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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P06732 | KCRM_HUMAN | MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTGVDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDDLDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMTEKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISMEKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLAHLSKHPKFEEILTRLRLQKR... | 2.7.3.2 | null | phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310] | cytosol [GO:0005829]; extracellular space [GO:0005615] | ATP binding [GO:0005524]; creatine kinase activity [GO:0004111] | PF00217;PF02807; | 1.10.135.10;3.30.590.10; | ATP:guanido phosphotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; Evidence={ECO:0000250|UniProtKB:P00563, ECO:0000255|PROSITE-ProRule:PRU10029}; | null | null | null | null | FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. {ECO:0000250|UniProtKB:P... | Homo sapiens (Human) |
P06733 | ENOA_HUMAN | MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDL... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18560153}; Note=Binds two Mg(2+) per subunit. Required for catalysis and for stabilizing the dimer. {ECO:0000269|PubMed:18560153}; | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway [GO:1903298]; negative regulati... | cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; M band [GO:0031430]; membrane [GO:0016020]; nuclear outer membrane [GO:0005640]; nucleus [GO:0005634]; phosphopyruvate hydratase complex [GO:0000015]; ... | cadherin binding [GO:0045296]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; GTPase binding [GO:0051020]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; RNA polymerase... | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | PTM: ISGylated. {ECO:0000269|PubMed:16139798, ECO:0000269|PubMed:16815975}.; PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the phosphopyruvate hydratase activity. {ECO:0000269|PubMed:29775581}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10802057}. Cell membrane {ECO:0000269|PubMed:10802057}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:10802057}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to... | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:29775581}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000305|PubMed:1369209}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Enolase activity is lost above pH 9.0. Immunoglobulin production stimulating activity is retained at pH 13.0. {ECO:0000269|PubMed:1369209}; | null | FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:1369209, PubMed:29775581). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:297... | Homo sapiens (Human) |
P06734 | FCER2_HUMAN | MEEGQYSEIEELPRRRCCRRGTQIVLLGLVTAALWAGLLTLLLLWHWDTTQSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLH... | null | null | B cell antigen processing and presentation [GO:0002450]; Fc receptor-mediated immune complex endocytosis [GO:0160006]; immune response [GO:0006955]; macrophage activation [GO:0042116]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of killing of c... | external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; IgE binding [GO:0019863]; integrin binding [GO:0005178]; low-affinity IgE receptor activity [GO:0019769]; metal ion binding [GO:0046872] | PF00059; | 3.10.100.10; | null | PTM: N- and O-glycosylated.; PTM: The secreted form sCD23 is produced by ADAM10-mediated ectodomain shedding. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor. Secreted {ECO:0000269|PubMed:37453717}. Note=Also exists as a soluble excreted form, sCD23. | null | null | null | null | null | FUNCTION: Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B cells. On B cells, initiates IgE-dependent antigen uptake and presentation to T cells (PubMed:2167225). On macrophages, upon IgE binding and antigen cross-link... | Homo sapiens (Human) |
P06736 | HLYC_ECOLX | MNINKPLEILGHVSWLWASSPLHRNWPVSLFAINVLPAIQANQYVLLTRDDYPVAYCSWANLSLENEIKYLNDVTSLVAEDWTSGDRKWFIDWIAPFGDNGALYKYMRKKFPDELFRAIRVDPKTHVGKVSEFHGGKIDKQLANKIFKQYHHELITEVKRKSDFNFSLTG | 2.3.1.- | null | killing of cells of another organism [GO:0031640]; toxin metabolic process [GO:0009404] | cytoplasm [GO:0005737] | ACP-dependent peptidyl-lysine N6-myristoyltransferase activity [GO:0140769]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; peptidyl-lysine N6-myristoyltransferase activity [GO:0018030] | PF02794; | null | RTX toxin acyltransferase family | PTM: Proteolytically cleaved by the protease systems ClpAP, ClpXP and FtsH, leading to its degradation. {ECO:0000269|PubMed:11278516}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-tetradecanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:70611, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15437, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for tetradecanoyl-CoA {ECO:0000269|PubMed:11695909}; KM=3.6 uM for HlyA peptide {ECO:0000269|PubMed:11695909}; Vmax=4667 pmol/min/mg enzyme {ECO:0000269|PubMed:11695909}; | null | null | null | FUNCTION: Protein-lysine myristoyltransferase that catalyzes myristoylation of the protoxin (HlyA) at two internal lysine residues, thereby converting it to the active toxin. {ECO:0000269|PubMed:10079090, ECO:0000269|PubMed:10413532, ECO:0000269|PubMed:11278516, ECO:0000269|PubMed:11695909, ECO:0000269|PubMed:15065878,... | Escherichia coli |
P06737 | PYGL_HUMAN | MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFGST... | 2.4.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:10980448, ECO:0000269|PubMed:12204691, ECO:0007744|PDB:1EM6, ECO:0007744|PDB:1EXV, ECO:0007744|PDB:1FA9, ECO:0007744|PDB:1FC0, ECO:0007744|PDB:1L5Q, ECO:0007744|PDB:1L5R, ECO:0007744|PDB:1L5S, ECO:0... | 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; glucose homeostasis [GO:0042593]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; necroptotic process [GO:0070266]; response to bacterium [GO:0009617] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; secretory granule lumen [GO:0034774] | AMP binding [GO:0016208]; ATP binding [GO:0005524]; bile acid binding [GO:0032052]; glucose binding [GO:0005536]; glycogen phosphorylase activity [GO:0008184]; identical protein binding [GO:0042802]; linear malto-oligosaccharide phosphorylase activity [GO:0102250]; purine nucleobase binding [GO:0002060]; pyridoxal phos... | PF00343; | 3.40.50.2000; | Glycogen phosphorylase family | PTM: Acetylation, which is up-regulated by glucose and insulin and down-regulated by glucagon, inhibits the glycogen phosphorylase activity by promoting PPP1R3B-mediated recruitment of phosphatase PP1 and Ser-15 dephosphorylation. {ECO:0000269|PubMed:22225877}.; PTM: Phosphorylation at Ser-15 converts inactive phosphor... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:22225877}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; Evidence={ECO:0000269|PubMed:22225877}; Physiological... | null | null | null | null | FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. {ECO:0000269|PubMed:22225877}. | Homo sapiens (Human) |
P06738 | PHSG_YEAST | MPPASTSTTNDMITEEPTSPHQIPRLTRRLTGFLPQEIKSIDTMIPLKSRALWNKHQVKKFNKAEDFQDRFIDHVETTLARSLYNCDDMAAYEAASMSIRDNLVIDWNKTQQKFTTRDPKRVYYLSLEFLMGRALDNALINMKIEDPEDPAASKGKPREMIKGALDDLGFKLEDVLDQEPDAGLGNGGLGRLAACFVDSMATEGIPAWGYGLRYEYGIFAQKIIDGYQVETPDYWLNSGNPWEIERNEVQIPVTFYGYVDRPEGGKTTLSASQWIGGERVLAVAYDFPVPGFKTSNVNNLRLWQARPTTEFDFAKFNNGD... | 2.4.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | glycogen catabolic process [GO:0005980] | cytoplasm [GO:0005737] | glycogen phosphorylase activity [GO:0008184]; linear malto-oligosaccharide phosphorylase activity [GO:0102250]; pyridoxal phosphate binding [GO:0030170]; SHG alpha-glucan phosphorylase activity [GO:0102499] | PF00343; | 3.40.50.2000; | Glycogen phosphorylase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24146988}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; | null | null | null | null | FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06744 | G6PI_HUMAN | MAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLL... | 5.3.1.9 | null | carbohydrate metabolic process [GO:0005975]; erythrocyte homeostasis [GO:0034101]; gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glucose homeostasis [GO:0042593]; glycolytic process [GO:0006096]; hemostasis [GO:0007599]; humoral immune response [GO:0006959]; in utero embryonic develo... | ciliary membrane [GO:0060170]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; secretory granule lumen [GO:0034774] | carbohydrate derivative binding [GO:0097367]; cytokine activity [GO:0005125]; glucose-6-phosphate isomerase activity [GO:0004347]; growth factor activity [GO:0008083]; monosaccharide binding [GO:0048029]; ubiquitin protein ligase binding [GO:0031625] | PF00342; | 1.10.1390.10; | GPI family | PTM: Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway. {ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:15637053}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11437381}. Secreted {ECO:0000269|PubMed:11437381}. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; Evidence={ECO:0000269|PubMed:28803808}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000269|PubMed:28803808}. | null | null | FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimu... | Homo sapiens (Human) |
P06745 | G6PI_MOUSE | MAALTRNPQFQKLLEWHRANSANLKLRELFEADPERFNNFSLNLNTNHGHILVDYSKNLVNKEVMQMLVELAKSRGVEAARDNMFSGSKINYTENRAVLHVALRNRSNTPIKVDGKDVMPEVNRVLDKMKSFCQRVRSGDWKGYTGKSITDIINIGIGGSDLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLASLSPETSLFIIASKTFTTQETITNAETAKEWFLEAAKDPSAVAKHFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDHFEQLLSGAHWMDQHFLKTPLEKNAPVLL... | 5.3.1.9 | null | canonical glycolysis [GO:0061621]; erythrocyte homeostasis [GO:0034101]; fructose 6-phosphate metabolic process [GO:0006002]; gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glucose homeostasis [GO:0042593]; glycolytic process [GO:0006096]; glycolytic process through glucose-6-phosphat... | ciliary membrane [GO:0060170]; cytosol [GO:0005829]; extracellular space [GO:0005615]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886] | carbohydrate derivative binding [GO:0097367]; cytokine activity [GO:0005125]; glucose-6-phosphate isomerase activity [GO:0004347]; growth factor activity [GO:0008083]; monosaccharide binding [GO:0048029]; ubiquitin protein ligase binding [GO:0031625] | PF00342; | 1.10.1390.10; | GPI family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06744}. Secreted {ECO:0000250|UniProtKB:P06744}. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; Evidence={ECO:0000269|PubMed:2344351, ECO:0000269|PubMed:8417789}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000269|PubMed:2344351, ECO:0000269|PubMed:7277315, ECO:0000269|PubMed:8417789}. | null | null | FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:2344351, PubMed:7277315, PubMed:8417789). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an ang... | Mus musculus (Mouse) |
P06746 | DPOLB_HUMAN | MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIF... | 2.7.7.7; 4.2.99.-; 4.2.99.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9287163}; Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:9287163}; | base-excision repair [GO:0006284]; base-excision repair, gap-filling [GO:0006287]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA-templated DNA replication [GO:0006261]; double-strand break repair via nonhomologous end joining [GO:0006303]; homeostasis of number of cells [GO:0048872]; immunoglobulin hea... | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spindle microtubule [GO:0005876] | 5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; DNA-directed DNA polymerase activity [GO:0003887]; enzyme binding [GO:0019899]... | PF14792;PF14791;PF10391;PF14716; | 1.10.150.20;3.30.460.10;1.10.150.110;3.30.210.10; | DNA polymerase type-X family | PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. {ECO:0000269|PubMed:16600869}.; PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. | 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; CATALYTIC ACTIVITY: Reaction=a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 uM for DNA with an intact AP site {ECO:0000269|PubMed:9614142}; KM=0.5 uM for DNA with a preincised AP site {ECO:0000269|PubMed:9614142}; Note=kcat is 0.075 sec(-1) for 5'-deoxyribose-phosphate lyase activity (at pH 7.0 and 37 degrees Celsius) (PubMed:9614142).... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9 for 5'-deoxyribose-phosphate lyase activity. {ECO:0000269|PubMed:9614142}; | null | FUNCTION: Repair polymerase that plays a key role in base-excision repair (PubMed:10556592, PubMed:9207062, PubMed:9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxy... | Homo sapiens (Human) |
P06747 | PHOSP_RABVP | MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDNLPEDMGRLHLDDGKSPNPGEMAKVGEGKYREDFQMDEGEDPSLLFQSYLDNVGVQIVRQIRSGERFLKIWSQTVEEIISYVAVNFPNPPGKSSEDKSTQTTGRELKKETTPTPSQRESQSSKARMAAQTASGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGILLYNFEQLKMNLDDIVKEAKNVPGVTRLARDGSKLPLRCVLGWVALANSKKFQLLVESNKLSKIMQDDLNRYTSC | null | null | microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity [GO:0039723]; symbiont-mediated suppression of host J... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | RNA-dependent RNA polymerase activity [GO:0003968] | PF03012; | 6.10.140.1560;1.20.120.820; | Lyssavirus protein P family | PTM: Phosphorylated by host PKC and by an unknown kinase. {ECO:0000250}. | SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P4]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P5]: Host nuc... | null | null | null | null | null | FUNCTION: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by bin... | Rabies virus (strain Pasteur vaccins / PV) (RABV) |
P06748 | NPM_HUMAN | MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL | null | null | cellular response to UV [GO:0034644]; cellular senescence [GO:0090398]; centrosome cycle [GO:0007098]; chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; intracellular protein transport [GO:0006886]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; granular component [GO:0001652]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]; ribonucleoprotein... | chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription factor binding [GO:0140297]; histone binding [GO:0042393]; NF-kappaB binding [GO:0051059]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein kinase inhibitor act... | PF16276;PF03066; | 1.10.10.2100;2.60.120.340; | Nucleoplasmin family | PTM: Acetylated at C-terminal lysine residues, thereby increasing affinity to histones. {ECO:0000269|PubMed:16107701, ECO:0000269|Ref.17}.; PTM: ADP-ribosylated.; PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 by PLK2 in S phase is required for centriole duplication and is sufficient to trigger... | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25818168, ECO:0000269|PubMed:25956029}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25818168}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Genera... | null | null | null | null | null | FUNCTION: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein s... | Homo sapiens (Human) |
P06750 | AGGL_RICCO | MYAVATWLCFGSTSGWSFTLEDNNIFPKQYPIINFTTADATVESYTNFIRAVRSHLTTGADVRHEIPVLPNRVGLPISQRFILVELSNHAELSVTLALDVTNAYVVGCRAGNSAYFFHPDNQEDAEAITHLFTDVQNSFTFAFGGNYDRLEQLGGLRENIELGTGPLEDAISALYYYSTCGTQIPTLARSFMVCIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFNVYDVSILIPIIALMVYRCAPPPSSQFSLLIRPVVPNFNADVCMDPEPIVRIVGRNG... | 3.2.2.22 | null | defense response [GO:0006952]; negative regulation of translation [GO:0017148] | endoplasmic reticulum [GO:0005783] | carbohydrate binding [GO:0030246]; nucleotide binding [GO:0000166]; rRNA N-glycosylase activity [GO:0030598]; toxin activity [GO:0090729] | PF00652;PF00161; | 2.80.10.50;3.40.420.10;4.10.470.10; | Ribosome-inactivating protein family, Type 2 RIP subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22; | null | null | null | null | null | Ricinus communis (Castor bean) |
P06752 | ENV_FLVSA | MESPTHPKPSKDKTFPWNLVFLVGILFQIDMGMANPSPHQVYNVTWVITNVQTNSRANATSMLGTLTDAYPTLYVDLCDLVGDTWEPIAPDPRSWARYSSSTHGCKTTDRKKQQQTYPFYVCPGHAPSMGPKGTYCGGAQDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSNQDNSCKGKCNPLVLQFTQKGRQASWDRPKMWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQTKSKVTTQRPQITSSTPRSVASATMGPKRIGTGDRLINLVQGTYLALNATDPNKTKDCWLCLVSRPPYY... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: 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}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Feline leukemia virus (strain C/Sarma) |
P06753 | TPM3_HUMAN | MMEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI | null | null | actin filament organization [GO:0007015]; muscle contraction [GO:0006936] | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; muscle thin filament tropomyosin [GO:0005862]; stress fiber [GO:0001725] | actin filament binding [GO:0051015] | PF00261; | 1.20.5.170;1.20.5.340; | Tropomyosin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. | null | null | null | null | null | FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in sta... | Homo sapiens (Human) |
P06754 | TPM1_DROME | MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNKKKTTKMTTSIPQGTLLDVLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKER... | null | null | actin filament organization [GO:0007015]; dendrite morphogenesis [GO:0048813]; mitotic cytokinesis [GO:0000281]; muscle contraction [GO:0006936]; oogenesis [GO:0048477]; pole plasm assembly [GO:0007315]; pole plasm oskar mRNA localization [GO:0045451]; regulation of lamellipodium assembly [GO:0010591]; response to hype... | actin filament [GO:0005884]; actomyosin contractile ring [GO:0005826]; cytosol [GO:0005829]; investment cone [GO:0070865]; sarcomere [GO:0030017] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; protein kinase binding [GO:0019901] | PF00261; | 1.20.5.170;1.20.5.340; | Tropomyosin family | null | SUBCELLULAR LOCATION: [Isoform 9A]: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | Drosophila melanogaster (Fruit fly) |
P06756 | ITAV_HUMAN | MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDY... | null | null | angiogenesis [GO:0001525]; apolipoprotein A-I-mediated signaling pathway [GO:0038027]; apoptotic cell clearance [GO:0043277]; calcium ion transmembrane transport [GO:0070588]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-... | alphav-beta3 integrin-HMGB1 complex [GO:0035868]; alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; alphav-beta3 integrin-PKCalpha complex [GO:0035866]; cell surface [GO:0009986]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; filopodium membrane [GO:00315... | coreceptor activity [GO:0015026]; extracellular matrix binding [GO:0050840]; extracellular matrix protein binding [GO:1990430]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; opsonin binding [GO:0001846]; protease binding [GO:0002020]; protein kinase C binding [GO:00050... | PF01839;PF08441;PF20805;PF20806;PF00357; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}. | null | null | null | null | null | FUNCTION: The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may... | Homo sapiens (Human) |
P06757 | ADH1_RAT | MSTAGKVIKCKAAVLWEPHKPFTIEDIEVAPPKAHEVRIKMVATGVCRSDDHAVSGSLFTPLPAVLGHEGAGIVESIGEGVTCVKPGDKVIPLFSPQCGKCRICKHPESNLCCQTKNLTQPKGALLDGTSRFSCRGKPIHHFISTSTFSQYTVVDDIAVAKIDAAAPLDKVCLIGCGFSTGYGSAVQVAKVTPGSTCAVFGLGGVGLSVVIGCKTAGAAKIIAVDINKDKFAKAKELGATDCINPQDYTKPIQEVLQEMTDGGVDFSFEVIGRLDTMTSALLSCHSACGVSVIVGVPPSAQSLSVNPMSLLLGRTWKGAI... | 1.1.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | acetaldehyde biosynthetic process [GO:0046186]; animal organ regeneration [GO:0031100]; behavioral response to ethanol [GO:0048149]; ethanol catabolic process [GO:0006068]; ethanol oxidation [GO:0006069]; response to progesterone [GO:0032570]; response to retinoic acid [GO:0032526]; response to steroid hormone [GO:0048... | cytosol [GO:0005829]; mitochondrion [GO:0005739] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; ethanol binding [GO:0035276]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NAD-retinol dehydrogenase activity [GO:0004745]; organic cyclic compound binding [GO:0097159]; zinc ion binding... | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Class-I subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ... | null | null | null | null | null | Rattus norvegicus (Rat) |
P06759 | APOC3_RAT | MQPRMLLIVALVALLASARADEGEGSLLLGSMQGYMEQASKTVQDALSSMQESDIAVVASRGWMDNRFKSLKGYWSKFTDKFTGLWESGPEDQLTTPTLEP | null | null | cellular response to glucose stimulus [GO:0071333]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance [GO:0034382]; G protein-coupled receptor signaling pathway [GO:0007186]; high-density lipoprotein particle remodeling [GO:0... | chylomicron [GO:0042627]; extracellular space [GO:0005615]; intermediate-density lipoprotein particle [GO:0034363]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | enzyme regulator activity [GO:0030234]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; lipid transporter activity [GO:0005319]; phospholipid binding [GO:0005543] | PF05778; | 6.10.90.10; | Apolipoprotein C3 family | PTM: The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-96 with a core 1 o... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}. | null | null | null | null | null | FUNCTION: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and ... | Rattus norvegicus (Rat) |
P06760 | BGLR_RAT | MSPRRSVCWFVLGQLLCSCAVALQGGMLFPKETPSRELKVLDGLWSFRADYSNNRLQGFEKQWYRQPLRESGPTLDMPVPSSFNDITQEAELRNFIGWVWYEREAVLPQRWTQDTDRRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADITKLVQSGPLTTFRVTIAINNTLTPYTLPPGTIVYKTDPSMYPKGYFVQDISFDFFNYAGLHRSVVLYTTPTTYIDDITVTTDVDRDVGLVNYWISVQGSDHFQLEVRLLDEDGKIVARGTGNEGQLKVPRAHLWWPYLMHEHPAYLYSLEVTMTTPESVSDFYTLPV... | 3.2.1.31 | null | carbohydrate metabolic process [GO:0005975]; chondroitin sulfate catabolic process [GO:0030207]; glucuronoside catabolic process [GO:0019391]; heparan sulfate proteoglycan catabolic process [GO:0030200]; hyaluronan catabolic process [GO:0030214] | extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764] | beta-glucuronidase activity [GO:0004566]; carbohydrate binding [GO:0030246]; hydrolase activity [GO:0016787]; protein domain specific binding [GO:0019904]; signaling receptor binding [GO:0005102] | PF00703;PF02836;PF02837; | 2.60.120.260;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 2 family | PTM: Undergoes a post-transcriptional proteolytic cleavage near its C-terminal end, which reduces its size by approximately 3 kDa. The site of this cleavage has as yet not been determined. | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31; Evidence={ECO:0000305|PubMed:3355537}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17634; Evidence={ECO:0000305|... | null | null | null | null | FUNCTION: Plays an important role in the degradation of dermatan and keratan sulfates. | Rattus norvegicus (Rat) |
P06761 | BIP_RAT | MKFTVVAAALLLLCAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSE... | 3.6.4.10 | null | cellular response to antibiotic [GO:0071236]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular response to gamma radiation [GO:0071480]; cellular response to glucose starvation [GO:0042149]; cellular response to interleukin-4 [GO:0071353]; cellular response to manganese io... | cell surface [GO:0009986]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; endoplasm... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; misfolded protein binding [GO:0051787]; protein domain specific binding [GO:0019904]; protein folding chaperone [GO:0044183]; riboso... | PF00012; | 1.20.1270.10;3.30.420.40; | Heat shock protein 70 family | PTM: In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins. In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activi... | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}. Melanosome {ECO:0000250|UniProtKB:P11021}. Cytoplasm {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epi... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:G3I8R9}; | null | null | null | null | FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC... | Rattus norvegicus (Rat) |
P06762 | HMOX1_RAT | MERPQLDSMSQDLSEALKEATKEVHIRAENSEFMRNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTPATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQALLTEEHKDQSPSQTEFLRQRPASLVQDTTSAETPRGKSQISTSSSQTPLLRWVLTLSFLLATVAVGIYAM | 1.14.14.18 | null | angiogenesis [GO:0001525]; cellular response to arsenic-containing substance [GO:0071243]; cellular response to cadmium ion [GO:0071276]; cellular response to cisplatin [GO:0072719]; cellular response to heat [GO:0034605]; cellular response to hypoxia [GO:0071456]; cellular response to nutrient [GO:0031670]; epithelial... | caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | arachidonic acid omega-hydroxylase activity [GO:0052869]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phospholipase D activity [GO:0004630]; protein homodimerization activity [GO:00428... | PF01126; | 1.20.910.10; | Heme oxygenase family | PTM: A soluble form arises by proteolytic removal of the membrane anchor. {ECO:0000305|PubMed:1935972}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:3865203}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. | CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:1724... | null | null | null | null | FUNCTION: [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:1575508, PubMed:1935972, PubMed:3865203). Affords protection against programm... | Rattus norvegicus (Rat) |
P06765 | PLF4_RAT | MSAAAVFRGLRPSPELLLLGLLLLPAVVAVTRASPEESDGDLSCVCVKTSSSRIHLKRITSLEVIKAGPHCAVPQLIATLKNGSKICLDRQVPLYKKIIKKLLES | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; cytokine-mediated signaling pathway [GO:0... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; platelet alpha granule [GO:0031091]; protein-containing complex [GO:0032991]; vesicle [GO:0031982] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; heparin binding [GO:0008201] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is modified with sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:8033893}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Chemokine released during platelet aggregation that plays a role in different biological processes including hematopoiesis, cell proliferation, differentiation, and activation. Acts via different functional receptors including CCR1, CXCR3A or CXCR3B. Upon interaction with CXCR3A receptor, induces activated T-... | Rattus norvegicus (Rat) |
P06766 | DPOLB_RAT | MSKRKAPQETLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEVKKLDPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIF... | 2.7.7.7; 4.2.99.-; 4.2.99.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P06746}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:P06746}; | apoptotic process [GO:0006915]; base-excision repair [GO:0006284]; base-excision repair, gap-filling [GO:0006287]; DNA damage response [GO:0006974]; DNA replication [GO:0006260]; double-strand break repair via nonhomologous end joining [GO:0006303]; homeostasis of number of cells [GO:0048872]; immunoglobulin heavy chai... | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spindle microtubule [GO:0005876] | 5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; enzyme binding [GO:0019899]; lyase activity [GO:0016829]; metal ion bindi... | PF14792;PF14791;PF10391;PF14716; | 1.10.150.20;3.30.460.10;1.10.150.110;3.30.210.10; | DNA polymerase type-X family | PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. {ECO:0000250}.; PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. {ECO:0000250|UniProtKB:P06746}. | 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:0000250|UniProtKB:P06746}; CATALYTIC ACTIVITY: Reaction=a 5'-end ... | null | null | null | null | FUNCTION: Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site actin... | Rattus norvegicus (Rat) |
P06767 | TKN1_RAT | MKILVAVAVFFLVSTQLFAEEIGANDDLNYWSDWSDSDQIKEAMPEPFEHLLQRIARRPKPQQFFGLMGKRDADSSIEKQVALLKALYGHGQISHKRHKTDSFVGLMGKRALNSVAYERSAMQNYERRRK | null | null | associative learning [GO:0008306]; cellular response to nerve growth factor stimulus [GO:1990090]; chemical synaptic transmission [GO:0007268]; inflammatory response [GO:0006954]; long-term memory [GO:0007616]; negative regulation of heart rate [GO:0010459]; neuropeptide signaling pathway [GO:0007218]; positive regulat... | axon [GO:0030424]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; synapse [GO:0045202] | substance K receptor binding [GO:0031837]; substance P receptor binding [GO:0031835] | PF02202; | null | Tachykinin family | PTM: [Substance P]: The substance P form is cleaved at Pro-59 by the prolyl endopeptidase FAP (seprase) activity (in vitro). Substance P is also cleaved and degraded by Angiotensin-converting enzyme (ACE) and neprilysin (MME). {ECO:0000250|UniProtKB:P20366}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. | Rattus norvegicus (Rat) |
P06774 | HAP2_YEAST | MSADETDAKFHPLETDLQSDTAAATSTAAASRSPSLQEKPIEMPLDMGKAPSPRGEDQRVTNEEDLFLFNRLRASQNRVMDSLEPQQQSQYTSSSVSTMEPSADFTSFSAVTTLPPPPHQQQQQQQQQQQQQQLVVQAQYTQNQPNLQSDVLGTAIAEQPFYVNAKQYYRILKRRYARAKLEEKLRISRERKPYLHESRHKHAMRRPRGEGGRFLTAAEIKAMKSKKSGASDDPDDSHEDKKITTKIIQEQPHATSTAAAADKKT | null | null | carbon catabolite activation of transcription from RNA polymerase II promoter [GO:0000436]; regulation of carbohydrate metabolic process [GO:0006109]; regulation of cellular respiration [GO:0043457]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | CCAAT-binding factor complex [GO:0016602]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981] | PF02045; | 6.10.250.2430; | NFYA/HAP2 subunit family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP2 has primarily a structural ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06777 | RAD1_YEAST | MSQLFYQGDSDDELQEELTRQTTQASQSSKIKNEDEPDDSNHLNEVENEDSKVLDDDAVLYPLIPNEPDDIETSKPNINDIRPVDIQLTLPLPFQQKVVENSLITEDALIIMGKGLGLLDIVANLLHVLATPTSINGQLKRALVLVLNAKPIDNVRIKEALEELSWFSNTGKDDDDTAVESDDELFERPFNVVTADSLSIEKRRKLYISGGILSITSRILIVDLLSGIVHPNRVTGMLVLNADSLRHNSNESFILEIYRSKNTWGFIKAFSEAPETFVMEFSPLRTKMKELRLKNVLLWPRFRVEVSSCLNATNKTSHNK... | null | null | DNA amplification [GO:0006277]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via single-strand annealing, removal of nonhomologous ends [GO:0000736]; meiotic mismatch repair [GO:0000710]; mitotic recombination [GO:0006312]; nucleotide-excision repair [GO:0006289]; nuc... | endonuclease complex [GO:1905348]; nucleotide-excision repair factor 1 complex [GO:0000110]; nucleus [GO:0005634] | damaged DNA binding [GO:0003684]; single-stranded DNA binding [GO:0003697]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014] | PF02732; | 3.40.50.10130;1.10.150.20; | XPF family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD10 forms an endonuclease that specifically degrades single-stranded DNA. {ECO:0000269|PubMed:8479526}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06778 | RAD52_YEAST | MNEIMDMDEKKPVFGNHSEDIQTKLDKKLGPEYISKRVGFGTSRIAYIEGWRVINLANQIFGYNGWSTEVKSVVIDFLDERQGKFSIGCTAIVRVTLTSGTYREDIGYGTVENERRKPAAFERAKKSAVTDALKRSLRGFGNALGNCLYDKDFLAKIDKVKFDPPDFDENNLFRPTDEISESSRTNTLHENQEQQQYPNKRRQLTKVTNTNPDSTKNLVKIENTVSRGTPMMAAPAEANSKNSSNKDTDLKSLDASKQDQDDLLDDSLMFSDDFQDDDLINMGNTNSNVLTTEKDPVVAKQSPTASSNPEAEQITFVTAK... | null | null | DNA amplification [GO:0006277]; DNA recombinase assembly [GO:0000730]; double-strand break repair via break-induced replication [GO:0000727]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via single-strand annealing [GO:0045002]; meiotic joint molecule formation [GO:00... | mitochondrion [GO:0005739]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634] | DNA strand exchange activity [GO:0000150]; DNA/DNA annealing activity [GO:1990814] | PF04098; | 3.30.390.80; | RAD52 family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06779 | RAD7_YEAST | MYRSRNRPKRGGENEVKGPNSALTQFLREEGISAENIKQKWYQRQSKKQEDATDEKKGKAEDDSFTAEISRVVEDEEIDEIGTGSGTETERAQVSYDARMKLVPADSDEEEYETSHISDTPVSLSSANDRESLTKKRQNTAKIIQNRRRKRKRAADLLDRRVNKVSSLQSLCITKISENISKWQKEADESSKLVFNKLRDVLGGVSTANLNNLAKALSKNRALNDHTLQLFLKTDLKRLTFSDCSKISFDGYKTLAIFSPHLTELSLQMCGQLNHESLLYIAEKLPNLKSLNLDGPFLINEDTWEKFFVIMKGRLEEFHI... | null | null | global genome nucleotide-excision repair [GO:0070911]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; protein localization [GO:0008104]; response to UV [GO:0009411]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; ubiquitin-dependent protein catabolic process [GO:... | Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; nucleotide-excision repair factor 4 complex [GO:0000113]; SCF ubiquitin ligase complex [GO:0019005] | null | null | 3.80.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. This protein is one of 10 proteins (RAD1, 2,3,4,7,10,14, 16,23 and MMS19) involved in excision repair of DNA damaged with UV light, bulky addu... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06780 | RHO1_YEAST | MSQQVGNSIRRKLVIVGDGACGKTCLLIVFSKGQFPEVYVPTVFENYVADVEVDGRRVELALWDTAGQEDYDRLRPLSYPDSNVVLICFSIDLPDSLENVQEKWIAEVLHFCQGVPIILVGCKVDLRNDPQTIEQLRQEGQQPVTSQEGQSVADQIGATGYYECSAKTGYGVREVFEAATRASLMGKSKTNGKAKKNTTEKKKKKCVLL | 3.6.5.2 | null | (1->3)-beta-D-glucan biosynthetic process [GO:0006075]; actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; ascospore wall assembly [GO:0030476]; budding cell bud growth [GO:0007117]; cellular bud neck septin ring organization [GO:0032186]; fungal-type cell wall biogenesis [GO:000927... | 1,3-beta-D-glucan synthase complex [GO:0000148]; cell periphery [GO:0071944]; cellular bud [GO:0005933]; cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endosome membrane [GO:0010008]; fungal-type cell wall [GO:0009277]; fungal-type vacuole membra... | G-protein beta-subunit binding [GO:0031681]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | null | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Endosome membrane; Lipid-anchor. Peroxisome membrane; Lipid-anchor. Note=Plasma membrane-associated at sites of polarized growth such as incipient bud sites, bud tips, the bud neck during cytokinesis, and the neck and tip of mating projections. Also found on internal m... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P61586}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Acts as a central regulator in the cell wall integrity signaling pathway, which is regulated by the cell cycle and in response to various types of cell wall stress. Integrates signals from different cell surface sensors, and activates a set of effectors, regulating processes including beta-glucan synthesis at... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06781 | RHO2_YEAST | MSEKAVRRKLVIIGDGACGKTSLLYVFTLGKFPEQYHPTVFENYVTDCRVDGIKVSLTLWDTAGQEEYERLRPFSYSKADIILIGFAVDNFESLINARTKWADEALRYCPDAPIVLVGLKKDLRQEAHFKENATDEMVPIEDAKQVARAIGAKKYMECSALTGEGVDDVFEVATRTSLLMKKEPGANCCIIL | 3.6.5.2 | null | actin filament organization [GO:0007015]; establishment of cell polarity [GO:0030010]; fungal-type cell wall organization [GO:0031505]; microtubule-based process [GO:0007017]; regulation of actin cytoskeleton organization [GO:0032956]; signal transduction [GO:0007165]; small GTPase-mediated signal transduction [GO:0007... | cell periphery [GO:0071944]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P61586}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06782 | SNF1_YEAST | MSSNNNTNTAPANANSSHHHHHHHHHHHHHGHGGSNSTLNNPKSSLADGAHIGNYQIVKTLGEGSFGKVKLAYHTTTGQKVALKIINKKVLAKSDMQGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRDKMSEQEARRFFQQIISAVEYCHRHKIVHRDLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYVMLCRRLPFDDESIPVLFKNISNGVYTLPKFLSPGAAGLIKRMLIVNPLNRISIHEIMQDDWFKVDLPEYLLPPDLK... | 2.7.11.1 | null | establishment of mitotic spindle orientation [GO:0000132]; filamentous growth [GO:0030447]; fungal-type cell wall assembly [GO:0071940]; intracellular signal transduction [GO:0035556]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of translation [GO:0017148]; phosphorylation [GO:00... | cellular bud neck septin ring [GO:0000144]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nuclear envelope lumen [GO:0005641]; nuclear membrane [GO:0031965]; nucleotide-activated protein kinase complex [GO:0031588]; nucleus [GO:0005634]; vacuolar membrane [GO:0005774] | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; molecular function activator activity [GO:0140677]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein se... | PF16579;PF00069;PF08587; | 1.10.8.10;3.30.310.80;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily | PTM: Phosphorylation at Thr-210 in response to glucose limitation leads to activation of kinase activity (PubMed:11486005, PubMed:12748292). ADP, but not AMP, protects the enzyme from dephosphorylation at Thr-210 by GLC7 (PubMed:22019086). {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:22019086}.; PTM: Sumoylation by... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25869125}. Nucleus {ECO:0000269|PubMed:25869125}. Nucleus membrane {ECO:0000269|PubMed:17237508}; Peripheral membrane protein {ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions (PubMed:25869125). {ECO:0000... | 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:15719021, ECO:000026... | null | null | null | null | FUNCTION: Serine/threonine protein kinase essential for release from glucose repression (PubMed:1944227, PubMed:25869125, PubMed:3049551, PubMed:3526554, PubMed:6366512, PubMed:8289797, PubMed:8628258). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a centra... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06784 | STE7_YEAST | MFQRKTLQRRNLKGLNLNLHPDVGNNGQLQEKTETHQGQSRIEGHVMSNINAIQNNSNLFLRRGIKKKLTLDAFGDDQAISKPNTVVIQQPQNEPVLVLSSLSQSPCVSSSSSLSTPCIIDAYSNNFGLSPSSTNSTPSTIQGLSNIATPVENEHSISLPPLEESLSPAAADLKDTLSGTSNGNYIQLQDLVQLGKIGAGNSGTVVKALHVPDSKIVAKKTIPVEQNNSTIINQLVRELSIVKNVKPHENIITFYGAYYNQHINNEIIILMEYSDCGSLDKILSVYKRFVQRGTVSSKKTWFNELTISKIAYGVLNGLDH... | 2.7.12.2 | null | cell wall integrity MAPK cascade [GO:0000196]; invasive growth in response to glucose limitation [GO:0001403]; MAPK cascade [GO:0000165]; pheromone response MAPK cascade [GO:0071507]; phosphorylation [GO:0016310]; pseudohyphal growth [GO:0007124]; signal transduction involved in filamentous growth [GO:0001402] | cytoplasm [GO:0005737]; mating projection tip [GO:0043332] | ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase 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=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it is phosphorylated by the ste11 protein kinase and that it can phosphorylate the FUS3 and or KSS1 kinases. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06785 | TYSY_YEAST | MTMDGKNKEEEQYLDLCKRIIDEGEFRPDRTGTGTLSLFAPPQLRFSLRDDTFPLLTTKKVFTRGIILELLWFLAGDTDANLLSEQGVKIWDGNGSREYLDKMGFKDRKVGDLGPVYGFQWRHFGAKYKTCDDDYTGQGIDQLKQVIHKLKTNPYDRRIIMSAWNPADFDKMALPPCHIFSQFYVSFPKEGEGSGKPRLSCLLYQRSCDMGLGVPFNIASYALLTRMIAKVVDMEPGEFIHTLGDAHVYKDHIDALKEQITRNPRPFPKLKIKRDVKDIDDFKLTDFEIEDYNPHPRIQMKMSV | 2.1.1.45 | null | dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; methylation [GO:0032259] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear periphery [GO:0034399] | dihydrofolate reductase activity [GO:0004146]; thymidylate synthase activity [GO:0004799] | PF00303; | 3.30.572.10; | Thymidylate synthase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8132557}. Note=Localizes to the nuclear periphery. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000269|PubMed:7028756}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for dUMP {ECO:0000269|PubMed:7028756}; KM=70 uM for 5,10-methylene-tetrahydropteroylglutamate {ECO:0000269|PubMed:7028756}; | PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8-7.2. {ECO:0000269|PubMed:7028756}; | null | FUNCTION: Thymidylate synthase required for de novo biosynthesis of pyrimidine deoxyribonucleotides. Required for both nuclear and mitochondrial DNA synthesis. {ECO:0000269|PubMed:17248617, ECO:0000269|PubMed:334734, ECO:0000269|PubMed:4580573, ECO:0000269|PubMed:6287238, ECO:0000269|PubMed:7028756}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06786 | TOP2_YEAST | MSTEPVSASDKYQKISQLEHILKRPDTYIGSVETQEQLQWIYDEETDCMIEKNVTIVPGLFKIFDEILVNAADNKVRDPSMKRIDVNIHAEEHTIEVKNDGKGIPIEIHNKENIYIPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFILETADLNVGQKYVQKWENNMSICHPPKITSYKKGPSYTKVTFKPDLTRFGMKELDNDILGVMRRRVYDINGSVRDINVYLNGKSLKIRNFKNYVELYLKSLEKKRQLDNGEDGAAKSDIPTILYERINNRWEVAFAVSDISFQQISFVNSIATTMGGTHVNYI... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342}; Name=Ca(2+); Xref=ChEB... | chromatin organization [GO:0006325]; chromatin remodeling at centromere [GO:0031055]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA topological change [GO:0006265]; reciprocal meiotic recombination [GO:0007131]; regulation of mitotic recombination [GO:0000019]; replication fork progression beyond ... | DNA replication termination region [GO:0097047]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; synaptonemal complex [GO:0000795] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF00204;PF00521;PF02518;PF01751;PF16898; | 3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10; | Type II topoisomerase family | PTM: Phosphorylation enhances the activity. Stimulates decatenation activity. {ECO:0000269|PubMed:1316274}. | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:23022727, ECO:0000269|PubMed:9685374}; | null | null | null | null | FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. {ECO:0000269|PubMed:23022727, ECO:0000269|PubMed:9685374}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06787 | CALM_YEAST | MSSNLTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSPSEAEVNDLMNEIDVDGNHQIEFSEFLALMSRQLKSNDSEQELLEAFKVFDKNGDGLISAAELKHVLTSIGEKLTDAEVDDMLREVSDGSGEINIQQFAALLSK | null | null | cell budding [GO:0007114]; cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; microautophagy [GO:0016237]; phosphatidylinositol biosynthetic process [GO:0006661]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:20006... | actin cortical patch [GO:0030479]; cellular bud [GO:0005933]; cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; central plaque of spindle pole body [GO:0005823]; incipient cellular bud site [GO:0000131]; mating projection tip [GO:0043332]; myosin I complex [GO:0045160]; myosin II complex [GO:0016460]; myos... | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; enzyme regulator activity [GO:0030234]; mitogen-activated protein kinase binding [GO:0051019] | PF13499; | 1.10.238.10; | Calmodulin family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:8247006}. | null | null | null | null | null | FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Component of the spindle pole body (SPB) required for the proper execution of spindle p... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06789 | VE1_HPV18 | MADPEGTDGEGTGCNGWFYVQAIVDKKTGDVISDDEDENATDTGSDMVDFIDTQGTFCEQAELETAQALFHAQEVHNDAQVLHVLKRKFAGGSTENSPLGERLEVDTELSPRLQEISLNSGQKKAKRRLFTISDSGYGCSEVEATQIQVTTNGEHGGNVCSGGSTEAIDNGGTEGNNSSVDGTSDNSNIENVNPQCTIAQLKDLLKVNNKQGAMLAVFKDTYGLSFTDLVRNFKSDKTTCTDWVTAIFGVNPTIAEGFKTLIQPFILYAHIQCLDCKWGVLILALLRYKCGKSRLTVAKGLSTLLHVPETCMLIQPPKLR... | 3.6.4.12 | null | DNA replication [GO:0006260]; viral genome replication [GO:0019079] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678] | PF00519;PF20450;PF00524; | 3.40.1310.10;3.40.50.300;1.10.10.510; | Papillomaviridae E1 protein family | PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04000}.; PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_04000}. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04000}; | null | null | null | null | FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a ... | Human papillomavirus type 18 |
P06795 | MDR1B_MOUSE | MEFEENLKGRADKNFSKMGKKSKKEKKEKKPAVGVFGMFRYADWLDKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAEASILPSITNQSGPNSTLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLV... | 7.6.2.1; 7.6.2.2 | null | ceramide translocation [GO:0099040]; establishment of endothelial blood-brain barrier [GO:0014045]; phospholipid translocation [GO:0045332]; response to xenobiotic stimulus [GO:0009410]; Sertoli cell barrier remodeling [GO:0061843] | apical plasma membrane [GO:0016324]; external side of apical plasma membrane [GO:0098591]; Golgi membrane [GO:0000139]; intercellular canaliculus [GO:0046581]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ABC-type oligopeptide transporter activity [GO:0015421]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; floppase activity [GO:0140328]; phosphatidylcholine floppase activity [GO:009055... | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily | PTM: Several phosphorylated serine residues are present in the linker domain. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08183}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane {ECO:0000250|UniProtKB:P08183}. Cytoplasm {ECO:0000250|UniProtKB:P08183}. Note=ABCB1 localization is influenced by C1orf115 expression levels (plasma membrane vers... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:P08183}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P08183}; CATALYTIC ACTIVI... | null | null | null | null | FUNCTION: Translocates drugs and phospholipids across the membrane. Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins. Energy-dependent e... | Mus musculus (Mouse) |
P06797 | CATL1_MOUSE | MNLLLLLAVLCLGTALATPKFDQTFSAEWHQWKSTHRRLYGTNEEEWRRAIWEKNMRMIQLHNGEYSNGQHGFSMEMNAFGDMTNEEFRQVVNGYRHQKHKKGRLFQEPLMLKIPKSVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHAQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEFAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKNLDHGVLLVGYGYEGTDSNKNKYWLVKNSWGSEWGMEGYIKIAKDRDN... | 3.4.22.15 | null | antigen processing and presentation of peptide antigen [GO:0048002]; autophagic cell death [GO:0048102]; CD4-positive, alpha-beta T cell lineage commitment [GO:0043373]; cell communication [GO:0007154]; cellular response to starvation [GO:0009267]; collagen catabolic process [GO:0030574]; decidualization [GO:0046697]; ... | apical plasma membrane [GO:0016324]; chromaffin granule [GO:0042583]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; microvillus [GO:0005902]; neuron ... | aminopeptidase activity [GO:0004177]; cysteine-type carboxypeptidase activity [GO:0016807]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activity [GO:0004175]; histone binding [GO:0042393]; kininogen binding [... | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (PubMed:11483509). Autocleavage; produces the single-chain CTSL after cleavage of the propep... | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:11483509, ECO:0000269|PubMed:12782676}. Apical cell membrane {ECO:0000269|PubMed:12782676}; Peripheral membrane protein {ECO:0000269|PubMed:12782676}; Extracellular side {ECO:0000269|PubMed:12782676}. Secreted, extracellular space {ECO:0000269|PubMed:12417635}. Secrete... | CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.; EC=3.4.22.15; Evidence={ECO:0000269|PubMed:8554545}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:10716919}; | null | FUNCTION: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed:12782676). ... | Mus musculus (Mouse) |
P06800 | PTPRC_MOUSE | MTMGLWLKLLAFGFALLDTEVFVTGQTPTPSDELSTTENALLLPQSDPLPARTTESTPPSISERGNGSSETTYHPGVLSTLLPHLSPQPDSQTPSAGGADTQTFSSQADNPTLTPAPGGGTDPPGVPGERTVPGTIPADTAFPVDTPSLARNSSAASPTHTSNVSTTDISSGASLTTLTPSTLGLASTDPPSTTIATTTKQTCAAMFGNITVNYTYESSNQTFKADLKDVQNAKCGNEDCENVLNNLEECSQIKNISVSNDSCAPATTIDLYVPPGTDKFSLHDCTPKEKANTSICLEWKTKNLDFRKCNSDNISYVLHC... | 3.1.3.48 | null | alpha-beta T cell proliferation [GO:0046633]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; bone marrow development [GO:0048539]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell cycle phase transition [GO:0044770]... | bleb [GO:0032059]; cell periphery [GO:0071944]; cell surface [GO:0009986]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; membrane microdomain [GO:0098857]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | ankyrin binding [GO:0030506]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]; signaling receptor binding [GO:0005102]; spectrin binding [GO:0030507] | PF12567;PF12453;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 1/6 subfamily | PTM: Heavily N- and O-glycosylated. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08575}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:P08575}. Synapse {ECO:0000250|UniProtKB:P08575}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:P08575}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-ce... | Mus musculus (Mouse) |
P06801 | MAOX_MOUSE | MEPRAPRRRHTHQRGYLLTRDPHLNKDLAFTLEERQQLNIHGLLPPCIISQELQVLRIIKNFERLNSDFDRYLLLMDLQDRNEKLFYSVLMSDVEKFMPIVYTPTVGLACQQYSLAFRKPRGLFISIHDKGHIASVLNAWPEDVVKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGVNPQQCLPITLDVGTENEELLKDPLYIGLRHRRVRGPEYDAFLDEFMEAASSKYGMNCLIQFEDFANRNAFRLLNKYRNKYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTVLFQGAGEAALGIAHLVVMAMEKE... | 1.1.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P48163}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P48163}; Note=Divalent metal cations. Prefers magnesium or manganese. {ECO:0000250|UniProtKB:P48163}; | malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; NADP metabolic process [GO:0006739]; protein homotetramerization [GO:0051289]; pyruvate metabolic process [GO:0006090]; regulation of NADP metabolic process [GO:1902031]; response to hormone [GO:0009725] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; malate dehydrogenase (decarboxylating) (NADP+) activity [GO:0004473]; malic enzyme activity [GO:0004470]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxaloacetate decarboxylase activity [GO:0008948] | PF00390;PF03949; | 3.40.50.10380;3.40.50.720; | Malic enzymes family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48163}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate; Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40; Evidence={ECO:0000250|UniProtKB:P48163}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18254; Evidence={ECO... | null | null | null | null | FUNCTION: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate. {ECO:0000250|UniProtKB:P48163}. | Mus musculus (Mouse) |
P06802 | ENPP1_MOUSE | MERDGDQAGHGPRHGSAGNGRELESPAAASLLAPMDLGEEPLEKAERARPAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFSNCRCDAACVSLGNCCLDFQETCVEPTHIWTCNKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDKKSWVEETCESIDTPECPAEFESPPTLLFSLDGFRAEYLHTWGGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEIDGILPDIYK... | 3.1.4.1; 3.6.1.9 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:30356045}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:30356045}; | adipose tissue development [GO:0060612]; adult locomotory behavior [GO:0008344]; adult walking behavior [GO:0007628]; aorta development [GO:0035904]; apoptotic process involved in development [GO:1902742]; artery development [GO:0060840]; articular cartilage development [GO:0061975]; ATP metabolic process [GO:0046034];... | apical dendrite [GO:0097440]; basal dendrite [GO:0097441]; basolateral plasma membrane [GO:0016323]; cell body [GO:0044297]; cell projection [GO:0042995]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membra... | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; ATP diphosphatase activity [GO:0047693]; calcium ion binding [GO:0005509]; coenzyme A diphosphatase activity [GO:0010945]; cyclic-GMP-AMP hydrolase activity [GO:0106177]; dinucleotide phosphatase activity [GO:0004551]; GTP diphosphatase activity [GO:0036219]; id... | PF01223;PF01663;PF01033; | 4.10.410.20;3.40.720.10;3.40.570.10; | Nucleotide pyrophosphatase/phosphodiesterase family | PTM: N-glycosylated. {ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:8223581}.; PTM: The secreted form is produced through cleavage at Lys-85 by intracellular processing. {ECO:0000269|PubMed:23041369}. | SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase family member 1]: Cell membrane {ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:3104326, ECO:0000269|PubMed:3917281}; Single-pass type II membrane protein. Basolateral cell membrane {ECO:0000269|PubMed:11598187, ECO:0000269|PubMed:15075217}; Single... | CATALYTIC ACTIVITY: Reaction=Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.; EC=3.1.4.1; Evidence={ECO:0000269|PubMed:11027689, ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:8223581}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphat... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 uM for ATP {ECO:0000269|PubMed:23027977}; KM=4.3 mM for UTP {ECO:0000269|PubMed:23027977}; KM=4.2 mM for GTP {ECO:0000269|PubMed:23027977}; KM=1.2 mM for CTP {ECO:0000269|PubMed:23027977}; Note=kcat is 16 sec(-1) with ATP as substrate. kcat is 200 sec(-1) with U... | null | null | null | FUNCTION: Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:22510396, PubMed:25260930, PubMed:9662402). PPi inhibits bone mineralization and soft tis... | Mus musculus (Mouse) |
P06803 | PIM1_MOUSE | MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSDFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEDLARGFFWQVLEAVRHCHNCGVLHRDIKDENILIDLSRGEIKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIKGQVFFRQTVSSECQHLIKWCLSLRPSDRPSFEEIRNHPWMQGDLLPQAASEIHLHSLSPGSSK | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11309}; | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cellular detoxification [GO:1990748]; cellular response to type II interferon [GO:0071346]; negative regulation of apoptotic process [GO:0043066]; negative regulation of innate immune response [GO:0045824]; positive regulation of brown fat cell differentiation [G... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; manganese ion binding [GO:0030145]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ribosomal small subunit binding [GO:0043024] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, PIM subfamily | PTM: Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity). {ECO:0000250|UniProtKB:P11309}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P11309}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1825810}. Nucleus {ECO:0000269|PubMed:1825810}. Cell membrane {ECO:0000269|PubMed:1825810}. Note=Mainly located in the cytoplasm. | 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: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis (PubMed:15199164, PubMed:1825810). Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle... | Mus musculus (Mouse) |
P06804 | TNFA_MOUSE | MSTESMIRDVELAEEALPQKMGGFQNSRRCLCLSLFSFLLVAGATTLFCLLNFGVIGPQRDEKFPNGLPLISSMAQTLTLRSSSQNSSDKPVAHVVANHQVEEQLEWLSQRANALLANGMDLKDNQLVVPADGLYLVYSQVLFKGQGCPDYVLLTHTVSRFAISYQEKVNLLSAVKSPCPKDTPEGAELKPWYEPIYLGGVFQLEKGDQLSAEVNLPKYLDFAESGQVYFGVIAL | null | null | animal organ morphogenesis [GO:0009887]; antiviral innate immune response [GO:0140374]; apoptotic signaling pathway [GO:0097190]; calcium-mediated signaling [GO:0019722]; cellular extravasation [GO:0045123]; cellular response to amino acid stimulus [GO:0071230]; cellular response to amyloid-beta [GO:1904646]; cellular ... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; secretory granule [GO:00... | cytokine activity [GO:0005125]; death receptor agonist activity [GO:0038177]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; receptor ligand activity [GO:0048018]; transcription cis-regulatory region binding [GO:0000976]; tumor necrosis factor receptor binding [GO:0005164] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space (By similarity). The soluble form derives ... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted.; SUBCELLULAR LOCATION: [C-domain 1... | null | null | null | null | null | FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain c... | Mus musculus (Mouse) |
P06811 | LAC1_NEUCR | MKFLGIAALVAGLLAPSLVLGAPAPGTEGVNLLTPVDKRQDSQAERYGGGGGGGCNSPTNRQCWSPGFNINTDYELGTPNTGKTRRYKLTLTETDNWIGPDGVIKDKVMMVNDKIIGPTIQADWGDYIEITVINKLKSNGTSIHWHGMHQRNSNIQDGVNGVTECPIPPRGGSKVYRWRATQYGTSWYHSHFSAQYGNGIVGPIVINGPASANYDVDLGPFPLTDYYYDTADRLVLLTQHAGPPPSNNVLFNGFAKHPTTGAGQYATVSLTKGKKHRLRLINTSVENHFQLSLVNHSMTIISADLVPVQPYKVDSLFLGV... | 1.10.3.2 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q70KY3}; Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3}; | lignin catabolic process [GO:0046274] | extracellular region [GO:0005576] | copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716]; oxidoreductase activity [GO:0016491] | PF00394;PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000250|UniProtKB:Q70KY3}; | null | null | null | null | FUNCTION: Lignin degradation and detoxification of lignin-derived products. {ECO:0000250|UniProtKB:Q70KY3}. | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P06814 | CAN2_RABIT | QKLIRIRNPWGEVEWTGRWNDNCPNWNTVDPEVRERLAERHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYVIKLEEEDEDQEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELRGQTNIHLGKNFFLTTRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKNGDFCVRVFSEKKADYQAVDDEIEADLEEADVSEDDIDDGFRRLFAQLAGEDAEISAFELQNILRRVLAKRQDIKTDGLSIETCKIMVDMLDSDGTGKLGLKEFY... | 3.4.22.53 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 7 Ca(2+) ions. {ECO:0000250}; | cellular response to amino acid stimulus [GO:0071230]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198] | PF01067;PF13833;PF00648; | 2.60.120.380;3.90.70.10;1.10.238.10; | Peptidase C2 family | null | SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding. | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.53; | null | null | null | null | FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor ac... | Oryctolagus cuniculus (Rabbit) |
P06815 | CAN1_RABIT | RESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPRELVGQPALHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKRAGTQELDDQIQANLPDEQVLSAEEIDENFKALFRQLAGEDLEISVRELQTILNRITSKHKDLRTKGFSMESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLAIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA | 3.4.22.52 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P07384, ECO:0000269|PubMed:3038855}; Note=Binds 4 Ca(2+) ions. {ECO:0000250|UniProtKB:P07384, ECO:0000269|PubMed:3038855}; | proteolysis [GO:0006508]; regulation of catalytic activity [GO:0050790]; self proteolysis [GO:0097264] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; peptidase activity [GO:0008233] | PF01067;PF13833; | 2.60.120.380;1.10.238.10; | Peptidase C2 family | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:3667575}.; PTM: Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms (By si... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07384}. Cell membrane {ECO:0000250|UniProtKB:P07384}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250|UniProtKB:P07384}. | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52; Evidence={ECO:0000250|UniProtKB:P07384}; | null | null | null | null | FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1. Cleaves and activates caspase-7 (CASP7). {ECO:0000250|UniProtKB:P07384}. | Oryctolagus cuniculus (Rabbit) |
P06820 | NRAM_I67A0 | MNPNQKIITIGSVSLTIATVCFLMQIAILVTTVTLHFKQHECDSPASNQVMPCEPIIIERNITEIVYLNNTTIEKEICPKVVEYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNELGVPFHLGTRQVCIAWSSSSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVMTDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSG... | 3.2.1.18 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809}; | carbohydrate metabolic process [GO:0005975]; viral budding from plasma membrane [GO:0046761] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; metal ion binding [GO:0046872] | PF00064; | 2.120.10.10; | Glycosyl hydrolase 34 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | null | null | null | null | FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell ... | Influenza A virus (strain A/Tokyo/3/1967 H2N2) |
P06821 | M2_I34A1 | MSLLTEVETPIRNEWGCRCNGSSDPLAIAANIIGILHLILWILDRLFFKCIYRRFKYGLKGGPSTEGVPKSMREEYRKEQQSAVDADDGHFVSIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]; uncoating of virus [GO:0019061] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P06829 | L_SENDE | MDGQESSQNPSDILYPECHLNSPIVRGKIAQLHVLLDVNQPYRLKDDSIINITKHKIRNGGLSPRQIKIRSLGKALQRTIKDLDRYTFEPYPTYSQELLRLDIPEICDKIRSVFAVSDRLTRELSSGFQDLWLNIFKQLGNIEGREGYDPLQDISTIPEITDKYSRNRWYRPFLTWFSIKYDMRWMQKTRPGGPIDTSNSHNLLECKSYTLVTYGDLVMILNKLTLTGYILTPELVLMYCDVVEGRWNMSAAGHLDKRSIGITSKGEELWELVDSLFSSLGEEIYNVIALLEPLSLALIQLNDPVIPLRGAFMRHVLTEL... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | null | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF14318;PF00946; | null | Paramyxovirus L protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a 5'-end... | null | null | null | null | FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all vir... | Sendai virus (strain Enders) (SeV) |
P06836 | NEUM_BOVIN | MLCCMRRTKQVEKNDEDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKGDAPAAEAEANEKDEAAVAEGTEKKEGEGSTPAEAAPGAGPKPEEKTGKAGETPSEEKKGEGAPDAATEQAAPQAPAPSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATAPAAEDAAAMATAQPPTETAESSQAEEKIEAVDETKPKDSARQDEGKGEEREADQEHA | null | null | axon choice point recognition [GO:0016198]; axon regeneration [GO:0031103]; localization [GO:0051179]; regulation of growth [GO:0040008]; tissue regeneration [GO:0042246] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium membrane [GO:0031527]; growth cone membrane [GO:0032584]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] | calmodulin binding [GO:0005516]; lipid binding [GO:0008289]; lysophosphatidic acid binding [GO:0035727]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylserine binding [GO:0001786] | PF00612;PF06614;PF10580; | 1.20.5.190; | Neuromodulin family | PTM: Phosphorylated (PubMed:1828073, PubMed:2140056, PubMed:8454596). Phosphorylation of this protein by a protein kinase C is specifically correlated with certain forms of synaptic plasticity (PubMed:2140056). {ECO:0000269|PubMed:1828073, ECO:0000269|PubMed:2140056, ECO:0000269|PubMed:8454596}.; PTM: Palmitoylated by ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic s... | null | null | null | null | null | FUNCTION: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction (By similarity). {ECO:0000250|UniProtKB:P17677}. | Bos taurus (Bovine) |
P06837 | NEUM_MOUSE | MLCCMRRTKQVEKNDEDQKIEQDGVKPEDKAHKAATKIQASFRGHITRKKLKGEKKGDAPAAEAEAKEKDDAPVADGVEKKEGDGSATTDAAPATSPKAEEPSKAGDAPSEEKKGEGDAAPSEEKAGSAETESAAKATTDNSPSSKAEDGPAKEEPKQADVPAAVTDAAATTPAAEDAATKAAQPPTETAESSQAEEEKDAVDEAKPKESARQDEGKEDPEADQEHA | null | null | astrocyte differentiation [GO:0048708]; axon choice point recognition [GO:0016198]; axon guidance [GO:0007411]; axon regeneration [GO:0031103]; cell fate commitment [GO:0045165]; radial glial cell differentiation [GO:0060019]; regulation of filopodium assembly [GO:0051489]; regulation of growth [GO:0040008]; regulation... | axon [GO:0030424]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium membrane [GO:0031527]; GABA-ergic synapse [GO:0098982]; growth cone membrane [GO:0032584]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynapse [GO:0098793] | calmodulin binding [GO:0005516]; lysophosphatidic acid binding [GO:0035727]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylserine binding [GO:0001786] | PF00612;PF06614;PF10580; | 1.20.5.190; | Neuromodulin family | PTM: Phosphorylated (PubMed:18493953). Phosphorylation of this protein by a protein kinase C is specifically correlated with certain forms of synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:P07936, ECO:0000269|PubMed:18493953}.; PTM: Palmitoylated by ZDHHC3 (PubMed:27875292). Palmitoylation is regulated by ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic s... | null | null | null | null | null | FUNCTION: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction. {ECO:0000250|UniProtKB:P17677}. | Mus musculus (Mouse) |
P06838 | RAD10_YEAST | MNNTDPTSFESILAGVAKLRKEKSGADTTGSQSLEIDASKLQQQEPQTSRRINSNQVINAFNQQKPEEWTDSKATDDYNRKRPFRSTRPGKTVLVNTTQKENPLLNHLKSTNWRYVSSTGINMIYYDYLVRGRSVLFLTLTYHKLYVDYISRRMQPLSRNENNILIFIVDDNNSEDTLNDITKLCMFNGFTLLLAFNFEQAAKYIEYLNL | null | null | DNA amplification [GO:0006277]; double-strand break repair via single-strand annealing, removal of nonhomologous ends [GO:0000736]; meiotic mismatch repair [GO:0000710]; mitotic recombination [GO:0006312]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; removal ... | endonuclease complex [GO:1905348]; ERCC4-ERCC1 complex [GO:0070522]; nucleotide-excision repair factor 1 complex [GO:0000110]; nucleus [GO:0005634] | damaged DNA binding [GO:0003684]; endonuclease activity [GO:0004519]; single-stranded DNA binding [GO:0003697] | PF03834; | 3.40.50.10130; | ERCC1/RAD10/SWI10 family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD1 forms an endonuclease that specifically degrades single-stranded DNA. {ECO:0000269|PubMed:8479526}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06839 | RAD3_YEAST | MKFYIDDLPVLFPYPKIYPEQYNYMCDIKKTLDVGGNSILEMPSGTGKTVSLLSLTIAYQMHYPEHRKIIYCSRTMSEIEKALVELENLMDYRTKELGYQEDFRGLGLTSRKNLCLHPEVSKERKGTVVDEKCRRMTNGQAKRKLEEDPEANVELCEYHENLYNIEVEDYLPKGVFSFEKLLKYCEEKTLCPYFIVRRMISLCNIIIYSYHYLLDPKIAERVSNEVSKDSIVIFDEAHNIDNVCIESLSLDLTTDALRRATRGANALDERISEVRKVDSQKLQDEYEKLVQGLHSADILTDQEEPFVETPVLPQDLLTEA... | 3.6.4.12 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305|PubMed:16973432}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305|PubMed:16973432}; | nucleotide-excision repair [GO:0006289]; positive regulation of mitotic recombination [GO:0045951]; regulation of mitotic recombination [GO:0000019]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367] | cytosol [GO:0005829]; nucleotide-excision repair factor 3 complex [GO:0000112]; nucleus [GO:0005634]; transcription factor TFIIH core complex [GO:0000439]; transcription factor TFIIH holo complex [GO:0005675] | 4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; metal ion binding [GO:0046872] | PF06733;PF06777;PF13307; | 1.10.275.40;1.10.30.20;3.40.50.300; | Helicase family, RAD3/XPD subfamily | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06843 | SPT2_YEAST | MSFLSKLSQIRKSTTASKAQVQDPLPKKNDEEYSLLPKNYIRDEDPAVKRLKELRRQELLKNGALAKKSGVKRKRGTSSGSEKKKIERNDDDEGGLGIRFKRSIGASHAPLKPVVRKKPEPIKKMSFEELMKQAENNEKQPPKVKSSEPVTKERPHFNKPGFKSSKRPQKKASPGATLRGVSSGGNSIKSSDSPKPVKLNLPTNGFAQPNRRLKEKLESRKQKSRYQDDYDEEDNDMDDFIEDDEDEGYHSKSKHSNGPGYDRDEIWAMFNRGKKRSEYDYDELEDDDMEANEMEILEEEEMARKMARLEDKREEAWLKK... | null | null | chromatin organization [GO:0006325]; heterochromatin formation [GO:0031507]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334]; regulation of DNA-templated transcription [GO:0006355]; transcription by RNA polymerase I [GO:0006360]; transcription elongation-coupled ... | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA secondary structure binding [GO:0000217]; histone binding [GO:0042393]; histone chaperone activity [GO:0140713] | PF08243; | null | SPT2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2072912, ECO:0000269|PubMed:26109053}. | null | null | null | null | null | FUNCTION: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin (PubMed:26109053). Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription (PubMed:26109053). Global... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06844 | SPT3_YEAST | MMDKHKYRVEIQQMMFVSGEINDPPVETTSLIEDIVRGQVIEILLQSNKTAHLRGSRSILPEDVIFLIRHDKAKVNRLRTYLSWKDLRKNAKDQDASAGVASGTGNPGAGGEDDLKKAGGGEKDEKDGGNMMKVKKSQIKLPWELQFMFNEHPLENNDDNDDMDEDEREANIVTLKRLKMADDRTRNMTKEEYVHWSDCRQASFTFRKNKRFKDWSGISQLTEGKPHDDVIDILGFLTFEIVCSLTETALKIKQREQVLQTQKDKSQQSSQDNTNFEFASSTLHRKKRLFDGPENVINPLKPRHIEEAWRVLQTIDMRHR... | null | null | chromatin organization [GO:0006325]; invasive growth in response to glucose limitation [GO:0001403]; pseudohyphal growth [GO:0007124]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366] | cytosol [GO:0005829]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; SLIK (SAGA-like) complex [GO:0046695] | protein heterodimerization activity [GO:0046982]; transcription coregulator activity [GO:0003712] | PF02269; | 1.10.20.10; | SPT3 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machi... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06845 | TYRO_STRGA | MTVRKNQATLTADEKRRFVAAVLELKRSGRYDEFVTTHNAFIIGDTDAGERTGHRSPSFLPWHRRYLLEFERALQSVDASVALPYWDWSADRTARASLWAPDFLGGTGRSLDGRVMDGPFAASAGNWPINVRVDGRAYLRRSLGTAVRELPTRAEVESVLGMATYDTAPWNSASDGFRNHLEGWRGVNLHNRVHVWVGGQMATGMSPNDPVFWLHHAYVDKLWAEWQRRHPGSGYLPAAGTPDVVDLNDRMKPWNDTSPADLLDHTAHYTFDTD | 1.14.18.1 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:1901488, ECO:0000269|PubMed:2846043}; Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:1901488, ECO:0000269|PubMed:2846043}; | melanin biosynthetic process [GO:0042438]; pigmentation [GO:0043473] | null | metal ion binding [GO:0046872]; tyrosinase activity [GO:0004503] | PF00264; | 1.10.1280.10; | Tyrosinase family | null | null | CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEB... | null | null | null | null | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. | Streptomyces glaucescens |
P06850 | CRF_HUMAN | MRLPLLVSAGVLLVALLPCPPCRALLSRGPVPGARQAPQHPQPLDFFQPPPQSEQPQQPQARPVLLRMGEEYFLRLGNLNKSPAAPLSPASSLLAGGSGSRPSPEQATANFFRVLLQQLLLPRRSLDSPAALAERGARNALGGHQEAPERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK | null | null | adrenal gland development [GO:0030325]; associative learning [GO:0008306]; cellular response to cocaine [GO:0071314]; cellular response to dexamethasone stimulus [GO:0071549]; chemical synaptic transmission [GO:0007268]; diterpenoid metabolic process [GO:0016101]; female pregnancy [GO:0007565]; glucocorticoid biosynthe... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; synapse [GO:0045202]; varicosity [GO:0043196] | corticotropin-releasing hormone activity [GO:0017045]; corticotropin-releasing hormone receptor 1 binding [GO:0051430]; corticotropin-releasing hormone receptor 2 binding [GO:0051431]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102] | PF00473; | 6.10.250.1920; | Sauvagine/corticotropin-releasing factor/urotensin I family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06296}. | null | null | null | null | null | FUNCTION: Hormone regulating the release of corticotropin from pituitary gland (By similarity). Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (By similarity). {ECO:0000250|UniProtKB:P06296, ECO:0000250|UniProtKB:Q8CIT0}. | Homo sapiens (Human) |
P06856 | DPOL_VACCW | MDVRCINWFESHGENRFLYLKSRCRNGETVFIRFPHYFYYVVTDEIYQSLSPPPFNARPLGKMRTIDIDETISYNLDIKDRKCSVADMWLIEEPKKRSIQNATMDEFLNISWFYISNGISPDGCYSLDEQYLTKINNGCYHCDDPRNCFAKKIPRFDIPRSYLFLDIECHFDKKFPSVFINPISHTSYCYIDLSGKRLLFTLINEEMLTEQEIQEAVDRGCLRIQSLMEMDYERELVLCSEIVLLRIAKQLLELTFDYVVTFNGHNFDLRYITNRLELLTGEKIIFRSPDKKEAVYLCIYERNQSSHKGVGGMANTTFHV... | 2.7.7.7; 3.1.11.- | null | base-excision repair, gap-filling [GO:0006287]; DNA recombination [GO:0006310]; DNA replication proofreading [GO:0045004]; nucleotide-excision repair, DNA gap filling [GO:0006297]; SOS response [GO:0009432]; viral DNA genome replication [GO:0039693] | 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]; nucleotide binding [GO:0000166] | PF00136;PF08408;PF03104;PF08452; | 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; | null | null | null | null | FUNCTION: Catalyzes DNA synthesis. Acquires processivity by associating with a heterodimeric processivity factor comprised of the viral OPG148/A20 and OPG116/D4 proteins, thereby forming the DNA polymerase holoenzyme. Displays 3'- to 5' exonuclease activity. Might participate in viral DNA recombination. Does not perfor... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P06857 | LIPR1_CANLF | MVSIWTIALFLLGAAKAKEVCYEQIGCFSDAEPWAGTAIRPLKVLPWSPERIGTRFLLYTNKNPNNFQTLLPSDPSTIEASNFQTDKKTRFIIHGFIDKGEENWLLDMCKNMFKVEEVNCICVDWKKGSQTSYTQAANNVRVVGAQVAQMLSMLSANYSYSPSQVQLIGHSLGAHVAGEAGSRTPGLGRITGLDPVEASFQGTPEEVRLDPTDADFVDVIHTDAAPLIPFLGFGTSQQMGHLDFFPNGGEEMPGCKKNALSQIVDLDGIWEGTRDFVACNHLRSYKYYSESILNPDGFASYPCASYRAFESNKCFPCPDQ... | null | null | lipid catabolic process [GO:0016042] | extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; carboxylic ester hydrolase activity [GO:0052689] | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9726421}. | null | null | null | null | null | FUNCTION: May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters (in vitro). | Canis lupus familiaris (Dog) (Canis familiaris) |
P06858 | LIPL_HUMAN | MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKV... | 3.1.1.32; 3.1.1.34 | null | cellular response to fatty acid [GO:0071398]; cellular response to nutrient [GO:0031670]; cholesterol homeostasis [GO:0042632]; chylomicron remodeling [GO:0034371]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; high-density lipoprotein particle remodeling [GO:0034375]; low-den... | catalytic complex [GO:1902494]; cell surface [GO:0009986]; chylomicron [GO:0042627]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; apolipoprotein binding [GO:0034185]; calcium ion binding [GO:0005509]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; lipoprotein particle binding [GO:0071813]; phosphatidylse... | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:1371284, ECO:0000269|PubM... | 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=3.1.1.34; Evidence={ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12032167... | null | null | null | null | FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:11342582, PubMed:27578112, PubMed:8675619... | Homo sapiens (Human) |
P06859 | PA2A1_PROFL | MRTLWIMAVLLVGVDGGLWQFENMIIKVVKKSGILSYSAYGCYCGWGGRGKPKDATDRCCFVHDCCYGKVTGCNPKLGKYTYSWNNGDIVCEGDGPCKEVCECDRAAAICFRDNLDTYDRNKYWRYPASNCQEDSEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that is highly lipolytic and myolytic. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:1288500}. | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
P06865 | HEXA_HUMAN | MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLG... | 3.2.1.52 | null | adult walking behavior [GO:0007628]; carbohydrate metabolic process [GO:0005975]; cell morphogenesis involved in neuron differentiation [GO:0048667]; dermatan sulfate catabolic process [GO:0030209]; ganglioside catabolic process [GO:0006689]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabo... | azurophil granule [GO:0042582]; beta-N-acetylhexosaminidase complex [GO:1905379]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; membrane [GO:0016020] | acetylglucosaminyltransferase activity [GO:0008375]; beta-N-acetylhexosaminidase activity [GO:0004563]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]; protein heterodimerization activity [GO:0046982] | PF00728;PF14845; | 3.30.379.10;3.20.20.80; | Glycosyl hydrolase 20 family | PTM: N-linked glycan at Asn-115 consists of Man(3)-GlcNAc(2) (Probable) (PubMed:1533633, PubMed:16698036, PubMed:19159218). N-linked glycan at Asn-157 consists of either GlcNAc or GlcNAc(2)-Man(7-9). N-linked glycan at Asn-295 consists of either GlcNAc, GlcNAc-Fuc, or GlcNAc(2)-Man(4) (Probable). {ECO:0000269|PubMed:15... | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000269|PubMed:11707436, ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-beta-D-g... | null | null | null | null | FUNCTION: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides (PubMed:11707436, PubMed:8123671, PubMed:8672428, PubMed:9694901). The isozyme S is as... | Homo sapiens (Human) |
P06866 | HPT_RAT | MRALGAVVTLLLWGQLFAVELGNDATDIEDDSCPKPPEIANGYVEHLVRYRCRQFYKLQTEGDGIYTLNSEKQWVNPAAGDKLPKCEAVCGKPKHPVDQVQRIIGGSMDAKGSFPWQAKMISRHGLTTGATLISDQWLLTTAQNLFLNHSENATAKDIAPTLTLYVGKNQLVEIEKVVLHPERSVVDIGLIKLKQKVLVTEKVMPICLPSKDYVAPGRMGYVSGWGRNVNFRFTERLKYVMLPVADQEKCELHYEKSTVPEKKGAVSPVGVQPILNKHTFCAGLTKYEEDTCYGDAGSAFAVHDTEEDTWYAAGILSFDK... | null | null | acute-phase response [GO:0006953]; animal organ regeneration [GO:0031100]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; liver development [GO:0001889]; negative regulation of hydrogen peroxide catabolic process [GO:2000296]; Notch signaling pathway [GO:0007219]; response to bacterium ... | blood microparticle [GO:0072562]; extracellular space [GO:0005615]; haptoglobin-hemoglobin complex [GO:0031838] | antioxidant activity [GO:0016209]; hemoglobin binding [GO:0030492]; identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.10.70.10;2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity and p... | Rattus norvegicus (Rat) |
P06867 | PLMN_PIG | MDHKEVVLLLLLFLKSGLGDSLDDYVNTQGAFLFSLSRKQVAARSVEECAAKCEAETNFICRAFQYHSKDQQCVVMAENSKTSPIARMRDVVLFEKRIYLSECKTGNGKNYRGTTSKTKSGVICQKWSVSSPHIPKYSPEKFPLAGLEENYCRNPDNDEKGPWCYTTDPETRFDYCDIPECEDECMHCSGEHYEGKISKTMSGIECQSWGSQSPHAHGYLPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPNKRWEFCDIPRCTTPPPTSGPTYQCLKGRGENYRGTVSVTASGHTCQRWSAQSPHKHNRTPENFPCKNLE... | 3.4.21.7 | null | blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]; proteolysis [GO:0006508]; tissue remodeling [GO:0048771] | extracellular space [GO:0005615] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102] | PF00051;PF00024;PF00089; | 3.50.4.10;2.40.20.10;2.40.10.10; | Peptidase S1 family, Plasminogen subfamily | PTM: N-linked glycan contains N-acetyllactosamine, sialic acid and is core fucosylated. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:3356193}.; PTM: In the presence of the inhibitor, the activation involves only cleavag... | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.; EC=3.4.21.7; | null | null | null | null | FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, co... | Sus scrofa (Pig) |
P06868 | PLMN_BOVIN | MLPASPKMEHKAVVFLLLLFLKSGLGDLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAENSKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSPEKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAKTMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDIPRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPEN... | 3.4.21.7 | null | blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]; proteolysis [GO:0006508]; response to heat [GO:0009408]; tissue remodeling [GO:0048771] | extracellular space [GO:0005615] | endopeptidase activity [GO:0004175]; protein domain specific binding [GO:0019904]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102] | PF00051;PF00024;PF00089; | 3.50.4.10;2.40.20.10;2.40.10.10; | Peptidase S1 family, Plasminogen subfamily | PTM: N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:3356193, ECO:0000269|PubMed:3846532}.; PTM: In the presence of the inhibitor, the activation involves only ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.; EC=3.4.21.7; | null | null | null | null | FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, co... | Bos taurus (Bovine) |
P06869 | UROK_MOUSE | MKVWLASLFLCALVVKNSEGGSVLGAPDESNCGCQNGGVCVSYKYFSRIRRCSCPRKFQGEHCEIDASKTCYHGNGDSYRGKANTDTKGRPCLAWNAPAVLQKPYNAHRPDAISLGLGKHNYCRNPDNQKRPWCYVQIGLRQFVQECMVHDCSLSKKPSSSVDQQGFQCGQKALRPRFKIVGGEFTEVENQPWFAAIYQKNKGGSPPSFKCGGSLISPCWVASAAHCFIQLPKKENYVVYLGQSKESSYNPGEMKFEVEQLILHEYYREDSLAYHNDIALLKIRTSTGQCAQPSRSIQTICLPPRFTDAPFGSDCEITGF... | 3.4.21.73 | null | angiogenesis [GO:0001525]; fibrinolysis [GO:0042730]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of plasminogen activation [GO:0010757]; plasminogen activation [GO:0031639]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; ... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; protein complex involved in cell-matrix adhesion [GO:0098637]; serine protease inhibitor complex [GO:0097180]; serine-type endopeptidase complex [GO:1905370] | peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00051;PF00089; | 2.10.25.10;2.40.20.10;2.40.10.10; | Peptidase S1 family | PTM: Produced as an inactive single-chain protein (pro-uPA or sc-uPA), is processed into the active disulfide-linked two-chain form of PLAU/uPA by a proteolytic event mediated, at least, by TMPRSS4. {ECO:0000250|UniProtKB:P00749}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00749}. | CATALYTIC ACTIVITY: Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.73; | null | null | null | null | FUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. {ECO:0000250|UniProtKB:P00749}. | Mus musculus (Mouse) |
P06870 | KLK1_HUMAN | MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQAALYHFSTFQCGGILVHRQWVLTAAHCISDNYQLWLGRHNLFDDENTAQFVHVSESFPHPGFNMSLLENHTRQADEDYSHDLMLLRLTEPADTITDAVKVVELPTEEPEVGSTCLASGWGSIEPENFSFPDDLQCVDLKILPNDECKKAHVQKVTDFMLCVGHLEGGKDTCVGDSGGPLMCDGVLQGVTSWGYVPCGTPNKPSVAVRVLSYVKWIEDTIAENS | 3.4.21.35 | null | regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | extracellular exosome [GO:0070062]; nucleus [GO:0005634]; secretory granule [GO:0030141] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | PTM: The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167 are probably the mucin type linked to GalNAc. In PubMed:3163150, GalNAc was detected with the corresponding peptides but not located. {ECO:0000269|PubMed:15651049, ECO:0000269|PubMed:3163150}. | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35; | null | null | null | null | FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.; FUNCTION: (Microbial infection) Cleaves Neisseria meningitidis NHBA in saliva; Neisseria is an obligate commensal of the nasopharyngeal mucosa. {ECO:0000269|PubMed:31369555}. | Homo sapiens (Human) |
P06873 | PRTK_PARAQ | MRLSVLLSLLPLALGAPAVEQRSEAAPLIEARGEMVANKYIVKFKEGSALSALDAAMEKISGKPDHVYKNVFSGFAATLDENMVRVLRAHPDVEYIEQDAVVTINAAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQSSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTSILSTWIGG... | 3.4.21.64 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; | proteolysis [GO:0006508] | extracellular space [GO:0005615] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | PF05922;PF00082; | 3.30.70.80;3.40.50.200; | Peptidase S8 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.; EC=3.4.21.64; | null | null | null | null | FUNCTION: Hydrolyzes keratin at aromatic and hydrophobic residues. | Parengyodontium album (Tritirachium album) |
P06875 | PAC_ECOLX | MKNRNRMIVNCVTASLMYYWSLPALAEQSSSEIKIVRDEYGMPHIYANDTWHLFYGYGYVVAQDRLFQMEMARRSTQGTVAEVLGKDFVKFDKDIRRNYWPDAIRAQIAALSPEDMSILQGYADGMNAWIDKVNTNPETLLPKQFNTFGFTPKRWEPFDVAMIFVGTMANRFSDSTSEIDNLALLTALKDKYGVSQGMAVFNQLKWLVNPSAPTTIAVQESNYPLKFNQQNSQTAALLPRYDLPAPMLDRPAKGADGALLALTAGKNRETIAAQFAQGGANGLAGYPTTSNMWVIGKSKAQDAKAIMVNGPQFGWYAPAY... | 3.5.1.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per dimer.; | antibiotic biosynthetic process [GO:0017000]; response to antibiotic [GO:0046677] | periplasmic space [GO:0042597] | metal ion binding [GO:0046872]; penicillin amidase activity [GO:0008953] | PF01804; | 1.10.1400.10;1.10.287.150;2.30.120.10;3.60.20.10;1.10.439.10; | Peptidase S45 family | null | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=a penicillin + H2O = 6-aminopenicillanate + a carboxylate; Xref=Rhea:RHEA:18693, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:51356, ChEBI:CHEBI:57869; EC=3.5.1.11; | null | null | null | null | null | Escherichia coli |
P06876 | MYB_MOUSE | MARRPRHSIYSSDEDDEDIEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQEPSKASQTPVATSFQKNNHLMGFGHASPPSQLSPSGQSSVNSEYPYYHIAEAQNISSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQALPTQNH... | null | null | B cell differentiation [GO:0030183]; calcium ion transport [GO:0006816]; cellular response to interleukin-6 [GO:0071354]; cellular response to leukemia inhibitory factor [GO:1990830]; embryonic digestive tract development [GO:0048566]; G1/S transition of mitotic cell cycle [GO:0000082]; homeostasis of number of cells [... | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA bindi... | PF09316;PF07988;PF00249; | 1.10.10.60; | null | PTM: SUMOylated by TRAF7; leading to MYB transcriptional activity inhibition. {ECO:0000269|PubMed:16162816}.; PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated by NLK on multiple sites, which induces proteasomal degradation.; PTM: Phosphoryl... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16162816}. | null | null | null | null | null | FUNCTION: Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells. {ECO:0000269|PubMed:16162816}. | Mus musculus (Mouse) |
P06879 | PRL_MOUSE | MNSQGSAQKAGTLLLLLISNLLFCQNVQPLPICSAGDCQTSLRELFDRVVILSHYIHTLYTDMFIEFDKQYVQDREFMVKVINDCPTSSLATPEDKEQALKVPPEVLLNLILSLVQSSSDPLFQLITGVGGIQEAPEYILSRAKEIEEQNKQLLEGVEKIISQAYPEAKGNGIYFVWSQLPSLQGVDEESKILSLRNTIRCLRRDSHKVDNFLKVLRCQIAHQNNC | null | null | cell population proliferation [GO:0008283]; epithelial cell proliferation [GO:0050673]; female pregnancy [GO:0007565]; lactation [GO:0007595]; mammary gland development [GO:0030879]; maternal behavior [GO:0042711]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141] | hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation. | Mus musculus (Mouse) |
P06880 | SOMA_MOUSE | MATDSRTSWLLTVSLLCLLWPQEASAFPAMPLSSLFSNAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKEEAQQRTDMELLRFSLLLIQSWLGPVQFLSRIFTNSLMFGTSDRVYEKLKDLEEGIQALMQELEDGSPRVGQILKQTYDKFDANMRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF | null | null | animal organ development [GO:0048513]; cellular response to alkaline pH [GO:0071469]; cellular response to insulin stimulus [GO:0032869]; cellular response to thyroid hormone stimulus [GO:0097067]; female pregnancy [GO:0007565]; growth hormone receptor signaling pathway [GO:0060396]; lung alveolus development [GO:00482... | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; trans-Golgi network [GO:0005802] | growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; hormone activity [GO:0005179]; metal ion binding [GO:0046872] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. | Mus musculus (Mouse) |
P06881 | CALCA_HUMAN | MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSRIIAQKRACDTATCVTHRLAGLLSRSGGVVKNNFVPTNVGSKAFGRRRRDLQA | null | null | activation of adenylate cyclase activity [GO:0007190]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcitonin gene-related peptide receptor signaling pathway [GO:1990408]; cell-cell signaling [GO:0007267]; endothelial cell migration [GO:0043542]; endothelial cell proliferatio... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcitonin receptor binding [GO:0031716]; hormone activity [GO:0005179]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF00214; | 6.10.250.2190; | Calcitonin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. It also elevates platelet cAMP. {ECO:0000269|PubMed:1318039}. | Homo sapiens (Human) |
P06882 | THYG_RAT | MMTLVLWVSTLLSSVCLVAANIFEYQVDAQPLRPCELQREKAFLKQDEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTACLSFCQLHKQRILLSSYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRCPRSCEIRSRRLLHGVGDKSPPQCDADGEFMPVQCKFVNTTDMMIFDLIHNYNRFPDAFVTFSAFRNRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDQASTFTQSTMYRILQRRFLAIQLVISGRFRCPTKCEVEQFTATSFGHPYIPSC... | null | null | hormone biosynthetic process [GO:0042446]; iodide transport [GO:0015705]; regulation of myelination [GO:0031641]; response to lipopolysaccharide [GO:0032496]; response to pH [GO:0009268]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590]; thyroid hormone metabolic process [GO:0042403]; tra... | extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991] | anion binding [GO:0043168]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; signaling receptor binding [GO:0005102] | PF00135;PF07699;PF00086; | 3.40.50.1820;4.10.800.10;2.10.50.10; | Type-B carboxylesterase/lipase family | PTM: Iodinated on tyrosine residues by TPO (By similarity). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-25 is coupled to donor Tyr-150 or Tyr-235, acceptor Tyr-2574 is coupled to donor Tyr-2541, acceptor Tyr-2766 in monomer 1 is coupled to donor Tyr-2766 in monomer 2 and acceptor Tyr-1310 i... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08710}. Note=Secreted into the thyroid follicle lumen. Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers. {ECO:0000250|UniProtKB:O08710}. | null | null | null | null | null | FUNCTION: Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (By similarity). Following TG re-internalization ... | Rattus norvegicus (Rat) |
P06883 | GLUC_RAT | MKTVYIVAGLFVMLVQGSWQHAPQDTEENARSFPASQTEPLEDPDQINEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIAEELGRRHADGSFSDEMNTILDNLATRDFINWLIQTKITDKK | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cellular response to glucagon stimulus [GO:0071377]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; negative regulation of apop... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | glucagon receptor binding [GO:0031769]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; receptor ligand activity [GO:0048018] | PF00123; | 6.10.250.590; | Glucagon family | PTM: Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-te... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01275}.; SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted {ECO:0000250|UniProtKB:P01275}. | null | null | null | null | null | FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maint... | Rattus norvegicus (Rat) |
P06899 | H2B1J_HUMAN | MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK | null | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; chromatin organization [GO:0006325]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response in mucosa [GO... | CENP-A containing nucleosome [GO:0043505]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; lipopolysaccharide binding [GO:0001530]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H2B family | PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specif... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Homo sapiens (Human) |
P06907 | MYP0_RAT | MAPGAPSSSPSPILAALLFSSLVLSPTLAIVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPSWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKVPTRYGVVLGAVIGGILGVVLLLLLLFYLIRYCWLRRQAALQRRLSAMEKGKFHKSSKDSSKRGRQTPVLYAMLDHSRSTKAASEKKSKGLGESRKDKK | null | null | cell aggregation [GO:0098743]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cell-cell junction maintenance [GO:0045217]; myelination [GO:0042552]; negative regulation of apoptotic process [GO:0043066] | basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | null | PF10570;PF07686; | 2.60.40.10; | Myelin P0 protein family | PTM: N-glycosylated; contains sulfate-substituted glycan. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25189}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25189}. | null | null | null | null | null | FUNCTION: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction. {ECO:0000250|UniProtKB:P25189}. | Rattus norvegicus (Rat) |
P06909 | CFAH_MOUSE | MRLSARIIWLILWTVCAAEDCKGPPPRENSEILSGSWSEQLYPEGTQATYKCRPGYRTLGTIVKVCKNGKWVASNPSRICRKKPCGHPGDTPFGSFRLAVGSQFEFGAKVVYTCDDGYQLLGEIDYRECGADGWINDIPLCEVVKCLPVTELENGRIVSGAAETDQEYYFGQVVRFECNSGFKIEGHKEIHCSENGLWSNEKPRCVEILCTPPRVENGDGINVKPVYKENERYHYKCKHGYVPKERGDAVCTGSGWSSQPFCEEKRCSPPYILNGIYTPHRIIHRSDDEIRYECNYGFYPVTGSTVSKCTPTGWIPVPRC... | null | null | activation of membrane attack complex [GO:0001905]; angiogenesis [GO:0001525]; ATP metabolic process [GO:0046034]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; determination of adult lifespan [GO:0008340]; gene expression [GO:0010467]; glomerulus development [GO:0032835];... | axon [GO:0030424]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025] | complement component C3b binding [GO:0001851]; heparin binding [GO:0008201] | PF00084; | 2.10.70.10; | null | PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P08603}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P08603}. | null | null | null | null | null | FUNCTION: Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces. Accelerates th... | Mus musculus (Mouse) |
P06915 | CSP_PLABE | MKKCTILVVASLLLVNSLLPGYGQNKIIQAQRNLNELCYNEGNDNKLYHVLNSKNGKIYNRNTVNRLLPMLRRKKNEKKNEKIERNNKLKQPPPPPNPNDPPPPNPNDPPPPNPNDPPPPNPNDPPPPNANDPPPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPPPPNPNDPAPPQGNNNPQPQPRPQPQPQPQPQPQPQPQPQPRPQPQPQPGGNNNNKNNNNDDSYIPSAEKILEFVKQIRDSITEEWSQCNVTCGSGIRVRKRKGSNKKAEDLTLEDIDTEICKMDKCSSIF... | null | null | positive regulation of developmental process [GO:0051094] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | null | PF00090; | 2.20.100.10; | Plasmodium circumsporozoite protein family | PTM: During host cell invasion, proteolytically cleaved at the cell membrane in the region I by a papain-like cysteine protease of parasite origin. Cleavage is triggered by the sporozoite contact with highly sulfated heparan sulfate proteoglycans (HSPGs) present on the host hepatocyte cell surface. Cleavage exposes the... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23093}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P23093}. Note=Localizes to the cytoplasm and the cell membrane in oocysts at day 6 post infection and then gradually distributes over the entire cell surface of the sporoblast and... | null | null | null | null | null | FUNCTION: Essential sporozoite protein (PubMed:9002517). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (PubMed:9002517). In the vertebrate host, required for sporozoite migration through the host dermis and inf... | Plasmodium berghei |
P06922 | VE4_HPV16 | MADPAAATKYPLLKLLGSTWPTTPPRPIPKPSPWAPKKHRRLSSDQDQSQTPETPATPLSCCTETQWTVLQSSLHLTAHTKDGLTVIVTLHP | null | null | symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | null | PF02711; | null | Papillomaviridae E4 protein family | PTM: Phosphorylated by host ERK. The phosphorylation triggers a structural change that enhances keratin binding and protein stability. {ECO:0000269|PubMed:19211765}. | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:17360743}. Host nucleus {ECO:0000269|PubMed:17360743}. | null | null | null | null | null | FUNCTION: Contributes to multiple aspects of the viral life cycle including viral genome amplification, suppression of suprabasal cell differentiation and egress of newly formed virions. Induces host cell cycle arrest at the G2 phase by associating with and preventing the nuclear entry of host CDK1/cyclin B1 complexes.... | Human papillomavirus type 16 |
P06935 | POLG_WNV | MSKKPGGPGKNRAVNMLKRGMPRGLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKHLLSFKKELGTLTSAINRRSTKQKKRGGTAGFTILLGLIACAGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRAMDVGYLCEDTITYECPVLAAGNDPEDIDCWCTKSSVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWLDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAILLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSC... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; positive regulation of viral genome replication [GO:0045070]; proteolysis [GO:0006508]; RNA 5'-cap (guanine-N7)-methylation [GO:0106005... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; protein-DNA complex [GO:0032993]; ribonucleoprotein complex [GO:1990904]; viral capsid [GO:0019028]; viral envelope [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA/DNA annealing activity [GO:1990814]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activi... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:19889084}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface pr... | West Nile virus (WNV) |
P06939 | VPX_HV2RO | MTDPRETVPPGNSGEETIGEAFAWLNRTVEAINREAVNHLPRELIFQVWQRSWRYWHDEQGMSESYTKYRYLCIIQKAVYMHVRKGCTCLGRGHGPGGWRPGPPPPPPPGLV | null | null | viral life cycle [GO:0019058]; virus-mediated perturbation of host defense response [GO:0019049] | host cell nucleus [GO:0042025]; virion component [GO:0044423] | null | PF00522; | 1.20.5.4730; | Lentivirus VPX protein family | null | SUBCELLULAR LOCATION: Virion. Host nucleus. Note=Nuclear just after virion uncoating, or if expressed in the absence of unprocessed GAG. | null | null | null | null | null | FUNCTION: Plays a role in nuclear translocation of the viral pre-integration complex (PIC), thus is required for the virus to infect non-dividing cells. Targets specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction wit... | Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2) |
P06959 | ODP2_ECOLI | MAIEIKVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTQTGALIMIFDSADGAADAAPAQAEEKKEAAPAAAPAAAAAKDVNVPDIGSDEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAGAAAPAAKQEAAPAAAPAPAAGVKEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMIFEVEGAAPAAAPAKQEAAAPAPAAKAEAPAAAPAAKAEGKSEF... | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 3 lipoyl cofactors covalently.; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; glycolytic process [GO:0006096]; pyruvate catabolic process [GO:0042867]; pyruvate metabolic process [GO:0006090] | cytoplasm [GO:0005737]; pyruvate dehydrogenase complex [GO:0045254] | acetyltransferase activity [GO:0016407]; dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742]; lipoic acid binding [GO:0031405] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; | null | null | null | null | FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). | Escherichia coli (strain K12) |
P06960 | OTC2_ECOLI | MSDLYKKHFLKLLDFTPAQFTSLLTLAAQLKADKKNGKEVQKLTGKNIALIFEKDSTRTRCSFEVAAFDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAQYAGVPVWNGLTNEFHPTQLLADLMTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLLAPKACWPEESLVAECSALAEKHGGKITLTEDVAAGVKGADFIYTDVWVSMGEAKEKWAERIALLRGYQVNAQMMALTDNPNVKFLHCLPAFHDDQTTLGKQMAKEFDLHGGMEVTDEVFESAASIVFDQAENR... | 2.1.3.3 | null | arginine biosynthetic process via ornithine [GO:0042450]; citrulline biosynthetic process [GO:0019240]; DNA damage response [GO:0006974] | cytoplasm [GO:0005737] | amino acid binding [GO:0016597]; metal ion binding [GO:0046872]; ornithine carbamoyltransferase activity [GO:0004585] | PF00185;PF02729; | 3.40.50.1370; | Aspartate/ornithine carbamoyltransferase superfamily, OTCase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01109}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.02 mM for carbamoyl phosphate {ECO:0000269|PubMed:789338}; KM=5 mM for L-ornithine {ECO:0000269|PubMed:789338}; | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000305}. | null | null | FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. {ECO:0000269|PubMed:789338}. | Escherichia coli (strain K12) |
P06961 | CCA_ECOLI | MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAPDVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALMREMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPAKWHPEIDTGIHTLMTLSMAAMLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPKTIV... | 2.7.7.72; 3.1.3.-; 3.1.4.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O28126}; Note=Magnesium is required for nucleotidyltransferase activity. {ECO:0000250|UniProtKB:O28126}; COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Note=Nickel for phosphatase activity. {ECO:0000269|PubMed:15210699}; | RNA repair [GO:0042245]; tRNA 3'-terminal CCA addition [GO:0001680]; tRNA surveillance [GO:0106354] | null | ATP binding [GO:0005524]; CCA tRNA nucleotidyltransferase activity [GO:0004810]; CCACCA tRNA nucleotidyltransferase activity [GO:0160016]; cyclic-nucleotide phosphodiesterase activity [GO:0004112]; magnesium ion binding [GO:0000287]; phosphatase activity [GO:0016791]; tRNA binding [GO:0000049] | PF01966;PF01743;PF12627; | 3.30.460.10;1.10.3090.10; | TRNA nucleotidyltransferase/poly(A) polymerase family, Bacterial CCA-adding enzyme type 1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72; Evidence={ECO:0000269|PubMed:3516995}; CAT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.33 mM for ATP (in the tRNA-NT activity assay) {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.03 mM for CTP (in the tRNA-NT activity assay) {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; KM=0.015 mM for tRNA-CC {ECO:0000269|PubMed:1521... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4 for AMP incorporation, 10.0 for CMP incorporation, and 7.0 for the phosphatase and phosphodiesterase activities. {ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995}; | null | FUNCTION: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template (PubMed:3516995). Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate (PubMed:3516995... | Escherichia coli (strain K12) |
P06968 | DUT_ECOLI | MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ | 3.6.1.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15208312}; | dUMP biosynthetic process [GO:0006226]; dUTP catabolic process [GO:0046081]; protein homotrimerization [GO:0070207] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | dUTP diphosphatase activity [GO:0004170]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287] | PF00692; | 2.70.40.10; | DUTPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1311056, ECO:0000305|PubMed:9261872}. | CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000269|PubMed:9261872}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.28 uM for dUTP {ECO:0000269|PubMed:9261872}; Note=kcat is 5.15 sec(-1). {ECO:0000269|PubMed:9261872}; | PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. | null | null | FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000269|PubMed:9261872}. | Escherichia coli (strain K12) |
P06971 | FHUA_ECOLI | MARSKTAQPKHSLRKIAVVVATAVSGMSVYAQAAVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFD... | null | null | intracellular iron ion homeostasis [GO:0006879]; siderophore transmembrane transport [GO:0044718] | cell outer membrane [GO:0009279]; membrane [GO:0016020]; transmembrane transporter complex [GO:1902495] | iron ion binding [GO:0005506]; protein domain specific binding [GO:0019904]; siderophore uptake transmembrane transporter activity [GO:0015344]; signaling receptor activity [GO:0038023]; toxic substance binding [GO:0015643]; virion binding [GO:0046790] | PF07715;PF00593; | 2.40.170.20;2.170.130.10; | TonB-dependent receptor family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2066336, ECO:0000269|PubMed:8916906, ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}; Multi-pass membrane protein {ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}. | null | null | null | null | null | FUNCTION: Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane (PubMed:1089064, PubMed:2066336). In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog... | Escherichia coli (strain K12) |
P06972 | FHUB_ECOLI | MSKRIALFPALLLALLVIVATALTWMNFSQALPRSQWAQAAWSPDIDVIEQMIFHYSLLPRLAISLLVGAGLGLVGVLFQQVLRNPLAEPTTLGVATGAQLGITVTTLWAIPGAMASQFAAQAGACVVGLIVFGVAWGKRLSPVTLILAGLVVSLYCGAINQLLVIFHHDQLQSMFLWSTGTLTQTDWGGVERLWPQLLGGVMLTLLLLRPLTLMGLDDGVARNLGLALSLARLAALSLAIVISALLVNAVGIIGFIGLFAPLLAKMLGARRLLPRLMLASLIGALILWLSDQIILWLTRVWMEVSTGSVTALIGAPLLL... | null | null | iron ion import across plasma membrane [GO:0098711]; siderophore-dependent iron import into cell [GO:0033214] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; plasma membrane [GO:0005886] | transmembrane transporter activity [GO:0022857] | PF01032; | 1.10.3470.10; | Binding-protein-dependent transport system permease family, FecCD subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:15919996}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:1551849, ECO:0000269|PubMed:3020380, ECO:0000269|PubMed:34887516}. | Escherichia coli (strain K12) |
P06974 | FLIM_ECOLI | MGDSILSQAEIDALLNGDSEVKDEPTASVSGESDIRPYDPNTQRRVVRERLQALEIINERFARHFRMGLFNLLRRSPDITVGAIRIQPYHEFARNLPVPTNLNLIHLKPLRGTGLVVFSPSLVFIAVDNLFGGDGRFPTKVEGREFTHTEQRVINRMLKLALEGYSDAWKAINPLEVEYVRSEMQVKFTNITTSPNDIVVNTPFHVEIGNLTGEFNICLPFSMIEPLRELLVNPPLENSRNEDQNWRDNLVRQVQHSQLELVANFADISLRLSQILKLNPGDVLPIEKPDRIIAHVDGVPVLTSQYGTLNGQYALRIEHL... | null | null | bacterial-type flagellum-dependent swarming motility [GO:0071978]; bacterial-type flagellum-dependent swimming motility [GO:0071977]; chemotaxis [GO:0006935]; positive chemotaxis [GO:0050918] | bacterial-type flagellum [GO:0009288]; bacterial-type flagellum basal body, C ring [GO:0009433]; bacterial-type flagellum rotor complex [GO:0120107]; plasma membrane [GO:0005886] | cytoskeletal motor activity [GO:0003774] | PF02154;PF01052; | 3.40.1550.10;2.30.330.10; | FliM family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. Bacterial flagellum basal body. | null | null | null | null | null | FUNCTION: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Escherichia coli (strain K12) |
P06983 | HEM3_ECOLI | MLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVILDTPLAKVGGKGLFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNYDSLDALPAGSIVGTSSLRRQCQLAERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAGLKRLGLESRIRAALPPEISLPAVGQGAVGIECRLDDSRTRELLAALNHHETALRVTAERAMNTRLEGGCQVPIGSYAELIDGEIWLRALVGAPDGSQIIRGERRGAPQDAEQMGISLAEELLNNGAREILAEVYNGDAPA | 2.5.1.61 | COFACTOR: Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; Note=Binds 1 dipyrromethane group covalently.; | heme biosynthetic process [GO:0006783]; protoporphyrinogen IX biosynthetic process [GO:0006782]; tetrapyrrole biosynthetic process [GO:0033014] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | hydroxymethylbilane synthase activity [GO:0004418] | PF01379;PF03900; | 3.40.190.10;3.30.160.40; | HMBS family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61; Evidence={ECO:0000269|PubMed:3052434}; | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. {ECO:0000305|PubMed:3052434}. | null | null | FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. {ECO:0000269|PubMed:3529035}. | Escherichia coli (strain K12) |
P06988 | HISX_ECOLI | MSFNTIIDWNSCTAEQQRQLLMRPAISASESITRTVNDILDNVKARGDEALREYSAKFDKTTVTALKVSAEEIAAASERLSDELKQAMAVAVKNIETFHTAQKLPPVDVETQPGVRCQQVTRPVASVGLYIPGGSAPLFSTVLMLATPASIAGCKKVVLCSPPPIADEILYAAQLCGVQDVFNVGGAQAIAALAFGTESVPKVDKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVLVIADSGATPDFVASDLLSQAEHGPDSQVILLTPAADMARRVAEAVERQLAELPRAETARQALNASRLIVTKDLAQCVEIS... | 1.1.1.23 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11842181}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11842181}; | histidine biosynthetic process [GO:0000105] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | histidinol dehydrogenase activity [GO:0004399]; manganese ion binding [GO:0030145]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; zinc ion binding [GO:0008270] | PF00815; | 1.20.5.1300;3.40.50.1980; | Histidinol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01024}; | null | PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. {ECO:0000255|HAMAP-Rule:MF_01024}. | null | null | FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000255|HAMAP-Rule:MF_01024}. | Escherichia coli (strain K12) |
P06992 | RSMA_ECOLI | MNNRVHQGHLARKRFGQNFLNDQFVIDSIVSAINPQKGQAMVEIGPGLAALTEPVGERLDQLTVIELDRDLAARLQTHPFLGPKLTIYQQDAMTFNFGELAEKMGQPLRVFGNLPYNISTPLMFHLFSYTDAIADMHFMLQKEVVNRLVAGPNSKAYGRLSVMAQYYCNVIPVLEVPPSAFTPPPKVDSAVVRLVPHATMPHPVKDVRVLSRITTEAFNQRRKTIRNSLGNLFSVEVLTGMGIDPAMRAENISVAQYCQMANYLAENAPLQES | 2.1.1.182 | null | maturation of SSU-rRNA [GO:0030490]; response to antibiotic [GO:0046677]; ribosomal small subunit assembly [GO:0000028]; rRNA base methylation [GO:0070475]; rRNA methylation [GO:0031167]; rRNA processing [GO:0006364] | cytosol [GO:0005829] | 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity [GO:0052908]; double-stranded DNA binding [GO:0003690]; mRNA binding [GO:0003729]; ribosomal small subunit binding [GO:0043024]; rRNA (adenine-N6,N6-)-dimethyltransferase activity [GO:0000179] | PF00398; | 1.10.8.100;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, rRNA adenine N(6)-methyltransferase family, RsmA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19609, Rhea:RHEA-COMP:10232, Rhea:RHEA-COMP:10233, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChE... | null | null | null | null | FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Has also a DNA glycosylase/AP lyase activity that removes C mispaired with oxidized T from DNA, and ma... | Escherichia coli (strain K12) |
P06993 | MALT_ECOLI | MLIPSKLSRPVRLDHTVVRERLLAKLSGANNFRLALITSPAGYGKTTLISQWAAGKNDIGWYSLDEGDNQQERFASYLIAAVQQATNGHCAICETMAQKRQYASLTSLFAQLFIELAEWHSPLYLVIDDYHLITNPVIHESMRFFIRHQPENLTLVVLSRNLPQLGIANLRVRDQLLEIGSQQLAFTHQEAKQFFDCRLSSPIEAAESSRICDDVSGWATALQLIALSARQNTHSAHKSARRLAGINASHLSDYLVDEVLDNVDLATRHFLLKSAILRSMNDALITRVTGEENGQMRLEEIERQGLFLQRMDDTGEWFCY... | null | null | positive regulation of carbohydrate metabolic process [GO:0045913]; positive regulation of DNA-templated transcription [GO:0045893] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; trisaccharide binding [GO:0048031] | PF00196;PF17874; | 3.40.50.300;1.25.40.10;1.10.10.10; | MalT family | null | null | null | null | null | null | null | FUNCTION: Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides (PubMed:2524384, PubMed:2538630, PubMed:3305511, PubMed:7040340). Specifically binds to the promoter region of its target genes, recognizing a short DNA motif c... | Escherichia coli (strain K12) |
P06996 | OMPC_ECOLI | MKVKVLSLLVPALLVAGAANAAEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVD... | null | null | DNA damage response [GO:0006974]; monoatomic ion transmembrane transport [GO:0034220]; receptor-mediated virion attachment to host cell [GO:0046813] | cell outer membrane [GO:0009279]; pore complex [GO:0046930] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; porin activity [GO:0015288]; virus receptor activity [GO:0001618] | PF00267; | 2.40.160.10; | Gram-negative porin family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2464593}; Multi-pass membrane protein {ECO:0000269|PubMed:16949612}. | null | null | null | null | null | FUNCTION: Forms pores that allow passive diffusion of small molecules across the outer membrane.; FUNCTION: (Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF. {ECO:0000305|PubMed:27723824}.; FUNCTION: (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane rece... | Escherichia coli (strain K12) |
P06999 | PFKB_ECOLI | MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRCIVDSSGEALSAALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLSR | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16866375}; | DNA damage response [GO:0006974]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | 6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; tagatose-6-phosphate kinase activity [GO:0009024] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000269|PubMed:16866375, ECO:0000269|PubMed:23823238}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for ATP {ECO:0000269|PubMed:23823238}; KM=6 uM for fructose 6-phosphate {ECO:0000269|PubMed:23823238}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000269|PubMed:16866375}. | Escherichia coli (strain K12) |
P07001 | PNTA_ECOLI | MRIGIPRERLTNETRVAATPKTVEQLLKLGFTVAVESGAGQLASFDDKAFVQAGAEIVEGNSVWQSEIILKVNAPLDDEIALLNPGTTLVSFIWPAQNPELMQKLAERNVTVMAMDSVPRISRAQSLDALSSMANIAGYRAIVEAAHEFGRFFTGQITAAGKVPPAKVMVIGAGVAGLAAIGAANSLGAIVRAFDTRPEVKEQVQSMGAEFLELDFKEEAGSGDGYAKVMSDAFIKAEMELFAAQAKEVDIIVTTALIPGKPAPKLITREMVDSMKAGSVIVDLAAQNGGNCEYTVPGEIFTTENGVKVIGYTDLPGRLP... | 7.1.1.1 | null | NADPH regeneration [GO:0006740]; proton export across plasma membrane [GO:0120029] | plasma membrane [GO:0005886] | NAD(P)+ transhydrogenase (AB-specific) activity [GO:0008750]; NAD(P)+ transhydrogenase activity [GO:0008746]; NADP binding [GO:0050661]; protein dimerization activity [GO:0046983] | PF01262;PF05222;PF12769; | 3.40.50.720; | AlaDH/PNT family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+); Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1; Evidence={ECO:0000269|PubMed:16083909}; | null | null | null | null | FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. {ECO:0000269|PubMed:16083909}. | Escherichia coli (strain K12) |
P07003 | POXB_ECOLI | MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDVALKPAPEGATMHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRALL... | 1.2.5.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:5336022, ECO:0000269|PubMed:6752142}; Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:6752142}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_... | pyruvate catabolic process [GO:0042867]; pyruvate metabolic process [GO:0006090] | cytosol [GO:0005829]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; magnesium ion binding [GO:0000287]; pyruvate dehydrogenase (quinone) activity [GO:0052737]; thiamine pyrophosphate binding [GO:0030976]; ubiquinone binding [GO:0048039] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | PTM: Activated by limited proteolytic digestion in vitro. This cleavage produces a peptide (alpha-peptide) and mimics the activation of enzyme by phospholipids (PubMed:334770, PubMed:334771, PubMed:3902830, PubMed:5336022). Protease activation and lipid-activation are mutually exclusive. Proteolytic cleavage results in... | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:365232, ECO:0000305|PubMed:5336022}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:365232, ECO:0000305|PubMed:5336022}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:... | CATALYTIC ACTIVITY: Reaction=a ubiquinone + H2O + pyruvate = a ubiquinol + acetate + CO2; Xref=Rhea:RHEA:27405, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:16389, ChEBI:CHEBI:16526, ChEBI:CHEBI:17976, ChEBI:CHEBI:30089; EC=1.2.5.1; Evidence={ECO:0000255|HAMAP-Rule:MF_0085... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90 mM for pyruvate, non-activated form {ECO:0000269|PubMed:18988747}; KM=12 mM for pyruvate, activated form {ECO:0000269|PubMed:18988747}; Note=kcat is 7 sec(-1) for non-activated, 200 sec(-1) for activated form. {ECO:0000269|PubMed:18988747}; | null | null | null | FUNCTION: A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone (By similarity) (PubMed:18988747, PubMed:2663858, PubMed:365232). The main pathway for ace... | Escherichia coli (strain K12) |
P07004 | PROA_ECOLI | MLEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSEIILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDVRQVCNLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALKSCGLPAGAVQAIDNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESVEIAEALKVIVNAKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLQAGPAKVVAVKAEEYDDEFLSLDLNV... | 1.2.1.41 | null | L-proline biosynthetic process [GO:0055129] | cytosol [GO:0005829] | glutamate-5-semialdehyde dehydrogenase activity [GO:0004350]; identical protein binding [GO:0042802]; NADP binding [GO:0050661] | PF00171; | null | Gamma-glutamyl phosphate reductase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}. | CATALYTIC ACTIVITY: Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41; Evidence={ECO:0000255|HAMAP-Rule:MF_00412, ECO:00002... | null | PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00412, ECO:0000269|PubMed:7035170}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:7035170}; | null | FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412, ECO:0000269|PubMed:7034716, ECO:0000269|PubMed:7035170}. | Escherichia coli (strain K12) |
P07012 | RF2_ECOLI | MFEINPVNNRIQDLTERSDVLRGYLDYDAKKERLEEVNAELEQPDVWNEPERAQALGKERSSLEAVVDTLDQMKQGLEDVSGLLELAVEADDEETFNEAVAELDALEEKLAQLEFRRMFSGEYDSADCYLDIQAGSGGTEAQDWASMLERMYLRWAESRGFKTEIIEESEGEVAGIKSVTIKISGDYAYGWLRTETGVHRLVRKSPFDSGGRRHTSFSSAFVYPEVDDDIDIEINPADLRIDVYRTSGAGGQHVNRTESAVRITHIPTGIVTQCQNDRSQHKNKDQAMKQMKAKLYELEMQKKNAEKQAMEDNKSDIGWG... | null | null | translational termination [GO:0006415] | cytosol [GO:0005829] | translation release factor activity, codon specific [GO:0016149] | PF03462;PF00472; | 3.30.160.20;3.30.70.1660;1.20.58.410; | Prokaryotic/mitochondrial release factor family | PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2. Is absent when the factor is overproduced. {ECO:0000269|PubMed:11118225, ECO:0000269|PubMed:11805295, ECO:0000269|PubMed:11847124, ECO:0000269|PubMed:17932046}. | SUBCELLULAR LOCATION: Cytoplasm. Note=Recruited to the 70S ribosome by ArfA even in the absence of mRNA (PubMed:22922063, PubMed:25355516, PubMed:27934701). {ECO:0000269|PubMed:22922063, ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27934701}. | null | null | null | null | null | FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA hydrolase (PubMed:22857598, PubMed:27934701). In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 in... | Escherichia coli (strain K12) |
P07013 | PRIB_ECOLI | MTNRLVLSGTVCRAPLRKVSPSGIPHCQFVLEHRSVQEEAGFHRQAWCQMPVIVSGHENQAITHSITVGSRITVQGFISCHKAKNGLSKMVLHAEQIELIDSGD | null | null | DNA replication initiation [GO:0006270]; DNA replication, synthesis of RNA primer [GO:0006269]; DNA unwinding involved in DNA replication [GO:0006268]; plasmid maintenance [GO:0006276]; replication fork processing [GO:0031297]; response to radiation [GO:0009314] | DnaB-DnaC-DnaT-PriA-PriB complex [GO:1990158]; pre-primosome complex [GO:1990099]; primosome complex [GO:1990077] | identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697] | PF00436; | 2.40.50.140; | PriB family | null | null | null | null | null | null | null | FUNCTION: Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT. {ECO:0000255|HAMAP-Rule:MF_00720, ECO:0000269|PubMed:1646811, ECO:0000269|PubMed:1856227, ECO:0000269|PubMed:8366072}. | Escherichia coli (strain K12) |
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