKAFLDSRTRLKTTLSSEAPTTQQLSEYFKHAKGQTRTAIRNGQVWEESFKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRL... | 1.11.1.7 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:... | antibacterial humoral response [GO:0019731]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; peroxidase activity [GO:0004601]; thiocyanate peroxidase activity [GO:0036393] | PF03098; | 1.10.640.10; | Peroxidase family, XPO subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12071645, ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:12071645, ECO:0000305|PubMed:19339248}; PhysiologicalDirection=left-to-right; Xref=Rh... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.82 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (at pH 6.0 and 60 degrees Celsius) {ECO:0000269|PubMed:12071645}; KM=0.77 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (at pH 6.0 and 25 degrees Celsius) {ECO:0000269|PubMed:1207164... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:12071645}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:12071645}; | FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (Probable). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity)... | Bubalus bubalis (Domestic water buffalo) |
A5JYS0 | PCS1_CAEEL | MSQRRHFKMSVTAKNFYRRPLPETCIEFSSELGKKLFTEALVRGSANIYFKLASQFRTQDEPAYCGLSTLVMVLNALEVDPEKVWKAPWRFYHESMLDCCVPLENIRKSGINLQQFSCLAKCNRLKSTVSYGDNSPDFLKKFRTSLVNSVRSDDQVLVASYDRSVLGQTGSGHFSPLAAYHEDSDQVLIMDVARFKYPPHWVKLETLQKALCSVDVTTKLPRGLVELELKKGTRPLIMYGLKAYVNINDSDFATSVISWNQFLLCDPLEDDEEEFQLCCRKFGQCFAPHAMCCTQKTFDADQKNSCTECSTDQNEACKMI... | 2.3.2.15 | null | cellular detoxification of cadmium ion [GO:0098849]; detoxification of cadmium ion [GO:0071585]; detoxification of copper ion [GO:0010273]; detoxification of mercury ion [GO:0050787]; detoxification of zinc ion [GO:0010312]; phytochelatin biosynthetic process [GO:0046938] | null | glutathione gamma-glutamylcysteinyltransferase activity [GO:0016756]; metal ion binding [GO:0046872] | PF05023; | 3.90.70.30; | Phytochelatin synthase family | null | null | CATALYTIC ACTIVITY: Reaction=[Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine; Xref=Rhea:RHEA:17917, Rhea:RHEA-COMP:12438, Rhea:RHEA-COMP:12439, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:131728; EC=2.3.2.15; Evidence={ECO:0000269|PubMed:11313333, ECO:0000269|PubMed:202... | null | null | null | null | FUNCTION: Involved in the synthesis of phytochelatins, which are heavy metal binding proteins required for the detoxification of heavy metals such as cadmium, arsenic and copper. {ECO:0000269|PubMed:11313333, ECO:0000269|PubMed:20221439, ECO:0000269|PubMed:26907254}. | Caenorhabditis elegans |
A5JYW9 | SIN3_CAEEL | MYNPPPGGGGGNNGGDQSQQQPTNNATLFLLQMIQQSQHQQQHQNQQQQQLELQIRDQERILIEQQRMQHQQQQNQLLQGLNQFPFNPLGLFQVQAAVQAAQAQFAQNAQGSPIPFHIGSPLQPSHSPAASALQQQYLLPSHSPAITPFARNSEAARNIEQFIAQEEAANVPRANSQQQSPLIRPIPQQQALNIQNLTSTQQAQQILAHHRQVPVQQVQHQQHIPTPPLALPIAQQGPISNEVPSVPPVVPATSAGCPQREPRQQQGGRRQNRPGRRKKPEGPPRVDEALAYLRVIKSTFSSDVPVYHRFLEIMKDFRAQ... | null | null | cell fate specification [GO:0001708]; chromatin remodeling [GO:0006338]; defense response to other organism [GO:0098542]; locomotion [GO:0040011]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode male tail mating organ morphogenesis [GO:0090597]; response to endoplasmic reticulum stress ... | chromatin [GO:0000785]; histone deacetylase complex [GO:0000118]; Sin3-type complex [GO:0070822] | transcription corepressor activity [GO:0003714] | PF02671;PF08295;PF16879; | 1.20.1160.11; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}. | null | null | null | null | null | FUNCTION: Probable transcriptional repressor required for the deposition of dimethylated 'Lys-9' of histone H3 (H3K9me2) on asynapsed chromosome pairs (both autosomes and sex chromosomes) during meiosis, but this does not seem to solely affect the transcriptional status (PubMed:21909284). Plays a role in ray fusion and... | Caenorhabditis elegans |
A5JYX5 | DHS3_CAEEL | MPYVFLLSPQLEIASQWDGYYEKTFEVSDHVHKEIILKVSGQTVLITGSGSGLGRLMAFEFGKLGARLVLWDINEQGNKETLKELEAMGVEAKAYTVDLSEYKEINRTADLVKSEVGKVDILVNNAGIVTGKKLLQCPDELMVKTVSVNTNALFFTTKNFLPGMLESNKGHIVTIASMAGKCGVAGLVDYCASKHGAVGFNDSLASELYALKKDVKTTVVCPIYINTGMFDGIATKWPTLLPILSPEYVVDCIMEAVLTDRAFLAIPKFSYIFIALAGLLPTEVLNLYGDHFGITHSMDHFKGRQSRQA | 1.1.1.1 | null | response to oxidative stress [GO:0006979] | lipid droplet [GO:0005811] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:26025681, ECO:0000269|PubMed:26121959}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10001}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+)... | null | null | null | null | FUNCTION: May play a role in lipid droplet formation. May modulate triglyceride levels. {ECO:0000269|PubMed:26025681}. | Caenorhabditis elegans |
A5JYX8 | NCLN_CAEEL | MQDEIIDFFRSPALLFYMTLMLTICVVNGSQQVGEVVETEFHAYRLHQYEISGNIYGCKNYRVSYEAVSLGARTLRRTMVTTWRDLLTTDVDDMWALSTGAVLIFIPDNLDELNDIDRKAFIDLEAKLLSAKTDLAVYVAPFNDDAVSILHDVNTRSEKAPTALQHLLQSLSGNTISITSSDQSPELPPSYKPLNIVGRLSSGDRAAPTIAFVAHYDTQSAVPGVSPGADSNGSGIVALLELLAVLSKFYDSPSTRPPYNILFIWTAAGKLNYQGTRHWIDEYQKGFDSADYAKSGLSRKGFSDDRVDLAICIEAIGRKT... | null | null | protein-containing complex assembly [GO:0065003]; regulation of protein targeting to membrane [GO:0090313]; regulation of signal transduction [GO:0009966] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | null | PF05450; | 3.40.630.10; | Nicastrin family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19609303}; Single-pass type I membrane protein {ECO:0000255}. Note=During the assembly of acetylcholine receptor in muscles, colocalizes with L-AChR component unc-29 in the ER. {ECO:0000269|PubMed:19609303}. | null | null | null | null | null | FUNCTION: Involved in the recognition and selection of protein complexes to exit the endoplasmic reticulum (ER) (PubMed:19609303, PubMed:24567339). In muscles, regulates levamisole-sensitive nicotinic acetylcholine receptor (L-AChR) subunit composition, possibly by allowing only specific L-AChR subunit combinations to ... | Caenorhabditis elegans |
A5K302 | PLM5_PLAVS | MVGASLGPPGRGSLSRLIRLVICVLTLCALSVQGRSESTEGHSKDLLYKYKLYGDIDEYAYYFLDIDIGTPEQRISLILDTGSSSLSFPCAGCKNCGVHMENPFNLNNSKTSSILYCENEECPFKLNCVKGKCEYMQSYCEGSQISGFYFSDVVSVVSYNNERVTFRKLMGCHMHEESLFLYQQATGVLGMSLSKPQGIPTFVNLLFDNAPQLKQVFTICISENGGELIAGGYDPAYIVRRGGSKSVSGQGSGPVSESLSESGEDPQVALREAEKVVWENVTRKYYYYIKVRGLDMFGTNMMSSSKGLEMLVDSGSTFTH... | 3.4.23.- | null | proteolysis [GO:0006508] | endoplasmic reticulum membrane [GO:0005789] | aspartic-type endopeptidase activity [GO:0004190] | PF00026;PF14543; | 2.40.70.10; | Peptidase A1 family | PTM: It is not clear if the zymogen has a cleavable propeptide (By similarity). Cleavage of the putative propeptide is dispensable for catalytic activity (By similarity). {ECO:0000250|UniProtKB:Q8I6Z5}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24983235}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8I6Z5}. | null | null | null | null | null | FUNCTION: During the asexual blood stage, plays an essential role in the export of several proteins into the host erythrocytes by cleaving the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence (PubMed:24983235). Specifically... | Plasmodium vivax (strain Salvador I) |
A5K3U9 | AMPL_PLAVS | MPLLRSSQHIKNTYWNIPKKSFRTGVPQFAESKKTRILHLHPLCKSASGVESPPFFDSQTFSSISNRKEFRKMATTVPQVVSLDPTTIPIDYHTPIDDLSIEVKDISAEACPADEGLIVFLLNSAPKHSSSGGSGGNGGSAGSSGNGEGGAQIKINSSVKDNTINEFLKEGNMENFTGKLGTSKSFYIANDQKKYVSLAYVGCGPANEETELEIRKVAYALVTLLHDSKHKKVSIIFEIKIEEALFRFFLEHLFYEYVTDERFKSADKSTETDFIKNLSLHIANADAYKGQIDKARVYFYGTYYAAQLIAAPSNYCNPVS... | 3.4.11.1; 3.4.13.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19931315, ECO:0000269|PubMed:33303633}; Note=Binds 2 Zn(2+) ions per subunit (PubMed:33303633). Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals (PubMed:333... | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytoplasm [GO:0005737] | manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; metallodipeptidase activity [GO:0070573]; zinc ion binding [GO:0008270] | PF00883; | 3.40.220.10;3.40.630.10; | Peptidase M17 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19931315}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.95 uM for H-Leu-NHMec {ECO:0000269|PubMed:19931315}; KM=31 uM for H-Leu-NHMec (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:34133730}; KM=20.1 uM for H-Leu-NHMec (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 (PubMed:19931315). Optimum pH is 7-8 for the cleavage of the Cys-Gly dipeptide (PubMed:33303633). {ECO:0000269|PubMed:19931315, ECO:0000269|PubMed:33303633}; | null | FUNCTION: Aminopeptidase which preferentially cleaves leucine residues from the N-terminus of peptides (PubMed:19931315, PubMed:34133730). Also, has some activity towards tryptophan and methionine and has very low activity towards alanine, arginine, asparagine, phenylalanine and tyrosine (PubMed:19931315, PubMed:341337... | Plasmodium vivax (strain Salvador I) |
A5K464 | SYFB_PLAVS | MPTISVHEEDLIEKLGEKIEEEKLNDICFEFGIEIDDVEYKGEKKIYKIEVPANRYDLVCVEGLCRALKSFIGKYENVSYALLTNSEEACVKEKHFMRVDESVDERRSYVVSAVLKNVKMNENVYNNIIELQEKLHHNLGKKRILLAIGIHDYDKINFPVAYKFEEKEKINFIPLNETQNVNGNNFINFYQDNINLKSYLKIISDFEKFPVIVDAGGQILSLPPIINCDYTKITYDTRNLFIECTAIDRNKAEIAVNIICSMLSEYCTPKYSIHSFFVQYDKNHKAEKGNGYLYPVFKNKTLTCHMDYVRKLSGILNLSV... | 6.1.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:33436639}; | phenylalanyl-tRNA aminoacylation [GO:0006432]; protein heterotetramerization [GO:0051290] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phenylalanine-tRNA ligase complex [GO:0009328] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; RNA binding [GO:0003723] | PF03483;PF03484;PF18262;PF17759; | 3.30.56.10;3.50.40.10; | Phenylalanyl-tRNA synthetase beta subunit family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NSD9}. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6... | null | null | null | null | null | Plasmodium vivax (strain Salvador I) |
A5K9M4 | PNPH_PLAVS | MEGEMQRHIKLTKAQTTPVVLVVGDPGRVDKVKVLCDSYVDLAYNREYKSVECTYKGQKFLCVSHGVGSAGCAICFEELMNNGAKVIIRAGSCGSLQPTQMKRGDICICNAAVREDRVSHLMIYSDFPAVADYEVYATLNQVAEELKVPVFNGISLSSDMYYPHKIIPTRLEDYSKANVAVVEMEVATLMVMGTLRKVKTGGIFIVDGCPLKWDEGDFDNNLVPERLENMIKISLETCARLAKKY | 2.4.2.1 | null | inosine catabolic process [GO:0006148]; purine nucleotide catabolic process [GO:0006195]; purine ribonucleoside salvage [GO:0006166]; uridine catabolic process [GO:0006218] | cytosol [GO:0005829] | purine-nucleoside phosphorylase activity [GO:0004731]; uridine phosphorylase activity [GO:0004850] | PF01048; | 3.40.50.1580; | PNP/MTAP phosphorylase family | null | null | CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:19575810}; CATALYTIC ACTIVITY: Reaction=guanosine + phosphate = alpha-D-ribose 1-phosph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.4 uM for inosine {ECO:0000269|PubMed:19575810}; KM=11.2 uM for guanosine {ECO:0000269|PubMed:19575810}; KM=61.4 uM for 2'-deoxyinosine {ECO:0000269|PubMed:19575810}; KM=35.1 uM for 2'-deoxyguanosine {ECO:0000269|PubMed:19575810}; Note=kcat is 1.2 sec(-1) with in... | PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000269|PubMed:19575810}. | null | null | FUNCTION: As part of the purine salvage pathway, catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (PubMed:19575810). Preferentially acts on inosine and guanosine, and to a lesser... | Plasmodium vivax (strain Salvador I) |
A5K9S0 | SYFA_PLAVS | MQAKAQEEQKGEELSQFLQALEEEFALCQEGGGDKREADGPSLENAEAEELANRRAYYLQLKEERNVLVEESKHVTSLHMSSKHNIEHAKVLGMAKKLETLYYVVNHVRSFNTYQLTEEGKEYLRDGSPEHVTLRYVMEQEGCTLEDLKKLFGKKGEIGLNINLKKKKIELRKSDKRLFPHVEGSAHSLVDETRCYLQKVEAHGNDEGALVSHLKGILPPEKGEKKEEDEANNLIKELKKRKLIEAKKISYIYIIRTNLFTKEIKKQITDLTYLLIKNEEYKKYQVKKYNFFSSGKKMNKGNIHLLIRQMRTFKDVFVSL... | 6.1.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:33436639}; | phenylalanyl-tRNA aminoacylation [GO:0006432]; protein heterotetramerization [GO:0051290] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phenylalanine-tRNA ligase complex [GO:0009328] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049] | PF01409; | 1.10.10.2320;1.10.10.2330;3.30.1370.240; | Class-II aminoacyl-tRNA synthetase family, Phe-tRNA synthetase alpha subunit type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q505J8}. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6... | null | null | null | null | null | Plasmodium vivax (strain Salvador I) |
A5KE01 | ADA_PLAVS | MNILQEPIDFLKKEELKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFVSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIKVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYNLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHKADFVGFDHGGHEVDLKEYKEIFDYVRESGVPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVAESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNIN... | 3.5.4.31; 3.5.4.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:18602399, ECO:0000305|PubMed:19728741}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741}; | adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166] | cytosol [GO:0005829]; external side of plasma membrane [GO:0009897] | 2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872] | PF00962; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=9.5 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 1.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.13 sec(-1) with 5'-methylthioadenosine... | PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000269|PubMed:19728741}. | null | null | FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential rol... | Plasmodium vivax (strain Salvador I) |
A5LGW7 | POLG_HAVJ8 | MNMSRQGIFQTVGSGLDHILSLADVEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGAHQSEPLKTSVDKPGSKRTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDASQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQ... | 2.7.7.48; 3.4.22.28; 3.6.1.15 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; viral RNA genome re... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell mitochondrial outer membrane [GO:0044193]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF20758;PF12944;PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | Picornaviridae polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precu... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:000025... | 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:0000250|UniProtKB:P08617, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a d... | Human hepatitis A virus genotype IIIB (isolate HAJ85-1) (HHAV) (Human hepatitis A virus (isolate Human/Japan/HAJ85-1/1985)) |
A5LHG2 | ADM5_PIG | MTAHILLLWLFASSILGDPDSAGRLTRHQVSLKSGRLCSLGTCQTHRLPEIIYWLRSASTKELSGKAGRKPQDPYSYGRRRRRRRRRREARLLRRLQDPSLRRAQLAG | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; positive regulation of heart rate [GO:0010460]; regulation of systemic arterial blood pressure [GO:0003073]; regulation of urine volume [GO:0035809] | extracellular region [GO:0005576] | hormone activity [GO:0005179] | null | null | Adrenomedullin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Seems to have a peripheral vasodepressor effect and a central vasopressor effect. {ECO:0000269|PubMed:18434369}. | Sus scrofa (Pig) |
A5LHX3 | PSB11_HUMAN | MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV | 3.4.25.1 | null | CD8-positive, alpha-beta T cell differentiation [GO:0043374]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; proteolysis [GO:0006508]; T cell differentiation in thymus [GO:0033077] | cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome core complex, beta-subunit complex [GO:0019774] | endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; threonine-type endopeptidase activity [GO:0004298] | PF00227; | 3.60.20.10; | Peptidase T1B family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; | null | null | null | null | FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this ... | Homo sapiens (Human) |
A5PF10 | NEUR1_PIG | MTAERPGAVPLGRPGRPPMLGLGEAYRAQVFASIFLLLLSPAGVGARAKNDFNLVHPLVTMEQLLWVSGKQIGSVDTFRIPLITTTPRGTLLAFAEARKMSASDKGAKFIALRRSMDQGSTWSPTAFIVDDGETPDGLNLGAVVSDTTTGVVFLFYSLCAHKAGCRVASTMLVWSKDDGISWSSPRNLSLDIGTEMFAPGPGSGIQKQWAPQKGRLIVCGHGTLERDGVFCLLSDDHGASWRYGSGISGIPYGQPKRENDFNPDECQPYELPDGSVVINARNQNNYHCRCRIVLRSYDACDTLRPRDVTFDPELVDPVVA... | 3.2.1.18 | null | ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; exo-alpha-sialidase activity [GO:0004308] | PF13088; | 2.120.10.10; | Glycosyl hydrolase 33 family | PTM: N-glycosylated. {ECO:0000250}.; PTM: Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane. {ECO:0000250}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Lysosome lumen {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but ... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; | null | null | null | null | FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (By similarity). {ECO:0000250}. | Sus scrofa (Pig) |
A5PHD6 | PKS1_SARSH | MAAHGQTSKRGNNTLLLFGALVQSHDVSTLRSMRESIVVQHGEHSWLVDSIKALPQDFEAALPHLPFFDQATTTTIHQLLVDAVSSFLTGSFETLVSPLPAALLIPLAVATQLAHYVEYSRQSPTGLAEGKEALGFCTGILSAFAVASSHDVCDLAKYGAAAMRLGMLVGLVVDCEDAAAGQGRYRSVSAGWDSEEKHAAMLKIVQSFEEAYVSVHFDKNRATITTSPGTISNLTRQLQKEGLVASDMGLLGRFHFAGSTKPREVTVDQLVSFCNSPAGALFRLPDADSLRLATRINDRDGGLITQGSLHEHALQSILVK... | 2.3.1.- | null | fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; secondary metabolite biosynthetic process [GO:0044550]; terpenoid biosynthetic process [GO:0016114] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177] | PF00698;PF18558;PF00109;PF02801;PF08242;PF07993;PF00550;PF16073; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.40.50.720;3.10.129.110;3.40.50.150; | null | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:17912413, ECO:0000269|PubMed:20552126, ECO:0000269|PubMed:29773797}. | null | null | FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor (PubMed:17912413, PubMed:20552126, PubMed:29773797). The first step of xenov... | Sarocladium schorii (Acremonium strictum (strain IMI 501407)) |
A5PJM4 | FSP1_BOVIN | MGSQVSMDAGAVHVVIVGGGFGGIAAASQLQALNIPFVLVDMKDSFHHNVAALRASVESGFAKKTFISYSVTFKENFRQGLVVEIDLKNQTVLLEDGQALPFSHLILATGSTGLFPGKFNQVSSQQMAIQAYEDMVTQVQRSQSIVVVGGGSAGVEMAAEIKTEYPEKEVTLIHSKMALADTELLPCVRQEVKEILLRKGVQLLLSERVSNLEALPVNERRECIKVQTDKGTEVDANLVIVCNGIKINSAAYRSAFGDRLASNGALRVNEYLQVEGYSHIYAIGDCADVREPKMAYHASLHANVAVANIVNSMKQRPLKT... | 1.6.5.- | COFACTOR: Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; Note=Binds 6-hydroxy-FAD non-covalently. {ECO:0000250|UniProtKB:Q9BRQ8}; | apoptotic mitochondrial changes [GO:0008637]; positive regulation of apoptotic process [GO:0043065]; regulation of cellular response to oxidative stress [GO:1900407]; vitamin K metabolic process [GO:0042373] | cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | electron-transferring-flavoprotein dehydrogenase activity [GO:0004174]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655] | PF07992; | 3.50.50.100; | FAD-dependent oxidoreductase family | PTM: N-myristoylation at Gly-2 mediates the recruitment to lipid droplets and plasma membrane. {ECO:0000250|UniProtKB:Q9BRQ8}. | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q9BRQ8}. Cell membrane {ECO:0000250|UniProtKB:Q9BRQ8}; Lipid-anchor {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9BRQ8}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BRQ8}. Nucleus {ECO:0000250|UniProtKB:Q9BRQ8}. | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10; Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985; Evidence={ECO:000025... | null | null | null | null | FUNCTION: A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to supp... | Bos taurus (Bovine) |
A5PJN2 | ERO1A_BOVIN | MGRRWGFLIGFLVAVGLLGLGHGEQQPSETAAQRCFCQVSGYLDDCTCDVETIDKFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDINQCGRRDCAVKPCHSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEVDDIQSPDAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGKSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDTWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVVP... | 1.8.4.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q96HE7}; | cell redox homeostasis [GO:0045454]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]; release of sequestered calcium ion into cytosol [GO:0051209]; response to endoplasmic reticulum stress... | dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491]; protein-disulfide reductase activity [GO:0015035]; thiol oxidase activity [GO:0016972] | PF04137; | null | EROs family | PTM: The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397. The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (By... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96HE7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96HE7}; Lumenal side {ECO:0000250|UniProtKB:Q96HE7}. Golgi apparatus lumen {ECO:0000250|UniProtKB:Q96HE7}. Secreted {ECO:0000250|UniProtKB:Q96HE7}. Cell projection, dendrite {ECO:0000... | null | null | null | null | null | FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen... | Bos taurus (Bovine) |
A5PJP6 | BRCC3_BOVIN | MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDLRNDPKFTYTGTEMRTVAEKVDTVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESPRGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHVQELQQEKEELLQELSSLE | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:E2AXC7, ECO:0000250|UniProtKB:P46736}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:E2AXC7}; | cell division [GO:0051301]; chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of DNA repair [GO:0045739]; positive regulation of NLRP3 inflammasome complex assem... | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle pole [GO:0000922] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. {ECO:0000250|UniPr... | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to targ... | Bos taurus (Bovine) |
A5PJS6 | UBP10_BOVIN | MALRSPQYIFGDFSPDEFNQFFVTPRASVELPPYGGTVLCGAQAADDLPDGHDYQRIEFGVNEVIEPSDTLPRTPNYSISSTLNPQAPEFILSCTTSKKLPDDIDKEVNYSSANCQYPGPALALDGGSPAEAEALENDGVSGGLGQRERKKKKKRPPGYYSYLKDGGEGGPSAEALVNGHAGPAVSNSVGAEDTDLMGDVPTAGTPRTWGSPQDATDFVSDAGPAGAFPGALDGGARTAGQLEGCPGADSEASCLPAEAGRDTLLRTAVAQPSVGTDTTENLGVTNGQILESLGEGTAANGVELHTVESSDSDPAKAESA... | 3.4.19.12 | null | autophagy [GO:0006914]; cellular response to interleukin-1 [GO:0071347]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA repair [GO:0006281]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of stress gran... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; p53 binding [GO:0002039]; transmembrane transporter binding [GO:0044325] | PF07145;PF00443; | 3.90.70.10; | Peptidase C19 family, USP10 subfamily | PTM: Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus. {ECO:0000250}.; PTM: Ubiquitinated. Deubiquitinated by USP13 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}. Nucleus {ECO:0000250|UniProtKB:Q14694}. Early endosome {ECO:0000250|UniProtKB:Q14694}. Note=Cytoplasmic in normal conditions (By similarity). After DNA damage, translocates to the nucleus following phosphorylation by ATM (By similarity). {ECO:0000250|UniPr... | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q14694}; | null | null | null | null | FUNCTION: Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and s... | Bos taurus (Bovine) |
A5PJW8 | RPB2_BOVIN | MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVEDAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTYSAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLDPGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSMLARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEMVKPSLDEAFVIQEQNVALNF... | 2.7.7.48; 2.7.7.6; 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P30876}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P30876}; | null | chromosome, telomeric region [GO:0000781]; RNA polymerase II, core complex [GO:0005665] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; DNA/RNA hybrid binding [GO:0071667]; hydrolase activity [GO:0016787]; ribonucleoside binding [GO:0032549]; RNA polymerase II activity [GO:0001055]; RNA-dependent RNA polymerase activity [GO:0003968]; zinc ... | PF04563;PF04561;PF04565;PF04566;PF04567;PF00562;PF04560; | 2.40.50.150;3.90.1070.20;3.90.1100.10;2.40.270.10;3.90.1800.10;3.90.1110.10; | RNA polymerase beta chain family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30876}. | 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=2.7.7.6; Evidence={ECO:0000269|PubMed:16769904, ECO:0000269|PubMed:26789250}; PhysiologicalDirec... | null | null | null | null | FUNCTION: Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (PubMed:16769904, PubMed:26789250). Pol II-mediated transcription cycle proceeds through transc... | Bos taurus (Bovine) |
A5PJZ1 | SCMC1_BOVIN | MLRWLRGFVLPTAACQDVEPPTRYETLFQKLDRNGDGVVDISELQEGLKSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQILGLTISEQQAELILQSIDADGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGVAGAVSRTSTAPLDRLKVMMQVHGSKSAKMNIYGGFQQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKIGTFERFVSGSMAGATAQTFIYPMEVLKTRLAVGK... | null | null | adenine nucleotide transport [GO:0051503]; ADP transport [GO:0015866]; ATP transport [GO:0015867] | mitochondrial inner membrane [GO:0005743] | adenine nucleotide transmembrane transporter activity [GO:0000295]; ADP:inorganic phosphate antiporter activity [GO:0140988]; ATP transmembrane transporter activity [GO:0005347]; ATP:inorganic phosphate antiporter activity [GO:0140987]; calcium ion binding [GO:0005509] | PF13499;PF00153; | 1.10.238.10;1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6NUK1}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + H(+)(out) + phosphate(in) = ADP(in) + H(+)(in) + ph... | null | null | null | null | FUNCTION: Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleo... | Bos taurus (Bovine) |
A5PK42 | ODAD4_BOVIN | MADPENEVLRSTFPSYMAEGERLYLCGEFAKAAHSFSNALHLQSGDKNCLVARSKCFLKMGELEKSLEDAEASLQGDPTFCKGILQKAETLYTMGDFEFALVFYHRGYKLRPDREFKVGIQKAQEAINNSVGSPSSIKLENKGDLSFLSKQAESMRAQQKPHPVRQLIHHPKRESKRKGSLKSEKIVRQLLGELYVDKEYLEKLLLDEDLIKGTIKHGLTVEDLIMTGINYLETRSDFWRQQKPIYARERDRKLMQEKWLRDRKRRPSQTARYILKSLEDIDMLLTSGSAEGSLQKAEKVLKKVLEWNKEEVPNKDELVG... | null | null | brain development [GO:0007420]; cerebrospinal fluid circulation [GO:0090660]; cilium movement [GO:0003341]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; heart development [GO:0007507]; lung development [GO:0030324]; mucociliary clearance [GO:0120197]; outer dynein arm assem... | 9+0 motile cilium [GO:0097728]; 9+2 motile cilium [GO:0097729]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; outer dynein arm docking complex [GO:0120228] | null | PF13181; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. | null | null | null | null | null | FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Plays an essential role for the assembly of ODA-DC and for the docking of ODA in ciliary axoneme. {ECO:0000269|PubMed:34715025}. | Bos taurus (Bovine) |
A5PK46 | LIPR2_BOVIN | MLPSWTIGLLLLATVRGKEICYEPFGCFSDEKPWTGILQRPLKLFPWSPEDIDAHFLLYTNENPNNYQRINITDLATVRASNFQLDRKTRFVIHGFIDDGDSGWPTDLCKKMFKVEKVNCICVDWEHGAWTKYTQAVHNTRVVGAEIAFFIQGLSTELGYGPENVHLIGHSLGAQLAAEAGRRLGGQVGRITGLDPAQPCFEGTPEEVRLDPSDAMFVDVIHTDSASIIPFLSLGIRQKVGHLDFYPNGGKEMPGCQKNILSTIIDINGIWQGIQDFVACSHLRSYKYYSSSILNPDGFLGYPCASYEEFQEGGCFPCPA... | 3.1.1.26; 3.1.1.3 | null | cellular defense response [GO:0006968]; galactolipid catabolic process [GO:0019376]; intestinal lipid catabolic process [GO:0044258]; phospholipid catabolic process [GO:0009395]; phospholipid metabolic process [GO:0006644]; response to bacterium [GO:0009617]; triglyceride catabolic process [GO:0019433] | extracellular space [GO:0005615]; neuron projection [GO:0043005]; zymogen granule membrane [GO:0042589] | 1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity [GO:0102549]; acylglycerol lipase activity [GO:0047372]; calcium ion binding [GO:0005509]; galactolipase activity [GO:0047714]; phospholipase activity [GO:0004620]; triglyceride lipase activity [GO:0004806] | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:... | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12... | null | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000250|UniProtKB:P54317}.; PATHWAY: Glycolipid metabolism. {ECO:0000250|UniProtKB:P54317}. | null | null | FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides. In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides. Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional... | Bos taurus (Bovine) |
A5PK74 | RIOX1_BOVIN | MDGLRASAGLLRRGRLRRRRQQQPHSGSVLALPLRPRKIRRQLRRSVSSRMAALRAQTLQSEDSEDSRVESTVGEPGDPLAGGTAALSDATGREPHGQLGPVELLEASPASRSLQTPRALVEAQTPAARLVEAQTPAARLVEAHTPAARLVEAHTPPARLVEASALPARLVETSALLCSTQHLAAVPPSVAPAMLSGPQGESTGEELPWDSPLQRILAELNRIPSSRRRAARLFEWLISPMPPDHFYRRLWEREAVLVRRQDHSYYQGLFSTAVLDSILRNEEVQFGQHLDAARYINGRRETLNPPGRALPAAAWSLYRA... | 1.14.11.27; 1.14.11.79 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q9JJF3}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9JJF3}; | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of osteoblast differentiation [GO:0045668] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone H3K36 demethylase activity [GO:0051864]; histone H3K36me/H3K36me2 demethylase activity [GO:0140680]; histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; iron ion binding [GO:0005506]; peptid... | PF08007;PF21233; | 3.90.930.40;2.60.120.650;1.10.10.1500; | ROX family, NO66 subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6W3}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H6W3}. Note=Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli. {ECO:0000250|UniProtKB:Q9H6W3}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29... | null | null | null | null | FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and... | Bos taurus (Bovine) |
A5PKJ4 | MK07_BOVIN | MAEPLKEDDGEDGSGEPPGPVKAEPAGTAASVAAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMTVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQA... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | calcineurin-NFAT signaling cascade [GO:0033173]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to transforming growth factor beta stimulus [GO:0071560]; intracellular signal... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; mitogen-activated protein kinase binding [GO:0051019]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body {ECO:0000250}. Note=Translocates to the nucleus upon activation. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-indep... | Bos taurus (Bovine) |
A5PKP9 | UB2D4_XENLA | MALKRIQKELMDLQRDPPAQCSAGPVGEDLFHWQATIMGPNDSPFQGGVFFLTIHFPTDYPFKPPKVAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPEIAHTYKADREKYNRLAREWTQKYAM | 2.3.2.23 | null | pronephric nephron tubule development [GO:0039020]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567] | nucleus [GO:0005634] | ATP binding [GO:0005524]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000250|UniProtKB:Q9Y2X8, ECO:0000255|PROSITE-ProR... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9Y2X8, ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Regulates pronephros development, possibly by promoting ubiquitination and thus inactivation or degradation of map3k10/mlk2. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:18021256}. | Xenopus laevis (African clawed frog) |
A5PKW4 | PSD1_HUMAN | MAQGAMRFCSEGDCAISPPRCPRRWLPEGPVPQSPPASMYGSTGSLLRRVAGPGPRGRELGRVTAPCTPLRGPPSPRVAPSPWAPSSPTGQPPPGAQSSVVIFRFVEKASVRPLNGLPAPGGLSRSWDLGGVSPPRPTPALGPGSNRKLRLEASTSDPLPARGGSALPGSRNLVHGPPAPPQVGADGLYSSLPNGLGGPPERLATLFGGPADTGFLNQGDTWSSPREVSSHAQRIARAKWEFFYGSLDPPSSGAKPPEQAPPSPPGVGSRQGSGVAVGRAAKYSETDLDTVPLRCYRETDIDEVLAEREEADSAIESQPS... | null | null | neuron projection development [GO:0031175]; regulation of ARF protein signal transduction [GO:0032012]; signal transduction [GO:0007165] | cleavage furrow [GO:0032154]; dendritic spine [GO:0043197]; postsynaptic density, intracellular component [GO:0099092]; ruffle membrane [GO:0032587] | guanyl-nucleotide exchange factor activity [GO:0005085]; phospholipid binding [GO:0005543] | PF15410;PF01369; | 1.10.1000.11;2.30.29.30; | PSD family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23603394}. Cell projection, ruffle membrane {ECO:0000269|PubMed:23603394}. Cleavage furrow {ECO:0000269|PubMed:23603394}. Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches ... | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor for ARF6 (PubMed:23603394). Induces cytoskeletal remodeling (By similarity). {ECO:0000250|UniProtKB:Q5DTT2, ECO:0000269|PubMed:23603394}. | Homo sapiens (Human) |
A5PLL7 | PDES1_HUMAN | MAGAENWPGQQLELDEDEASCCRWGAQHAGARELAALYSPGKRLQEWCSVILCFSLIAHNLVHLLLLARWEDTPLVILGVVAGALIADFLSGLVHWGADTWGSVELPIVGKAFIRPFREHHIDPTAITRHDFIETNGDNCLVTLLPLLNMAYKFRTHSPEALEQLYPWECFVFCLIIFGTFTNQIHKWSHTYFGLPRWVTLLQDWHVILPRKHHRIHHVSPHETYFCITTGWLNYPLEKIGFWRRLEDLIQGLTGEKPRADDMKWAQKIK | 1.14.19.77 | null | ether lipid biosynthetic process [GO:0008611]; fatty acid metabolic process [GO:0006631] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | plasmanylethanolamine desaturase activity [GO:0050207] | PF10520; | null | Fatty acid desaturase CarF family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11076860, ECO:0000269|PubMed:31604315}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=1-(1,2-saturated alkyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:22956, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:31604315}. | null | null | FUNCTION: Plasmanylethanolamine desaturase involved in plasmalogen biogenesis in the endoplasmic reticulum membrane (PubMed:31604315, PubMed:32209662, PubMed:33859415). Plasmalogens are glycerophospholipids with a hydrocarbon chain linked by a vinyl ether bond at the glycerol sn-1 position, and are involved in antioxid... | Homo sapiens (Human) |
A5PN09 | UBP20_DANRE | MTDSGDLCPHLDSIGEVTKEELIQKSKGTCQSCGVGGPNLWACLQCDCPYVGCGESYSDHSTIHAQAKKHNLTVNLTTFRVWCYVCEREVFLEPKPVTPVSSAHRCKPHDQDPVSQTTCYPLKAVPIAVADEEGSESEEDELKPRGLTGMKNIGNSCYMNAALQALSNCPPLTQFFQDCSGLVRTDKKPALCKSYQKLISELWHKKRPSYVVPTTLFHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPLFDCSGGISEVEPDLSLDSCNLVDGDRSPSEDEFLSCDSGSGSERGDGERAGGEAELLIQDECVAVR... | 3.4.19.12 | null | central nervous system morphogenesis [GO:0021551]; cranial skeletal system development [GO:1904888]; endocytosis [GO:0006897]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of G protein-coup... | centrosome [GO:0005813]; perinuclear region of cytoplasm [GO:0048471] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; zinc ion binding [GO:0008270] | PF06337;PF00443;PF02148; | 3.90.70.10;3.30.2230.10;3.30.40.10; | Peptidase C19 family, USP20/USP33 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; | null | null | null | null | FUNCTION: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (adrb2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (adrb2). Plays a central role in adrb2 recycling and resensitization after prolonged agonist stimula... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5PN28 | OTO1A_DANRE | MPNILHPFIIIMTLLVVATGNQASIDKTTQWPRMKPTKKPPPRDEGPSKLGSISTTVSPTAIGITEEVTDAMMDAYTITSTGSTTFSSDTYSADYHTEAMVPPGVGPGNYTLDYNECFFNFCECCPPERGPPGPVGEKGLPGIPGGKGEMGPPGPPGQEGLTGAPGTHGVKGEKGDTGASGLPGIPGVTGKQGEKGESGPKGDKGDTGFPGLKGDPGERGEPGWNGTKGGMGEPGKQGLTGPPGPDGIKGEKGDKGDCPFGEKGQKGSIGEPGPQGPKGDPGVPGTNGTDGLPGSKGPKGDPGPLSKQGEPGPPGPQGPP... | null | null | extracellular matrix organization [GO:0030198]; otolith development [GO:0048840]; otolith mineralization [GO:0045299]; protein complex oligomerization [GO:0051259] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF00386;PF01391; | 2.60.120.40; | OTOL1 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q4ZJM7}. Note=Localized in both the surrounding otoconial matrix and otoconia. {ECO:0000250|UniProtKB:Q4ZJM7}. | null | null | null | null | null | FUNCTION: Collagen-like protein, which provides an organic scaffold for otoliths onto the sensory epithelium of the inner ear (PubMed:15905077, PubMed:29076638). Acts as a scaffold for biomineralization by sequestering calcium (PubMed:29076638). {ECO:0000269|PubMed:15905077, ECO:0000269|PubMed:29076638}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5TY85 | PKNA_MYCTA | MSPRVGVTLSGRYRLQRLIATGGMGQVWEAVDNRLGRRVAVKVLKSEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESQMNGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDASPASDVYSLGVVGYEAVSGKRPFAGDGALTVAMKHIKEPPPPLPPDLPPNVRELIEITLVKNPAMRYRSGGPFADAVAAVRAGRRPPRPSQTPPPGRAAPAAIPSGTTARVAANSAGRTAASRRSR... | 2.7.11.1 | null | phosphorylation [GO:0016310]; regulation of primary metabolic process [GO:0080090] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11856348, ECO:000026... | null | null | null | null | FUNCTION: Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins such as FtsZ and MurD. Shows a strong preference for Thr versus Ser as the phosphoacceptor... | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U1U6 | KGD_MYCTA | MANISSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYSPEPTSQPAAEPTRVTSPLVAERAAAAAPQAPPKPADTAAAGNGVVAALAAKTAVPPPAEGDEVAVLRGAAAAVVKNMSASLEVPTATSVRAVPAKLLIDNRIVINNQLKRTRGGKISFTHLLGYALVQAVKKFPNMNRHYTEVDGKPTAVTPAHTNLGLAIDLQGKDGKRSLVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTTEDFAGVTISLTNPGTIGTVHSVPRLMPGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQ... | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [... | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RH... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutar... | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U2Z7 | LYSX_MYCTA | MGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSL... | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2... | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to t... | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U493 | BLAC_MYCTA | MRNRGFGRRELLVAMAMLVSVTGCARHASGARPASTTLPAGADLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQQHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAIALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFPADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRAGGGYDAEPREALLAEAATCVAGVLA | 3.5.2.6 | null | beta-lactam antibiotic catabolic process [GO:0030655]; response to antibiotic [GO:0046677] | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | beta-lactamase activity [GO:0008800] | PF13354; | 3.40.710.10; | Class-A beta-lactamase family | PTM: Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000250|UniProtKB:P9WKD3}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P9WKD3}. Secreted {ECO:0000269|PubMed:9624479}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:9624479}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for benzylpenicillin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=38 uM for phenoxymethylpenicillin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=94 uM for amoxicillin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=185 uM for azlocillin (at pH 6.0) {ECO:0000269|... | null | null | null | FUNCTION: Extended spectrum beta-lactamase (ESBL) that inactivates beta-lactam antibiotics by hydrolyzing the amide group of the beta-lactam ring. Exhibits predominant penicillinase activity. Also displays high levels of cephalosporinase activity as well as measurable activity with carbapenems, including imipenem and m... | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U4N0 | ADOK_MYCTA | MTIAVTGSIATDHLMRFPGRFSEQLLPEHLHKVSLSFLVDDLVMHRGGVAGNMAFAIGVLGGEVALVGAAGADFADYRDWLKARGVNCDHVLISETAHTARFTCTTDVDMAQIASFYPGAMSEARNIKLADVVSAIGKPELVIIGANDPEAMFLHTEECRKLGLAFAADPSQQLARLSGEEIRRLVNGAAYLFTNDYEWDLLLSKTGWSEADVMAQIDLRVTTLGPKGVDLVEPDGTTIHVGVVPETSQTDPTGVGDAFRAGFLTGRSAGLGLERSAQLGSLVAVLVLESTGTQEWQWDYEAAASRLAGAYGEHAAAEIV... | 2.7.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:14594827}; | AMP salvage [GO:0044209]; fructose metabolic process [GO:0006000]; purine ribonucleoside salvage [GO:0006166]; regulation of glycogen metabolic process [GO:0070873]; response to fructose [GO:0009750]; response to glucose [GO:0009749]; response to insulin [GO:0032868]; response to sucrose [GO:0009744]; response to zinc ... | null | adenosine kinase activity [GO:0004001]; ATP binding [GO:0005524]; ketohexokinase activity [GO:0004454] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine + ATP = ADP + AMP + H(+); Xref=Rhea:RHEA:20824, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20; Evidence={ECO:0000269|PubMed:14594827}; CATALYTIC ACTIVITY: Reaction=adenosine + GTP = AMP + GDP + H(+); Xref=Rhea:RHEA:525... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for adenosine (in the presence of 10 mM KCl) {ECO:0000269|PubMed:14594827}; KM=3.4 uM for adenosine (in the absence of KCl) {ECO:0000269|PubMed:14594827}; KM=79 uM for methyl-adenosine (in the presence of 10 mM KCl) {ECO:0000269|PubMed:14594827}; KM=709 uM f... | PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1. {ECO:0000305|PubMed:14594827}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-11. Activity decreases rapidly at values above pH 11 and below pH 8. Is inactive at pH 4.3. {ECO:0000269|PubMed:14594827}; | null | FUNCTION: Catalyzes the phosphorylation of adenosine to adenosine monophosphate (AMP). Can also catalyze the phosphorylation of the adenosine analog 2-methyladenosine (methyl-Ado) to methyl-AMP, the first step in the metabolism of this compound to an active form that displays antitubercular activity. Is not active on g... | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U654 | PPGK_MYCTA | MTSTGPETSETPGATTQRHGFGIDVGGSGIKGGIVDLDTGQLIGDRIKLLTPQPATPLAVAKTIAEVVNGFGWRGPLGVTYPGVVTHGVVRTAANVDKSWIGTNARDTIGAELGGQQVTILNDADAAGLAETRYGAGKNNPGLVVLLTFGTGIGSAVIHNGTLIPNTEFGHLEVGGKEAEERAASSVKEKNDWTYPKWAKQVIRVLIAIENAIWPDLFIAGGGISRKADKWVPLLENRTPVVPAALQNTAGIVGAAMASVADTTH | 2.7.1.2; 2.7.1.63 | null | null | null | ATP binding [GO:0005524]; glucokinase activity [GO:0004340]; polyphosphate-glucose phosphotransferase activity [GO:0047330] | PF00480; | 3.30.420.40; | ROK (NagC/XylR) family | null | null | CATALYTIC ACTIVITY: Reaction=[phosphate](n) + D-glucose = [phosphate](n-1) + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:22036, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:61548; EC=2.7.1.63; Evidence={ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:870... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.4 uM for (Phosphate)(32) (at pH 8.6) {ECO:0000269|PubMed:8381043}; KM=13.9 uM for polyphosphate type 35 (Sigma) (at pH 7.5) {ECO:0000269|PubMed:8703950}; KM=6.1 uM for polyphosphate type 35 (Sigma) (at pH 8.6) {ECO:0000269|PubMed:8703950}; KM=0.28 mM for D-gluco... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5 and 9.6-9.5 with poly(P)(32) and ATP as the phosphoryl donors, respectively. {ECO:0000269|PubMed:8381043}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius for both activities. {ECO:0000269|PubMed:8381043}; | FUNCTION: Catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor (PubMed:8381043, PubMed:8703950). Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in M.tuberculosis (PubMed:8703950). GTP, UTP and CTP can replace ATP as phosphoryl donor (PubMed:83... | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U6Z7 | DBH_MYCTA | MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK | 1.16.3.1 | null | chromosome condensation [GO:0030261]; intracellular iron ion homeostasis [GO:0006879] | cytosol [GO:0005829]; nucleoid [GO:0009295] | DNA binding [GO:0003677]; oxidoreductase activity [GO:0016491]; structural constituent of chromatin [GO:0030527] | PF00216; | 4.10.520.10; | Bacterial histone-like protein family, Long actinobacterial subfamily | PTM: Phosphorylated in vivo on Ser and Thr-residues; the protein is degraded during purification so most sites were not identified, but at least one of Thr-43 and/or Thr-45 are modified in vivo. In vitro at least PknE, PknF and PknB phosphorylate HupB; PknE is the most active and phosphorylates many sites in vitro incl... | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:24916461}. | CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000250|UniProtKB:Q9XB18}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149; Evidence={ECO:000... | null | null | null | null | FUNCTION: A nucleoid-associated protein (NAP) that plays a role in local chromosome architecture (Probable) (PubMed:24916461). Binds DNA non-sequence specifically; in vitro phosphorylation of an N-terminal fragment decreases DNA-binding (PubMed:24816602). Stimulates supercoiling relaxation by topoisomerase 1 (Top1, top... | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U8S6 | PAND_MYCTA | MLRTMLKSKIHRATVTCADLHYVGSVTIDADLMDAADLLEGEQVTIVDIDNGARLVTYAITGERGSGVIGINGAAAHLVHPGDLVILIAYATMDDARARTYQPRIVFVDAYNKPIDMGHDPAFVPENAGELLDPRLGVG | 4.1.1.11 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_00446}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_00446}; | alanine biosynthetic process [GO:0006523]; pantothenate biosynthetic process [GO:0015940]; response to antibiotic [GO:0046677] | cytosol [GO:0005829] | aspartate 1-decarboxylase activity [GO:0004068] | PF02261; | 2.40.40.20; | PanD family | PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. {ECO:0000255|HAMAP-Rule:MF_00446}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00446}; | null | PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00446}. | null | null | FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446}.; FUNCTION: Overexpression of wild-type or mutant proteins confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA), when grown on ag... | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5W059 | HMGA_PSEP1 | MNTLIGKTGIVVRNIQRAELDSIDALGRLGVATVHEAQNRKGLLSSKMRPIQQGTSLAGSAVTVLVAPGDNWMFHVAVEQCRPGDVLVVSPSSPCTDGYFGDLLATSLQARGVRALIVDAGVRDTQTLRDMGFAVWARAINAQGTVKETLGSVNLPVICGGQLINPGDIVVADDDGVVVVRRDECESTLVAAAERAGLEEEKRLRLAAGELGLDIYKMRERLEAKGLRYVDNIEDLEG | 4.1.1.112; 4.1.3.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20843800}; | null | null | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity [GO:0047443]; metal ion binding [GO:0046872]; oxaloacetate decarboxylase activity [GO:0008948] | PF03737; | 3.50.30.40; | LigK/PcmE family | null | null | CATALYTIC ACTIVITY: Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate; Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276; EC=4.1.3.17; Evidence={ECO:0000269|PubMed:20843800, ECO:0000269|PubMed:24359411}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate; Xr... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mM for oxaloacetate (in presence of 1 mM of magnesium) {ECO:0000269|PubMed:20843800}; KM=0.036 mM for oxaloacetate (in presence of 1 mM of manganese) {ECO:0000269|PubMed:20843800}; KM=0.26 mM for 4-hydroxy-4-methyl-2-oxoglutarate (in presence of 1 mM of magnesi... | null | null | null | FUNCTION: Catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway. The preferred substrates of the enzyme are 2-keto-4-hydroxy acids with a 4-carboxylate substitution. Catalyzes the conversion of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) to pyruvate. Also catalyzes the conversion of 4-carboxy-4-hydr... | Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) |
A5WMW1 | LYSX_MYCTF | MGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSL... | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2... | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to t... | Mycobacterium tuberculosis (strain F11) |
A5WVX9 | ZDH17_DANRE | MADALVGYEKEAGCVPILHPEEIKPQSHYNHGYNESRKSHVDDYSTWDIVKATQYGIFERCRELVEAGYDVRQPDKENVTLLHWAAINNRVDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCVHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEANANVDAQNIKGETPLDLAKQRKNVWMINHLQEARQAKGYDSPSYLKRLKMDKEFRQKVMLGTPFLVIWLVGFIADLDIDSWLIKG... | 2.3.1.-; 2.3.1.225 | null | axonogenesis [GO:0007409]; habituation [GO:0046959]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of neurotrophin TRK receptor signaling pathway [GO:0051386] | cell projection [GO:0042995]; cytoplasmic vesicle membrane [GO:0030659]; Golgi membrane [GO:0000139]; presynaptic membrane [GO:0042734] | palmitoyltransferase activity [GO:0016409]; protein-cysteine S-myristoyltransferase activity [GO:0019705]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; protein-cysteine S-stearoyltransferase activity [GO:0140439] | PF12796;PF01529; | 1.25.40.20; | DHHC palmitoyltransferase family, AKR/ZDHHC17 subfamily | PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q8IUH5}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein {ECO:000... | CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:Q8IUH5}; CATALYT... | null | null | null | null | FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octad... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5X5Y0 | 5HT3E_HUMAN | MEGSWFHRKRFSFYLLLGFLLQGRGVTFTINCSGFGQHGADPTALNSVFNRKPFRPVTNISVPTQVNISFAMSAILDVNEQLHLLSSFLWLEMVWDNPFISWNPEECEGITKMSMAAKNLWLPDIFIIELMDVDKTPKGLTAYVSNEGRIRYKKPMKVDSICNLDIFYFPFDQQNCTLTFSSFLYTVDSMLLDMEKEVWEITDASRNILQTHGEWELLGLSKATAKLSRGGNLYDQIVFYVAIRRRPSLYVINLLVPSGFLVAIDALSFYLPVKSGNRVPFKITLLLGYNVFLLMMSDLLPTSGTPLIGVYFALCLSLMV... | null | null | inorganic cation transmembrane transport [GO:0098662]; serotonin receptor signaling pathway [GO:0007210] | neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; serotonin-activated cation-selective channel complex [GO:1904602]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; serotonin-gated monoatomic cation channel activity [GO:0022850]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic mem... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily, HTR3E sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305|PubMed:17392525}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17392525, ECO:0000269|PubMed:19012743}; Multi-pass membrane protein {ECO:0000255}. Note=Presumably retained within the endoplasmic reticulum unless complexed with ... | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out... | null | null | null | null | FUNCTION: Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation-selective channel complexes, which when activated cause fast, depolarizing responses in neurons. {ECO:0000269|PubMed:17392525}. | Homo sapiens (Human) |
A5Y5L5 | CIN_NICSU | MNHHLIITPIFHLQIMLPVATLKRPPPPAATCSIYSFSRGTPSLVSKARLSTAAVGGMKNEPSPNHYSDISSSDLNLTRRSGNYGPTMWDFEYIQSIHNDYTEKKYMNRLNKLKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLFREYGFHISQEIFGGLSETHTEDTKGMLYLYEASFLATEGESELEKARNWTEKHLREYLENKNDDQNVAELVHHALELPLHWRMLRIEARWFINFYKKKQDMIPLLLELAILDFNIVQAAHIEDLKYVARWWKETCLAENLPF... | 4.2.3.-; 4.2.3.106; 4.2.3.108; 4.2.3.111; 4.2.3.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17611797}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17611797}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000269|PubMed:17611797}; | alpha-pinene biosynthetic process [GO:0046248]; circadian rhythm [GO:0007623]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; limonene biosynthetic process [GO:0046250]; monoterpene biosynthetic process [GO:0043693] | chloroplast [GO:0009507] | (E)-beta-ocimene synthase activity [GO:0034768]; 1,8-cineole synthase activity [GO:0102313]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate; Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108; Evidence={ECO:0000269|PubMed:17611797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32544; Evidence={ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 uM for (2E)-geranyl diphosphate {ECO:0000269|PubMed:17611797}; Note=kcat is 0.33 sec(-1) with (2E)-geranyl diphosphate as substrate. {ECO:0000269|PubMed:17611797}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:17611797}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:17611797}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:17611797}; | FUNCTION: Monoterpene synthase involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent (PubMed:17611797). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole and, as minor products, limonene, sabinene, (E)-beta-ocimene, b... | Nicotiana suaveolens (Australian tobacco) |
A5YKK6 | CNOT1_HUMAN | MNLDSLSLALSQISYLVDNLTKKNYRASQQEIQHIVNRHGPEADRHLLRCLFSHVDFSGDGKSSGKDFHQTQFLIQECALLITKPNFISTLSYAIDNPLHYQKSLKPAPHLFAQLSKVLKLSKVQEVIFGLALLNSSSSDLRGFAAQFIKQKLPDLLRSYIDADVSGNQEGGFQDIAIEVLHLLLSHLLFGQKGAFGVGQEQIDAFLKTLRRDFPQERCPVVLAPLLYPEKRDILMDRILPDSGGVAKTMMESSLADFMQEVGYGFCASIEECRNIIVQFGVREVTAAQVARVLGMMARTHSGLTDGIPLQSISAPGSGI... | null | null | miRNA-mediated post-transcriptional gene silencing [GO:0035195]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulatio... | CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634]; P-body [GO:0000932]; peroxisomal membrane [GO:0005778] | armadillo repeat domain binding [GO:0070016]; molecular adaptor activity [GO:0060090]; nuclear estrogen receptor binding [GO:0030331]; nuclear retinoic acid receptor binding [GO:0042974]; protein domain specific binding [GO:0019904]; RNA binding [GO:0003723] | PF16415;PF16418;PF16417;PF12842;PF04054; | 1.25.40.180;1.25.40.790;1.25.40.800;1.25.40.840; | CNOT1 family | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:21976065}. Nucleus {ECO:0000305|PubMed:21976065}. Note=NANOS2 promotes its localization to P-body. {ECO:0000250|UniProtKB:Q6ZQ08}. | null | null | null | null | null | FUNCTION: Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional c... | Homo sapiens (Human) |
A5YM72 | CRNS1_HUMAN | MLLCLSPAWLMKVPAPGQPGEAALLVSKAVSFHPGGLTFLDDFVPPRRATYFLAGLGLGPGRGREAAELARDLTCPTGASAELARLLEDRLLTRQLLAQQGGVAVPATLAFTYKPPGLLRGGDASLGLRLVELSGKEGQETLVKEEVEAFLRSEALGDILQVAVKLSGWRWRGRQAWRLHPRAELGAVVDTVLALLEKLEEEESVLVEAVYPPAQLPCSDGPSPGPGLAVRICAVVCRTQGDRPLLSKVVCGVGRGDRPLRHHNSLPRTLEVALAQCGLGEEAQVAAVRQRVKAAAEAALAAVLALEAGLSAEQRGGRRA... | 6.3.2.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | carnosine biosynthetic process [GO:0035499]; histidine catabolic process [GO:0006548] | cytosol [GO:0005829] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; carnosine synthase activity [GO:0047730]; homocarnosine synthase activity [GO:0102102]; metal ion binding [GO:0046872] | PF18130;PF15632; | 3.40.50.20;3.30.470.20; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-alanine + L-histidine = ADP + carnosine + H(+) + phosphate; Xref=Rhea:RHEA:19297, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57485, ChEBI:CHEBI:57595, ChEBI:CHEBI:57966, ChEBI:CHEBI:456216; EC=6.3.2.11; PhysiologicalDirection=left-to-right; Xref=Rhea:RHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for beta-alanine {ECO:0000269|PubMed:20097752}; KM=1.84 mM for 4-aminobutanoate {ECO:0000269|PubMed:20097752}; KM=0.37 mM for L-histidine {ECO:0000269|PubMed:20097752}; KM=4.67 mM for L-lysine {ECO:0000269|PubMed:20097752}; KM=7.66 mM for L-ornithine {ECO:0... | null | null | null | FUNCTION: Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine. {ECO:0000269|PubMed:20097752}. | Homo sapiens (Human) |
A5YVK8 | ERVA_TABDI | AVIPLKNQGKCGSCWAFSTVTTVESINQIRTGNLISLSEQQLVDCSKKNHGCKGGYFDRAYQYIIANGGIDTEANYPYKAFQGPCRAAKKVVRIDGCKGVPQCNENALKNAVASQPSVVAIDASSKQFQHYKSGIFTGPCGTKLNHGVVIVGYGKDYWIVRNSWGRHWGEQGYTRMKRVGGCGL | 3.4.22.- | null | proteolysis involved in protein catabolic process [GO:0051603] | extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83654}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.071 mM for N-benzoyl-Phe-Val-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=0.75 mM for D-Val-Leu-Lys-pNA {ECO:0000269|PubMed:18167146}; KM=1.666 mM for D-Ile-Phe-Lys-pNA {ECO:0000269|PubMed:18167146}; KM=0.501 mM for Ala-Ala-Val-Ala-pNA {ECO:0000269|PubMed:18167146};... | null | null | null | FUNCTION: Cysteine proteinase. {ECO:0000269|PubMed:18167146}. | Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria) |
A5Z1X6 | ITB1_CAMBA | MNLQLIFWIGLISSVCCVFGQADEDRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCHPNDTENPRGSKDIKKNKNVTNRSKGTAEKLQPEDITQIQPQQLVLQLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTNEQNCTSPFSYKNVLSLTDKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLKNDVYTMSHYYDYPSIA... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520]; negativ... | cell surface [GO:0009986]; focal adhesion [GO:0005925]; integrin alpha9-beta1 complex [GO:0034679]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; membrane [GO:0016020]; recycling endosome [GO:0055037]; ruffle membrane [GO:0032587] | C-X3-C chemokine binding [GO:0019960]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding involved in cell-matrix adhesion [GO:0098640]; laminin binding [GO:0043236]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982] | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass ty... | null | null | null | null | null | FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, a... | Camelus bactrianus (Bactrian camel) |
A6BM07 | I7GT1_SOYBN | MKDTIVLYPNLGRGHLVSMVELGKLILTHHPSLSITILILTPPTTPSTTTTTLACDSNAQYIATVTATTPSITFHRVPLAALPFNTPFLPPHLLSLELTRHSTQNIAVALQTLAKASNLKAIVIDFMNFNDPKALTENLNNNVPTYFYYTSGASTLALLLYYPTIHPTLIEKKDTDQPLQIQIPGLSTITADDFPNECKDPLSYACQVFLQIAETMMGGAGIIVNTFEAIEEEAIRALSEDATVPPPLFCVGPVISAPYGEEDKGCLSWLNLQPSQSVVLLCFGSMGRFSRAQLKEIAIGLEKSEQRFLWVVRTELGGAD... | 2.4.1.170 | null | null | null | isoflavone 7-O-glucosyltransferase activity [GO:0050004] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a 7-hydroxyisoflavone + UDP-alpha-D-glucose = a 7-hydroxyisoflavone 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:56344, ChEBI:CHEBI:15378, ChEBI:CHEBI:55465, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140301; EC=2.4.1.170; Evidence={ECO:0000269|PubMed:17565994}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 uM for genistein {ECO:0000269|PubMed:17565994}; KM=190 uM for UDP-glucose {ECO:0000269|PubMed:17565994}; Note=kcat is 0.74 sec(-1)for genistein (at pH 8.5 and 30 degrees Celsius).; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:17565994}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:17565994}; | FUNCTION: Involved in the biosynthesis of isoflavonoids. Specific for UDP-glucose. Can use genistein > daidzein > formononetin > quercetin > kaempferol > 4,2',4',6'-tetrahydroxychalcone > apigenin > aureusidin > esculetin > naringenin as substrates, but not cyanidin, trans-p-coumaric acid, caffeic acid, benzoic acid, m... | Glycine max (Soybean) (Glycine hispida) |
A6BM72 | MEG11_HUMAN | MVLSLTGLIAFSFLQATLALNPEDPNVCSHWESYAVTVQESYAHPFDQIYYTRCTDILNWFKCTRHRISYKTAYRRGLRTMYRRRSQCCPGYYESGDFCIPLCTEECVHGRCVSPDTCHCEPGWGGPDCSSGCDSDHWGPHCSNRCQCQNGALCNPITGACVCAAGFRGWRCEELCAPGTHGKGCQLPCQCRHGASCDPRAGECLCAPGYTGVYCEELCPPGSHGAHCELRCPCQNGGTCHHITGECACPPGWTGAVCAQPCPPGTFGQNCSQDCPCHHGGQCDHVTGQCHCTAGYMGDRCQEECPFGSFGFQCSQHCDC... | null | null | homotypic cell-cell adhesion [GO:0034109]; retina layer formation [GO:0010842] | basolateral plasma membrane [GO:0016323] | null | PF12661;PF00053; | 2.10.25.10;2.170.300.10; | MEGF family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17498693}; Single-pass type I membrane protein {ECO:0000269|PubMed:17498693}. Basolateral cell membrane {ECO:0000269|PubMed:17498693}; Single-pass type I membrane protein {ECO:0000269|PubMed:17498693}. Note=Forms an irregular, mosaic-like adhesion pattern in regio... | null | null | null | null | null | FUNCTION: May regulate the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements (By similarity).... | Homo sapiens (Human) |
A6BMK7 | NEUR1_BOVIN | MTEEGPGIVSLGKLRRPRMLRLWGICRVQIFSAIFMLMSPAGVGAGAKDDFSLVHPLVTMEQLLWVSGKQIGSVDTFRIPLITTTPRGTLLAFAEARKMSTSDKGAKFIALRRSMDQGSTWSPTAFIVDDGETPDGLNLGAVVSDTTTGVVFLFYSLCAHKAGCQVASTMLVWSKDDGVSWSSPRNLSLDIGTEMFAPGPGSGIQKQREPRKGRLIVCGHGTLERDGVFCLLSDDHGVSWRYGGGVSGIPYGQPKRENDFNPDECQPYELPDGSVVINARNQNNYHCHCRIILRSYDACDTLRPRDVTFDTELVDPVVAA... | 3.2.1.18 | null | ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; exo-alpha-sialidase activity [GO:0004308] | PF13088; | 2.120.10.10; | Glycosyl hydrolase 33 family | PTM: N-glycosylated. {ECO:0000250}.; PTM: Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane. {ECO:0000250}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Lysosome lumen {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but ... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; | null | null | null | null | FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
A6H5Y3 | METH_MOUSE | MKKTLQDEIEAILRKRIMVLDGGMGTMIQRYKLSEEHFQGQEFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNKCSADVARKAAEEITLQTGVKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVDAYQEQAKGLLDGRVDILLIETIFDTANAKAALFAIQNLFEENYAPPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCSLGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHIR... | 2.1.1.13 | COFACTOR: Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115; Evidence={ECO:0000250|UniProtKB:P13009}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P13009}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P13009}; | axon regeneration [GO:0031103]; cellular response to nitric oxide [GO:0071732]; cobalamin metabolic process [GO:0009235]; homocysteine metabolic process [GO:0050667]; methionine biosynthetic process [GO:0009086]; methionine metabolic process [GO:0006555]; methylation [GO:0032259]; response to axon injury [GO:0048678]; ... | cytosol [GO:0005829] | amino acid binding [GO:0016597]; cobalamin binding [GO:0031419]; folic acid binding [GO:0005542]; methionine synthase activity [GO:0008705]; methyltransferase activity [GO:0008168]; zinc ion binding [GO:0008270] | PF02310;PF02607;PF02965;PF00809;PF02574; | 3.40.50.280;1.10.288.10;3.20.20.20;3.20.20.330;1.10.1240.10;3.10.196.10; | Vitamin-B12 dependent methionine synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99707}. | CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13; Evidence={ECO:0000250|UniProtKB:Q9Z2Q4}; PhysiologicalDirection=left-to-righ... | null | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. {ECO:0000250|UniProtKB:Q9Z2Q4}. | null | null | FUNCTION: Catalyzes the transfer of a methyl group from methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound cob(I)alamin and methionine in the cytosol. MeCbl is an active form of cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis. Cob(I)alamin form is regenerated to MeCbl by a transf... | Mus musculus (Mouse) |
A6H630 | ARMT1_MOUSE | MAESPAFLSAKDEGSFAYLTIKDRTPQILTKVIDTLHRHKSEFFEKHGEEGIEAEKKAISLLSKLRNELQTDKPITPLVDKCVDTHIWNQYLEYQRSLLNEGDGEPRWFFSPWLFVECYMYRRIHEAIMQSPPIHDFDVFKESKEENFFESQGSIDALCSHLLQLKPVKGLREEQIQDEFFKLLQISLWGNKCDLSLSGGESSSQKANIINCLQDLKPFILINDTESLWALLSKLKKTVETPVVRVDIVLDNSGFELITDLVLADFLFSSELATEIHFHGKSIPWFVSDVTEHDFNWIVEHMKSSNLESMSTCGACWEAY... | 2.1.1.-; 3.1.3.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q04371}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250|UniProtKB:Q04371}; | DNA damage response [GO:0006974]; methylation [GO:0032259] | nucleus [GO:0005634] | enzyme binding [GO:0019899]; fructose 6-phosphate aldolase activity [GO:0097023]; fructose-1-phosphatase activity [GO:0103026]; metal ion binding [GO:0046872]; phosphatase activity [GO:0016791]; protein carboxyl O-methyltransferase activity [GO:0051998]; protein-glutamate O-methyltransferase activity [GO:0008983]; S-ad... | PF01937; | 1.20.930.60;3.40.50.10880; | Damage-control phosphatase family, Sugar phosphate phosphatase III subfamily | PTM: Automethylated. {ECO:0000250|UniProtKB:Q9H993}. | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate; Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721, ChEBI:CHEBI:43474, ChEBI:CHEBI:138881; Evidence={ECO:0000250|UniProtKB:Q04371}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + d... | null | null | null | null | FUNCTION: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-... | Mus musculus (Mouse) |
A6H639 | DRC5_MOUSE | MQETPSVPSNSSSHSQSVLTIQRQVSALGSSSTGPTSLKTSSTPTPGQLKTKVPNVRRMRRIISEDAEWSLAIVPLLTELCIQHIVKNFQNNPILKQLPLEHQKKVLSNLPPELPLTVTANLIDDENYWHRCCIKRWSVCHVSRHGGSWKRMFFERHLENLLKLFIPGTTDPNVILDLLPLCRNYVRRIHVDQFLPPVRMPTPLQGEEQSDSGSEGEGSEPEKDHYQLQTLVGGLKHLEELDLVYGVKDCGMNFEWNLFLFTYRDCYSLAATIKACHTLKIFKLTRSKVDDDKARILIRSLLDHPALEELDLSHNLIGDR... | null | null | flagellated sperm motility [GO:0030317]; microtubule-based movement [GO:0007018] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; sperm flagellum [GO:0036126] | null | PF13516; | 3.80.10.10; | DRC5 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|Ref.2}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8HMZ4}. Note=Detected along the length of the sperm flagellum. {ECO:0000269|Ref.2}. | null | null | null | null | null | FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. May play a role in the assembly of N-DRC (By similarity). Required for sperm motility (... | Mus musculus (Mouse) |
A6H687 | SAC31_MOUSE | MGRFKGENRSQARWIMGGVSKGRGSGKSRKPRQAAFGQTGARVCPSSPQQDAVPRFRWPGDAECASSTHTPTMSGCKLPMGLCPDMCPAAERARRERERRLHRLEVEPGGRGNAPRADPKRTVKEYSRPAAGKPRPPPSLLRPPPVLLATVRYLAGEVAGRGDVSCAEVASFVADRLRAVRLDLSLQGVDDADAATVLEAALATLLAVVARVRPEETRGAADPVLLQTQVQEGFGSLRRCYARGKGPYPRQAAFQGLFLLYNLGSVEALQEVLQLPAALRACPPLQAALAVDAAFREDNHARLFRLLRTLPYLQSCAVQE... | null | null | cell division [GO:0051301]; centrosome duplication [GO:0051298]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; regulation of immune response [GO:0050776]; spindle assembly [GO:0051225] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; spindle [GO:0005819] | null | PF03399; | 1.25.40.990; | SAC3 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15322101}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15322101}. Note=Localizes on centrosomes in interphase cells and at spindles in mitosis. | null | null | null | null | null | FUNCTION: Involved in centrosome duplication and mitotic progression. {ECO:0000269|PubMed:15322101}. | Mus musculus (Mouse) |
A6H6A9 | RBG1L_MOUSE | MEVRASFQKVSGSSDSVATLNSEEFVLVSQHTDATSIKDDGKPQLKIASNGDEQLEKAMEEILRDSEKGQSGLPVDCQGSSEISDCPFGDVPASQTTKPPLQLILDPSNTEISTPRPSSPSRFPEEDSVLFNKLTYLGCMKVSSPRSEVEALRAMATMRASSQYPFAVTLYVPNVPEGSVRIIDQSSNVEIASFPIYKVLFCARGHDGTAESNCFAFTESSHGSEEFQIHVFSCEIKEAVSRILYSFCTAFKRSSRQVSDVKDSVIPTPDSDVFTFSVSLEVKEDDGKGNFSPVPKDRDKFYFKIKQGIEKKVVITVQQL... | null | null | endocytosis [GO:0006897]; megakaryocyte development [GO:0035855]; protein transport [GO:0015031]; regulation of protein localization [GO:0032880] | early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634] | GTPase activator activity [GO:0005096]; small GTPase binding [GO:0031267] | PF12473;PF00566; | 2.30.29.30;1.10.8.270;1.10.10.750;1.10.472.80; | null | null | SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:27718357}. Golgi apparatus {ECO:0000250|UniProtKB:Q5R372}. Note=Colocalizes on endosomes partially with EEA1 (By similarity). Colocalizes and cotransports on motile vesicles with ANK2 (PubMed:27718357). {ECO:0000250|UniProtKB:Q5R372, ECO:0000269|PubMed:27718357}. | null | null | null | null | null | FUNCTION: GTP-hydrolysis activating protein (GAP) for small GTPase RAB22A, converting active RAB22A-GTP to the inactive form RAB22A-GDP (By similarity). Plays a role in endocytosis and intracellular protein transport. Recruited by ANK2 to phosphatidylinositol 3-phosphate (PI3P)-positive early endosomes, where it inacti... | Mus musculus (Mouse) |
A6H6E2 | MMRN2_MOUSE | MIPTLLLGFGVYLSWGLLGSWAQDPGTKFSHLNRPGMPEGWRLGAEDTSRDPIRRNWCPYQKSRLVTFVAACKTEKFLVHSQQPCPQGAPDCQGVRVMYRVAQKPVYQVQQKVLISVDWRCCPGFQGPDCQDHNPTANPEPTEPSGKLQETWDSMDGFELGHPVPEFNEIKVPQEQQENLLQNLQNDAQSVEDGFPGSWEAPPSNLTDEMTEANLTEFEFPGRTSEHLLQPHIDAFLKAHFSPIWKNFNDSLHSLSQAIRNLSLDVEANHQAIKMIQEGTVARADFQELGAKFEAKVQQNSQRLGQLWQDVEDQLHAQRR... | null | null | cell adhesion [GO:0007155]; cell migration involved in sprouting angiogenesis [GO:0002042]; negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903588]; negative regulation of cell migration [GO:0030336]; negative regulation of cell migration involved in sprouting ... | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; multimerin complex [GO:1990972] | null | PF00386;PF07546; | 2.60.120.40; | null | PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9H8L6}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9H8L6}. | null | null | null | null | null | FUNCTION: Inhibits endothelial cells motility and acts as a negative regulator of angiogenesis; it down-regulates KDR activation by binding VEGFA. {ECO:0000250}. | Mus musculus (Mouse) |
A6H730 | PPAP_BOVIN | MRNAALLMTRATSLRLSLLLLLSFLPDLDGGVRAKELRFVTLVFRHGDRSPIETFPNDPIKESSWPQGFGQLTQLGMAQHYELGQYIRKRYENFLNESYKREQVHVRSTDIDRTLMSAMTNLAALFPPEGISIWNPSLPWQPIPVHTVPVSEDQLLYLPFRNCPRFQELQSETLISEEFQKRLQPYKDFIEVLPKLTGYHDQDLLGIWSKVYDPLFCEGVHNFTLPSWATEDTMTKLKEISELSLLSLYGIHKQKEKSRLQGGVLINEILNHMKSATQPSNRRKLIMYSAHDTTVSGLQMALDVYNGILPPYASCHMMEL... | 3.1.3.2; 3.1.3.48 | null | adenosine metabolic process [GO:0046085]; dephosphorylation [GO:0016311]; lipid metabolic process [GO:0006629]; lysosome organization [GO:0007040]; positive regulation of adenosine receptor signaling pathway [GO:0060168]; regulation of sensory perception of pain [GO:0051930]; thiamine metabolic process [GO:0006772] | extracellular space [GO:0005615]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506] | 5'-nucleotidase activity [GO:0008253]; acid phosphatase activity [GO:0003993]; lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatase activity [GO:0016791]; protein tyrosine phosphatase activity [GO:0004725]; thiamine phosphate phosphatase activity [GO:0042131] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15309}. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000250|UniProtKB:P15309}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-... | null | null | null | null | FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (By similarity... | Bos taurus (Bovine) |
A6H737 | LOXL2_BOVIN | MERRGSSCLCRCLALLALLPTLSLAQYESWRHYPEYFQEPAPEYHRPEVPSDVAKIQLRLAGQKRKHSEGRVEVYYDGQWGTVCDDDFTIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNVYCTGSEATLAACSSNGWGVTDCKHTEDVGVVCSEKRIPGFKFDNSLINSIENMNIQVEDIRIRAILSAFRKRTPVTEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMFGFPGEKTYNTKVYKMFAARKKQRYWPYSMDCTGTEAHISSCKLGPQVSLDPVKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYK... | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0}; | collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell... | basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; oligosaccharide binding [GO:0070492]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}.; PTM: N-glycosylated. N-glycosylation on Asn-455 and Asn-644 may be essential for proper folding and secretion; may be... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is... | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:... | null | null | null | null | FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transc... | Bos taurus (Bovine) |
A6H772 | PP4C_BOVIN | MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; | double-strand break repair via homologous recombination [GO:0000724]; protein phosphorylation [GO:0006468]; regulation of double-strand break repair via homologous recombination [GO:0010569] | centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein phosphatase 4 complex [GO:0030289] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-4 (PP-X) subfamily | PTM: Methylation at the C-terminal Leu-307 is critical for interactions with regulatory subunits and functions in DNA repair. {ECO:0000250|UniProtKB:P60510}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-... | null | null | null | null | FUNCTION: Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint s... | Bos taurus (Bovine) |
A6H782 | TEKT3_BOVIN | MELLGSTLTATYAHPRPTPTNFLPAISTMASTYRDRFPHYNLTHSLSLPWRPSTYYKAASNWPTLDPYCTRSQRVSESTMLPFVSNRTTLFTRYTPDDWYRSNLTNFQESNTSRHNSERLRVDTSRLIQDKYQQTRKTQADSTQNLGERVNDIGFWKSEIIHELDAMIGETNELTDIKKRLERALMETEAPLQVARECLFHREKRMGIDLVHDEVEKELLTEVDTILCCQERMKLYLDKAIAQLAANRAAQHELEKDLSDKQSAYRIDDKCHHLRNTSDGVSYFHGVERVDATVSVPESWAKFTDDNILRSQSERAASAK... | null | null | cilium assembly [GO:0060271]; cilium movement involved in cell motility [GO:0060294]; flagellated sperm motility [GO:0030317]; regulation of brood size [GO:0060378] | acrosomal membrane [GO:0002080]; acrosomal vesicle [GO:0001669]; axonemal microtubule [GO:0005879]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; outer acrosomal membrane [GO:0002081]; sperm flagellum [GO:0036126] | null | PF03148; | null | Tektin family | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:26268136}.; PTM: May be proteolytically processed during the epididymal transit of spermatozoa. {ECO:0000269|PubMed:26268136}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:27883267}. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000269|PubMed:19478333, ECO:0000269|PubMed:26268136, ECO:0000269|PubMed:27883267}; Peripher... | null | null | null | null | null | FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (PubMed:34715025). Required for normal sperm mobility (By similarity). {ECO:0000250|UniProtKB:Q6X6Z7, ECO:00002... | Bos taurus (Bovine) |
A6H7G2 | DBNL_BOVIN | MAVNLSRNGPALLEAYQQVVNEKSSTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACANHVSTMAGFLKGAHVTINARAEEDVEPECIMQKVARASGANYTFHKESSRFQDTGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEERQQLEQERRERELREAALREQRYQEQGGEAGLQRKYEQHEVLSRNREEQPAHPREIFKQKERAMSTTSISSPQPGKLKSPFLQKQLTQPDTPISRESPHATSRPRADLREEPVPSIPPC... | null | null | adaptive immune response [GO:0002250]; endocytosis [GO:0006897]; neuron projection morphogenesis [GO:0048812]; podosome assembly [GO:0071800]; positive regulation of axon extension [GO:0045773]; positive regulation of dendritic spine morphogenesis [GO:0061003]; postsynaptic actin cytoskeleton organization [GO:0098974];... | actin filament [GO:0005884]; anchoring junction [GO:0070161]; clathrin-coated vesicle membrane [GO:0030665]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome [GO:0005769]; Golgi membrane [GO:0000139]; lamellipodium [GO:0030027]; perikaryon [GO:0043204]; podosome [GO:... | actin filament binding [GO:0051015] | PF00241;PF14604; | 3.40.20.10;2.30.30.40; | ABP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q62418}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q62418}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JHL4}. Synapse {ECO:0000... | null | null | null | null | null | FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not ... | Bos taurus (Bovine) |
A6H7I5 | DYN2_BOVIN | MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRTALAAERKFFLSHPAYRHIADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPD... | 3.6.5.5 | null | actin filament bundle organization [GO:0061572]; autophagy [GO:0006914]; centrosome cycle [GO:0007098]; membrane tubulation [GO:0097749]; neuron projection morphogenesis [GO:0048812]; phagocytosis [GO:0006909]; protein polymerization [GO:0051258]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO... | anchoring junction [GO:0070161]; cell junction [GO:0030054]; centriole [GO:0005814]; centrosome [GO:0005813]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; endosome [GO:0005768]; microtubule [GO:0005874]; midbody [GO:0030496]; neuron projection [GO:0043005]; phagocytic ... | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein self-association [GO:0043621] | PF01031;PF00350;PF02212;PF00169; | 1.20.120.1240;3.40.50.300;2.30.29.30; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | PTM: Phosphorylation at Ser-844 by GSK3-alpha relieves the inhibition of BIN1 and promotes endocytosis. Phosphorylation at Ser-760 by CDK1 is greatly increased upon mitotic entry (By similarity). It regulates cytokinesis downstream of calcineurin, and does not affect clathrin-mediated endocytosis (By similarity). Depho... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P50570}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P50570}. Cell projection, uropodium {ECO:0000250|UniProtKB:P50570}. Endosome {ECO:0000250|UniProtKB:P50570}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosom... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000250|UniProtKB:P50570}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission at plasma membrane during endocytosis and filament remodeling at many actin structures during organization of the actin cytoskeleton. Plays an important role in vesicular trafficking processes, namely clathrin-mediated endocy... | Bos taurus (Bovine) |
A6H7J1 | INSM1_BOVIN | MPRGFLVKRSKKSTPVSYRIRGGEDGDRALLLLPGCGGARASPPAPGPGPVPGPLQPPPPTERAHAALAAALACAPGPPPPPPGLRAAHFGNPEAAHPAPLYSPTRPVSREHEKHKYFERSFNLGSPVSAESFPTPAALLVGGGGGGGGGGANGAGGGGTCSGDPLLFAPAELKMGTAFSAAAEAARGPGPGPPLPPAAALRPPGKRPSPPASAAAAAEPPAKVAKAPGSKKPKAIRKLHFEDEVTTSPVLGLKIKEGPVEAPRGRAGGAARPLGEFICQLCKEEYADPFALAQHKCSRIVRVEYRCPECAKVFSCPANL... | null | null | adrenal chromaffin cell differentiation [GO:0061104]; cell cycle [GO:0007049]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; nora... | nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | chromatin DNA binding [GO:0031490]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | INSM1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q63ZV0}. | null | null | null | null | null | FUNCTION: Sequence-specific DNA-binding transcriptional regulator that plays a key role in neurogenesis and neuroendocrine cell differentiation during embryonic and/or fetal development. Binds to the consensus sequence 5'-[TG][TC][TC][TT][GA]GGG[CG]A-3' in target promoters. Acts as a transcriptional repressor of NEUROD... | Bos taurus (Bovine) |
A6H8H2 | DEN4C_MOUSE | MIEDKGPRVTDYFVVAGLTDTSTLLDQEINRTDTNSIGPKAPITDIAVIIKSAGETVPEGYTCVEATPSALQANLNYGSLKSPELFLCYRRGRDKPPLTDIGVLYEGKERLMPGCEVIQATPYGRCANVNNSSTTSQRIFITYRRAPPVRSQNSLAVTDICVIITSKGETPPHTFCKVDKNLNCGMWGSNVFLCYKKSVPASNAIAYKAGLIFRYPEEDYESFPLSPSVPLFCLPMGATIECWDPQIKYPLPVFSTFVLTGSSAEKVYGAAIQFYEPYSQERLTEKQLTQLGLLTLVEKRVVSKPINSNKCICLLSHWPF... | null | null | cellular response to insulin stimulus [GO:0032869]; protein localization to plasma membrane [GO:0072659]; protein transport [GO:0015031]; regulation of Rab protein signal transduction [GO:0032483] | cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; insulin-responsive compartment [GO:0032593]; plasma membrane [GO:0005886]; retromer complex [GO:0030904] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF03455;PF02141;PF03456; | 2.100.10.50;3.40.50.11500;1.25.40.10; | null | PTM: Phosphorylated in response to insulin. {ECO:0000269|PubMed:21454697}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21454697}. Cell membrane {ECO:0000269|PubMed:21454697}. Cytoplasm, cytosol {ECO:0000269|PubMed:21454697}. Note=Associates with SLC2A4/GLUT4 storage vesicles. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269|PubMed... | Mus musculus (Mouse) |
A6H8H5 | KCNB2_MOUSE | MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPEKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQENDEFGQPSDNRKLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTG... | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; protein localization to plasma membrane [GO:0072659] | dendrite [GO:0030425]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO:0032809]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251]; protein heterodimerization activity [GO:0046982]; transmembrane transporter binding [GO:0044325] | PF02214;PF00520;PF03521; | 1.10.287.70;1.20.120.350; | Potassium channel family, B (Shab) (TC 1.A.1.2) subfamily, Kv2.2/KCNB2 sub-subfamily | PTM: Phosphorylated (By similarity). Phosphorylation at Ser-608 of the FFAT motif activates interaction with MOSPD2, VAPA and VAPB (By similarity). {ECO:0000250|UniProtKB:Q63099, ECO:0000250|UniProtKB:Q92953}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q63099}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q63099}. Perikaryon {ECO:0000250|UniProtKB:Q63099}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63099}. Note=Localized uniformly throughout cell bodies and dendrites. Colocalizes with KCNB1 to hi... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents which are activated during membrane depolarization, i.e within a risetime of about 20 msec. After that, inactiva... | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradien... | Mus musculus (Mouse) |
A6H8Y1 | BDP1_HUMAN | MFRRARLSVKPNVRPGVGARGSTASNPQRGRESPRPPDPATDSASKPAEPTDVPTVDFGGAEPQEKAPRSSTEKTGGDNDVEESSRSSSTVSQRRKRISSTSSLVKSSVSVPSESHPLSTINQEAPQPTATSTKEKQPCSDRYRIYKAQKLREMLKEELRKEKKQWKNKYAINESQRPPDRSKMTMRDFIYYLPDNNPMTSSLEQEKKTEKPSTPVQTREQEGKSTPNAEDNEMEEETDDGPLLVPRVKVAEDGSIILDEESLTVEVLRTKGPCVVEENDPIFERGSTTTYSSFRKNYYSKPWSNKETDMFFLAISMVGT... | null | null | RNA polymerase III preinitiation complex assembly [GO:0070898] | nucleoplasm [GO:0005654]; transcription factor TFIIIB complex [GO:0000126] | TFIIIC-class transcription factor complex binding [GO:0001156] | PF15963; | null | null | PTM: Phosphorylated by CSNK2A1 during mitosis, resulting in its release from chromatin and suppression of polymerase III transcription. {ECO:0000269|PubMed:15469824}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11161782}. | null | null | null | null | null | FUNCTION: General activator of RNA polymerase III transcription. Requires for transcription from all three types of polymerase III promoters. Requires for transcription of genes with internal promoter elements and with promoter elements upstream of the initiation site. {ECO:0000269|PubMed:11040218}. | Homo sapiens (Human) |
A6H8Z2 | F221B_HUMAN | MEAHEIIEEPHITMDAEKHPPSKDPSAEDLQENHISESFLKPSTSETPLEPHTSESPLVPSPSQIPLEAHSPETHQEPSISETPSETPTYEASLDSPISVVPEKHLTLPPQSRDYVCLSSSDTLKEDLSSESSSNEVPWTRRSTHLSESESLPEHCLSGPSSQVQVDTTEKQEEEAGEVEKGVDASDSTAHTAQPGHQLGNTARPVFPARQTELVEVAKAMHREEFGAQVNNLFQWEKDAALNAIQTGLYIGWRCPHYLWDCFRIGDESRCFCGHLLREHRIISDISVPCKVSQCRCFMFCFIPSRPEEVGEFWLKRRAT... | null | null | null | null | null | PF14753; | null | FAM221 family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
A6HD62 | CHIP_RAT | MKGKEEKEGGARLGTGGGGSPDKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQPEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLTRLIAAERERELEECQRNHEGDEDDGHIRAQQACIEAKHDKYMADMNELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY | 2.3.2.27 | null | cellular response to misfolded protein [GO:0071218]; DNA repair [GO:0006281]; endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negativ... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear inclusion body [GO:0042405]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]; ubiquitin ligase complex [GO:0000151]; Z disc [GO:0030018] | enzyme binding [GO:0019899]; G protein-coupled receptor binding [GO:0001664]; heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; kinase binding [GO:0019900]; misfolded protein binding [GO:0051787]; protein homodimerization activity [GO:0042803]; protein-fold... | PF12895;PF18391;PF04564; | 6.10.140.2020;1.25.40.10;3.30.40.10; | null | PTM: Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2 and enhanced in the presence of MAP2K5 (By similarity). Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3 (By similarity). {ECO:0000250|UniProtKB:Q9UNE7, ECO:0000250|UniProtKB:Q9WUD1}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19237536, ECO:0000269|PubMed:19483080, ECO:0000269|PubMed:30980393}. Nucleus {ECO:0000269|PubMed:19237536, ECO:0000269|PubMed:30980393}. Mitochondrion {ECO:0000269|PubMed:29934347}. Note=Translocates to the nucleus in response to inflammatory signals in regulatory T-c... | 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:Q9WUD1}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9WUD1}. | null | null | FUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation (PubMed:26265139). Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to ce... | Rattus norvegicus (Rat) |
A6K136 | PPM1K_RAT | MLSTAFITLVRSGRNQVKKRVLLSSILLQDHRQMTPACYCSISEPRCSRFDPDGSGQPATWDNFGIWDNRIDEPILLPPSIKYGKPIPKISLENVGCASLIGKRKENEDRFGFAQLTEEVLYFAVYDGHGGPAAADFCHTHMEKCVTDLLPREKDLETVLTLAFLEIDKAFSSYAHLSADASLLTSGTTATVALLRDGVELVVASVGDSRALLCRKGKPMKLTTDHTPERKDEKERIKKCGGFVAWNSLGQPHVNGRLAMTRSIGDLDLKASGVIAEPETTRIKLYHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPK... | 3.1.3.16; 3.1.3.52 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8N3J5}; Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q8N3J5}; | branched-chain amino acid catabolic process [GO:0009083]; regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902108] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | manganese ion binding [GO:0030145]; protein serine/threonine phosphatase activity [GO:0004722] | PF00481; | 3.60.40.10; | PP2C family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N3J5, ECO:0000305|PubMed:29779826}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000269|PubMed:29779826}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] + phosphate; Xref=Rhea:RHEA:77247, Rhea:RHEA-COMP:13695, Rhea:RHEA-COMP:13696, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.52; Evidence=... | null | PATHWAY: Protein modification. {ECO:0000269|PubMed:29779826}. | null | null | FUNCTION: Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the ... | Rattus norvegicus (Rat) |
A6M931 | IF4A3_PIG | MAATATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIM... | 3.6.4.13 | null | embryonic cranial skeleton morphogenesis [GO:0048701]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of translation [GO:0006417]... | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; U2-type catalytic step 1 spliceosome [GO:0071006] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, eIF4A subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3B8Q2}. Nucleus speckle {ECO:0000250|UniProtKB:P38919}. Cytoplasm {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the ... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P38919}; | null | null | null | null | FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cyt... | Sus scrofa (Pig) |
A6M9B7 | GLCT_ECOLX | MKIAYVVSSKKKCGPNIVILNIVKELANKHEMEIFFLDESDDDVFECVNVKSTQIKKASDLKEHLKRFDIIHSSGIRPDALVVLCKVIYRVKCKIITTIHNYVFQDLYYSYGLVKSLIGGLLWCSIWLFFDKLVILSKNADNYYWFLPSAKKNIIYNGIDDNDCLQNKKCNYRKEFNIPDDGILAGSCANLTKRKGIDLVIQTLTKEHKIYYIVAGNGIEKHNLINLVKARKLHERVYFIDFLDEPESFMSQLDVFLMPSRSEGFGLTVLESTKLGIPVITSNIPIFMELFDQMCLTFDIKNPSTLIDVITYAKKNRLHL... | 2.4.1.- | null | glycolipid biosynthetic process [GO:0009247]; Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; lipopolysaccharide biosynthetic process [GO:0009103]; O antigen biosynthetic process [GO:0009243]; sulfolipid biosynthetic process [GO:0046506] | Gram-negative-bacterium-type cell wall [GO:0009276]; membrane [GO:0016020] | glucosyltransferase activity [GO:0046527]; glycogen (starch) synthase activity [GO:0004373]; UDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity [GO:0046510] | PF13439;PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.345 mM for Gal-beta1-3GalNAc-PP-PhU {ECO:0000269|PubMed:32421169}; Vmax=152 nmol/h/mg enzyme with Gal-beta1-3GalNAc-PP-PhU as substrate {ECO:0000269|PubMed:32421169}; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:21968437, ECO:0000269|PubMed:32421169}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. Retains 24% of maximal activity at pH 5 and 14% of activity at pH 9. {ECO:0000269|PubMed:32421169}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Retains 50% of the activity in elution buffer/20% glycerol for four days at 4 degrees Celsius. Retains 60% of the activity in several days storage at -20 degrees Celsius with 20% glycerol.; | FUNCTION: Involved in the assembly of the O-repeating unit during O-antigen biosynthesis. Glucosyltransferase accountable for the alpha-D-Glc-1,4-beta-D-Gal linkage within the O-antigen (PubMed:21968437, PubMed:32421169). Transfers alpha-1,4-Glc to the Gal moiety of a specific Gal-beta1-3GalNAc-alpha-OPO3-PO3-phenoxyun... | Escherichia coli |
A6MEY4 | PA2B_BUNFA | MNPAHLLVLLAVCVSLLGAANIPPQSLNLYQFKNMIQCAGTQLCVAYVKYGCYCGPGGTGTPLDQLDRCCQTHDHCYDNAKKFGNCIPYFKTYEYTCNKPDLTCTDAKGSCARNVCDCDRAAAICFAAAPYNLANFGINKETHCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits blood coagulation and shows bactericidal activities against both Gram-negative and -positive bacteria (E.coli, MIC=0.4 uM and S.aureus, MIC=0.1 uM). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|Pu... | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
A6MFK7 | FAXD1_DEMVE | MAPQLLLCLIQTFLWSLPEAESNVFLKSNVANRFLQRTKRANSGFEEIYPANFERECVEERCSKEEAREVFEDDEKTEAFWTVYVDGDQCLSNPCHYGGTCKDGIGSYTCTCLAGYEGKNCEHDLLKSCRVDNGNCWHFCKPVQNDTQCSCAEGYRLGDNGFSCIAEGEFSCGRNIKSRNKREASLPDFQTDFSDDYDAIDENNLIETVQSQSATLLKKSDNPNPDIRIVNGLDCKLGECPWQAVLIDEKGTAFGGGTILSPYFVLTAAHCINKTKSIAVVVGQVDISRKETRRLLSVDKVYTHPKYVHVTNDYDIAIIQ... | 3.4.21.6 | null | blood coagulation [GO:0007596]; envenomation resulting in positive regulation of blood coagulation in another organism [GO:0044469]; induction of blood coagulation in another organism [GO:0035807]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; peptidase activator activity [GO:0016504]; serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17608513}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6; | null | null | null | null | FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa (By similarity). {ECO:0000250}. | Demansia vestigiata (Lesser black whip snake) (Demansia atra) |
A6MFK8 | FAXD2_DEMVE | MAPQLLLCLILTFLWSLPEAESNVFLKSNVANRFLQRTKRANSIFEEIRPGNIERECVEEKCSKEEAREVFQDNEKTEAFWTVYVDGDQCLSNPCHYRGTCKDGIGSYTCTCLPGYEGKNCEHVVVKSCRLFNGNCWHFCKTVQNDTQCSCAEGYRLGVDGFSCIAEGDFSCGRIIKSRNKREASLPDFHFSDDYDAIDENNLVETVQSQSATLLKKSDNPSPDIRIVSGLDCKLGECPWQAVLIDEHGKAFGGGTILSPYFVLTAAHCLNQTKSIAVVVGQVDISRKETRHLLHVDKAYMHSKYVRATYDHDIAILRLR... | 3.4.21.6 | null | blood coagulation [GO:0007596]; envenomation resulting in positive regulation of blood coagulation in another organism [GO:0044469]; induction of blood coagulation in another organism [GO:0035807]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; peptidase activator activity [GO:0016504]; serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17608513}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6; | null | null | null | null | FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa (By similarity). {ECO:0000250}. | Demansia vestigiata (Lesser black whip snake) (Demansia atra) |
A6N3Q4 | CC14C_SYMSY | MKRKSEGRSSWAAATCSPCCSLTSPSVKKIRSPTQQDPRHRDPQDDVYLDITDRLRLAILYSRPKSASNVHYFSIDNELEYENFSEDFGPLNLAMVYRYCCKINKKLKSITMLRKKIVHFTGSDQRKQANAAFLVGCYMVIYLGRTPEEAYRTLIFGDTSYIPFRDAAYGSCNFYITLLDCFHAVKKAMQYGFLNFNSFNLDEYEHYEKAENGDLNWIIPDRFIAFCGPHSRARLESGYHQHSPETYIQYFKNRNVTTIIRLNKKMYDAKCFTDAGFDHHDLFFADGSSPTDAIVKGFLDICENAEGAIAVHCKAGLGRT... | 3.1.3.16; 3.1.3.48 | null | cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of cytokinesis [GO:0032467]; regulation of exit from mitosis [GO:0007096] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; spindle pole [GO:0000922] | myosin phosphatase activity [GO:0017018]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138] | PF00782;PF14671; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class CDC14 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus, nucleolus. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18547142}. Note=Nucleolar during interphase (By similarity). Microtubular association (PubMed:18547142). {ECO:0000250, ECO:0000269|PubMed:18547142}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVI... | null | null | null | null | FUNCTION: Dual-specificity phosphatase. Preferentially dephosphorylates proteins modified by proline-directed kinases (By similarity). {ECO:0000250}. | Symphalangus syndactylus (Siamang) (Hylobates syndactylus) |
A6N6J5 | WDR35_RAT | MFFYLSKKIAVPNNVKLKCISWNKDQGFIACGGEDGLLKVLRLETQTDDSKLRGLAAPSNLSMNQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVWMLYKGSWYEEMINNRNKSVVRSMSWNADGQKICIVYEDGAVIVGSVDGNRIWGKDLKGIQLCHVTWSADSKILLFGMANGEIHIYDNQGNFIMKMKLNCLVNVTGAISIAGIHWYHGTEGYVEPDCPCLAICFDNGRCQIMRHENDQNPVLIDTGMYVVGIQWNHIGSVLAVAGSQKVVTQDKDVNIVQFYTPFGEHLGTLKVPGKQMCSLSWEGGGLKIAL... | null | null | cellular response to glucose stimulus [GO:0071333]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to xenobiotic stimulus [GO:0071466]; cilium assembly [GO:0060271]; intraciliary retrograde transport [GO:0035721]; intraciliary tra... | axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; intraciliary transport particle A [GO:0030991]; non-motile cilium [GO:0097730] | null | PF12894;PF00400; | 1.25.40.470;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8BND3}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q8BND3}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8BND3}. | null | null | null | null | null | FUNCTION: As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking (By similarity). May promote CASP3 activation and TNF-stimulated apoptosis (PubMed:201936... | Rattus norvegicus (Rat) |
A6NC98 | CC88B_HUMAN | MEGGKGPRLRDFLSGSLATWALGLAGLVGEAEDSEGEEEEEEEEPPLWLEKRFLRLSDGALLLRVLGIIAPSSRGGPRMLRGLDGPAAWRVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSLMGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPSRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAE... | null | null | cytoplasmic microtubule organization [GO:0031122]; cytoskeleton-dependent intracellular transport [GO:0030705]; defense response to protozoan [GO:0042832]; positive regulation of cytokine production [GO:0001819]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell proliferation [GO:0042... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleoplasm [GO:0005654] | dynein light intermediate chain binding [GO:0051959]; microtubule binding [GO:0008017] | PF19047; | 1.10.418.10; | CCDC88 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q4QRL3}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:25762780}. Endoplasmic reticulum {ECO:0000269|PubMed:21289099}. Golgi apparatus {ECO:0000269|PubMed:21289099}. Cytoplasm {ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: Acts as a positive regulator of T-cell maturation and inflammatory function. Required for several functions of T-cells, in both the CD4(+) and the CD8(+) compartments and this includes expression of cell surface markers of activation, proliferation, and cytokine production in response to specific or non-speci... | Homo sapiens (Human) |
A6NCS4 | NKX26_HUMAN | MLLSPVTSTPFSVKDILRLERERSCPAASPHPRVRKSPENFQYLRMDAEPRGSEVHNAGGGGGDRKLDGSEPPGGPCEAVLEMDAERMGEPQPGLNAASPLGGGTRVPERGVGNSGDSVRGGRSEQPKARQRRKPRVLFSQAQVLALERRFKQQRYLSAPEREHLASALQLTSTQVKIWFQNRRYKCKRQRQDKSLELAGHPLTPRRVAVPVLVRDGKPCLGPGPGAPAFPSPYSAAVSPYSCYGGYSGAPYGAGYGTCYAGAPSGPAPHTPLASAGFGHGGQNATPQGHLAATLQGVRAW | null | null | atrial cardiac muscle cell development [GO:0055014]; cell differentiation [GO:0030154]; digestive tract development [GO:0048565]; embryonic heart tube development [GO:0035050]; epithelial cell apoptotic process [GO:1904019]; epithelial cell differentiation [GO:0030855]; epithelial cell proliferation [GO:0050673]; hypot... | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | NK-2 homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator (PubMed:15649947). In conjunction with NKX2-5, may play a role in both pharyngeal and cardiac embryonic development. {ECO:0000250|UniProtKB:P43688, ECO:0000269|PubMed:15649947}. | Homo sapiens (Human) |
A6ND01 | JUNO_HUMAN | MACWWPLLLELWTVMPTWAGDELLNICMNAKHHKRVPSPEDKLYEECIPWKDNACCTLTTSWEAHLDVSPLYNFSLFHCGLLMPGCRKHFIQAICFYECSPNLGPWIQPVGSLGWEVAPSGQGERVVNVPLCQEDCEEWWEDCRMSYTCKSNWRGGWDWSQGKNRCPKGAQCLPFSHYFPTPADLCEKTWSNSFKASPERRNSGRCLQKWFEPAQGNPNVAVARLFASSAPSWELSYTIMVCSLFLPFLS | null | null | cell adhesion [GO:0007155]; fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; single fertilization [GO:0007338]; sperm-egg recognition [GO:0035036] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886] | signaling receptor activity [GO:0038023]; signaling receptor binding [GO:0005102] | PF03024; | null | Folate receptor family | PTM: The protein is rapidly cleaved following fertilization, being only weakly detectable in zona-intact fertilized eggs at telophase II and undetectable at the pronuclear stage. Sheding is probably required to block to polyspermy and ensuring egg fusion with a single sperm. {ECO:0000250|UniProtKB:Q9EQF4}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9EQF4}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9EQF4}. Cell projection, microvillus membrane {ECO:0000269|PubMed:36070373}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9EQF4}. Note=GPI-anchored at the oolemma microvilli. {ECO:0000250|UniProtKB:Q... | null | null | null | null | null | FUNCTION: Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. ... | Homo sapiens (Human) |
A6ND36 | FA83G_HUMAN | MAFSQVQCLDDNHVNWRSSESKPEFFYSEEQRLALEALVARGRDAFYEVLKRENIRDFLSELELKRILETIEVYDPGSEDPRGTGPSQGPEDNGVGDGEEASGADGVPIEAEPLPSLEYWPQKSDRSIPQLDLGWPDTIAYRGVTRASVYMQPPIDGQAHIKEVVRKMISQAQKVIAVVMDMFTDVDIFKDLLDAGFKRKVAVYIIVDESNVKYFLHMCERACMHLGHLKNLRVRSSGGTEFFTRSATKFKGALAQKFMFVDGDRAVCGSYSFTWSAARTDRNVISVLSGQVVEMFDRQFQELYLMSHSVSLKGIPMEKE... | null | null | BMP signaling pathway [GO:0030509]; epidermal growth factor receptor signaling pathway [GO:0007173]; intermediate filament cytoskeleton organization [GO:0045104]; positive regulation of cell cycle G1/S phase transition [GO:1902808]; positive regulation of cell migration [GO:0030335]; protein localization to mitotic spi... | cytosol [GO:0005829]; keratin filament [GO:0045095]; membrane [GO:0016020]; mitotic spindle pole [GO:0097431]; nucleus [GO:0005634] | keratin filament binding [GO:1990254]; protein kinase binding [GO:0019901] | PF07894; | 3.30.870.10; | FAM83 family | PTM: BMP signaling induces the phosphorylation by BMPR1A at Ser-610, Ser-614 and Ser-616. Phosphorylation at Ser-610 is necessary for the activation of SMAD4-independent BMP target genes such as NEDD9 and ASNS. {ECO:0000269|PubMed:24554596}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24554596}. Nucleus {ECO:0000269|PubMed:24554596}. Note=Detected predominantly in the cytosol. Upon BMP stimulation, a small portion localizes the nucleus. {ECO:0000269|PubMed:24554596}. | null | null | null | null | null | FUNCTION: Substrate for type I BMP receptor kinase involved in regulation of some target genes of the BMP signaling pathway. Also regulates the expression of several non-BMP target genes, suggesting a role in other signaling pathways. {ECO:0000269|PubMed:24554596}. | Homo sapiens (Human) |
A6NDB9 | PALM3_HUMAN | MAESSLYRQRLEVIAEKRRLQEEIRAARREVEEEKLRVERLKRKSLRERWLMDGAAAVPEPSEDPTSKDPQSPEGQAQARIRNLEDSLFTLQSQLQLLQSASTGAQHKPSGRPSWRRQGHRPLSQSIVEAGSVGQTDLNKRASLPAGLVGTPPESPSEPREDVLGFLPGPRQVPGAAGDSSEANGPCPSPIPTPEQGLSQRAVPSEGRVGEAKGGGVVSVVWEGLRATEDCATGATGPELEAKVEEVVLEAIGDRKGAGSLELPAWVKEDRGIVEVVWEGVGGSDAEAMGEIGRVPEVVQTSSPRLQERLEAAASIEGED... | null | null | negative regulation of cytokine-mediated signaling pathway [GO:0001960]; regulation of cell shape [GO:0008360]; response to lipopolysaccharide [GO:0032496]; Toll signaling pathway [GO:0008063] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524] | PF03285; | null | Paralemmin family | PTM: Palmitoylated on Cys-667 and Cys-669 and prenylated on Cys-670; which is required for membrane association. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. | null | null | null | null | null | FUNCTION: ATP-binding protein, which may act as a adapter in the Toll-like receptor (TLR) signaling. {ECO:0000269|PubMed:21187075}. | Homo sapiens (Human) |
A6NDE4 | RBY1B_HUMAN | MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSQEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHS... | null | null | male gonad development [GO:0008584]; mRNA processing [GO:0006397]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; RNA splicing [GO:0008380]; spermatogenesis [GO:0007283] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681] | RNA binding [GO:0003723] | PF08081;PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis. | Homo sapiens (Human) |
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