Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P04394 | NDUV2_BOVIN | MFLSAALRARAAGLAAHWGKHIRNLHKTAVQNGAGGALFVHRDTPENNPETPFDFTPENYKRIEAIVKNYPEGHKAAAVLPVLDLAQRQNGWLPISAMNKVAEILQVPPMRVYEVATFYTMYNRKPVGKYHIQVCTTTPCMLRNSDSILEAIQKKLGIKVGETTPDKLFTLIEVECLGACVNAPMVQINDNYYEDLTPKDIEEIIDELKAGKIPKPGPRSGRFSCEPAGGLTSLTEPPKGPGFGVQAGL | 7.1.1.2 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:27509854}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:27509854}; | mitochondrial electron transport, NADH to ubiquinone [GO:0006120] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF01257; | 3.40.30.10;1.10.10.1590; | Complex I 24 kDa subunit family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Peripheral membrane protein {ECO:0000305|PubMed:25209663}; Matrix side {ECO:0000305|PubMed:25209663}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000305|PubMed:10852722, ECO:000030... | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:10852722, PubMed:18721790, PubMed:25209663, PubMed:27509854). Parts of the peripheral arm of t... | Bos taurus (Bovine) |
P04395 | 3MG2_ECOLI | MYTLNWQPPYDWSWMLGFLAARAVSSVETVADSYYARSLAVGEYRGVVTAIPDIARHTLHINLSAGLEPVAAECLAKMSRLFDLQCNPQIVNGALGRLGAARPGLRLPGCVDAFEQGVRAILGQLVSVAMAAKLTARVAQLYGERLDDFPEYICFPTPQRLAAADPQALKALGMPLKRAEALIHLANAALEGTLPMTIPGDVEQAMKTLQTFPGIGRWTANYFALRGWQAKDVFLPDDYLIKQRFPGMTPAQIRRYAERWKPWRSYALLHIWYTEGWQPDEA | 3.2.2.21 | null | base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; DNA damage response [GO:0006974]; DNA dealkylation involved in DNA repair [GO:0006307]; DNA repair [GO:0006281] | cytoplasm [GO:0005737]; protein-DNA complex [GO:0032993] | alkylated DNA binding [GO:0032131]; alkylbase DNA N-glycosylase activity [GO:0003905]; DNA-3-methyladenine glycosylase activity [GO:0008725]; DNA-3-methylguanine glycosylase activity [GO:0052822]; DNA-7-methyladenine glycosylase activity [GO:0052821]; DNA-7-methylguanine glycosylase activity [GO:0043916] | PF06029;PF00730; | 3.30.310.20;1.10.1670.10; | Alkylbase DNA glycosidase AlkA family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21; | null | null | null | null | FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions. | Escherichia coli (strain K12) |
P04397 | GAL10_YEAST | MTAQLQSESTSKIVLVTGGAGYIGSHTVVELIENGYDCVVADNLSNSTYDSVARLEVLTKHHIPFYEVDLCDRKGLEKVFKEYKIDSVIHFAGLKAVGESTQIPLRYYHNNILGTVVLLELMQQYNVSKFVFSSSATVYGDATRFPNMIPIPEECPLGPTNPYGHTKYAIENILNDLYNSDKKSWKFAILRYFNPIGAHPSGLIGEDPLGIPNNLLPYMAQVAVGRREKLYIFGDDYDSRDGTPIRDYIHVVDLAKGHIAALQYLEAYNENEGLCREWNLGSGKGSTVFEVYHAFCKASGIDLPYKVTGRRAGDVLNLTA... | 5.1.3.2; 5.1.3.3 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; | galactose catabolic process via UDP-galactose [GO:0033499] | cytosol [GO:0005829] | aldose 1-epimerase activity [GO:0004034]; carbohydrate binding [GO:0030246]; UDP-glucose 4-epimerase activity [GO:0003978] | PF01263;PF01370; | 2.70.98.10;3.40.50.720;3.90.25.10; | NAD(P)-dependent epimerase/dehydratase family; Aldose epimerase family | null | null | CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose; Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=5.1.3.2; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264, ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3; Evidence={ECO:0000255|PROSITE-ProRule:P... | null | PATHWAY: Carbohydrate metabolism; galactose metabolism.; PATHWAY: Carbohydrate metabolism; hexose metabolism. | null | null | FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity). {ECO:0000250}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04401 | IL5_MOUSE | MRRMLLHLSVLTLSCVWATAMEIPMSTVVKETLTQLSAHRALLTSNETMRLPVPTHKNHQLCIGEIFQGLDILKNQTVRGGTVEMLFQNLSLIKKYIDRQKEKCGEERRRTRQFLDYLQEFLGVMSTEWAMEG | null | null | cytokine-mediated signaling pathway [GO:0019221]; immune response [GO:0006955]; interleukin-5-mediated signaling pathway [GO:0038043]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-binding transcription factor acti... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-5 receptor binding [GO:0005137] | PF02025; | 1.20.1250.10; | IL-5 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Homodimeric cytokine expressed predominantly by T-lymphocytes and NK cells that plays an important role in the survival, differentiation, and chemotaxis of eosinophils (PubMed:10444455, PubMed:1873482). Acts also on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation... | Mus musculus (Mouse) |
P04404 | CMGA_PIG | SAAALALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERSHQQKKQSSYEDELSEVLEKQNDQAELKEGTEEASSKEAAEKRGDSKEVEKNDEDADGAKPQASLEPPXXXEAEDQTPGEEEAASTHPLASLPSKKRPGAQAEEDHEGPSQGPVDREKGPSAEQGPQAEREEEEEAEAGEKAVPEEEGPRSEAFDSHPSLGYKEMQRGWPQAPAMDGAGKTGAEEAQPPEGKGAREHSRQEEEEETAGAPQGLFRGGKRGEPAQEEEERLSE... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation [GO:0086030]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; mast cell activation [GO:0045576]; mast c... | chromaffin granule [GO:0042583]; extracellular space [GO:0005615]; neuronal dense core vesicle [GO:0098992]; transport vesicle [GO:0030133] | null | PF01271; | null | Chromogranin/secretogranin protein family | PTM: O-glycosylated; contains chondroitin sulfate (CS). CS attachment is pH-dependent, being observed at mildly acidic conditions of pH 5 but not at neutral pH, and promotes self-assembly in vitro. {ECO:0000250|UniProtKB:P10645}.; PTM: Parathyroid CHGA is sulfated on tyrosine residues, whereas adrenal CHGA seems to be ... | SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000250|UniProtKB:P26339}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniP... | null | null | null | null | null | FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: [Parastatin]: Inhibits low calcium-stimulated parathyroid cell secretion.; FUNCTION: [Catestatin]: Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nico... | Sus scrofa (Pig) |
P04405 | GLYG2_SOYBN | MAKLVLSLCFLLFSGCFALREQAQQNECQIQKLNALKPDNRIESEGGFIETWNPNNKPFQCAGVALSRCTLNRNALRRPSYTNGPQEIYIQQGNGIFGMIFPGCPSTYQEPQESQQRGRSQRPQDRHQKVHRFREGDLIAVPTGVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQQQQGGSQSQKGKQQEEENEGSNILSGFAPEFLKEAFGVNMQIVRNLQGENEEEDSGAIVTVKGGLRVTAPAMRKPQQEEDDDDEEEQPQCVETDKGCQRQSKRSRNGIDETICTMRLRQNIGQNSS... | null | null | null | endoplasmic reticulum [GO:0005783]; protein storage vacuole [GO:0000326] | nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 11S seed storage protein (globulins) family | PTM: During soybean germination, seed storage proteins are hydrolyzed by protease/26S proteasome. {ECO:0000269|PubMed:29037738}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P04776}. Protein storage vacuole {ECO:0000250|UniProtKB:P04776}. Note=Hexamers are assembled in the endoplasmic reticulum and later sorted to the protein storage vacuoles. {ECO:0000250|UniProtKB:P04776}. | null | null | null | null | null | FUNCTION: Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating... | Glycine max (Soybean) (Glycine hispida) |
P04406 | G3P_HUMAN | MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY... | 1.2.1.12; 2.6.99.- | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to type II interferon [GO:0071346]; defense response to fungus [GO:0050832]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; killing by host of symbiont cells [GO:0051873]; killing of cells o... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; GAIT complex [GO:0097452]; intracellular membrane-bounded organelle [GO:0043231]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear r... | aspartic-type endopeptidase inhibitor activity [GO:0019828]; disordered domain specific binding [GO:0097718]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050... | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | PTM: S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus (By similarity). S-nitrosylation of Cys-247 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to inter... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12829261}. Nucleus {ECO:0000250|UniProtKB:P04797}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12829261}. Membrane {ECO:0000269|PubMed:12829261}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitros... | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PR... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by conve... | Homo sapiens (Human) |
P04409 | KPCA_BOVIN | MADVFPAAEPAAPQDVANRFARKGALRQKNVHEVKNHRFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVTDEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPRWDESFTFKLKPSDKDRRLSEEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNVELRQKFEKAKLGPAGNKVISP... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P05696}; | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; intracellular signal transduction [GO:0035556]; negative regulation of glial cell apoptotic process [GO:0034351]; positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106071]; positive... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; photoreceptor disc membrane [GO:0097381]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; PDZ domain binding [GO:0030165]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; scaffold protein binding [GO:0097110]; zinc ion binding [GO:0008270] | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly... | Bos taurus (Bovine) |
P04412 | EGFR_DROME | MLLRRRNGPCPFPLLLLLLAHCICIWPASAARDRYARQNNRQRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKICIGTKSRLSVPSNKEHHYRNLRDRYTNCTYVDGNLKLTWLPNENLDLSFLDNIREVTGYILISHVDVKKVVFPKLQIIRGRTLFSLSVEEEKYALFVTYSKMYTLEIPDLRDVLNGQVGFHNNYNLCHMRTIQWSEIVSNGTDAYYNYDFTAPERECPKCHESCTHGCWGEGPKNCQKFSKLTCSPQCAGGRCYGPKPRECCHLFCAGGCTGPTQKDCI... | 2.7.10.1 | null | behavioral response to ethanol [GO:0048149]; border follicle cell migration [GO:0007298]; cell projection assembly [GO:0030031]; chorion-containing eggshell pattern formation [GO:0030381]; compound eye cone cell differentiation [GO:0042675]; compound eye development [GO:0048749]; compound eye photoreceptor cell differe... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; epidermal growth factor receptor activity [GO:0005006]; identical protein binding [GO:0042802]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00757;PF14843;PF07714;PF01030; | 3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily | PTM: Ubiquitination by Cbl in response to high spi, promotes its interaction with Graf and thus facilitates its GPI-enriched endocytic compartment (GEEC) mediated endocytosis and its subsequent degradation. {ECO:0000269|PubMed:28993397}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase, binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:22140578, PubMed:23579691, PubMed:8070664, PubMed:9882502). Known ligands include spitz, gurken, vein and giant-lens (PubMed:19718021,... | Drosophila melanogaster (Fruit fly) |
P04413 | US03_HHV11 | MACRKFCRVYGGQGRRKEEAVPPETKPSRVFPHGPFYTPAEDACLDSPPPETPKPSHTTPPSEAERLCHLQEILAQMYGNQDYPIEDDPSADAADDVDEDAPDDVAYPEEYAEELFLPGDATGPLIGANDHIPPPCGASPPGIRRRSRDEIGATGFTAEELDAMDREAARAISRGGKPPSTMAKLVTGMGFTIHGALTPGSEGCVFDSSHPDYPQRVIVKAGWYTSTSHEARLLRRLDHPAILPLLDLHVVSGVTCLVLPKYQADLYTYLSRRLNPLGRPQIAAVSRQLLSAVDYIHRQGIIHRDIKTENIFINTPEDIC... | 2.7.11.1 | null | modulation by virus of host chromatin organization [GO:0039525]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of protein localization to nucleus [GO:1900181]; phosphorylation [GO:0016310]; symbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | ATP binding [GO:0005524]; protein sequestering activity [GO:0140311]; 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: Phosphorylated by UL13; this phosphorylation regulates subsequent phosphorylation of UL31 and UL34 by US3. Autophosphorylated. {ECO:0000269|PubMed:16415024}. | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:24807716}. Host nucleus {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:24049179, ECO:000026... | null | null | null | null | FUNCTION: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and inhibition of host immune response (PubMed:25907557, PubMed:31249678, PubMed:34935440). Phosphorylates UL31 and UL34, two critical regul... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P04415 | DPOL_BPT4 | MKEFYISIETVGNNIVERYIDENGKERTREVEYLPTMFRHCKEESKYKDIYGKNCAPQKFPSMKDARDWMKRMEDIGLEALGMNDFKLAYISDTYGSEIVYDRKFVRVANCDIEVTGDKFPDPMKAEYEIDAITHYDSIDDRFYVFDLLNSMYGSVSKWDAKLAAKLDCEGGDEVPQEILDRVIYMPFDNERDMLMEYINLWEQKRPAIFTGWNIEGFDVPYIMNRVKMILGERSMKRFSPIGRVKSKLIQNMYGSKEIYSIDGVSILDYLDLYKKFAFTNLPSFSLESVAQHETKKGKLPYDGPINKLRETNHQRYISY... | 2.7.7.7; 3.1.11.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:9665720}; | base-excision repair, gap-filling [GO:0006287]; bidirectional double-stranded viral DNA replication [GO:0039686]; DNA replication proofreading [GO:0045004]; nucleotide-excision repair, DNA gap filling [GO:0006297]; SOS response [GO:0009432] | null | 3'-5' exonuclease activity [GO:0008408]; 3'-5'-DNA exonuclease activity [GO:0008296]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00136;PF03104; | 1.20.1280.300;3.30.342.10;3.40.1820.10;1.10.287.690;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:1332748}; | null | null | null | null | FUNCTION: Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose. {ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:1332748, ECO:0000269|PubMe... | Enterobacteria phage T4 (Bacteriophage T4) |
P04418 | END5_BPT4 | MTRINLTLVSELADQHLMAEYRELPRVFGAVRKHVANGKRVRDFKISPTFILGAGHVTFFYDKLEFLRKRQIELIAECLKRGFNIKDTTVQDISDIPQEFRGDYIPHEASIAISQARLDEKIAQRPTWYKYYGKAIYA | 3.2.2.17; 4.2.99.18 | null | DNA repair [GO:0006281] | null | class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; deoxyribodipyrimidine endonucleosidase activity [GO:0033959]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; endonuclease activity [GO:0004519]; pyrimidine dimer DNA N-glycosylase activity [GO:0000704] | PF03013; | 1.10.440.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.; EC=3.2.2.17; Evidence={ECO:0000269|PubMed:6254991, ECO:0000269|PubMed:8347626}; CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribos... | null | null | null | null | FUNCTION: Participates in the repair of UV-damaged DNA by excising pyrimidine dimers that are the major UV-lesions (PubMed:6254991). DNA glycosylase activity hydrolyzes the glycosylic bond of the 5' pyrimidine of the dimer (PubMed:6254991). This leaves apurinic/apyrimidic (AP) sites in the DNA. These AP sites are remov... | Enterobacteria phage T4 (Bacteriophage T4) |
P04421 | LYSC_BOVIN | MKALVILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCRELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL | 3.2.1.17 | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; digestion [GO:0007586]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | null | lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; | null | null | null | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. | Bos taurus (Bovine) |
P04424 | ARLY_HUMAN | MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPST... | 4.3.2.1 | null | ammonia assimilation cycle [GO:0019676]; arginine biosynthetic process [GO:0006526]; arginine biosynthetic process via ornithine [GO:0042450]; arginine metabolic process [GO:0006525]; locomotory behavior [GO:0007626]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; post-embryonic development [GO:... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062] | argininosuccinate lyase activity [GO:0004056]; identical protein binding [GO:0042802] | PF14698;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Lyase 1 family, Argininosuccinate lyase subfamily | PTM: Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TSA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition... | null | CATALYTIC ACTIVITY: Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine; Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682, ChEBI:CHEBI:57472; EC=4.3.2.1; Evidence={ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433, ECO:0000269|PubMed:2263616, ECO:0000269|PubMed:9045711}; PhysiologicalDire... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 mM for 2-(N(omega)-L-arginino)succinate {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433}; Vmax=10.36 umol/min/mg enzyme toward 2-(N(omega)-L-arginino)succinate {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433}; | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000305|PubMed:11747433}.; PATHWAY: Nitrogen metabolism; urea cycle; L-arginine and fumarate from (N(omega)-L-arginino)succinate: step 1/1. {ECO:0000305|PubMed:11747433}. | null | null | FUNCTION: Catalyzes the reversible cleavage of L-argininosuccinate to fumarate and L-arginine, an intermediate step reaction in the urea cycle mostly providing for hepatic nitrogen detoxification into excretable urea as well as de novo L-arginine synthesis in nonhepatic tissues (PubMed:11747432, PubMed:11747433, PubMed... | Homo sapiens (Human) |
P04425 | GSHB_ECOLI | MIKLGIVMDPIANINIKKDSSFAMLLEAQRRGYELHYMEMGDLYLINGEARAHTRTLNVKQNYEEWFSFVGEQDLPLADLDVILMRKDPPFDTEFIYATYILERAEEKGTLIVNKPQSLRDCNEKLFTAWFSDLTPETLVTRNKAQLKAFWEKHSDIILKPLDGMGGASIFRVKEGDPNLGVIAETLTEHGTRYCMAQNYLPAIKDGDKRVLVVDGEPVPYCLARIPQGGETRGNLAAGGRGEPRPLTESDWKIARQIGPTLKEKGLIFVGLDIIGDRLTEINVTSPTCIREIEAEFPVSITGMLMDAIEARLQQQ | 6.3.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; | glutathione biosynthetic process [GO:0006750]; protein homotetramerization [GO:0051289] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; glutathione synthase activity [GO:0004363]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287] | PF02955;PF02951; | 3.40.50.20;3.30.1490.20;3.30.470.20; | Prokaryotic GSH synthase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.3; | null | PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. | null | null | null | Escherichia coli (strain K12) |
P04426 | WNT1_MOUSE | MGLWALLPSWVSTTLLLALTALPAALAANSSGRWWGIVNIASSTNLLTDSKSLQLVLEPSLQLLSRKQRRLIRQNPGILHSVSGGLQSAVRECKWQFRNRRWNCPTAPGPHLFGKIVNRGCRETAFIFAITSAGVTHSVARSCSEGSIESCTCDYRRRGPGGPDWHWGGCSDNIDFGRLFGREFVDSGEKGRDLRFLMNLHNNEAGRTTVFSEMRQECKCHGMSGSCTVRTCWMRLPTLRAVGDVLRDRFDGASRVLYGNRGSNRASRAELLRLEPEDPAHKPPSPHDLVYFEKSPNFCTYSGRLGTAGTAGRACNSSSP... | null | null | animal organ morphogenesis [GO:0009887]; animal organ regeneration [GO:0031100]; astrocyte-dopaminergic neuron signaling [GO:0036520]; BMP signaling pathway [GO:0030509]; bone development [GO:0060348]; branching involved in ureteric bud morphogenesis [GO:0001658]; canonical Wnt signaling pathway [GO:0060070]; cell fate... | cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Wnt signalosome [GO:1990909] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; protein domain specific binding [GO:0019904]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Palmitoleoylation is necessary for proper trafficking to cell surface (By similarity). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway (By similarity). {ECO:0000250|UniProtKB:P56704, ECO:0000250|UniProtKB:Q91029}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P04628}. Secreted {ECO:0000250|UniProtKB:P04628}. | null | null | null | null | null | FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Acts in the canonical Wnt signaling pathway by promoting beta-catenin-dependent transcriptional activation (By similarity). In some developmental processes, is also a ligand for the coreceptor RYK, thus triggering Wnt signaling (PubMe... | Mus musculus (Mouse) |
P04439 | HLAA_HUMAN | MAVMAPRTLLLLLSGALALTQTWAGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHEAEQLRAYLDGTCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWELSSQPTIPIVGIIAGLVLLGA... | null | null | antibacterial humoral response [GO:0019731]; antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous pep... | cell surface [GO:0009986]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:00... | beta-2-microglobulin binding [GO:0030881]; CD8 receptor binding [GO:0042610]; peptide antigen binding [GO:0042605]; RNA binding [GO:0003723]; signaling receptor binding [GO:0005102]; T cell receptor binding [GO:0042608]; TAP binding [GO:0046977]; TAP complex binding [GO:0062061] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | PTM: (Microbial infection) Polyubiquitinated in a post ER compartment by interaction with human herpesvirus 8 MIR1 protein. This targets the protein for rapid degradation via the ubiquitin system. {ECO:0000269|PubMed:12006494}.; PTM: N-linked glycosylation at Asn-110. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:21... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21263072, ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:8805302}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:8805302}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted CD8-positive T cells, guiding antigen-sp... | Homo sapiens (Human) |
P04440 | DPB1_HUMAN | MMVLQVSAAPRTVALTALLMVLLTSVVQGRATPENYLFQGRQECYAFNGTQRFLERYIYNREEFARFDSDVGEFRAVTELGRPAAEYWNSQKDILEEKRAVPDRMCRHNYELGGPMTLQRRVQPRVNVSPSKKGPLQHHNLLVCHVTDFYPGSIQVRWFLNGQEETAGVVSTNLIRNGDWTFQILVMLEMTPQQGDVYTCQVEHTSLDSPVTVEWKAQSDSARSKTLTGAGGFVLGLIICGVGIFMHRRSKKVQRGSA | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]; posi... | cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membr... | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I... | null | null | null | null | null | FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mos... | Homo sapiens (Human) |
P04441 | HG2A_MOUSE | MDDQRDLISNHEQLPILGNRPREPERCSRGALYTGVSVLVALLLAGQATTAYFLYQQQGRLDKLTITSQNLQLESLRMKLPKSAKPVSQMRMATPLLMRPMSMDNMLLGPVKNVTKYGNMTQDHVMHLLTRSGPLEYPQLKGTFPENLKHLKNSMDGVNWKIFESWMKQWLLFEMSKNSLEEKKPTEAPPKVLTKCQEEVSHIPAVYPGAFRPKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKSRGRHNCSEPLDMEDLSSGLGVTRQELGQVTL | null | null | antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; chaperone cofactor-dependent protein refolding [GO:0051085]; defense response [GO:0006952]; immunoglobulin mediated immune response [GO:0016064]; intracellular protein transp... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0... | amyloid-beta binding [GO:0001540]; CD4 receptor binding [GO:0042609]; cytokine receptor activity [GO:0004896]; macrophage migration inhibitory factor binding [GO:0035718]; MHC class II protein binding [GO:0042289]; MHC class II protein binding, via antigen binding groove [GO:0042658]; nitric-oxide synthase binding [GO:... | PF09307;PF08831;PF00086; | 1.10.870.10;4.10.800.10; | null | null | SUBCELLULAR LOCATION: [Isoform Long]: Late endosome {ECO:0000269|PubMed:11483509}. Lysosome {ECO:0000269|PubMed:11483509}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04233}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P04233}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0423... | null | null | null | null | null | FUNCTION: Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to compartments where peptide loading of class II takes place. Enhance also the st... | Mus musculus (Mouse) |
P04443 | HBB0_MOUSE | MVHFTAEEKAAITSIWDKVDLEKVGGETLGRLLIVYPWTQRFFDKFGNLSSAQAIMGNPRIKAHGKKVLTSLGLAVKNMDNLKETFAHLSELHCDKLHADPENFKLLGNMLVIVLSSYFGKEFTAEAQAAWQKLVVGVATALSHKYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: This is a minor early embryonic beta chain. | Mus musculus (Mouse) |
P04444 | HBBZ_MOUSE | MVHFTAEEKAAITSIWDKVDLEKVGGETLGRLLIVYPWTQRFFDKFGNLSSALAIMGNPRIRAHGKKVLTSLGLGVKNMDNLKETFAHLSELHCDKLHVDPENFKLLGNMLVIVLSTHFAKEFTPEVQAAWQKLVIGVANALSHKYH | null | null | carbon dioxide transport [GO:0015670]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oxygen transport [GO:0015671] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]; protein-containing complex binding [GO:0044877] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: This is an embryonic beta-type chain. | Mus musculus (Mouse) |
P04456 | RL25_YEAST | MAPSAKATAAKKAVVKGTNGKKALKVRTSATFRLPKTLKLARAPKYASKAVPHYNRLDSYKVIEQPITSETAMKKVEDGNILVFQVSMKANKYQIKKAVKELYEVDVLKVNTLVRPNGTKKAYVRLTADYDALDIANRIGYI | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; preribosome, large subunit precursor [GO:0030687] | RNA binding [GO:0003723]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00276;PF03939; | 3.30.70.330; | Universal ribosomal protein uL23 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04485 | ICP22_HHV11 | MADISPGAFAPCVKARRPALRSPPLGTRKRKRPSRPLSSESEVESDTALESEVESETASDSTESGDQDEAPRIGGRRAPRRLGGRFFLDMSAESTTGTETDASVSDDPDDTSDWSYDDIPPRPKRARVNLRLTSSPDRRDGVIFPKMGRVRSTRETQPRAPTPSAPSPNAMLRRSVRQAQRRSSARWTPDLGYMRQCINQLFRVLRVARDPHGSANRLRHLIRDCYLMGYCRARLAPRTWCRLLQVSGGTWGMHLRNTIREVEARFDATAEPVCKLPCLETRRYGPECDLSNLEIHLSATSDDEISDATDLEAAGSDHTL... | null | null | symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523] | host cell nucleus [GO:0042025] | null | PF02479; | null | Herpesviridae ICP22 family | PTM: Phosphorylated by serine/threonine-protein kinase UL13 (PubMed:1323829, PubMed:8393574). Tyrosine phosphorylated. {ECO:0000269|PubMed:12504549, ECO:0000269|PubMed:1323829, ECO:0000269|PubMed:8393574}. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16877770, ECO:0000269|PubMed:24741100, ECO:0000269|PubMed:28611249}. Note=Localizes in small nuclear bodies early in infection then moves to a more diffuse distribution in viral compartments as infection progresses (PubMed:16877770). UL31 mediates the recruitment a... | null | null | null | null | null | FUNCTION: Transcriptional regulator that interacts with cellular elongation regulators to inhibit host cell transcription and promote viral gene expression in productive infection, mainly by mediating changes on the host RNA polymerase II (PubMed:17344289, PubMed:28611249, PubMed:34696162). One change, which is UL13 in... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P04487 | RNB_HHV11 | MSQTQPPAPVGPGDPDVYLKGVPSAGMHPRGVHAPRGHPRMISGPPQRGDNDQAAGQCGDSGLLRVGADTTISKPSEAVRPPTIPRTPRVPREPRVPRPPREPREPRVPRAPRDPRVPRDPRDPRQPRSPREPRSPREPRSPREPRTPRTPREPRTARGSV | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated perturbation of host cell cycle progression [GO:0044071]; symbiont-mediated perturbation of host transcription [GO:0052026]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 act... | host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]; host cell nucleus [GO:0042025] | DNA binding [GO:0003677]; endopeptidase activity [GO:0004175]; molecular sequestering activity [GO:0140313]; protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA binding [GO:0003723] | null | null | Simplex virus US11 protein family | PTM: May be phosphorylated on Ser residues by host kinases. {ECO:0000269|PubMed:7498183}. | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000269|PubMed:20633584}. Host cytoplasm {ECO:0000269|PubMed:20633584}. Note=Following infection, it is released into the cell cytoplasm. | null | null | null | null | null | FUNCTION: Plays a role in the inhibition of host immune response. Participates in the inhibition of host autophagy by interacting with and inhibiting host PKR/EIF2AK2. This interaction also prevents the interferon-induced shut down of protein synthesis following viral infection. Downmodulates the host RLR signaling pat... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P04488 | GE_HHV11 | MDRGAVVGFLLGVCVVSCLAGTPKTSWRRVSVGEDVSLLPAPGPTGRGPTQKLLWAVEPLDGCGPLHPSWVSLMPPKQVPETVVDAACMRAPVPLAMAYAPPAPSATGGLRTDFVWQERAAVVNRSLVIHGVRETDSGLYTLSVGDIKDPARQVASVVLVVQPAPVPTPPPTPADYDEDDNDEGEDESLAGTPASGTPRLPPPPAPPRSWPSAPEVSHVRGVTVRMETPEAILFSPGETFSTNVSIHAIAHDDQTYSMDVVWLRFDVPTSCAEMRIYESCLYHPQLPECLSPADAPCAASTWTSRLAVRSYAGCSRTNPP... | null | null | virus-mediated perturbation of host defense response [GO:0019049] | host cell endosome membrane [GO:0044175]; host cell Golgi membrane [GO:0044178]; host cell junction [GO:0044156]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | identical protein binding [GO:0042802] | PF02480;PF20418; | 2.60.40.10; | Alphaherpesvirinae glycoprotein E family | PTM: Phosphorylated on serines within the acidic cluster. Phosphorylation determines whether endocytosed viral gE traffics to the trans-Golgi network or recycles to the cell membrane. {ECO:0000305}.; PTM: N-glycosylated, and sulfated. {ECO:0000269|PubMed:6310034}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell junction. Host Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Host endosome membrane... | null | null | null | null | null | FUNCTION: In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate ... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P04499 | TERM_ADE05 | MALSVNDCARLTGQSVPTMEHFLPLRNIWNRVRDFPRASTTAAGITWMSRYIYGYHRLMLEDLAPGAPATLRWPLYRQPPPHFLVGYQYLVRTCNDYVFDSRAYSRLRYTELSQPGHQTVNWSVMANCTYTINTGAYHRFVDMDDFQSTLTQVQQAILAERVVADLALLQPMRGFGVTRMGGRGRHLRPNSAAAAAIDARDAGQEEGEEEVPVERLMQDYYKDLRRCQNEAWGMADRLRIQQAGPKDMVLLSTIRRLKTAYFNYIISSTSARNNPDRRPLPPATVLSLPCDCDWLDAFLERFSDPVDADSLRSLGGGVPT... | null | null | DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693]; viral DNA strand displacement replication [GO:0039687] | host cell nuclear matrix [GO:0044204]; host cell nucleus [GO:0042025] | DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; single-stranded DNA binding [GO:0003697] | PF02459; | null | Adenoviridae terminal protein family | PTM: Preterminal protein is used to replicate viral genome, upon genomic encapsidation it is processed first into iTP and finally into TP by adenovirus protease. {ECO:0000255|HAMAP-Rule:MF_04061}. | SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000269|PubMed:8416372, ECO:0000269|PubMed:8497057}. | null | null | null | null | null | FUNCTION: Protein covalently bound to the viral DNA that acts as a primer for viral genomic replication by DNA strand displacement. Assembles on the viral origin of replication in an initiation complex with viral polymerase, DBP, host NFIA and host POU2F1/OCT1. During initiation, the polymerase covalently couples the f... | Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) |
P04509 | VP6_ROTRF | MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFDFGLLGTTLLNLDANYVETARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLIKLSGIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPYSASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANTQQFEHIVQLRRVLTTATITLLPDAERFSFPRVITSADGATTWYFNPVILRPNNVEIEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLMRPPNMTPAVAALFPNAQPFEHHATV... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064] | T=13 icosahedral viral capsid [GO:0039621]; viral envelope [GO:0019031]; viral intermediate capsid [GO:0039626] | host cell surface receptor binding [GO:0046789]; metal ion binding [GO:0046872]; structural molecule activity [GO:0005198] | PF00980; | 2.60.120.170;1.10.1350.10; | Rotavirus VP6 family | PTM: The N-terminus is blocked. {ECO:0000255|HAMAP-Rule:MF_04129, ECO:0000269|PubMed:12610135}.; PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins seems to have a positive role on viral replication. {ECO:0000255|HAMAP-Rule:MF_04129}. | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04129, ECO:0000269|PubMed:11285213, ECO:0000269|PubMed:12097594}. Note=Component of the intermediate capsid (PubMed:11285213). Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral repli... | null | null | null | null | null | FUNCTION: Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices (PubMed:11285213). This capsid constitutes the middle concentric layer of the viral mature particle (PubMed:11285213). The i... | Rotavirus A (strain RVA/Cow/France/RF/1975/G6P6[1]) (RV-A) |
P04512 | NSP4_ROTS1 | MEKLTDLNYTLSVITLMNNTLHTILEDPGMAYFPYIASVLTGLFALNKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIYDKLTVQTTGEIDMTKEINQKNVRTLEEWESGKNPYEPREVTAAM | null | null | induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259] | extracellular region [GO:0005576]; host caveola [GO:0044155]; host cell rough endoplasmic reticulum membrane [GO:0044169]; membrane [GO:0016020] | metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; toxin activity [GO:0090729] | PF01452; | 1.20.5.430; | Rotavirus NSP4 family | PTM: The N-glycosyl content is primarily Man(9)GlcNAc, with a small amount of Man(8)GlcNAc. {ECO:0000255|HAMAP-Rule:MF_04091}. | SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08434, ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091, ECO:0000269|PubMed:17376898}; Single-pass type III membr... | null | null | null | null | null | FUNCTION: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associate... | Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain Both)) |
P04517 | POLG_TEV | MALIFGTVNANILKEVFGGARMACVTSAHMAGANGSILKKAEETSRAIMHKPVIFGEDYITEADLPYTPLHLEVDAEMERMYYLGRRALTHGKRRKVSVNNKRNRRRKVAKTYVGRDSIVEKIVVPHTERKVDTTAAVEDICNEATTQLVHNSMPKRKKQKNFLPATSLSNVYAQTWSIVRKRHMQVEIISKKSVRARVKRFEGSVQLFASVRHMYGERKRVDLRIDNWQQETLLDLAKRFKNERVDQSKLTFGSSGLVLRQGSYGPAHWYRHGMFIVRGRSDGMLVDARAKVTFAVCHSMTHYSDKSISEAFFIPYSKK... | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0... | PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680; | 3.30.505.20;3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Potyviral RNA is expressed as ... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate ... | CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but oth... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus (PubMed:2656254). Interacts with virions and aphid stylets (PubMed:9880030). Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcri... | Tobacco etch virus (TEV) |
P04524 | SIGML_BPT4 | MSETKPKYNYVNNKELLQAIIDWKTELANNKDPNKVVRQNDTIGLAIMLIAEGLSKRFNFSGYTQSWKQEMIADGIEASIKGLHNFDETKYKNPHAYITQACFNAFVQRIKKERKEVAKKYSYFVHNVYDSRDDDMVALVDETFIQDIYDKMTHYEESTYRTPGAEKKSVVDDSPSLDFLYEAND | null | null | late viral transcription [GO:0019086] | null | DNA binding [GO:0003677]; nucleotidyltransferase activity [GO:0016779]; sigma factor activity [GO:0016987] | null | null | Tevenvirinae RNA polymerase sigma-like factor family | null | null | null | null | null | null | null | FUNCTION: Plays a role in the transcription of the viral late genes by acting as a late promoter recognition subunit (PubMed:33602900). Associates with host RNA polymerase (RNAP) core and thus replaces the host sigma-70/rpoD subunit in the complex (PubMed:33602900). May also play a role in DNA packaging by interacting ... | Enterobacteria phage T4 (Bacteriophage T4) |
P04530 | HELIC_BPT4 | MVEIILSHLIFDQAYFSKVWPYMDSEYFESGPAKNTFKLIKSHVNEYHSVPSINALNVALENSSFTETEYSGVKTLISKLADSPEDHSWLVKETEKYVQQRAMFNATSKIIEIQTNAELPPEKRNKKMPDVGAIPDIMRQALSISFDSYVGHDWMDDYEARWLSYMNKARKVPFKLRILNKITKGGAETGTLNVLMAGVNVGKSLGLCSLAADYLQLGHNVLYISMEMAEEVCAKRIDANMLDVSLDDIDDGHISYAEYKGKMEKWREKSTLGRLIVKQYPTGGADANTFRSLLNELKLKKNFVPTIIIVDYLGICKSCR... | 3.6.4.- | null | bidirectional double-stranded viral DNA replication [GO:0039686]; DNA replication, synthesis of RNA primer [GO:0006269]; DNA unwinding involved in DNA replication [GO:0006268] | cytosol [GO:0005829] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; hydrolase activity [GO:0016787]; single-stranded DNA helicase activity [GO:0017116] | PF03796; | 3.40.50.300; | Helicase family, DnaB subfamily | null | null | null | null | null | null | null | FUNCTION: ATP-dependent DNA helicase essential for viral DNA replication and recombination (PubMed:10871615). The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synth... | Enterobacteria phage T4 (Bacteriophage T4) |
P04545 | M21_HRSVA | MSRRNPCKFEIRGHCLNGKRCHFSHNYFEWPPHALLVRQNFMLNRILKSMDKSIDTLSEISGAAELDRTEEYALGVVGVLESYIGSINNITKQSACVAMSKLLTELNSDDIKKLRDNEELNSPKIRVYNTVISYIESNRKNNKQTIHLLKRLPADVLKKTIKNTLDIHKSITINNPKESTVSDTNDHAKNNDTT | null | null | regulation of viral transcription [GO:0046782]; transcription antitermination [GO:0031564]; viral transcription [GO:0019083] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | metal ion binding [GO:0046872]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF06436; | 1.20.120.1350; | Pneumoviridae M2-1 protein family | PTM: Phosphorylated by host in infected cells (PubMed:10846068, PubMed:11711610, PubMed:29489893, PubMed:3339328). Only dephosphorylated M2-1 is competent for viral mRNA binding (PubMed:29489893). Cyclic turnover of phosphorylation-dephosphorylation of M2-1 is required for efficient viral transcription (PubMed:29489893... | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:23776214, ECO:0000269|PubMed:24760890}. Host cytoplasm {ECO:0000269|PubMed:11907323, ECO:0000269|PubMed:22675274, ECO:0000269|PubMed:27194388, ECO:0000269|PubMed:28916773, ECO:0000269|PubMed:29489893, ECO:0000269|PubMed:31649314}. Host nucleus {ECO:0000269|PubMed:1562977... | null | null | null | null | null | FUNCTION: Acts as a tetrameric transcription processivity factor that binds in a competitive manner to RNA and the phosphoprotein (P) to prevent premature termination during transcription (PubMed:19386701, PubMed:22675274). Transcription anti-terminator that enhances readthrough of intergenic junctions during viral tra... | Human respiratory syncytial virus A (strain A2) |
P04551 | CDK1_SCHPO | MENYQKVEKIGEGTYGVVYKARHKLSGRIVAMKKIRLEDESEGVPSTAIREISLLKEVNDENNRSNCVRLLDILHAESKLYLVFEFLDMDLKKYMDRISETGATSLDPRLVQKFTYQLVNGVNFCHSRRIIHRDLKPQNLLIDKEGNLKLADFGLARSFGVPLRNYTHEIVTLWYRAPEVLLGSRHYSTGVDIWSVGCIFAEMIRRSPLFPGDSEIDEIFKIFQVLGTPNEEVWPGVTLLQDYKSTFPRWKRMDLHKVVPNGEEDAIELLSAMLVYDPAHRISAKRALQQNYLRDFH | 2.7.11.22 | null | cell division [GO:0051301]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic G1 cell size control checkpoint signaling [GO:0031568]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; negative... | chromatin [GO:0000785]; chromosome, telomeric repeat region [GO:0140445]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; meiotic spindle [GO:0072687]; meiotic spindle pole body [GO:0035974]; mitotic spindle [GO:0072686]; mitotic spindle midzone [GO:199... | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein kinase activity [GO:0097472]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase activity [GO:0004672]; 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, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P24941}; CATALYT... | null | null | null | null | FUNCTION: Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles (PubMed:1896017, PubMed:2274045, PubMed:6581157, PubMed:7498766, PubMed:8087848, PubMed:9042863, Ref.6). Required to drive the G1-S and G2-M transitions, and initiation of premeiotic DNA replication and meiosis II (... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P04553 | HSP1_HUMAN | MARYRCCRSQSRSRYYRQRQRSRRRRRRSCQTRRRAMRCCRPRYRPRCRRH | null | null | chromosome condensation [GO:0030261]; chromosome organization [GO:0051276]; sperm DNA condensation [GO:0035092]; spermatogenesis [GO:0007283] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786] | DNA binding [GO:0003677] | PF00260; | null | Protamine P1 family | PTM: Phosphorylated by SRPK1. {ECO:0000269|PubMed:10390541}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. | Homo sapiens (Human) |
P04554 | PRM2_HUMAN | MVRYRVRSLSERSHEVYRQQLHGQEQGHHGQEEQGLSPEHVEVYERTHGQSHYRRRHCSRRRLHRIHRRQHRSCRRRKRRSCRHRRRHRRGCRTRKRTCRRH | null | null | chromosome condensation [GO:0030261]; chromosome organization [GO:0051276]; nucleus organization [GO:0006997]; sequestering of metal ion [GO:0051238]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283] | male germ cell nucleus [GO:0001673]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634] | cadmium ion binding [GO:0046870]; DNA binding [GO:0003677]; ion binding [GO:0043167]; zinc ion binding [GO:0008270] | PF00841; | null | Protamine P2 family | PTM: Proteolytic processing into mature chains is required for histone eviction during spermatogenesis. Transition proteins (TNP1 and TNP2) are required for processing. {ECO:0000250|UniProtKB:P07978}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07978}. Chromosome {ECO:0000250|UniProtKB:P07978}. | null | null | null | null | null | FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. {ECO:0000250|UniProtKB:P07978}. | Homo sapiens (Human) |
P04575 | UCP1_MESAU | MVNPTTSEVHPTMGVKIFSAGVAACLADIITFPLDTAKVRLQIQGEGQISSTIRYKGVLGTITTLAKTEGLPKLYSGLPAGIQRQISFASLRIGLYDTVQEYFSSGKETPPTLGNRISAGLMTGGVAVFIGQPTEVVKVRLQAQSHLHGIKPRYTGTYNAYRIIATTESFSTLWKGTTPNLLRNVIINCVELVTYDLMKGALVNNQILADDVPCHLLSAFVAGFCTTFLASPADVVKTRFINSLPGQYPSVPSCAMTMLTKEGPTAFFKGFVPSFLRLASWNVIMFVCFEQLKKELSKSRQTVDCTT | null | null | adaptive thermogenesis [GO:1990845]; cellular response to fatty acid [GO:0071398]; cellular response to hormone stimulus [GO:0032870]; cellular response to reactive oxygen species [GO:0034614]; mitochondrial transmembrane transport [GO:1990542]; proton transmembrane transport [GO:1902600]; regulation of reactive oxygen... | mitochondrial inner membrane [GO:0005743] | cardiolipin binding [GO:1901612]; long-chain fatty acid binding [GO:0036041]; oxidative phosphorylation uncoupler activity [GO:0017077]; purine ribonucleotide binding [GO:0032555] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: May undergo sulfenylation upon cold exposure. May increase the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects. {ECO:0000250|UniProtKB:P12242}.; PTM: May undergo ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:P04633}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04633}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P25874}; | null | null | null | null | FUNCTION: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. Functions as a long-chain fatty acid/... | Mesocricetus auratus (Golden hamster) |
P04577 | ENV_HV2RO | MMNQLLIAILLASACLVYCTQYVTVFYGVPTWKNATIPLFCATRNRDTWGTIQCLPDNDDYQEITLNVTEAFDAWNNTVTEQAIEDVWHLFETSIKPCVKLTPLCVAMKCSSTESSTGNNTTSKSTSTTTTTPTDQEQEISEDTPCARADNCSGLGEEETINCQFNMTGLERDKKKQYNETWYSKDVVCETNNSTNQTQCYMNHCNTSVITESCDKHYWDAIRFRYCAPPGYALLRCNDTNYSGFAPNCSKVVASTCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLSLHCKRPGNKTVKQIMLMS... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy a... | Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2) |
P04578 | ENV_HV1H2 | MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTI... | null | null | actin filament organization [GO:0007015]; clathrin-dependent endocytosis of virus by host cell [GO:0075512]; evasion of host immune response [GO:0042783]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishm... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Ru... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) |
P04579 | ENV_HV1RH | MRVMEMRKNCQHLWKWGTMLLGMLMICSAAEDLWVTVYYGVPVWKEATTTLFCASEAKAYKTEVHNVWAKHACVPTDPNPQEVLLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDANLNGTNVTSSSGGTMMENGEIKNCSFQVTTSRRDKTQKKYALFYKLDVVPIEKGNISPKNNTSNNTSYGNYTLIHCNSSVITQACPKVSFEPIPIHYCTPAGFAILKCNDKKFNGTGPCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTDNVKTIIVQLNASVQINCTRPNNNTRKSI... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1) |
P04580 | ENV_HV1Z6 | MRAREIERNCPNLWKWGIMLLGILMICSAADNLWVTVYYGVPVWKEATTTLFCASDAKSYKTEAHNIWATHACVPTDPNPQEIELENVTENFNMWRNNMVEQIHEDIISLWDQSLKPCVKLTPLCVTLNCTDESDEWMGNVTGKNVTEDIRMKNCSFNITTVVRDKTKQVHALFYRLDIVPIDNDNSTNSTNYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDKRFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNAKIIIVQLNESVAINCTRPYKNTRQSTPIGLGQALYTT... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype D (isolate Z6) (HIV-1) |
P04581 | ENV_HV1EL | MRARGIERNCQNWWKWGIMLLGILMTCSAADNLWVTVYYGVPVWKEATTTLFCASDAKSYETEAHNIWATHACVPTDPNPQEIALENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCSDELRNNGTMGNNVTTEEKGMKNCSFNVTTVLKDKKQQVYALFYRLDIVPIDNDSSTNSTNYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVIIRSENLTNNAKNIIAHLNESVKITCARPYQNTRQRTPIGLGQSLYTTR... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype D (isolate ELI) (HIV-1) |
P04582 | ENV_HV1B8 | MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYFGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSKRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLDTSVEINCTRPNNNTRKKIRIQRGPGRAFVTI... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate BH8) (HIV-1) |
P04583 | ENV_HV1MA | MRVREIQRNYQNWWRWGMMLLGMLMTCSIAEDLWVTVYYGVPVWKEATTTLFCASDAKSYETEVHNIWATHACVPTDPNPQEIELENVTEGFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTNVNGTAVNGTNAGSNRTNAELKMEIGEVKNCSFNITPVGSDKRQEYATFYNLDLVQIDDSDNSSYRLINCNTSVITQACPKVTFDPIPIHYCAPAGFAILKCNDKKFNGTEICKNVSTVQCTHGIKPVVSTQLLLNGSLAEEEIMIRSENLTDNTKNIIVQLNETVTINCTRPGNNTRRGIHFGPGQAL... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype A (isolate MAL) (HIV-1) |
P04584 | POL_HV2RO | MGARNSVLRGKKADELERIRLRPGGKKKYRLKHIVWAANKLDRFGLAESLLESKEGCQKILTVLDPMVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVRRHLVAETGTAEKMPSTSRPTAPSSEKGGNYPVQHVGGNYTHIPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAAEWDVQHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immun... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2) |
P04585 | POL_HV1H2 | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; protein processing [GO:0016485]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral life cycle [GO:0019058]; ... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; identical protein binding [GO:0042802]; integrase activity [GO:0008907]; lipid binding [GO:0008289]; peptidase activity [GO:0008233]; RNA stem-loop bin... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endoso... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:32053707, ECO:0000269|PubMed:33542150}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cl... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) |
P04587 | POL_HV1B5 | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate BH5) (HIV-1) |
P04588 | POL_HV1MA | MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETGEGCQQIMEQLQSTLKTGSEEIKSLYNTVATLYCVHQRIDVKDTKEALDKIEEIQNKSRQKTQQAAAAQQAAAATKNSSSVSQNYPIVQNAQGQMIHQAISPRTLNAWVKVIEEKAFSPEVIPMFSALSEGATPQDLNMMLNIVGGHQAAMQMLKDTINEEAADWDRVHPVHAGPIPPGQMREPRGSDIAGTTSTLQEQIGWMTSNPPIPVGDIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVK... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype A (isolate MAL) (HIV-1) |
P04589 | POL_HV1EL | MGARASVLSGGKLDKWEKIRLRPGGKKKYRLKHIVWASRELERYALNPGLLETSEGCKQIIGQLQPAIQTGTEELRSLYNTVATLYCVHKGIDVKDTKEALEKMEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIAWMTSNPPIPVGEIYKRWIIVGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTET... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype D (isolate ELI) (HIV-1) |
P04590 | GAG_HV2RO | MGARNSVLRGKKADELERIRLRPGGKKKYRLKHIVWAANKLDRFGLAESLLESKEGCQKILTVLDPMVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVRRHLVAETGTAEKMPSTSRPTAPSSEKGGNYPVQHVGGNYTHIPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAAEWDVQHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2) |
P04591 | GAG_HV1H2 | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nuclear membrane [GO:0044200]; host cell plasma membrane [GO:0020002]; host cellular component [GO:0018995]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association (PubMed:17656588)... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) |
P04592 | GAG_HV1EL | MGARASVLSGGKLDKWEKIRLRPGGKKKYRLKHIVWASRELERYALNPGLLETSEGCKQIIGQLQPAIQTGTEELRSLYNTVATLYCVHKGIDVKDTKEALEKMEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIAWMTSNPPIPVGEIYKRWIIVGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype D (isolate ELI) (HIV-1) |
P04593 | GAG_HV1B5 | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate BH5) (HIV-1) |
P04594 | GAG_HV1MA | MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETGEGCQQIMEQLQSTLKTGSEEIKSLYNTVATLYCVHQRIDVKDTKEALDKIEEIQNKSRQKTQQAAAAQQAAAATKNSSSVSQNYPIVQNAQGQMIHQAISPRTLNAWVKVIEEKAFSPEVIPMFSALSEGATPQDLNMMLNIVGGHQAAMQMLKDTINEEAADWDRVHPVHAGPIPPGQMREPRGSDIAGTTSTLQEQIGWMTSNPPIPVGDIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVK... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype A (isolate MAL) (HIV-1) |
P04601 | NEF_HV1H2 | MGGKWSKSSVIGWPTVRERMRRAEPAADRVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKIEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved conco... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:19912576}. Host Golgi apparatus membrane... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) |
P04602 | NEF_HV1Z6 | MGGRWSKSSIVGWPAIRERIRRTDPRRTDPAADGVGAASRDLEKHGAITSSNTRDTNADCAWLEAQEESEEVGFPVRPQVPLRPMTYKLAVDLSHFLKEKGGLEGLIWSKKRQEILDLWVYNTQGIFPDWQNYTPGPGIRYPLTFGWCFELVPVDPREVEEATEGETNCLLHPVCQHGMEDTEREVLKWRFNSRLAFEHKAREMHPEFYKDC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype D (isolate Z6) (HIV-1) |
P04603 | NEF_HV1MA | MGGKWSKSSIVGWPKIRERIRRTPPTETGVGAVSQDAVSQDLDKCGAAASSSPAANNASCEPPEEEEEVGFPVRPQVPLRPMTYKGAFDLSHFLKEKGGLDGLVWSPKRQEILDLWVYHTQGYFPDWQNYTPGPGIRFPLTFGWCFKLVPMSPEEVEEANEGENNCLLHPISQHGMEDAEREVLKWKFDSSLALRHRAREQHPEYYKDC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype A (isolate MAL) (HIV-1) |
P04604 | NEF_HV1EL | MGGKWSKSSIVGWPAIRERIRRTNPAADGVGAVSRDLEKHGAITSSNTASTNADCAWLEAQEESDEVGFPVRPQVPLRPMTYKEALDLSHFLKEKGGLEGLIWSKKRQEILDLWVYNTQGIFPDWQNYTPGPGIRYPLTFGWCYELVPVDPQEVEEDTEGETNSLLHPICQHGMEDPERQVLKWRFNSRLAFEHKAREMHPEFYKN | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype D (isolate ELI) (HIV-1) |
P04608 | TAT_HV1H2 | MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE | null | null | DNA-templated transcription [GO:0006351]; evasion of host immune response [GO:0042783]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive reg... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]; host cell nucleus [GO:0042025] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; molecular sequestering activity [GO:0140313]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-ac... | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:17267505}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. ... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:19888548}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:19888548, ECO:0000269|PubMed:23501106}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:19888548}. Note=Probably localizes ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) |
P04609 | TAT_HV1Z6 | MDPVDPNLEPWNHPGSQPKTACNRCHCKKCCYHCQVCFITKGLGISYGRKKRRQRRRPSQGGQTHQDPIPKQPSSQPRGNPTGPKE | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype D (isolate Z6) (HIV-1) |
P04610 | TAT_HV1BR | MEPVDPRLEPWKHPGSQPKTACTTCYCKKCCFHCQVCFTTKALGISYGRKKRRQRRRPPQGSQTHQVSLSKQPTSQPRGDPTGPKE | null | null | DNA-templated transcription [GO:0006351]; membrane hyperpolarization [GO:0060081]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of cellular respiration [GO:1901856]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of NF-kappaB transcrip... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; regulatory region RNA binding [GO:0001069]; RNA-binding transcription regulator activity [GO:0001070]; trans-acti... | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) |
P04611 | TAT_HV1EL | MDPVDPNLEPWNHPGSQPRTPCNKCHCKKCCYHCPVCFLNKGLGISYGRKKRRQRRGPPQGGQAHQVPIPKQPSSQPRGDPTGPKEQKKKVESEAETDP | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; regulatory region RNA binding [GO:0001069]; RNA-binding transcription regulator activity [GO:0001070]; trans-acti... | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype D (isolate ELI) (HIV-1) |
P04613 | TAT_HV1MA | MDPVDPNLEPWNHPGSQPRTPCNKCYCKKCCYHCQMCFITKGLGISYGRKKRRQRRRPPQGNQAHQDPLPEQPSSQHRGDHPTGPKE | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; regulatory region RNA binding [GO:0001069]; RNA-binding transcription regulator activity [GO:0001070]; trans-acti... | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype A (isolate MAL) (HIV-1) |
P04614 | TAT_HV1A2 | MEPVDPNLEPWKHPGSQPRTACNNCYCKKCCFHCYACFTRKGLGISYGRKKRRQRRRAPQDSQTHQASLSKQPASQSRGDPTGPTESKKKVERETETDPFD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) (HIV-1) |
P04616 | REV_HV1B1 | MAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILSTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGAKE | null | null | mRNA transport [GO:0051028]; protein export from nucleus [GO:0006611]; viral process [GO:0016032] | host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | DNA-binding transcription factor activity [GO:0003700]; RNA binding [GO:0003723] | PF00424; | 6.10.140.630; | HIV-1 REV protein family | PTM: Asymmetrically arginine dimethylated at one site by host PRMT6. Methylation impairs the RNA-binding activity and export of viral RNA from the nucleus to the cytoplasm. The methylation site is still unclear and either occurs at Arg-35, Arg-38 or Arg-39. {ECO:0000269|PubMed:17176473}.; PTM: Asymmetrically arginine d... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04077}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04077}. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04077}. | null | null | null | null | null | FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is es... | Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1) |
P04618 | REV_HV1H2 | MAGRSGDSDEELIRTVRLIKLLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILGTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGTKE | null | null | mRNA transport [GO:0051028]; viral process [GO:0016032] | host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF00424; | 6.10.140.630; | HIV-1 REV protein family | PTM: Asymmetrically arginine dimethylated at one site by host PRMT6. Methylation impairs the RNA-binding activity and export of viral RNA from the nucleus to the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04077}.; PTM: Phosphorylated by protein kinase CK2. Presence of, and maybe binding to the N-terminus of the regulatory b... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04077}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04077}. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04077}. | null | null | null | null | null | FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is es... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) |
P04624 | ENV_HV1H3 | MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHAGVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKKIRIQRGPGRAFVTI... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB3) (HIV-1) |
P04625 | THA_CHICK | MEQKPSTLDPLSEPEDTRWLDGKRKRKSSQCLVKSSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDGCCVIDKITRNQCQLCRFKKCISVGMAMDLVLDDSKRVAKRKLIEENRERRRKEEMIKSLQHRPSPSAEEWELIHVVTEAHRSTNAQGSHWKQKRKFLPEDIGQSPMASMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLSGEMAVKREQLKNGGLGVVSDAIFDLGKSLSAFNLDDTEVALLQAV... | null | null | cell differentiation [GO:0030154]; mRNA transcription by RNA polymerase II [GO:0042789]; negative regulation of RNA polymerase II transcription preinitiation complex assembly [GO:0017055]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of thyroid hormone mediated signaling p... | cytosol [GO:0005829]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | nuclear receptor activity [GO:0004879]; protein domain specific binding [GO:0019904]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]; TBP-class protein binding [GO:0017025]; thyroid hormone binding [GO:0070324]; zinc ion bin... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. | Gallus gallus (Chicken) |
P04626 | ERBB2_HUMAN | MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQ... | 2.7.10.1 | null | cell surface receptor signaling pathway [GO:0007166]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to growth factor stimulus [GO:0071363]; enzyme-linked receptor protein signaling pathway [GO:0007167]; ERBB2-EGFR signaling pathway [GO:0038134]; ERBB2-ERBB3 signaling pathway [GO:... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; ERBB3:ERBB2 complex [GO:0038143]; membrane [GO:0016020]; myelin sheath [GO:0043209]; neuromuscular junction [GO:0031594]; ... | ATP binding [GO:0005524]; coreceptor activity [GO:0015026]; ErbB-3 class receptor binding [GO:0043125]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein tyrosine kinase activity [GO:0004713]; receptor tyrosine kinase binding [GO:0030971]; RNA polymerase I core binding [G... | PF00757;PF14843;PF07714;PF01030;PF21314; | 1.20.5.100;4.10.1140.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily | PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit (Probable). Ligand-binding increases phosphorylation on tyrosine residues (PubMed:27134172, PubMed:33497358). Signaling via SEMA4C promotes phosphorylation at Tyr-... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32381043}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:34380438}; Single-pass type I membrane protein {ECO:0000255}. Note=Internalized from the cell membrane in response to EGF stimulation. {ECO:0000269|P... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowt... | Homo sapiens (Human) |
P04627 | ARAF_MOUSE | MEPPRGPPVSGAEPSRAVGTVKVYLPNKQRTVVTVREGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRRQFYHSIQDLSGGSRQQEAPSNLSVNELLTPQGPSPFTQQRDQEHFSFPAPANPPLQRIRSTSTPNVHMVSTTAPMDSSLMQFTAQSFSTDAAGRGGDGAPRGSPSPASVSSGRKSPHSKLPSEQRERKSLADEKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFG... | 2.7.11.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; Ras protein signal transduction [GO:0007265]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulat... | cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310] | PF00130;PF07714;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade (By similarity). Phosphorylates PFKFB2 (By similarity). {ECO:0000250|UniProtKB:P10398}. | Mus musculus (Mouse) |
P04628 | WNT1_HUMAN | MGLWALLPGWVSATLLLALAALPAALAANSSGRWWGIVNVASSTNLLTDSKSLQLVLEPSLQLLSRKQRRLIRQNPGILHSVSGGLQSAVRECKWQFRNRRWNCPTAPGPHLFGKIVNRGCRETAFIFAITSAGVTHSVARSCSEGSIESCTCDYRRRGPGGPDWHWGGCSDNIDFGRLFGREFVDSGEKGRDLRFLMNLHNNEAGRTTVFSEMRQECKCHGMSGSCTVRTCWMRLPTLRAVGDVLRDRFDGASRVLYGNRGSNRASRAELLRLEPEDPAHKPPSPHDLVYFEKSPNFCTYSGRLGTAGTAGRACNSSSP... | null | null | animal organ regeneration [GO:0031100]; astrocyte-dopaminergic neuron signaling [GO:0036520]; bone development [GO:0060348]; branching involved in ureteric bud morphogenesis [GO:0001658]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cell proliferation in midbrain [GO:0033278]; cell-c... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; plasma membrane [GO:0005886] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; morphogen activity [GO:0016015]; protein domain specific binding [GO:0019904]; receptor ligand activity [GO:0048018] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Palmitoleoylation is necessary for proper trafficking to cell surface (Probable). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway (By similarity). {ECO:0000250|UniProtKB:P56704, ECO:0000250|UniProtKB:Q91029, ECO:000030... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}. | null | null | null | null | null | FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Acts in the canonical Wnt signaling pathway by promoting beta-catenin-dependent transcriptional activation (PubMed:23499309, PubMed:23656646, PubMed:26902720, PubMed:28528193). In some developmental processes, is also a lig... | Homo sapiens (Human) |
P04629 | NTRK1_HUMAN | MLRGGRRGQLGWHSWAAGPGSLLAWLILASAGAAPCPDACCPHGSSGLRCTRDGALDSLHHLPGAENLTELYIENQQHLQHLELRDLRGLGELRNLTIVKSGLRFVAPDAFHFTPRLSRLNLSFNALESLSWKTVQGLSLQELVLSGNPLHCSCALRWLQRWEEEGLGGVPEQKLQCHGQGPLAHMPNASCGVPTLKVQVPNASVDVGDDVLLRCQVEGRGLEQAGWILTELEQSATVMKSGGLPSLGLTLANVTSDLNRKNVTCWAENDVGRAEVSVQVNVSFPASVQLHTAVEMHHWCIPFSVDGQPAPSLRWLFNGS... | 2.7.10.1 | null | axon guidance [GO:0007411]; axonogenesis involved in innervation [GO:0060385]; B cell differentiation [GO:0030183]; behavioral response to formalin induced pain [GO:0061368]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to nicotine [GO:0071316]; circadian rhythm [GO:0007623]; detect... | axon [GO:0030424]; cell surface [GO:0009986]; dendrite [GO:0030425]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; protein-containing compl... | ATP binding [GO:0005524]; GPI-linked ephrin receptor activity [GO:0005004]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; nerve growth factor binding [GO:0048406]; nerve growth factor receptor activity [GO:0010465]; neurotrophin binding [GO:0043121]; neurotrophin p75 receptor binding [GO:0005166]... | PF13855;PF16920;PF07714;PF18613; | 2.60.40.10;3.80.10.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: Ligand-mediated autophosphorylation (PubMed:1281417, PubMed:15488758, PubMed:27676246, PubMed:28177573, PubMed:2927393, PubMed:7510697, PubMed:8155326, PubMed:8325889). Interaction with SQSTM1 is phosphotyrosine-dependent. Autophosphorylation at Tyr-496 mediates interaction and phosphorylation of SHC1 (PubMed:1548... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1281417, ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:17196528, ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:2927393}; Single-pass type I membrane protein {ECO:0000269|PubMed:1281417, ECO:0000269|PubMed:15488758}. Early endosome membrane {ECO:0000250|UniProt... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand (PubMed:1281417, PubMed:1548875... | Homo sapiens (Human) |
P04631 | S100B_RAT | MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDEDGDGECDFQEFMAFVSMVTTACHEFFEHE | null | null | adaptive thermogenesis [GO:1990845]; astrocyte differentiation [GO:0048708]; cell adhesion [GO:0007155]; cellular response to hypoxia [GO:0071456]; learning or memory [GO:0007611]; long-term synaptic potentiation [GO:0060291]; memory [GO:0007613]; negative regulation of skeletal muscle cell differentiation [GO:2001015]... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ruffle [GO:0001726]; sarcoplasmic reticulum [GO:0016529] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; ion binding [GO:0043167]; protein homodimerization activity [GO:0042803]; RAGE receptor binding [GO:0050786]; S100 protein binding [GO:0044548]; signaling receptor binding [GO:0005102]; tau protein ... | PF00036;PF01023; | 1.10.238.10; | S-100 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04271}. Nucleus {ECO:0000250|UniProtKB:P04271}. Secreted {ECO:0000250|UniProtKB:P50114}. Note=Secretion into the medium is promoted by interaction with isoform CLSTN3beta of CLSTN3. {ECO:0000250|UniProtKB:P50114}. | null | null | null | null | null | FUNCTION: Small zinc- and- and calcium-binding protein that is highly expressed in astrocytes and constitutes one of the most abundant soluble proteins in brain (PubMed:14621986, PubMed:15823027, PubMed:18949447, PubMed:20351179). Weakly binds calcium but binds zinc very tightly-distinct binding sites with different af... | Rattus norvegicus (Rat) |
P04632 | CPNS1_HUMAN | MFLVNSFLKGGGGGGGGGGGLGGGLGNVLGGLISGAGGGGGGGGGGGGGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRTHYSNIEANESEEVRQFRRLFAQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKRWQAIYKQFDTDRSGTICSSELPGAFEAAGFHLNEHLYNMIIRRYSDESGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQEWLQLTMYS | null | null | positive regulation of cell population proliferation [GO:0008284]; proteolysis [GO:0006508]; regulation of macroautophagy [GO:0016241] | calpain complex [GO:0110158]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198] | null | 1.10.238.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium binding. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Essential for embryonic development (By similarity). {ECO:0000250|UniProtKB:O88456}. | Homo sapiens (Human) |
P04633 | UCP1_RAT | MVSSTTSEVQPTMGVKIFSAGVSACLADIITFPLDTAKVRLQIQGEGQASSTIRYKGVLGTITTLAKTEGLPKLYSGLPAGIQRQISFASLRIGLYDTVQEYFSSGRETPASLGSKISAGLMTGGVAVFIGQPTEVVKVRMQAQSHLHGIKPRYTGTYNAYRVIATTESLSTLWKGTTPNLMRNVIINCTELVTYDLMKGALVNHHILADDVPCHLLSALVAGFCTTLLASPVDVVKTRFINSLPGQYPSVPSCAMTMYTKEGPAAFFKGFAPSFLRLGSWNVIMFVCFEQLKKELMKSRQTVDCTT | null | null | adaptive thermogenesis [GO:1990845]; brown fat cell differentiation [GO:0050873]; cellular response to cold [GO:0070417]; cellular response to dehydroepiandrosterone [GO:1903495]; cellular response to fatty acid [GO:0071398]; cellular response to hormone stimulus [GO:0032870]; cellular response to reactive oxygen speci... | mitochondrial envelope [GO:0005740]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | cardiolipin binding [GO:1901612]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; long-chain fatty acid binding [GO:0036041]; oxidative phosphorylation uncoupler activity [GO:0017077]; proton transmembrane transporter activity [GO:0015078]; purine ribonucleotide binding [GO:0032555]; transmembrane transporter activ... | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: May undergo ubiquitin-mediated proteasomal degradation. {ECO:0000269|PubMed:22531154}.; PTM: May undergo sulfenylation upon cold exposure. May increase the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects. {ECO:0000250|UniProtKB:P12242}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein {ECO:0000269|PubMed:7691596}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:12479871, ECO:0000269|PubMed:22952235}; | null | null | null | null | FUNCTION: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance (By similarity). Functions as a long-c... | Rattus norvegicus (Rat) |
P04634 | LIPF_RAT | MWLLLITSVISTFGGAHGLFGKLGPGNPEANMNISQMITYWGYPCQEYEVVTEDGYILGVYRIPHGKNNSENIGKRPVVYLQHGLIASATNWIANLPNNSLAFMLADAGYDVWLGNSRGNTWSRKNVYYSPDSVEFWAFSFDEMAKYDLPATINFIVQKTGQEKIHYVGHSQGTTIGFIAFSTNPTLAKKIKTFYALAPVATVKYTQSPLKKISFIPTFLFKLMFGKKMFLPHTYFDDFLGTEVCSREVLDLLCSNTLFIFCGFDKKNLNVSRFDVYLGHNPAGTSVQDFLHWAQLVRSGKFQAFNWGSPSQNMLHYNQK... | 3.1.1.3 | null | lipid catabolic process [GO:0016042]; malate metabolic process [GO:0006108] | extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739] | lipase activity [GO:0016298]; malate dehydrogenase activity [GO:0016615]; triglyceride lipase activity [GO:0004806] | PF04083; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}. | 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:0000269|PubMed:3839077}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol (PubMed:3839077). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (By similarity). {ECO:0000250|UniProtKB:P07098, ECO:0000269|PubMed:3839077}. | Rattus norvegicus (Rat) |
P04635 | LIP_STAHY | MKETKHQHTFSIRKSAYGAASVMVASCIFVIGGGVAEANDSTTQTTTPLEVAQTSQQETHTHQTPVTSLHTATPEHVDDSKEATPLPEKAESPKTEVTVQPSSHTQEVPALHKKTQQQPAYKDKTVPESTIASKSVESNKATENEMSPVEHHASNVEKREDRLETNETTPPSVDREFSHKIINNTHVNPKTDGQTNVNVDTKTIDTVSPKDDRIDTAQPKQVDVPKENTTAQNKFTSQASDKKPTVKAAPEAVQNPENPKNKDPFVFVHGFTGFVGEVAAKGENHWGGTKANLRNHLRKAGYETYEASVSALASNHERAV... | 3.1.1.3; 3.1.1.32 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:2611229}; | lipid catabolic process [GO:0016042]; phosphatidylcholine catabolic process [GO:0034638]; triglyceride catabolic process [GO:0019433] | extracellular region [GO:0005576] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; calcium ion binding [GO:0005509]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]; phospholipase activity [GO:0004620]; triglyceride lipase activity [GO:0004806] | PF04650; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2611229}. | 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:0000269|PubMed:2611229}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-ph... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH around 9. {ECO:0000269|PubMed:2611229}; | null | FUNCTION: Has a broad substrate specificity hydrolyzing a variety of triglycerides and phosphatidylcholines. {ECO:0000269|PubMed:2611229}. | Staphylococcus hyicus |
P04636 | MDHM_RAT | MLSALARPVGAALRRSFSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETRANVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPEAMICIISNPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANTFVAELKGLDPARVNVPVIGGHAGKTIIPLISQCTPKVDFPQDQLATLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVIECSFVQSKETECTYFSTPLLLGKKGLEKNLGIGKITPFEEKMIAEAI... | 1.1.1.37 | null | aerobic respiration [GO:0009060]; gluconeogenesis [GO:0006094]; malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | L-malate dehydrogenase activity [GO:0030060]; malate dehydrogenase (NADP+) activity [GO:0046554]; malate dehydrogenase activity [GO:0016615]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 1 family | PTM: Acetylation is enhanced after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri- and tetraacetylations. Glucose also increases acetylation. {ECO:0000250|UniProtKB:P40926}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:24098488}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10004}; | null | null | null | null | null | Rattus norvegicus (Rat) |
P04637 | P53_HUMAN | MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKK... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1453... | autophagy [GO:0006914]; B cell lineage commitment [GO:0002326]; bone marrow development [GO:0048539]; cardiac muscle cell apoptotic process [GO:0010659]; cardiac septum morphogenesis [GO:0060411]; cellular response to actinomycin D [GO:0072717]; cellular response to gamma radiation [GO:0071480]; cellular response to gl... | centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; germ cell nucleus [GO:0043073]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:000... | 14-3-3 protein binding [GO:0071889]; ATP-dependent DNA/DNA annealing activity [GO:0036310]; chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; copper ion binding [GO:0005507]; core promoter sequence-specific DNA binding [GO:0001046]; disordered domain specific binding [GO:... | PF00870;PF08563;PF07710;PF18521; | 2.60.40.720;6.10.50.20;4.10.170.10; | P53 family | PTM: Acetylation of Lys-382 by CREBBP enhances transcriptional activity (PubMed:10656795, PubMed:15448695, PubMed:20228809, PubMed:23431171). Acetylation of Lys-382 by EP300 (PubMed:10656795, PubMed:15448695, PubMed:20228809, PubMed:23431171). Deacetylation of Lys-382 by SIRT1 impairs its ability to induce proapoptotic... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:19033443, ECO:0000269|PubMed:21597459, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24625977, ECO:0000269|PubMed:26634371}. Nucleus {ECO:0000269|PubMed:15340061, ECO:0000269|PubM... | null | null | null | null | null | FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17189187, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:2067399... | Homo sapiens (Human) |
P04638 | APOA2_RAT | MKLLAMVALLVTICSLEGALVRRQAAETDVQTLFSQYLQSLTDYGKDLMEKAQPSEIQNQAKAYFQNAQERLTPFVQRTGTNLMDFLSRLMSPEEKPAPAAK | null | null | animal organ regeneration [GO:0031100]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; diacylglycerol catabolic process [GO:0046340]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein ... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipas... | PF04711; | 6.10.250.100; | Apolipoprotein A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. | null | null | null | null | null | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. | Rattus norvegicus (Rat) |
P04639 | APOA1_RAT | MKAAVLAVALVFLTGCQAWEFWQQDEPQSQWDRVKDFATVYVDAVKDSGRDYVSQFESSTLGKQLNLNLLDNWDTLGSTVGRLQEQLGPVTQEFWANLEKETDWLRNEMNKDLENVKQKMQPHLDEFQEKWNEEVEAYRQKLEPLGTELHKNAKEMQRHLKVVAEEFRDRMRVNADALRAKFGLYSDQMRENLAQRLTEIKNHPTLIEYHTKASDHLKTLGEKAKPALDDLGQGLMPVLEAWKAKIMSMIDEAKKKLNA | null | null | acylglycerol homeostasis [GO:0055090]; adrenal gland development [GO:0030325]; animal organ regeneration [GO:0031100]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:007050... | cell surface [GO:0009986]; chylomicron [GO:0042627]; cytoplasmic vesicle [GO:0031410]; discoidal high-density lipoprotein particle [GO:0034365]; endocytic vesicle [GO:0030139]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:... | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; apolipoprotein receptor binding [GO:0034190]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; hig... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. | Rattus norvegicus (Rat) |
P04640 | OSTCN_RAT | MRTLSLLTLLALTAFCLSDLAGAKPSDSESDKAFMSKQEGSKVVNRLRRYLNNGLGAPAPYPDPLEPHREVCELNPNCDELADHIGFQDAYKRIYGTTV | null | null | biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to BMP stimulus [GO:0071773]; cellular response to growth factor stimulus [GO:0071363]; cellular response to insulin stimulus [GO:0032869]; cellular response to vitamin D [GO:0071305]; cellular r... | cell projection [GO:0042995]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; vesicle [GO:0031982] | calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147] | null | null | Osteocalcin/matrix Gla protein family | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86546}. | null | null | null | null | null | FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly ... | Rattus norvegicus (Rat) |
P04642 | LDHA_RAT | MAALKDQLIVNLLKEEQVPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLKTPKIVSSKDYSVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPQCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGVNVAGVSLKSLNPQLGTDADKEQWKDVHKQVVDSAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGIKEDVFLSVPCILGQNGISDVVKVTLTPDEEARLKKSA... | 1.1.1.27 | null | cellular response to extracellular stimulus [GO:0031668]; glucose catabolic process to lactate via pyruvate [GO:0019661]; lactate metabolic process [GO:0006089]; liver development [GO:0001889]; NAD metabolic process [GO:0019674]; positive regulation of apoptotic process [GO:0043065]; pyruvate catabolic process [GO:0042... | cytosol [GO:0005829]; mitochondrion [GO:0005739]; oxidoreductase complex [GO:1990204]; sperm fibrous sheath [GO:0035686] | identical protein binding [GO:0042802]; kinase binding [GO:0019900]; L-lactate dehydrogenase activity [GO:0004459]; lactate dehydrogenase activity [GO:0004457]; NAD binding [GO:0051287] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, LDH family | PTM: ISGylated. {ECO:0000250|UniProtKB:P00338}. | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; Evidence={ECO:0000250|UniProtKB:P00338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445; Evidence={ECO... | null | PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P00338}. | null | null | FUNCTION: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000250|UniProtKB:P00338}. | Rattus norvegicus (Rat) |
P04653 | CASA1_SHEEP | MKLLILTCLVAVALARPKHPIKHQGLSSEVLNENLLRFVVAPFPEVFRKENINELSKDIGSESIEDQAMEDAKQMKAGSSSSSEEIVPNSAEQKYIQKEDVPSERYLGYLEQLLRLKKYNVPQLEIVPKSAEEQLHSMKEGNPAHQKQPMIAVNQELAYFYPQLFRQFYQLDAYPSGAWYYLPLGTQYTDAPSFSDIPNPIGSENSGKITMPLW | null | null | response to 11-deoxycorticosterone [GO:1903496]; response to dehydroepiandrosterone [GO:1903494]; response to estradiol [GO:0032355]; response to progesterone [GO:0032570] | extracellular space [GO:0005615] | null | PF00363; | null | Alpha-casein family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Important role in the capacity of milk to transport calcium phosphate. | Ovis aries (Sheep) |
P04657 | CYC1_DROME | MGSGDAENGKKIFVQKCAQCHTYEVGGKHKVGPNLGGVVGRKCGTAAGYKYTDANIKKGVTWTEGNLDEYLKDPKKYIPGTKMVFAGLKKAEERADLIAFLKSNK | null | null | mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; oxidative phosphorylation [GO:0006119]; regulation of compound eye retinal cell programmed cell death [GO:0046669]; sperm individualization [GO:0007291] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; respirasome [GO:0070469] | cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Drosophila melanogaster (Fruit fly) |
P04670 | URIC1_SOYBN | MAQQEVVEGFKFEQRHGKERVRVARVWKTRQGQHFIVEWRVGITLFSDCVNSYLRDDNSDIVATDTMKNTVYAKAKECSDILSAEEFAILLAKHFVSFYQKVTGAIVNIVEKPWERVTVDGQPHEHGFKLGSEKHTTEAIVQKSGSLQLTSGIEGLSVLKTTQSGFVNFIRDKYTALPDTRERMVATEVTALWRYSYESLYSLPQKPLYFTEKYQEVKKVLADTFFGPPKGGVYSPSVQNTLYLMAKATLNRFPDIAYVSLKLPNLHFIPVNISNQDGPIVKFEDDVYLPTDEPHGSIQASLSRLWSKL | 1.7.3.3 | null | nodulation [GO:0009877]; purine nucleobase catabolic process [GO:0006145]; urate catabolic process [GO:0019628] | peroxisome [GO:0005777] | urate oxidase activity [GO:0004846] | PF01014; | 3.10.270.10; | Uricase family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Peroxisome. | CATALYTIC ACTIVITY: Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2; Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3; | null | PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3. | null | null | FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. | Glycine max (Soybean) (Glycine hispida) |
P04688 | TBA1_SCHPO | MREVISVHVGQAGVQIGNACWELYCLEHGIGPDGFPTENSEVHKNNSYLNDGFGTFFSETGQGKFVPRSIYVDLEPNVIDQVRTGPYKDLFHPEQMVTGKEDASNNYARGHYTVGKEMIDSVLERIRRMADNCSGLQGFLVFHSFGGGTGSGLGALLLERLNMEYGKKSNLQFSVYPAPQVSTSVVEPYNSVLTTHATLDNSDCTFMVDNEACYDICRRNLDIERPTYENLNRLIAQVVSSITASLRFAGSLNVDLNEFQTNLVPYPRIHFPLVTYSPIVSAAKAFHESNSVQEITNQCFEPYNQMVKCDPRTGRYMATC... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; nuclear division [GO:0000280]; nuclear migration by microtubule mediated pushing forces [GO:0098863] | astral microtubule [GO:0000235]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; spindle [GO:0005819] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P04689 | TBA2_SCHPO | MREIISIHVGQAGTQIGNACWELYCLEHGIQPNGYMNPETASQNSDGGFSTFFSETGQGKYVPRSIYVDLEPNVIDQVRTGPYRDLFHPEQLITGKEDASNNYARGHYTVGKELVDEVTDKIRRIADNCSGLQGFLVFHSFGGGTGSGFGALLLERLAMEYTKKSKLQFSVYPAPQVSTSVVEPYNSVLTTHATLDLADCTFMVDNESCYDICRRNLDIERPSYENLNRLIAQVVSSITASLRFEGSLNVDLAEFQTNLVPYPRIHFPLVTYAPIVSAAKAFHESNSVQEITNQCFEPYNQMVKCDPRAGRYMATCLLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | cytoplasmic microtubule organization [GO:0031122]; microtubule cytoskeleton organization [GO:0000226]; mitochondrion distribution [GO:0048311]; mitotic cell cycle [GO:0000278]; mitotic spindle organization [GO:0007052]; nuclear division [GO:0000280]; nuclear migration by microtubule mediated pushing forces [GO:0098863] | astral microtubule [GO:0000235]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle microtubule [GO:0005876] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P04692 | TPM1_RAT | MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI | null | null | actin filament capping [GO:0051693]; actin filament organization [GO:0007015]; cardiac muscle contraction [GO:0060048]; cellular response to reactive oxygen species [GO:0034614]; in utero embryonic development [GO:0001701]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; negative regulation of ce... | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; bleb [GO:0032059]; cytoplasm [GO:0005737]; myofibril [GO:0030016]; protein-containing complex [GO:0032991]; ruffle membrane [GO:0032587]; stress fiber [GO:0001725] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; cytoskeletal protein binding [GO:0008092]; disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00261; | 1.20.5.170;1.20.5.340; | Tropomyosin family | PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7568216}. Note=Associates with F-actin stress fibers (PubMed:7568216). {ECO:0000269|PubMed:7568216}. | null | null | null | null | null | FUNCTION: Binds to actin filaments in muscle and non-muscle cells (PubMed:22812662, PubMed:7568216). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:22812662). Smooth muscle contraction is regulated by interaction with... | Rattus norvegicus (Rat) |
P04693 | TYRB_ECOLI | MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNEDGIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIAPLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFPESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRFNDLLATLKTLPARSIVLLHPCCHNPTGADLTNDQWDAVIEILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPALVSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATVRRNYSSPPNFGAQVVAAVLNDEALKASWLAEVEEMRTRIL... | 2.6.1.107; 2.6.1.57 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | aspartate biosynthetic process [GO:0006532]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]; leucine biosynthetic process [GO:0009098]; tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate [GO:0019292] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | aromatic-amino-acid:2-oxoglutarate aminotransferase activity [GO:0008793]; identical protein binding [GO:0042802]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-phenylalanine:2-oxoglutarate aminotransferase activity [GO:0080130]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; pro... | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57; Evidence={ECO:0000269|PubMed:19731276}; CATALYTIC ACTIVITY: Reaction=(2S,3S)-3-methylphenylala... | null | PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from phenylpyruvate (ArAT route): step 1/1.; PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from (4-hydroxyphenyl)pyruvate: step 1/1. | null | null | FUNCTION: Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-m... | Escherichia coli (strain K12) |
P04694 | ATTY_RAT | MDSYVIQTDVDDSLSSVLDVHVNIGGRNSVQGRKKGRKARWDVRPSDMSNKTFNPIRAIVDNMKVQPNPNKTVISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGYLSSREEVASYYHCHEAPLEAKDVILTSGCSQAIELCLAVLANPGQNILIPRPGFSLYRTLAESMGIEVKLYNLLPEKSWEIDLKQLESLIDEKTACLVVNNPSNPCGSVFSKRHLQKILAVAERQCVPILADEIYGDMVFSDCKYEPLANLSTNVPILSCGGLAKRWLVPGWRLGWILIHDRRDIFGNEIRDGLVKLSQRILGPC... | 2.6.1.5 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:1682164, ECO:0000269|PubMed:2562840}; | 2-oxoglutarate metabolic process [GO:0006103]; amino acid metabolic process [GO:0006520]; biosynthetic process [GO:0009058]; glutamate metabolic process [GO:0006536]; L-phenylalanine catabolic process [GO:0006559]; response to dexamethasone [GO:0071548]; response to glucocorticoid [GO:0051384]; response to mercury ion ... | null | amino acid binding [GO:0016597]; identical protein binding [GO:0042802]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; pyridoxal phosphate binding [GO:0030170] | PF00155;PF07706; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5; Evidence={ECO:0000269|PubMed:1682164}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.2 mM for tyrosine {ECO:0000269|PubMed:1682164}; | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 2/6. | null | null | FUNCTION: Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine. {ECO:0000269|PubMed:1682164}. | Rattus norvegicus (Rat) |
P04695 | GNAT1_BOVIN | MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMT... | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; detection of light stimulus involved in visual perception [GO:0050908]; negative regulation of cyclic-nucleotide phosphodiesterase activity [GO:0051344]; phototransduction [GO:0007602]; phototransduction, visible light [GO:0007603];... | cytoplasm [GO:0005737]; G protein-coupled receptor complex [GO:0097648]; heterotrimeric G-protein complex [GO:0005834]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment membrane [GO:0042622] | acyl binding [GO:0000035]; G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901] | PF00503; | 1.10.400.10;3.40.50.300; | null | null | SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:23303210}. Membrane {ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:28655769}; Peripheral membrane protein {ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:28655769}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P20612... | null | null | null | null | null | FUNCTION: Functions as a signal transducer for the rod photoreceptor RHO (PubMed:21285355, PubMed:23303210, PubMed:28655769, PubMed:8259210). Required for normal RHO-mediated light perception by the retina (By similarity). Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-... | Bos taurus (Bovine) |
P04696 | GNAT2_BOVIN | MGSGASAEDKELAKRSKELEKKLQEDADKEAKTVKLLLLGAGESGKSTIVKQMKIIHQDGYSPEECLEYKAIIYGNVLQSILAIIRAMPTLGIDYAEVSCVDNGRQLNNLADSIEEGTMPPELVEVIRKLWKDGGVQACFDRAAEYQLNDSASYYLNQLDRITAPDYLPNEQDVLRSRVKTTGIIETKFSVKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDDEVNRMHESLHLFNSICNHKFFAATSIVLFLNKKDLFEEKIKKVHLSICFPEYDGNNSYEDAGNYIKSQFLDLNMRKDVKEIY... | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; visual perception [GO:0007601] | cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; photoreceptor outer segment membrane [GO:0042622] | G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | null | SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P50149}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P50149}. Note=Localizes mainly in the outer segment in the dark-adapted state, whereas is translocated to the inner part of the photoreceptors in the light-adapte... | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase. {ECO:0000269|PubMed:6586721}... | Bos taurus (Bovine) |
P04710 | ADT1_YEAST | MSHTETQTQQSHFGVDFLMGGVSAAIAKTGAAPIERVKLLMQNQEEMLKQGSLDTRYKGILDCFKRTATHEGIVSFWRGNTANVLRYFPTQALNFAFKDKIKSLLSYDRERDGYAKWFAGNLFSGGAAGGLSLLFVYSLDYARTRLAADARGSKSTSQRQFNGLLDVYKKTLKTDGLLGLYRGFVPSVLGIIVYRGLYFGLYDSFKPVLLTGALEGSFVASFLLGWVITMGASTASYPLDTVRRRMMMTSGQTIKYDGALDCLRKIVQKEGAYSLFKGCGANIFRGVAAAGVISLYDQLQLIMFGKKFK | null | null | aerobic respiration [GO:0009060]; heme biosynthetic process [GO:0006783]; heme transport [GO:0015886]; mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; mitochondrial transport [GO:0006839]; negative regulation of mitochondrial outer membrane permeabilizatio... | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739] | ATP:ADP antiporter activity [GO:0005471] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P18239}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:2167309}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; Evidence={ECO:0000269|PubMed:2167309}; | null | null | null | null | FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:2167309). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04711 | CAPP1_MAIZE | MASTKAPGPGEKHHSIDAQLRQLVPGKVSEDDKLIEYDALLVDRFLNILQDLHGPSLREFVQECYEVSADYEGKGDTTKLGELGAKLTGLAPADAILVASSILHMLNLANLAEEVQIAHRRRNSKLKKGGFADEGSATTESDIEETLKRLVSEVGKSPEEVFEALKNQTVDLVFTAHPTQSARRSLLQKNARIRNCLTQLNAKDITDDDKQELDEALQREIQAAFRTDEIRRAQPTPQAEMRYGMSYIHETVWKGVPKFLRRVDTALKNIGINERLPYNVSLIRFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAANLYI... | 4.1.1.31 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | carbon fixation [GO:0015977]; leaf development [GO:0048366]; photosynthesis [GO:0015979]; response to ammonium ion [GO:0060359]; response to cytokinin [GO:0009735]; response to nitrate [GO:0010167]; tricarboxylic acid cycle [GO:0006099] | apoplast [GO:0048046]; chloroplast [GO:0009507]; cytosol [GO:0005829] | phosphoenolpyruvate carboxylase activity [GO:0008964] | PF00311; | 1.20.1440.90; | PEPCase type 1 family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31; | null | PATHWAY: Photosynthesis; C4 acid pathway. | null | null | FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. | Zea mays (Maize) |
P04717 | RBL_PEA | MSPQTETKAKVGFKAGVKDYKLTYYTPDYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYEIEPVPGEDNQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPYAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMLKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRL... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01338}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338}; | photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253] | chloroplast [GO:0009507] | magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type I subfamily | PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000250|UniProtKB:P11383}. | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_01338}. | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:23295478, ECO:0000305... | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (Prob... | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
P04718 | RBL2_RHORU | MDQSSRYVNLALKEEDLIAGGEHVLCAYIMKPKAGYGYVATAAHFAAESSTGTNVEVCTTDDFTRGVDALVYEVDEARELTKIAYPVALFHRNITDGKAMIASFLTLTMGNNQGMGDVEYAKMHDFYVPEAYRALFDGPSVNISALWKVLGRPEVDGGLVVGTIIKPKLGLRPKPFAEACHAFWLGGDFIKNDEPQGNQPFAPLRDTIALVADAMRRAQDETGEAKLFSANITADDPFEIIARGEYVLETFGENASHVALLVDGYVAGAAAITTARRRFPDNFLHYHRAGHGAVTSPQSKRGYTAFVHCKMARLQGASGI... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4}; | reductive pentose-phosphate cycle [GO:0019253] | null | magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type II subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglyce... | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. | Rhodospirillum rubrum |
P04731 | MT1A_HUMAN | MDPNCSCATGGSCTCTGSCKCKECKCTSCKKSCCSCCPMSCAKCAQGCICKGASEKCSCCA | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of growth [GO:0045926] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; zinc ion binding [GO:0008270] | PF00131; | 4.10.10.10; | Metallothionein superfamily, Type 1 family | null | null | null | null | null | null | null | FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. | Homo sapiens (Human) |
P04732 | MT1E_HUMAN | MDPNCSCATGGSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCVCKGASEKCSCCA | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of growth [GO:0045926] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; zinc ion binding [GO:0008270] | PF00131; | 4.10.10.10; | Metallothionein superfamily, Type 1 family | null | null | null | null | null | null | null | FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. | Homo sapiens (Human) |
P04733 | MT1F_HUMAN | MDPNCSCAAGVSCTCAGSCKCKECKCTSCKKSCCSCCPVGCSKCAQGCVCKGASEKCSCCD | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of growth [GO:0045926] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; zinc ion binding [GO:0008270] | PF00131; | 4.10.10.10; | Metallothionein superfamily, Type 1 family | null | null | null | null | null | null | null | FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. | Homo sapiens (Human) |
P04737 | PIL1_ECOLI | MNAVLSVQGASAPVKKKSFFSKFTRLNMLRLARAVIPAAVLMMFFPQLAMAAGSSGQDLMASGNTTVKATFGKDSSVVKWVVLAEVLVGAVMYMMTKNVKFLAGFAIISVFIAVGMAVVGL | null | null | null | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | null | PF05513; | null | TraA family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1464628}; Multi-pass membrane protein {ECO:0000269|PubMed:1464628}. Secreted {ECO:0000269|PubMed:1464628}. Note=Propilin is directed to the inner membrane, where it is cleaved and acetylated. Mature pilin forms filaments that are secreted to form the conjuga... | null | null | null | null | null | FUNCTION: Propilin is the precursor of the pilus subunit, pilin, that forms conjugative pili, the filamentous surface appendages required for cell-to-cell contact during the earlier stages of bacterial conjugation, and that retract after contact is established. Mature pilin is assembled with the help of TraQ and TraX (... | Escherichia coli (strain K12) |
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