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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P10870 | SNF3_YEAST | MDPNSNSSSETLRQEKQGFLDKALQRVKGIALRRNNSNKDHTTDDTTGSIRTPTSLQRQNSDRQSNMTSVFTDDISTIDDNSILFSEPPQKQSMMMSICVGVFVAVGGFLFGYDTGLINSITSMNYVKSHVAPNHDSFTAQQMSILVSFLSLGTFFGALTAPFISDSYGRKPTIIFSTIFIFSIGNSLQVGAGGITLLIVGRVISGIGIGAISAVVPLYQAEATHKSLRGAIISTYQWAITWGLLVSSAVSQGTHARNDASSYRIPIGLQYVWSSFLAIGMFFLPESPRYYVLKDKLDEAAKSLSFLRGVPVHDSGLLEE... | null | null | carbohydrate transport [GO:0008643]; fructose transmembrane transport [GO:0015755]; glucose mediated signaling pathway [GO:0010255]; glucose transmembrane transport [GO:1904659]; mannose transmembrane transport [GO:0015761]; negative regulation of meiotic nuclear division [GO:0045835] | cell periphery [GO:0071944]; membrane [GO:0016020]; plasma membrane [GO:0005886] | carbohydrate:proton symporter activity [GO:0005351]; glucose binding [GO:0005536] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family | PTM: Phosphorylated in the C-terminal tail on Yck consensus sites in a yeast casein kinases YCK1 and YCK2 (Yck)-dependent manner. This phosphorylation is required for interaction with HXT corepressors MTH1 and STD1 and ultimately HXT expression. {ECO:0000250|UniProtKB:Q12300}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2406560, ECO:0000269|PubMed:3281163}; Multi-pass membrane protein {ECO:0000269|PubMed:3281163}. | null | null | null | null | null | FUNCTION: High-affinity low glucose sensor that is part of the sensor/receptor-repressor (SSR) glucose-signaling pathway, which detects extracellular glucose and induces expression of glucose transporters that bring glucose into the cell (PubMed:8901598, PubMed:9564039). The transporter-like sensor generates an intrace... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10880 | AROL_DICCH | MTEPIFMVGARGCGKTTVGRELARALGYEFVDTDIFMQHTSGMTVADVVAAEGWPGFRRRESEALQAVATPNRVVATGGGMVLLEQNRQFMRAHGTVVYLFAPAEELALRLQASPQAHQRPTLTGRPIAEEMEAVLREREALYQDVAHYVVDATQPPAAIVCELMQTMRLPAA | 2.7.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9600856}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:9600856}; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; shikimate kinase activity [GO:0004765] | PF01202; | 3.40.50.300; | Shikimate kinase family, AroL subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=310 uM for shikimate {ECO:0000269|PubMed:11369852}; KM=620 uM for ATP {ECO:0000269|PubMed:11369852}; | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. | null | null | FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. {ECO:0000269|PubMed:11369852}. | Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi) |
P10889 | CXCL2_MOUSE | MAPPTCRLLSAALVLLLLLATNHQATGAVVASELRCQCLKTLPRVDFKNIQSLSVTPPGPHCAQTEVIATLKGGQKVCLDPEAPLVQKIIQKILNKGKAN | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; inflammatory response [GO:0006954]; leukocyte chemotaxis [GO:0030595]; neutrophi... | extracellular space [GO:0005615] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. | Mus musculus (Mouse) |
P10894 | PLCB1_BOVIN | MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWEDDSTVVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKAPKDPKLRELLDVGNIGRLEHRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLAKKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQ... | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; | G protein-coupled receptor signaling pathway [GO:0007186]; lipid catabolic process [GO:0016042]; memory [GO:0007613]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; release of sequestered calcium ion into cytosol [GO:0051209] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607] | calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; phosphatidylinositol phospholipase C activity [GO:0004435] | PF06631;PF09279;PF17787;PF00388;PF00387;PF08703; | 2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10; | null | PTM: Palmitoylated. Palmitoylation at Cys-17 by ZDHHC21 regulates the signaling activity of PLCB1 and the function of the endothelial barrier. Palmitoylation by ZDHHC21 is stimulated by inflammation. {ECO:0000250|UniProtKB:Q9Z1B3}. | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein-coupled receptors. Regulates the function of the endothelial barrier. {ECO:0000250|UniProtKB:Q9Z1B3}. | Bos taurus (Bovine) |
P10896 | RCA_ARATH | MAAAVSTVGAINRAPLSLNGSGSGAVSAPASTFLGKKVVTVSRFAQSNKKSNGSFKVLAVKEDKQTDGDRWRGLAYDTSDDQQDITRGKGMVDSVFQAPMGTGTHHAVLSSYEYVSQGLRQYNLDNMMDGFYIAPAFMDKLVVHITKNFLTLPNIKVPLILGIWGGKGQGKSFQCELVMAKMGINPIMMSAGELESGNAGEPAKLIRQRYREAADLIKKGKMCCLFINDLDAGAGRMGGTTQYTVNNQMVNATLMNIADNPTNVQLPGMYNKEENARVPIICTGNDFSTLYAPLIRDGRMEKFYWAPTREDRIGVCKGIF... | null | null | leaf senescence [GO:0010150]; response to cold [GO:0009409]; response to jasmonic acid [GO:0009753]; response to light stimulus [GO:0009416] | apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane [GO:0009535]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; plant-type cell wall [GO:0009505]; plastoglobule [GO:0010287]; stromule [GO:0010319]; thylakoid [GO:000957... | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; enzyme regulator activity [GO:0030234]; mRNA binding [GO:0003729]; ribulose-1,5-bisphosphate carboxylase/oxygenase activator activity [GO:0046863] | PF00004;PF21228; | 1.10.8.1070;3.40.50.300; | RuBisCO activase family | PTM: Phosphorylated at Thr-78 by CK2. {ECO:0000269|PubMed:27064346}. | SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379}. | null | null | null | null | null | FUNCTION: Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure. | Arabidopsis thaliana (Mouse-ear cress) |
P10897 | CY561_BOVIN | MEGPASPARAPGALPYYVAFSQLLGLIVVAMTGAWLGMYRGGIAWESALQFNVHPLCMIIGLVFLQGDALLVYRVFRNEAKRTTKVLHGLLHVFAFVIALVGLVAVFEHHRKKGYADLYSLHSWCGILVFALFFAQWLVGFSFFLFPGASFSLRSRYRPQHVFFGAAIFLLSVATALLGLKEALLFELGTKYSMFEPEGVLANVLGLLLATFATVILYILTRADWKRPLQAEEQALSMDFKTLTEGDSPSSQ | 7.2.1.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:18501187, ECO:0000269|PubMed:9287327}; Note=Binds 2 heme b groups non-covalently. {ECO:0000305|PubMed:18501187, ECO:0000305|PubMed:9287327}; | ascorbate homeostasis [GO:0140576] | chromaffin granule membrane [GO:0042584]; lysosomal membrane [GO:0005765] | metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; transmembrane monodehydroascorbate reductase activity [GO:0140575] | PF03188; | 1.20.120.1770; | null | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000269|PubMed:2460342}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Note=Secretory vesicle containing catecholamines and amidated peptides. {ECO:0000269|PubMed:2460342}. | CATALYTIC ACTIVITY: Reaction=L-ascorbate(in) + monodehydro-L-ascorbate radical(out) = L-ascorbate(out) + monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:66524, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; Evidence={ECO:0000269|PubMed:1623014, ECO:0000269|PubMed:18501187, ECO:0000269|PubMed:3597367}; PhysiologicalDirection... | null | null | null | null | FUNCTION: Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce monodehydro-L-ascorbate radical in the lumen of secretory vesicles (PubMed:1623014, PubMed:18501187, PubMed:3597367). It is therefore involved the regeneration and homeostasis w... | Bos taurus (Bovine) |
P10902 | NADB_ECOLI | MNTLPEHSCDVLIIGSGAAGLSLALRLADQHQVIVLSKGPVTEGSTFYAQGGIAAVFDETDSIDSHVEDTLIAGAGICDRHAVEFVASNARSCVQWLIDQGVLFDTHIQPNGEESYHLTREGGHSHRRILHAADATGREVETTLVSKALNHPNIRVLERSNAVDLIVSDKIGLPGTRRVVGAWVWNRNKETVETCHAKAVVLATGGASKVYQYTTNPDISSGDGIAMAWRAGCRVANLEFNQFHPTALYHPQARNFLLTEALRGEGAYLKRPDGTRFMPDFDERGELAPRDIVARAIDHEMKRLGADCMFLDISHKPADF... | 1.4.3.16; 1.5.99.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:11294641, ECO:0000269|PubMed:11863440, ECO:0000269|PubMed:2187483, ECO:0000269|PubMed:7033218, ECO:0000269|PubMed:8706749}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11863440}; | 'de novo' NAD biosynthetic process from aspartate [GO:0034628] | cytosol [GO:0005829] | flavin adenine dinucleotide binding [GO:0050660]; L-aspartate oxidase activity [GO:0008734]; L-aspartate:fumarate oxidoreductase activity [GO:0044318] | PF00890;PF02910; | 3.50.50.60;1.20.58.100;3.90.700.10; | FAD-dependent oxidoreductase 2 family, NadB subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-aspartate + O2 = H2O2 + iminosuccinate; Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16; Evidence={ECO:0000269|PubMed:11294641, ECO:0000269|PubMed:12200425, ECO:0000269|PubMed:20149100, ECO:0000269|PubMed:2187483, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.63 mM for L-aspartate (at substrate concentrations between 0.25 and 1.25 mM) {ECO:0000269|PubMed:7033218}; KM=3.33 mM for L-aspartate (at substrate concentrations between 2.0 and 10.00 mM) {ECO:0000269|PubMed:7033218}; KM=0.5 mM for L-aspartate (at substrate conc... | PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1. {ECO:0000269|PubMed:7033218, ECO:0000305|PubMed:2841129}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:7033218}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:2187483}; | FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+) (PubMed:11294641, PubMed:2187483, PubMed:2841129, PubMed:7033218, PubMed:8706749, PubMed:8706750). Can use either oxygen or fumarate as electron acceptors, which allows the enzyme to be functional un... | Escherichia coli (strain K12) |
P10903 | NARK_ECOLI | MSHSSAPERATGAVITDWRPEDPAFWQQRGQRIASRNLWISVPCLLLAFCVWMLFSAVAVNLPKVGFNFTTDQLFMLTALPSVSGALLRVPYSFMVPIFGGRRWTAFSTGILIIPCVWLGFAVQDTSTPYSVFIIISLLCGFAGANFASSMANISFFFPKQKQGGALGLNGGLGNMGVSVMQLVAPLVVSLSIFAVFGSQGVKQPDGTELYLANASWIWVPFLAIFTIAAWFGMNDLATSKASIKEQLPVLKRGHLWIMSLLYLATFGSFIGFSAGFAMLSKTQFPDVQILQYAFFGPFIGALARSAGGALSDRLGGTRV... | null | null | nitrate assimilation [GO:0042128]; nitrate catabolic process [GO:0043602]; nitrate transmembrane transport [GO:0015706]; nitrite transport [GO:0015707] | plasma membrane [GO:0005886] | nitrate transmembrane transporter activity [GO:0015112]; nitrite transmembrane transporter activity [GO:0015113]; solute:inorganic anion antiporter activity [GO:0005452] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Nitrate/nitrite porter (TC 2.A.1.8) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23665960, ECO:0000269|PubMed:25959928}; Multi-pass membrane protein {ECO:0000269|PubMed:23665960, ECO:0000269|PubMed:25959928}. | CATALYTIC ACTIVITY: Reaction=nitrate(in) + nitrite(out) = nitrate(out) + nitrite(in); Xref=Rhea:RHEA:28743, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632; Evidence={ECO:0000269|PubMed:15667293, ECO:0000269|PubMed:23665960, ECO:0000269|PubMed:25959928, ECO:0000305|PubMed:2668029}; | null | null | null | null | FUNCTION: Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane (PubMed:11967075, PubMed:15667293, PubMed:16804183, PubMed:23665960, PubMed:25959928, PubMed:2668029). Functions as a nitrate/nitrite exchanger, and protons are unlikely to be co-transported (PubMed:15667293, PubMed:23... | Escherichia coli (strain K12) |
P10905 | UGPA_ECOLI | MSSSRPVFRSRWLPYLLVAPQLIITVIFFIWPAGEALWYSLQSVDPFGFSSQFVGLDNFVTLFHDSYYLDSFWTTIKFSTFVTVSGLLVSLFFAALVEYIVRGSRFYQTLMLLPYAVAPAVAAVLWIFLFNPGRGLITHFLAEFGYDWNHAQNSGQAMFLVVFASVWKQISYNFLFFYAALQSIPRSLIEAAAIDGAGPIRRFFKIALPLIAPVSFFLLVVNLVYAFFDTFPVIDAATSGGPVQATTTLIYKIYREGFTGLDLASSAAQSVVLMFLVIVLTVVQFRYVESKVRYQ | null | null | glycerol-3-phosphate transmembrane transport [GO:0015794]; glycerophosphodiester transmembrane transport [GO:0001407] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; glycerol-3-phosphate-transporting ATPase complex [GO:1902517]; membrane [GO:0016020]; plasma membrane [GO:0005886] | glycerol-3-phosphate transmembrane transporter activity [GO:0015169]; glycerophosphodiester transmembrane transporter activity [GO:0001406] | PF00528; | 1.10.3720.10; | Binding-protein-dependent transport system permease family, UgpAE subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import (PubMed:23013274, PubMed:2842304). Probably responsible for the translocation of the substrate across the membrane (Probable). Can also transport glycerophosphoryl diesters, which are hydrolyzed to G3P and alcohol dur... | Escherichia coli (strain K12) |
P10906 | UGPE_ECOLI | MIENRPWLTIFSHTMLILGIAVILFPLYVAFVAATLDKQAVYAAPMTLIPGTHLLENIHNIWVNGVGTNSAPFWRMLLNSFVMAFSITLGKITVSMLSAFAIVWFRFPLRNLFFWMIFITLMLPVEVRIFPTVEVIANLQMLDSYAGLTLPLMASATATFLFRQFFMTLPDELVEAARIDGASPMRFFCDIVFPLSKTNLAALFVITFIYGWNQYLWPLLIITDVDLGTTVAGIKGMIATGEGTTEWNSVMVAMLLTLIPPVVIVLVMQRAFVRGLVDSEK | null | null | glycerol-3-phosphate transmembrane transport [GO:0015794] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; glycerol-3-phosphate-transporting ATPase complex [GO:1902517]; membrane [GO:0016020]; plasma membrane [GO:0005886] | glycerol-3-phosphate transmembrane transporter activity [GO:0015169] | PF00528; | 1.10.3720.10; | Binding-protein-dependent transport system permease family, UgpAE subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import (PubMed:23013274, PubMed:2842304). Probably responsible for the translocation of the substrate across the membrane (Probable). Can also transport glycerophosphoryl diesters, which are hydrolyzed to G3P and alcohol dur... | Escherichia coli (strain K12) |
P10907 | UGPC_ECOLI | MAGLKLQAVTKSWDGKTQVIKPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTEGDIWINDQRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKQQIAERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNGGVAEQIGTPVEVYEKPASLFVASFIGSPAMNLLTGRVNNEGTHFELDGGIELPLNGGYRQYAGRKMTLGIRPEHIALSSQAEGGVPMVMDTLEILGADNLAHGRWGEQKL... | 7.6.2.10 | null | carbohydrate transport [GO:0008643]; glycerol-3-phosphate transmembrane transport [GO:0015794]; glycerophosphodiester transmembrane transport [GO:0001407] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; glycerol-3-phosphate-transporting ATPase complex [GO:1902517]; membrane [GO:0016020] | ABC-type glycerol-3-phosphate transporter activity [GO:0015430]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; glycerol-3-phosphate transmembrane transporter activity [GO:0015169]; glycerophosphodiester transmembrane transporter activity [GO:0001406] | PF00005;PF17912; | 2.40.50.100;2.40.50.140;3.40.50.300; | ABC transporter superfamily, sn-glycerol-3-phosphate importer (TC 3.A.1.1.3) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01727, ECO:0000305}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01727, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + sn-glycerol 3-phosphate(out) = ADP + H(+) + phosphate + sn-glycerol 3-phosphate(in); Xref=Rhea:RHEA:21668, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216; EC=7.6.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01727, E... | null | null | null | null | FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import (PubMed:23013274, PubMed:2842304, PubMed:363686, PubMed:7042685, PubMed:8282692). Responsible for energy coupling to the transport system (Probable). Can also transport glycerophosphoryl diesters, which are hydrolyzed... | Escherichia coli (strain K12) |
P10908 | UGPQ_ECOLI | MSNWPYPRIVAHRGGGKLAPENTLASIDVGAKYGHKMIEFDAKLSKDGEIFLLHDDNLERTSNGWGVAGELNWQDLLRVDAGSWYSKMFKGEPLPLLSQVAERCREHGMMANIEIKPTTGTGPLTGKMVALAARELWAGMTPPLLSSFEIDALEAAQQAAPELPRGLLLDEWRDDWRELTARLGCVSIHLNHKLLNKARVMQLKDAGLRILVYTVNKPQRAAELLRWGVDCICTDAIDVIGPNFTAQ | 3.1.4.46 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18083802}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:18083802}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18083802}; | glycerol metabolic process [GO:0006071]; lipid metabolic process [GO:0006629] | cytoplasm [GO:0005737] | glycerophosphocholine phosphodiesterase activity [GO:0047389]; glycerophosphodiester phosphodiesterase activity [GO:0008889]; glycerophosphoinositol glycerophosphodiesterase activity [GO:0047395]; magnesium ion binding [GO:0000287] | PF03009; | 3.20.20.190; | Glycerophosphoryl diester phosphodiesterase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18083802}. | CATALYTIC ACTIVITY: Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597, ChEBI:CHEBI:83408; EC=3.1.4.46; Evidence={ECO:0000269|PubMed:18083802}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 mM for glycerophosphoethanolamine {ECO:0000269|PubMed:18083802}; KM=0.66 mM for glycerophosphoserine {ECO:0000269|PubMed:18083802}; KM=0.62 mM for glycerophosphoglycerol {ECO:0000269|PubMed:18083802}; KM=0.39 mM for glycerophosphoinositol {ECO:0000269|PubMed:1... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:18083802}; | null | FUNCTION: Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. {ECO:0000269|PubMed:18083802}. | Escherichia coli (strain K12) |
P10909 | CLUS_HUMAN | MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQ... | null | null | cell morphogenesis [GO:0000902]; central nervous system myelin maintenance [GO:0032286]; chaperone-mediated protein complex assembly [GO:0051131]; chaperone-mediated protein folding [GO:0061077]; complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; immune complex clearance [GO:0002... | apical dendrite [GO:0097440]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; chromaffin granule [GO:0042583]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:... | amyloid-beta binding [GO:0001540]; low-density lipoprotein particle receptor binding [GO:0050750]; misfolded protein binding [GO:0051787]; protein carrier chaperone [GO:0140597]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; signaling receptor binding [GO:0005102]; tau... | PF01093; | null | Clusterin family | PTM: Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen (PubMed:2387851). Proteolytic cleavage is not necessary for its chaperone activity (PubMed:25402950). All non-secreted forms are not proteolytically cleaved (PubMed:24073260). Chaperone activity of uncleaved forms is d... | SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:2387851, ECO:0000269|PubMed:24073260, ECO:0000269|PubMed:2780565, ECO:0000269|PubMed:3154963, ECO:0000269|PubMed:8292612, ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: [Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP... | Homo sapiens (Human) |
P10911 | MCF2_HUMAN | MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELAETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHRQISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQQAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRCNELRYLSDILVNEIKAKRIQ... | null | null | cellular response to leukemia inhibitory factor [GO:1990830]; dendrite development [GO:0016358]; intracellular signal transduction [GO:0035556]; negative regulation of axonogenesis [GO:0050771]; regulation of small GTPase mediated signal transduction [GO:0051056] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; membrane [GO:0016020] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF13716;PF00169;PF00621; | 1.20.58.60;1.20.900.10;2.30.29.30; | MCF2 family | PTM: Phosphorylation by TNK2 enhances guanine nucleotide exchange factor (GEF) activity toward Rho family proteins. {ECO:0000269|PubMed:10652228}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15157669}.; SUBCELLULAR LOCATION: [Isoform 1]: Membrane.; SUBCELLULAR LOCATION: [Isoform 3]: Membrane. Note=Colocalizes with CDC42 to plasma membrane. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isofor... | Homo sapiens (Human) |
P10912 | GHR_HUMAN | MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLE... | null | null | cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to hormone stimulus [GO:0032870]; cellular response to insulin stimulus [GO:0032869]; cytokine-mediated signaling pathway [GO:0019221]; endocytosis [GO:0006897]; growth hormone receptor signaling pathway [GO:0060396]; horm... | cell surface [GO:0009986]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; growth hormone receptor complex [GO:0070195]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; p... | cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; growth hormone receptor activity [GO:0004903]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; peptide hormone binding [GO:0017046]; proline-rich region binding [GO:0070064]; protein homodimerization activity [GO:0042803]; protein ki... | PF09067;PF00041;PF12772; | 2.60.40.10; | Type I cytokine receptor family, Type 1 subfamily | PTM: The soluble form (GHBP) is produced by phorbol ester-promoted proteolytic cleavage at the cell surface (shedding) by ADAM17/TACE. Shedding is inhibited by growth hormone (GH) binding to the receptor probably due to a conformational change in GHR rendering the receptor inaccessible to ADAM17 (By similarity). {ECO:0... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protei... | null | null | null | null | null | FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway (By similarity). {ECO:0000250}.; FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling.; F... | Homo sapiens (Human) |
P10914 | IRF1_HUMAN | MPITRMRMRPWLEMQINSNQIPGLIWINKEEMIFQIPWKHAAKHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTKNQRKERKSKSSRDAKSKAKRKSCGDSSPDTFSDGLSSSTLPDDHSSYTVPGYMQDLEVEQALTPALSPCAVSSTLPDWHIPVEVVPDSTSDLYNFQVSPMPSTSEATTDEDEEGKLPEDIMKLLEQSEWQPTNVDGKGYLLNEPGVQPTSVYGDFSCKEEPEIDSPGGDIGLSLQRVFTDLKNMDATWLDSLLTPVRLPSIQA... | null | null | apoptotic process [GO:0006915]; CD8-positive, alpha-beta T cell differentiation [GO:0043374]; cellular response to interferon-beta [GO:0035458]; cellular response to mechanical stimulus [GO:0071260]; defense response to virus [GO:0051607]; immune system process [GO:0002376]; negative regulation of cell population proli... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulat... | PF00605; | 1.10.10.10; | IRF family | PTM: Phosphorylated by CK2 and this positively regulates its activity. {ECO:0000269|PubMed:10094406}.; PTM: Sumoylation represses the transcriptional activity and displays enhanced resistance to protein degradation (PubMed:17942705). Sumolyated by UBE2I/UBC9 and SUMO1 (By similarity). Inactivates the tumor suppressor a... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:37622993}. Cytoplasm {ECO:0000250|UniProtKB:P15314}. Note=MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88-associated IRF1. {ECO:0000250|UniProtKB:P15314}. | null | null | null | null | null | FUNCTION: Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses (PubMed:15226432, PubMed:15509808, PubMed:17516545, PubMed:17942705, PubMed:18497060, PubMed:19404407, PubMed:19851330, PubMed:22367195, PubMed:32385160). Regulates transcription of IFN and IFN-i... | Homo sapiens (Human) |
P10915 | HPLN1_HUMAN | MKSLLLLVLISICWADHLSDNYTLDHDRAIHIQAENGPHLLVEAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDYLKEVDVFVSMGYHKKTYGGYQGRVFLKGGSDSDASLVITDLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNYGFWDKDKSRYDVFCFTSNFNGRFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKILGYDRCDAGWLADGSVRYPISR... | null | null | cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; glial cell differentiation [GO:0010001]; positive regulation of neuroblast proliferation [GO:0002052]; skeletal system development [GO:0001501] | collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perineuronal net [GO:0072534]; synapse [GO:0045202] | hyaluronic acid binding [GO:0005540] | PF07686;PF00193; | 2.60.40.10;3.10.100.10; | HAPLN family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. | null | null | null | null | null | FUNCTION: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix. | Homo sapiens (Human) |
P10916 | MLRV_HUMAN | MAPKKAKKRAGGANSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD | null | null | cardiac muscle contraction [GO:0060048]; cardiac myofibril assembly [GO:0055003]; heart contraction [GO:0060047]; heart development [GO:0007507]; muscle cell fate specification [GO:0042694]; negative regulation of cell growth [GO:0030308]; positive regulation of the force of heart contraction [GO:0098735]; regulation o... | A band [GO:0031672]; cardiac myofibril [GO:0097512]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; myofibril [GO:0030016]; myosin complex [GO:0016459]; sarcomere [GO:0030017] | actin monomer binding [GO:0003785]; calcium ion binding [GO:0005509]; myosin heavy chain binding [GO:0032036]; structural constituent of muscle [GO:0008307] | PF13499; | 1.10.238.10; | null | PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000250|UniProtKB:P51667}.; PTM: Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle contraction and function (By similarity). Dephosphorylated by PPP1CB complexed to PPP1R12B (By similarity). The phosphorylated form in adult is expressed as gradients across t... | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:P08733}. | null | null | null | null | null | FUNCTION: Contractile protein that plays a role in heart development and function (PubMed:23365102, PubMed:32453731). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of ... | Homo sapiens (Human) |
P10922 | H10_MOUSE | MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKGDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAKTVKPKAKSSAKRASKKK | null | null | chromosome condensation [GO:0030261]; heterochromatin formation [GO:0031507]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334] | actin cytoskeleton [GO:0015629]; euchromatin [GO:0000791]; Golgi apparatus [GO:0005794]; nuclear body [GO:0016604]; nucleosome [GO:0000786]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: ADP-ribosylated on Ser-104 in response to DNA damage. {ECO:0000250|UniProtKB:P07305}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division. | Mus musculus (Mouse) |
P10923 | OSTP_MOUSE | MRLAVICFCLFGIASSLPVKVTDSGSSEEKLYSLHPDPIATWLVPDPSQKQNLLAPQNAVSSEEKDDFKQETLPSNSNESHDHMDDDDDDDDDDGDHAESEDSVDSDESDESHHSDESDETVTASTQADTFTPIVPTVDVPNGRGDSLAYGLRSKSRSFQVSDEQYPDATDEDLTSHMKSGESKESLDVIPVAQLLSMPSDQDNNGKGSHESSQLDEPSLETHRLEHSKESQESADQSDVIDSQASSKASLEHQSHKFHSHKDKLVLDPKSKEDDRYLKFRISHELESSSSEVN | null | null | bone mineralization [GO:0030282]; calcium ion homeostasis [GO:0055074]; cell adhesion [GO:0007155]; cellular response to fluid shear stress [GO:0071498]; cellular response to leukemia inhibitory factor [GO:1990830]; collecting duct development [GO:0072044]; intracellular calcium ion homeostasis [GO:0006874]; intracellu... | apical part of cell [GO:0045177]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; vesicle [GO:0031982] | cytokine activity [GO:0005125]; extracellular matrix binding [GO:0050840]; integrin binding [GO:0005178] | PF00865; | null | Osteopontin family | PTM: Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif (By similarity). The phosphorylated form inhibits hydroxyapatite crystallization (PubMed:23427088). Dephosphorylation via a mechanism involving ALPL/TNAP promotes hydroxyapatite crystallization (PubMed:2342... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P10451}. | null | null | null | null | null | FUNCTION: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. {ECO:0000250|UniProtKB:P31096}.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin... | Mus musculus (Mouse) |
P10933 | FENR1_PEA | MAAAVTAAVSLPYSNSTSLPIRTSIVAPERLVFKKVSLNNVSISGRVGTIRAQVTTEAPAKVVKHSKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNTFVYMCGL... | 1.18.1.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | electron transport chain [GO:0022900]; photosynthesis [GO:0015979] | chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane protein complex [GO:0098807] | ferredoxin-NADP+ reductase activity [GO:0004324]; NADPH dehydrogenase activity [GO:0003959] | PF00175; | 3.40.50.80;2.40.30.10; | Ferredoxin--NADP reductase type 1 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast thylakoid membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Stromal side {ECO:0000305}. Note=In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane. | CATALYTIC ACTIVITY: Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.2; | null | PATHWAY: Energy metabolism; photosynthesis. | null | null | FUNCTION: May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
P10937 | PNMT_RAT | MDRGSDPKHTAGMDSDSDPGQAEVALAYQRFEPRAYLRNNYAPPRGDLSNPDGVGPWKLRCMAQVFATGEVSGQVLIDIGSGPTIYQLLSACAHFEDITMTDFLEVNRQELGLWLREEPGAFDWSVYSQHVCLIEDKGESWQEKERQLRARVKRVLPIDVHKPQPLGASGLAPLPADALVSAFCLEAVSPDLPSFRQALYHITTLLRPGGNLLFIGALEESWYLAGEARLSVVPVSEEEVREALVCSGYEVRDLRTYIMPAHLRTGVDDVKGIFFAWAQKIEVQV | 2.1.1.28 | null | adrenal gland development [GO:0030325]; catecholamine biosynthetic process [GO:0042423]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to growth factor stimulus [GO:0071363]; cellular response to peptide hormone stimulus [GO:0071375]; epinephrine biosynthetic process [GO:0042418]; methylat... | axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; terminal bouton [GO:0043195]; varicosity [GO:0043196] | methyltransferase activity [GO:0008168]; phenylethanolamine N-methyltransferase activity [GO:0004603]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]; transferase activity [GO:0016740] | PF01234; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family | null | null | CATALYTIC ACTIVITY: Reaction=phenylethanolamine + S-adenosyl-L-methionine = H(+) + N-methylphenylethanolamine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12176, ChEBI:CHEBI:15378, ChEBI:CHEBI:57741, ChEBI:CHEBI:57856, ChEBI:CHEBI:57946, ChEBI:CHEBI:59789; EC=2.1.1.28; Evidence={ECO:0000269|PubMed:683413}; Physiological... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=288 uM for normetanephrine (enzyme found in the brain) {ECO:0000269|PubMed:683413}; KM=272 uM for normetanephrine (enzyme found in the adrenal gland) {ECO:0000269|PubMed:683413}; KM=1.9 uM for S-adenosyl-L-methionine (enzyme found in the brain) {ECO:0000269|PubMed:... | PATHWAY: Catecholamine biosynthesis; (R)-adrenaline biosynthesis; (R)-adrenaline from (R)-noradrenaline: step 1/1. {ECO:0000250|UniProtKB:P11086}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9 in phosphate buffer. {ECO:0000269|PubMed:683413}; | null | FUNCTION: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor (By similarity). Other substrates include phenylethanolamine, octopamine and normetanephrine (PubMed:13863458, PubMed:683413). {ECO:0000250|UniProtKB:P11086, ECO... | Rattus norvegicus (Rat) |
P10938 | PNMT_BOVIN | MSGTDRSQAAGAVPDSDPGLAAVSSAYQRFEPRAYLRNNYAPPRGDLSCPDGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTIYQLLSACAHFEDITMTDFLEVNRQELRLWLREEPGAFDWSVYSQHVCLIEGKGESWQEKECQLRARVKRILPIDVHRPQPLGAGGLAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLAVVPVREEEVREALVRTATRCGICARTPMPAHLQTGVDDVKGIFFTRAQKKVGV | 2.1.1.28 | null | catecholamine biosynthetic process [GO:0042423]; epinephrine biosynthetic process [GO:0042418]; methylation [GO:0032259] | cytosol [GO:0005829] | phenylethanolamine N-methyltransferase activity [GO:0004603] | PF01234; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:2363805}. | null | CATALYTIC ACTIVITY: Reaction=phenylethanolamine + S-adenosyl-L-methionine = H(+) + N-methylphenylethanolamine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12176, ChEBI:CHEBI:15378, ChEBI:CHEBI:57741, ChEBI:CHEBI:57856, ChEBI:CHEBI:57946, ChEBI:CHEBI:59789; EC=2.1.1.28; Evidence={ECO:0000250|UniProtKB:P11086}; Physiologi... | null | PATHWAY: Catecholamine biosynthesis; (R)-adrenaline biosynthesis; (R)-adrenaline from (R)-noradrenaline: step 1/1. {ECO:0000269|PubMed:5412063}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:5412063}; | null | FUNCTION: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor (PubMed:5412063). Other substrates include phenylethanolamine and octopamine (By similarity). Also methylates normetanephrine (PubMed:13863458, PubMed:5412063). ... | Bos taurus (Bovine) |
P10941 | POLA_CHPVE | MAQLRKPSQSLVLSESVDPTTVDPFVSVRTEEVVPAGCITLWEYRDSCGDVPGPLSHGDLRRLRTPDGVCKCQVHFELPTVLKSGSTGTVPEHPAVLAAFIGRPRRCSLEQRTKELDSRFLQLVHGGLPARPSYMIARPPRPVRGLCSSRNGSLAQFGQGYCYLSAIVDSARWRVARTTGWCVRVADYLRLLQWVGRRSFGSFQIEKSAVDHVYHVVVDAEYQSEQDGALFYQAILGLAEKDPLARIGGRLNPLAAEFAPGSALRVEPVTPQVTRRKGSTRMTGRDPTIVSVGKVGMAITSIQDALVATELRNVNFGRRD... | 3.4.22.- | null | proteolysis [GO:0006508]; virus-mediated perturbation of host defense response [GO:0019049] | null | cysteine-type endopeptidase activity [GO:0004197] | PF01830; | null | null | PTM: [Papain-like protease p29]: Autocatalytically processed. {ECO:0000269|PubMed:1996319}. | null | null | null | null | null | null | FUNCTION: P40 protein is involved in reduction of conidiation of the host. Not necessary for replication. Also involved in reduction of orange pigmentation of the host.; FUNCTION: [Papain-like protease p29]: Cysteine protease of the peptidase family C7 that contributes to hypovirulence-associated traits like the reduct... | Cryphonectria hypovirus 1 (strain EP713) (CHV-1/EP713) (Chestnut blight fungus hypovirulence-associated virus) |
P10943 | HUTP_BACSU | MTLHKERRIGRLSVLLLLNEAEESTQVEELERDGWKVCLGKVGSMDAHKVVAAIETASKKSGVIQSEGYRESHALYHATMEALHGVTRGEMLLGSLLRTVGLRFAVLRGNPYESEAEGDWIAVSLYGTIGAPIKGLEHETFGVGINHI | null | null | histidine metabolic process [GO:0006547]; positive regulation of gene expression [GO:0010628] | null | mRNA binding [GO:0003729] | PF09021; | 3.40.1510.10; | HutP family | null | null | null | null | null | null | null | FUNCTION: Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization. | Bacillus subtilis (strain 168) |
P10959 | EST1C_RAT | MWLCALVWASLAVCPIWGHPSSPPVVDTTKGKVLGKYVSLEGFTQPVAVFLGVPFAKPPLGSLRFAPPEPAEPWSFVKNTTTYPPMCSQDGVVGKLLADMLSTGKESIPLEFSEDCLYLNIYSPADLTKNSRLPVMVWIHGGGLIIGGASPYSGLALSAHENVVVVTIQYRLGIWGLFSTGDEHSRGNWAHLDQLAALRWVQDNIANFGGNPDSVTIFGESAGGVSVSALVLSPLAKNLFHRAISESGVVLTTNLDKKNTQAVAQMIATLSGCNNTSSAAMVQCLRQKTEAELLELTVKLDNTSMSTVIDGVVLPKTPEE... | 3.1.1.1 | null | lipid catabolic process [GO:0016042] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; lipid droplet [GO:0005811] | carboxylesterase activity [GO:0106435]; carboxylic ester hydrolase activity [GO:0052689]; protein homodimerization activity [GO:0042803] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomal membrane, lumen of endoplasmic reticulum. | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:9305911}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=69 uM for retinyl palmitate {ECO:0000269|PubMed:9305911}; Vmax=3.1 nmol/min/mg enzyme with retinyl palmitate as substrate {ECO:0000269|PubMed:9305911}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 4.0-8.0. {ECO:0000269|PubMed:9305911}; | null | FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Involved in the extracellular metabolism of lung surfactant (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
P10960 | SAP_RAT | MYALALLASLLVTALTSPVQDPKICSGGSAVVCRDVKTAVDCRAVKHCQQMVWSKPTAKSLPCDICKTVVTEAGNLLKDNATEEEILHYLEKTCAWIHDSSLSASCKEVVDSYLPVILDMIKGEMSNPGEVCSALNLCQSLQEYLAEQNQRQLESNKIPEVDLARVVAPFMSNIPLLLYPQDRPRSQPQPKANEDVCQDCMKLVTDIQTAVRTNSSFVQGLVDHVKEDCDRLGPGVSDICKNYVDQYSEVAVQMMMHMQPKEICVMVGFCDEVKRVPMRTLVPATEAIKNILPALELTDPYEQDVIQAQNVIFCQVCQLV... | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; antigen processing and presentation [GO:0019882]; cellular response to organic substance [GO:0071310]; cellular response to reactive oxygen species [GO:0034614]; ceramide metabolic process [GO:0006672]; cerebellar Purkinje cell diff... | aggresome [GO:0016235]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; late endosome [GO:0005770]; lysosome [GO:0005764] | G protein-coupled receptor binding [GO:0001664]; ganglioside GM1 binding [GO:1905573]; ganglioside GM2 binding [GO:1905574]; ganglioside GM3 binding [GO:1905575]; ganglioside GP1c binding [GO:1905577]; ganglioside GT1b binding [GO:1905576]; identical protein binding [GO:0042802]; lipid antigen binding [GO:0030882]; pho... | PF02199;PF05184;PF03489; | 1.10.225.10; | null | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:8573994, ECO:0000269|PubMed:8601692}.; SUBCELLULAR LOCATION: [Prosaposin]: Secreted {ECO:0000269|PubMed:3048385, ECO:0000269|PubMed:8573994, ECO:0000269|PubMed:8601692}. Note=Secreted as a fully glycosylated 70 kDa protein composed of complex glycans. {ECO:0000250|UniP... | null | null | null | null | null | FUNCTION: [Prosaposin]: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling. {ECO:0000250|UniProtKB:Q61207}.; FUNCTION: Saposin-A and saposin-C stimulat... | Rattus norvegicus (Rat) |
P10961 | HSF_YEAST | MNNAANTGTTNESNVSDAPRIEPLPSLNDDDIEKILQPNDIFTTDRTDASTTSSTAIEDIINPSLDPQSAASPVPSSSFFHDSRKPSTSTHLVRRGTPLGIYQTNLYGHNSRENTNPNSTLLSSKLLAHPPVPYGQNPDLLQHAVYRAQPSSGTTNAQPRQTTRRYQSHKSRPAFVNKLWSMLNDDSNTKLIQWAEDGKSFIVTNREEFVHQILPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSIQSSSDDKWQFENENFIRGREDLLEKIIRQKGSSNNHNSPSGNGNPANGSNIPLDNAAGSNNSNNNISSSNSFFN... | null | null | cellular response to heat [GO:0034605]; negative regulation of TORC1 signaling [GO:1904262]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of establishment of protein localization to chromosome [GO:0070202]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation o... | mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00447; | 1.10.10.10; | HSF family | PTM: Exhibits temperature-dependent phosphorylation that activates the transcriptional capacity. {ECO:0000269|PubMed:3044613}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:3044613}. | null | null | null | null | null | FUNCTION: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription. {ECO:0000269|PubMed:3044612, ECO:0000269|PubMed:3044613, ECO:0000269|PubMed:8175654}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10962 | MAK16_YEAST | MSDEIVWQVINQSFCSHRIKAPNGQNFCRNEYNVTGLCTRQSCPLANSKYATVKCDNGKLYLYMKTPERAHTPAKLWERIKLSKNYTKALQQIDEHLLHWSKFFRHKCKQRFTKLTQVMITERRLALREEERHYVGVAPKVKRREQNRERKALVAAKIEKAIEKELMDRLKSGAYGDKPLNVDEKVWKKIMGQMEEENSQDEEEDWDEEEESDDGEVEYVADDGEGEYVDVDDLEKWLADSDREASSASESESDSESESDSDSDEENKNSAKRRKKGTSAKTKRPKVEIEYEEEHEVQNAEQEVAQ | null | null | cell cycle [GO:0007049]; maturation of 5.8S rRNA [GO:0000460]; maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000466]; maturation of LSU-rRNA [GO:0000470]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; ribosomal lar... | nucleolus [GO:0005730]; preribosome, large subunit precursor [GO:0030687] | null | PF04874;PF01778; | 3.30.390.110; | MAK16 family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Its role might be as part of the apparatus concerned with the nuclear events of the cell cycle. {ECO:0000269|PubMed:3045810}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10964 | RPA1_YEAST | MDISKPVGSEITSVDFGILTAKEIRNLSAKQITNPTVLDNLGHPVSGGLYDLALGAFLRNLCSTCGLDEKFCPGHQGHIELPVPCYNPLFFNQLYIYLRASCLFCHHFRLKSVEVHRYACKLRLLQYGLIDESYKLDEITLGSLNSSMYTDDEAIEDNEDEMDGEGSKQSKDISSTLLNELKSKRSEYVDMAIAKALSDGRTTERGSFTATVNDERKKLVHEFHKKLLSRGKCDNCGMFSPKFRKDGFTKIFETALNEKQITNNRVKGFIRQDMIKKQKQAKKLDGSNEASANDEESFDVGRNPTTRPKTGSTYILSTEV... | 2.7.7.6 | null | nucleolar large rRNA transcription by RNA polymerase I [GO:0042790]; ribosome biogenesis [GO:0042254]; termination of RNA polymerase I transcription [GO:0006363]; transcription by RNA polymerase I [GO:0006360]; transcription elongation by RNA polymerase I [GO:0006362]; transcription initiation at RNA polymerase I promo... | nucleolus [GO:0005730]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase I activity [GO:0001054] | PF04997;PF00623;PF04983;PF05000;PF04998; | 1.10.132.30;1.10.150.390;1.10.357.120;2.40.40.20;3.30.70.2850;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:... | null | null | null | null | FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. RPA190 and RPA135 both contribute... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10966 | CD8B_HUMAN | MRPRLWLLLAAQLTVLHGNSVLQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRRARLRFMKQFYK | null | null | adaptive immune response [GO:0002250]; immune response [GO:0006955]; T cell activation [GO:0042110]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cell surface [GO:0009986]; early endosome membrane [GO:0031901]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; T cell receptor complex [GO:0042101] | coreceptor activity [GO:0015026]; MHC class I protein binding [GO:0042288] | PF07686; | 2.60.40.10; | null | PTM: Phosphorylated as a consequence of T-cell activation. {ECO:0000305}.; PTM: Palmitoylated at the cytoplasmic tail and thereby targets the heterodimer CD8A/CD8B to lipid rafts unlike CD8A homodimers. {ECO:0000269|PubMed:10925291}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:11714755, ECO:0000269|PubMed:3145196}; Single-pass type I membrane protein {ECO:0000305}. Note=Requires the partner CD8A for efficient cell surface expression (PubMed:3145196). The heterodimer CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic... | null | null | null | null | null | FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are de... | Homo sapiens (Human) |
P10980 | ACM2_RAT | MNNSTNSSNNGLAITSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKEKKEPVANQDPVSPSLVQGRIVKPNNNNMPGGDGGLEHNKIQNGKAPRDGVTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSRDDNS... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007... | asymmetric synapse [GO:0032279]; axon terminus [GO:0043679]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; symmetric... | arrestin family protein binding [GO:1990763]; G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM2 sub-subfamily | PTM: Phosphorylated in response to agonist treatment. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Phosphorylation in response to agonist binding promotes receptor internalization. {ECO:0000250}. | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipa... | Rattus norvegicus (Rat) |
P10981 | ACT5_DROME | MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMESCGIHETVYNSIMKCDVDIRKDLYANIVMSGGTTMYPGIADRMQKEITA... | 3.6.4.- | null | DNA repair-dependent chromatin remodeling [GO:0140861]; mitotic cytokinesis [GO:0000281] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; NuA4 histone acetyltransferase complex [GO:0035267] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787] | PF00022; | 3.30.420.40; | Actin family | PTM: N-terminal cleavage of acetylated cysteine of immature actin by ACTMAP. {ECO:0000250|UniProtKB:P68134}.; PTM: Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | 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; Evidence={ECO:0000250|UniProtKB:P68137}; | null | null | null | null | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. {ECO:0000269|PubMed:15528408}.; FUNCTION: Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome move... | Drosophila melanogaster (Fruit fly) |
P10984 | ACT2_CAEEL | MCDDDVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITVGNERFRCPEALFQPSFLGMESAGIHETSYNSIMKCDIDIRKDLYANTVLSGGTTMYPGIADRMQKEITA... | 3.6.4.- | null | anatomical structure morphogenesis [GO:0009653]; cortical actin cytoskeleton organization [GO:0030866]; embryo development ending in birth or egg hatching [GO:0009792]; locomotion [GO:0040011]; meiosis II cytokinesis [GO:0007111]; mitotic cytokinesis [GO:0000281]; regulation of transcription by RNA polymerase II [GO:00... | actin filament [GO:0005884]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787] | PF00022; | 3.30.420.40; | Actin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | 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; Evidence={ECO:0000250|UniProtKB:P68137}; | null | null | null | null | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | Caenorhabditis elegans |
P10987 | ACT1_DROME | MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA... | 3.6.4.- | null | chromatin remodeling [GO:0006338]; maintenance of protein location in cell [GO:0032507]; mitotic cytokinesis [GO:0000281]; regulation of transcription by RNA polymerase II [GO:0006357]; sperm individualization [GO:0007291]; tube formation [GO:0035148] | brahma complex [GO:0035060]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; Ino80 complex [GO:0031011]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787] | PF00022; | 3.30.420.40; | Actin family | PTM: N-terminal cleavage of acetylated cysteine of immature actin by ACTMAP. {ECO:0000250|UniProtKB:P68134}.; PTM: Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | 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; Evidence={ECO:0000250|UniProtKB:P68137}; | null | null | null | null | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; FUNCTION: Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. | Drosophila melanogaster (Fruit fly) |
P10989 | ACT_SCHPO | MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGIMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPCLLTEAPLNPKSNREKMTQIIFETFNAPAFYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAIMRLDLAGRDLTDYLMKILMERGYTFSTTAEREIVRDIKEKLCYVALDFEQELQTAAQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSALGLENAGIHEATYNSIMKCDVDIRKDLYGNVVMSGGTTMYPGIADRMQKEIQAL... | 3.6.4.- | null | chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; endocytosis [GO:0006897]; transcription initiation-coupled chromatin remodeling [GO:0045815] | actin cortical patch [GO:0030479]; actin filament [GO:0005884]; cell division site [GO:0032153]; cell tip [GO:0051286]; Ino80 complex [GO:0031011]; mating projection tip [GO:0043332]; mitotic actomyosin contractile ring, distal actin filament layer [GO:0120106]; mitotic actomyosin contractile ring, intermediate layer [... | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; structural constituent of cytoskeleton [GO:0005200] | PF00022; | 3.30.420.40; | Actin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | 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; Evidence={ECO:0000250|UniProtKB:P60010}; | null | null | null | null | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P10997 | IAPP_HUMAN | MGILKLQVFLIVLSVALNHLKATPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGKRNAVEVLKREPLNYLPL | null | null | amylin receptor signaling pathway [GO:0097647]; apoptotic process [GO:0006915]; bone resorption [GO:0045453]; cell-cell signaling [GO:0007267]; eating behavior [GO:0042755]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of bone resorption [GO:0045779]; negative regulation of mitochon... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | amyloid-beta binding [GO:0001540]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102] | PF00214; | 6.10.250.2190; | Calcitonin family | PTM: Amyloid fibrils are degraded by IDE. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17374526}. | null | null | null | null | null | FUNCTION: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. | Homo sapiens (Human) |
P11021 | BIP_HUMAN | MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSE... | 3.6.4.10 | null | cellular response to glucose starvation [GO:0042149]; cellular response to interleukin-4 [GO:0071353]; cerebellar Purkinje cell layer development [GO:0021680]; cerebellum structural organization [GO:0021589]; chaperone cofactor-dependent protein refolding [GO:0051085]; endoplasmic reticulum unfolded protein response [G... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; ext... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; misfolded protein binding [GO:0051787]; protein domain specific bin... | PF00012; | 1.20.1270.10;3.30.420.40; | Heat shock protein 70 family | PTM: AMPylated by FICD (PubMed:25601083). 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 (By similarity). In response to endoplasmic reticulum stress, de-AMPylation by ... | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:21080038, ECO:0000269|PubMed:21289099, ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:29497057}. Melanosome {ECO:0000269|PubMed:12643545}. Cytoplasm {ECO:0000250|UniProtKB:P20029}. Cell surface {ECO:0000269|PubMed:15098107, ECO:0000269|PubMed:204848... | 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:0000269|PubMed:26655470}; | null | null | null | null | FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC1... | Homo sapiens (Human) |
P11023 | RAB3A_BOVIN | MASATDARYGQKESSDQNFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEKMSESLDTADPAVTGAKQGPQLTDQQAPPHQDCAC | null | null | acrosomal vesicle exocytosis [GO:0060478]; axonogenesis [GO:0007409]; calcium-ion regulated exocytosis [GO:0017156]; evoked neurotransmitter secretion [GO:0061670]; insulin secretion [GO:0030073]; lung development [GO:0030324]; lysosome localization [GO:0032418]; maintenance of presynaptic active zone structure [GO:004... | acrosomal vesicle [GO:0001669]; axon [GO:0030424]; cytosol [GO:0005829]; endosome [GO:0005768]; lysosome [GO:0005764]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; synaptic vesi... | GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; GTPase activity [GO:0003924]; myosin V binding [GO:0031489]; protein-macromolecule adaptor activity [GO:0030674] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Phosphorylation of Thr-86 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2. {ECO:0000250|UniProtKB:P20336}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P63012}. Lysosome {ECO:0000250|UniProtKB:P20336}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P63012}. Cell projection, axon {ECO:0000250|UniProtKB:P63011}. Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:00... | null | null | null | null | null | FUNCTION: Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (By similarity). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RI... | Bos taurus (Bovine) |
P11024 | NNTM_BOVIN | MANLLKTVVTGCSCPFLSNLGSCKVLPGKKNFLRTFHTHRILWCSAPVKPGIPYKQLTVGVPKEIFQNEKRVALSPAGVQALVKQGFNVVVESGAGEASKFSDDHYRAAGAQIQGAKEVLASDLVVKVRAPMLNPTLGVHEADLLKTSGTLISFIYPAQNPDLLNKLSKRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFTGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIEAEMKLFAQQCKEVDILISTALI... | 7.1.1.1 | null | NADPH regeneration [GO:0006740]; proton transmembrane transport [GO:1902600]; reactive oxygen species metabolic process [GO:0072593] | mitochondrial inner membrane [GO:0005743] | NAD(P)+ transhydrogenase activity [GO:0008746]; NADP binding [GO:0050661] | PF01262;PF05222;PF02233;PF12769; | 3.40.50.720;3.40.50.1220; | AlaDH/PNT family; PNT beta subunit family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}. | 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:0000250|UniProtKB:Q2RSB2}; | 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 (By similarity). May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland (By similarity). {ECO:0000250|UniProtKB:P07001, ECO:0000250|UniProt... | Bos taurus (Bovine) |
P11029 | ACAC_CHICK | MEESSQPAKPLEMNPHSRFIIGSVSEDNSEDETSSLVKLDLLEEKERSLSPVSVCSDSLSDLGLPSAQDGLANHMRPSMSGLHLVKQGRDRKKVDVQRDFTVASPAEFVTRFGGNRVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWNGSGLRVDWQENDLQKRILNVPQELYEKGYVKDADDGLRAAEEVGYPVMIKASEGGGGKG... | 6.3.4.14; 6.4.1.2 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250|UniProtKB:O00763}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; | epigenetic regulation of gene expression [GO:0040029]; fatty acid biosynthetic process [GO:0006633]; malonyl-CoA biosynthetic process [GO:2001295]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; regulation of biological quality [GO:0065008]; respons... | cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin binding [GO:0009374]; biotin carboxylase activity [GO:0004075]; DNA binding domain binding [GO:0050692]; metal ion binding [GO:0046872]; nuclear thyroid hormone receptor binding [GO:0046966]; signaling receptor binding [GO:0005102]; sterol r... | PF08326;PF21385;PF02785;PF00289;PF00364;PF01039;PF02786; | 2.40.50.100;3.40.50.20;3.30.1490.20;3.30.470.20;2.40.460.10;3.90.1770.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000250|UniProtKB:Q5SWU9}; CATAL... | null | PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. | null | null | FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. {ECO:0000250|UniProtKB:Q13085}. | Gallus gallus (Chicken) |
P11030 | ACBP_RAT | MSQADFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKENAMKTYVEKVEELKKKYGI | null | null | acyl-CoA metabolic process [GO:0006637]; behavioral fear response [GO:0001662]; cellular response to nutrient [GO:0031670]; fatty acid metabolic process [GO:0006631]; glial cell proliferation [GO:0014009]; hair follicle development [GO:0001942]; lateral ventricle development [GO:0021670]; learning or memory [GO:0007611... | contractile fiber [GO:0043292]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; protein-lipid complex [GO:0032994]; synaptic vesicle [GO:0008021] | benzodiazepine receptor binding [GO:0030156]; fatty-acyl-CoA binding [GO:0000062]; identical protein binding [GO:0042802]; long-chain fatty acyl-CoA binding [GO:0036042] | PF00887; | 1.20.80.10; | ACBP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07108}. Golgi apparatus {ECO:0000250|UniProtKB:P07108}. Note=Golgi localization is dependent on ligand binding. {ECO:0000250|UniProtKB:P07108}. | null | null | null | null | null | FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as... | Rattus norvegicus (Rat) |
P11031 | TCP4_MOUSE | MPKSKELVSSSSSGSDSDSEVEKKLKRKKQAVPEKPVKKQKPGETSRALASSKQSSSSRDDNMFQIGKMRYVSVRDFKGKILIDIREYWMDSEGEMKPGRKGISLNMEQWSQLKEQISDIDDAVRKL | null | null | negative regulation of DNA duplex unwinding [GO:1905463]; negative regulation of DNA metabolic process [GO:0051053]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; protein homooligomerization [GO:0051260]; RNA polymerase II promoter clearance [GO:0001111] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA helicase activity [GO:0003678]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; single-stranded DNA binding [GO:0003697]; transcription coactivator activity [GO:0003713] | PF02229; | null | Transcriptional coactivator PC4 family | PTM: Activity is controlled by protein kinases that target the regulatory region. Phosphorylation inactivates both ds DNA-binding and cofactor function, but does not affect binding to ssDNA (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to dou... | Mus musculus (Mouse) |
P11032 | GRAA_MOUSE | MRNASGPRGPSLATLLFLLLIPEGGCERIIGGDTVVPHSRPYMALLKLSSNTICAGALIEKNWVLTAAHCNVGKRSKFILGAHSINKEPEQQILTVKKAFPYPCYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGRFGNKSAPSETLREVNITVIDRKICNDEKHYNFHPVIGLNMICAGDLRGGKDSCNGDSGSPLLCDGILRGITSFGGEKCGDRRWPGVYTFLSDKHLNWIKKIMKGSV | 3.4.21.78 | null | cytotoxic T cell pyroptotic process [GO:1902483]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; killing of cells of another organism [GO:0031640]; negative regulation of DNA binding [GO:0043392]; negative regulation of endodeoxyribonuclease activity [GO:0032078]; negative regulation of oxidore... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634] | protein homodimerization activity [GO:0042803]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Granzyme subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P12544}. Cytoplasmic granule {ECO:0000250|UniProtKB:P12544}. Note=Delivered into the target cell by perforin. {ECO:0000250|UniProtKB:P12544}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-Xaa-, -Lys-|-Xaa- >> -Phe-|-Xaa- in small molecule substrates.; EC=3.4.21.78; Evidence={ECO:0000250|UniProtKB:P12544}; | null | null | null | null | FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the ... | Mus musculus (Mouse) |
P11035 | NIA2_ARATH | MAASVDNRQYARLEPGLNGVVRSYKPPVPGRSDSPKAHQNQTTNQTVFLKPAKVHDDDEDVSSEDENETHNSNAVYYKEMIRKSNAELEPSVLDPRDEYTADSWIERNPSMVRLTGKHPFNSEAPLNRLMHHGFITPVPLHYVRNHGHVPKAQWAEWTVEVTGFVKRPMKFTMDQLVSEFAYREFAATLVCAGNRRKEQNMVKKSKGFNWGSAGVSTSVWRGVPLCDVLRRCGIFSRKGGALNVCFEGSEDLPGGAGTAGSKYGTSIKKEYAMDPSRDIILAYMQNGEYLTPDHGFPVRIIIPGFIGGRMVKWLKRIIVT... | 1.7.1.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=Binds 1 heme group per subunit. {ECO:0000250}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250}; Note=... | nitrate assimilation [GO:0042128]; nitric oxide biosynthetic process [GO:0006809]; response to herbicide [GO:0009635]; response to light stimulus [GO:0009416]; response to symbiotic fungus [GO:0009610]; sulfur compound metabolic process [GO:0006790] | mitochondrion [GO:0005739]; nucleus [GO:0005634]; plant-type vacuole [GO:0000325] | FAD binding [GO:0071949]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; mRNA binding [GO:0003729]; nitrate reductase (NADH) activity [GO:0009703]; nitrate reductase (NADPH) activity [GO:0050464]; nitrate reductase act... | PF00173;PF00970;PF03404;PF00175;PF00174; | 2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10; | Nitrate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate; Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.1; | null | null | null | null | FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. | Arabidopsis thaliana (Mouse-ear cress) |
P11043 | AROA_PETHY | MAQINNMAQGIQTLNPNSNFHKPQVPKSSSFLVFGSKKLKNSANSMLVLKKDSIFMQKFCSFRISASVATAQKPSEIVLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLSSDDIHYMLGALKTLGLHVEEDSANQRAVVEGCGGLFPVGKESKEEIQLFLGNAGTAMRPLTAAVTVAGGNSRYVLDGVPRMRERPISDLVDGLKQLGAEVDCFLGTKCPPVRIVSKGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIIDKLISVPYVEMTLKLMERFGISVEHSSSWDRFFVRGGQKYKSPGKAF... | 2.5.1.19 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; response to herbicide [GO:0009635] | chloroplast [GO:0009507] | 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866] | PF00275; | 3.65.10.10; | EPSP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000269|PubMed:1939260}; PhysiologicalDirection=left-to-right; Xref=R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for phosphoenolpyruvate {ECO:0000269|PubMed:1939260}; KM=7.8 uM for 3-phosphoshikimate {ECO:0000269|PubMed:1939260}; KM=1.9 uM for 5-O-(1-carboxyvinyl)-3-phosphoshikimate {ECO:0000269|PubMed:1939260}; KM=0.59 mM for phosphate {ECO:0000269|PubMed:1939260}; Note... | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000305|PubMed:1939260}. | null | null | FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate (PubMed:1939260). Involved in the accumulation of volatile benzoides in flowers, scent attracting pollinators (e.g... | Petunia hybrida (Petunia) |
P11046 | LAMB1_DROME | MLELRLIVVIVLALLSWQWDPVDSQRPPQHGRRDRPKYPPNKFIKTHPCERSSCYPATGNLLIGRENRLTASSTCGLHSPERFCILSHLQDKKCFLCDTREETKHDPYKNHRIGQIIYKTKPGTNIPTWWQSENGKENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSFDFGQTWHIYRYFAYDCKESFPGVPTVLENITDVMCTSRYSNVEPSRNGEVIFRVLPPNINVTDPYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENEEKYYYGISNMVVRGSCSCYGHASQCLPLDPAFSQADNEDGMVHGRCEC... | null | null | animal organ development [GO:0048513]; animal organ morphogenesis [GO:0009887]; axon guidance [GO:0007411]; basement membrane assembly [GO:0070831]; basement membrane organization [GO:0071711]; cardiac muscle cell development [GO:0055013]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; de... | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; laminin complex [GO:0043256] | null | PF00053;PF21199;PF00055; | 2.60.120.260;2.10.25.10;2.170.300.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:30260959}. | null | null | null | null | null | FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (By similarity). Required for Ndg localization to the basement membrane (PubMed:3... | Drosophila melanogaster (Fruit fly) |
P11047 | LAMC1_HUMAN | MRGSHRAAPALRPRGRLWPVLAVLAAAAAAGCAQAAMDECTDEGGRPQRCMPEFVNAAFNVTVVATNTCGTPPEEYCVQTGVTGVTKSCHLCDAGQPHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPSSINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGGDEQQALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGGRCKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCL... | null | null | animal organ morphogenesis [GO:0009887]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; endoderm development [GO:0007492]; extracellular matrix disassembly [GO:0022617]; hemidesmosome assembly [GO:0031581]; maintenance of blood-brain barrier [GO:0035633]; positive regulation of cell adhesion [GO:0045785]; pos... | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; laminin-1 complex [GO:0005606]; laminin-10 complex [GO:0043259]; laminin-11 complex [G... | extracellular matrix structural constituent [GO:0005201] | PF00052;PF00053;PF00055; | 2.60.120.260;2.10.25.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | Homo sapiens (Human) |
P11048 | LMNA_XENLA | METPGQKRATRSTHTPLSPTRITRLQEKEDLQGLNDRLAVYIDKVRSLELENARLRLRITESEDVISREVTGIKSAYETELADARKTLDSVAKERARLQLELSKIREEHKELKARNAKKESDLLTAQARLKDLEALLNSKDAALTTALGEKRNLENEIRELKAHIAKLEASLADTKKQLQDEMLRRVDTENRNQTLKEELEFQKSIYNEEMRETKRRHETRLVEVDNGRQREFESKLADALHELRAQHEGQIGLYKEELGKTYNAKLENAKQSAERNSSLVGEAQEEIQQSRIRIDSLSAQLSQLQKQLAAREAKLRDLE... | null | null | heterochromatin formation [GO:0031507]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear pore localization [GO:0051664]; protein localization to nuclear envelope [GO:0090435] | intermediate filament [GO:0005882]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654] | structural constituent of cytoskeleton [GO:0005200] | PF00038;PF00932; | 1.20.5.170;2.60.40.1260;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylation plays a key role in lamin organization, subcellular localization and nuclear envelope disintegration. Phosphorylation by CDK1 at Ser-18 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown. {ECO:0000250|UniProtKB:P14732}. | SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:3762708}. Nucleus envelope {ECO:0000269|PubMed:25157132}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25157132}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. | null | null | null | null | null | FUNCTION: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:3762708). Lamins provide a framework for the nuclear envelope, bridging the nucl... | Xenopus laevis (African clawed frog) |
P11049 | CD37_HUMAN | MSAQESCLSLIKYFLFVFNLFFFVLGSLIFCFGIWILIDKTSFVSFVGLAFVPLQIWSKVLAISGIFTMGIALLGCVGALKELRCLLGLYFGMLLLLFATQITLGILISTQRAQLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWFQVLILRGNGSEAHRVPCSCYNLSATNDSTILDKVILPQLSRLGHLARSRHSADICAVPAESHIYREGCAQGLQKWLHNNLISIVGICLGVGLLELGFMTLSIFLCRNLDHVYNRLARYR | null | null | null | extracellular exosome [GO:0070062]; immunological synapse [GO:0001772]; membrane [GO:0016020] | null | PF00335; | 1.10.1450.10; | Tetraspanin (TM4SF) family | PTM: Tyrosine phosphorylated; leading to activation of downstream signaling pathways. {ECO:0000269|PubMed:22624718}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17182550, ECO:0000269|PubMed:22624718, ECO:0000269|PubMed:26784544}; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Participates thereby in diverse biological functions such as cell signal transduction, adhesion, migration and protein trafficking (PubMed... | Homo sapiens (Human) |
P11055 | MYH3_HUMAN | MSSDTEMEVFGIAAPFLRKSEKERIEAQNQPFDAKTYCFVVDSKEEYAKGKIKSSQDGKVTVETEDNRTLVVKPEDVYAMNPPKFDRIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEIL... | null | null | actin filament-based movement [GO:0030048]; ATP metabolic process [GO:0046034]; embryonic limb morphogenesis [GO:0030326]; face morphogenesis [GO:0060325]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; muscle organ development [GO:0007517]; sarcomere organization [GO:0045214]; skeletal muscle c... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; muscle myosin complex [GO:0005859]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; sarcomere [GO:0030017] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; myosin phosphatase activity [GO:0017018] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Homo sapiens (Human) |
P11064 | PPAC_BOVIN | MAEQVTKSVLFVCLGNICRSPIAEAVFRKLVTDQNISDNWVIDSGAVSDWNVGRSPDPRAVSCLRNHGINTAHKARQVTKEDFVTFDYILCMDESNLRDLNRKSNQVKNCRAKIELLGSYDPQKQLIIEDPYYGNDADFETVYQQCVRCCRAFLEKVR | 3.1.3.2; 3.1.3.48 | null | null | cytoplasm [GO:0005737] | acid phosphatase activity [GO:0003993]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; protein tyrosine phosphatase activity [GO:0004725] | PF01451; | 3.40.50.2300; | Low molecular weight phosphotyrosine protein phosphatase family | PTM: Phosphorylated by LCK. Phosphorylation at Tyr-132 increases its phosphatase activity. {ECO:0000250|UniProtKB:P24666}. | SUBCELLULAR LOCATION: Cytoplasm. | 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:0000305|PubMed:8319676}; PhysiologicalDirection=lef... | null | null | null | null | FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. {ECO:0000269|PubMed:8319676}. | Bos taurus (Bovine) |
P11071 | ACEK_ECOLI | MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRG... | 2.7.11.5; 3.1.3.- | null | glucose metabolic process [GO:0006006]; glyoxylate cycle [GO:0006097]; phosphorylation [GO:0016310]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737] | [isocitrate dehydrogenase (NADP+)] kinase activity [GO:0008772]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; phosphoprotein phosphatase activity [GO:0004721]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine p... | PF06315;PF20423; | null | AceK family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase]; Xref=Rhea:RHEA:43540, Rhea:RHEA-COMP:10605, Rhea:RHEA-COMP:10606, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.5; Evidence={ECO:... | null | null | null | null | FUNCTION: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is f... | Escherichia coli (strain K12) |
P11075 | SEC7_YEAST | MSEQNSVVNAEKGDGEISSNVETASSVNPSVKPQNAIKEEAKETNGEDQKCKGPENAGSTAETKETSNDATNGMKTPEETEDTNDKRHDDEGEDGDEDEDEDEDEDEDNGDEDDEDVDSSSSETSSEDGEDSESVSGESTESSSGEDEESDESDGNTSNSSSGDESGSEEEEEEEEEEEEEENAGEPAIAHQDSVPTNDSTAPRSTHTRNISLSSNGSNTNSTIILVKTTLETILNDKDIKKNSNAQKAIERTLQKFKEFDPQTTNNPHYVDSILVFEALRASCRTKSSKVQSLALDCLSKLFSFRSLDETLLVNPPDSL... | null | null | autophagosome assembly [GO:0000045]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]; regulation of ARF protein signal transduction [GO:0032012] | cytosol [GO:0005829]; Golgi-associated vesicle [GO:0005798]; late endosome [GO:0005770]; trans-Golgi network [GO:0005802] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF20252;PF16213;PF01369;PF09324;PF12783; | 1.10.220.20;1.10.1000.11; | null | null | SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus. Note=Associated with the peripheral Golgi membrane. | null | null | null | null | null | FUNCTION: May play a role in vesicular budding and traffic between compartments of the Golgi apparatus. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11076 | ARF1_YEAST | MGLFASKLFSNLFGNKEMRILMVGLDGAGKTTVLYKLKLGEVITTIPTIGFNVETVQYKNISFTVWDVGGQDRIRSLWRHYYRNTEGVIFVVDSNDRSRIGEAREVMQRMLNEDELRNAAWLVFANKQDLPEAMSAAEITEKLGLHSIRNRPWFIQATCATSGEGLYEGLEWLSNSLKNST | 3.6.5.2 | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi to plasma membrane transport [GO:0006893]; Golgi vesicle transport [GO:0048193]; intracellular protein transport [GO:0006886]; macroautophagy [GO:0016236]; vesicle-mediated transport [GO:0016192] | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00025; | 3.40.50.300; | Small GTPase superfamily, Arf family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15504911}. | 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:P84077}; | null | null | null | null | FUNCTION: GTP-binding protein involved in Golgi vesicle trafficking (PubMed:15356266, PubMed:34830155). May modulate vesicle budding and uncoating within the Golgi apparatus (PubMed:15356266). May recruit the lipid transfer protein VPS13 to Golgi membranes (PubMed:34830155). Recruits polyadenylate-binding protein PAB1 ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11077 | MU1_REOVL | MGNASSIVQTINVTGDGNVFKPSAETSSTAVPSLSLSPGMLNPGGVPWIAIGDETSVTSPGALRRMTSKDIPETAIINTDNSSGAVPSESALVPYNDEPLVVVTEHAIANFTKAEMALEFNREFLDKLRVLSVSPKYSDLLTYVDCYVGVSARQALNNFQKQVPVITPTRQTMYVDSIQAALKALEKWEIDLRVAQTLLPTNVPIGEVSCPMQSVVKLLDDQLPDDSLIRRYPKEAAVALAKRNGGIQWMDVSEGTVMNEAVNAVAASALAPSASAPPLEEKSKLTEQAMDLVTAAEPEIIASLVPVPAPVFAIPPKPAD... | null | null | permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008] | host cell endoplasmic reticulum [GO:0044165]; host cell mitochondrion [GO:0033650]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral outer capsid [GO:0039624] | host cell surface binding [GO:0046812] | PF05993; | 2.60.120.420;3.90.1370.10;1.10.2040.10;1.10.2050.10; | Orthoreovirus mu-1 protein family | PTM: Cleaved during the endosomal proteolytic disassembly of the outer capsid. Mu-1 is proteolytically cleaved into mu-1N and mu-1C during the maturation step to generate the ISVP. Cleavage of mu-1 to mu-1C is dependent on myristoylation and binding to sigma-3 protein. Mu-1C is further cleaved into delta (59 kDa), and ... | SUBCELLULAR LOCATION: [Outer capsid protein mu-1]: Virion. Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Host endoplasmic reticulum. Host mitochondrion. Note=Found in the outer capsid. Seems to associate with cell membranes. This association is enhanced by myristoylation (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion par... | Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1) |
P11078 | MU1_REOVD | MGNASSIVQTINVTGDGNVFKPSAETSSTAVPSLSLSPGMLNPGGVPWIAVGDETSVTSPGALRRMTSKDIPETAIINTDNSSGAVPSESALVPYIDEPLVVVTEHAITNFTKAEMALEFNREFLDKMRVLSVSPKYSDLLTYVDCYVGVSARQALNNFQKQVPVITPTRQTMYVDSIQAALKALEKWEIDLRVAQTLLPTNVPIGEVSCPMQSVVKLLDDQLPDDSLIRRYPKEAAVALAKRNGGIQWMDVSEGTVMNEAVNAVAASALAPSASAPPLEEKSKLTEQAMDLVTAAEPEIIASLAPVPAPVFAIPPKPAD... | null | null | permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008] | host cell endoplasmic reticulum [GO:0044165]; host cell mitochondrion [GO:0033650]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral outer capsid [GO:0039624] | host cell surface binding [GO:0046812] | PF05993; | 2.60.120.420;3.90.1370.10;1.10.2040.10;1.10.2050.10; | Orthoreovirus mu-1 protein family | PTM: Cleaved during the endosomal proteolytic disassembly of the outer capsid. Mu-1 is proteolytically cleaved into mu-1N and mu-1C during the maturation step to generate the ISVP. Cleavage of mu-1 to mu-1C is dependent on myristoylation and binding to sigma-3 protein. Mu-1C is further cleaved into delta (59 kDa), and ... | SUBCELLULAR LOCATION: [Outer capsid protein mu-1]: Virion {ECO:0000250}. Host cell membrane; Lipid-anchor. Host endoplasmic reticulum {ECO:0000250}. Host mitochondrion {ECO:0000250}. Note=Found in the outer capsid. Seems to associate with cell membranes. This association is enhanced by myristoylation. | null | null | null | null | null | FUNCTION: Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion par... | Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) |
P11079 | LMBD2_REOVD | MANVWGVRLADSLSSPTIETRTRQYTLHDLCSDLDANPGREPWKPLRNQRTNNIVAVQLFRPLQGLVLDTQLYGFPGAFDDWERFMREKLRVLKYEVLRIYPISNYSNEHVNVFVANALVGAFLSNQAFYDLLPLLIINDTMIGDLLGTGASLSQFFQSHGDVLEVAAGRKYLQMENYSNDDDDPPLFAKDLSDYAKAFYSDTYEVLDRFFWTHDSSAGVLVHYDKPTNGHHYLLGTLTQMVSAPPYIINATDAMLLESCLEQFSANVRARPAQPVTRLDQCYHLRWGAQYVGEDSLTYRLGVLSLLATNGYQLARPIPR... | 2.1.1.56; 2.7.7.50 | null | null | icosahedral viral capsid [GO:0019030]; viral outer capsid [GO:0039624] | ATP binding [GO:0005524]; GTP binding [GO:0005525]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; mRNA guanylyltransferase activity [GO:0004484] | PF21062;PF21060;PF21061;PF06016;PF21063;PF21065;PF21066;PF21064; | 2.60.40.10;3.55.60.10;3.90.1810.10;3.40.50.10760;3.40.50.150; | Orthoreovirus lambda-2 protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617;... | null | null | null | null | FUNCTION: Outer capsid protein involved in mRNA capping. Catalyzes the last 3 enzymatic activities for formation of the 5' cap structure on the viral plus-strand transcripts, namely the RNA guanylyltransferase, RNA-7N- and RNA-2'O-methyltransferase activities. | Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) |
P11086 | PNMT_HUMAN | MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL | 2.1.1.28 | null | catecholamine biosynthetic process [GO:0042423]; epinephrine biosynthetic process [GO:0042418]; methylation [GO:0032259] | cytosol [GO:0005829] | phenylethanolamine N-methyltransferase activity [GO:0004603] | PF01234; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family | null | null | CATALYTIC ACTIVITY: Reaction=phenylethanolamine + S-adenosyl-L-methionine = H(+) + N-methylphenylethanolamine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12176, ChEBI:CHEBI:15378, ChEBI:CHEBI:57741, ChEBI:CHEBI:57856, ChEBI:CHEBI:57946, ChEBI:CHEBI:59789; EC=2.1.1.28; Evidence={ECO:0000269|PubMed:16363801, ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=99 uM for phenylethanolamine {ECO:0000269|PubMed:16363801}; KM=3.4 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:16363801}; KM=5.3 uM for octopamine {ECO:0000269|PubMed:16363801}; KM=23.5 uM for octopamine {ECO:0000269|PubMed:16277617}; KM=6.2 uM for S-adenosy... | PATHWAY: Catecholamine biosynthesis; (R)-adrenaline biosynthesis; (R)-adrenaline from (R)-noradrenaline: step 1/1. {ECO:0000269|PubMed:20496117}. | null | null | FUNCTION: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor (PubMed:20496117). Other substrates include phenylethanolamine and octopamine (PubMed:16277617, PubMed:16363801, PubMed:8812853). Also methylates normetanephrine... | Homo sapiens (Human) |
P11087 | CO1A1_MOUSE | MFSFVDLRLLLLLGATALLTHGQEDIPEVSCIHNGLRVPNGETWKPEVCLICICHNGTAVCDDVQCNEELDCPNPQRREGECCAFCPEEYVSPNSEDVGVEGPKGDPGPQGPRGPVGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFASQMSYGYDEKSAGVSVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGGSGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGPPGTAGARGNDGAVGAA... | null | null | blood vessel development [GO:0001568]; bone trabecula formation [GO:0060346]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to amino acid stimulus [GO:0071230]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth ... | collagen trimer [GO:0005581]; collagen type I trimer [GO:0005584]; collagen type II trimer [GO:0005585]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141] | extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protease binding [GO:0002020] | PF01410;PF01391;PF00093; | 2.60.120.1000;2.10.70.10; | Fibrillar collagen family | PTM: Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:25645914}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). | Mus musculus (Mouse) |
P11101 | STP2_RAT | MDTKMQSLPTTHPHPHSSSRPQSHTNNQCACSHHCRSCSQAGHPSSSSSPSPGPPTKHPKTPMHSRYSPSRPSHRGSCPKNRKTLEGKVSKRKAVRRRKRTHRAKRRSSGRRYK | null | null | acrosome reaction [GO:0007340]; binding of sperm to zona pellucida [GO:0007339]; flagellated sperm motility [GO:0030317]; penetration of zona pellucida [GO:0007341]; positive regulation of protein processing [GO:0010954]; sperm DNA condensation [GO:0035092]; spermatogenesis [GO:0007283] | male germ cell nucleus [GO:0001673]; nucleolus [GO:0005730]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; zinc ion binding [GO:0008270] | PF01254; | null | Nuclear transition protein 2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10961985, ECO:0000269|PubMed:14514679, ECO:0000269|PubMed:17682055}. Nucleus, nucleolus {ECO:0000269|PubMed:10961985, ECO:0000269|PubMed:14514679}. Chromosome {ECO:0000269|PubMed:14514679}. Note=Loaded onto the nucleosomes of condensing spermatids (By similarity). Nucle... | null | null | null | null | null | FUNCTION: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals (PubMed:11772016). In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction (By similarity). {ECO:000025... | Rattus norvegicus (Rat) |
P11103 | PARP1_MOUSE | MAEASERLYRVQYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGQSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVAGKGQDGSGGKAEKTLGDFAAEYAKSNRSMCKGCLEKIEKGQMRLSKKMVDPEKPQLGMIDRWYHPTCFVKKRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAIKNEGKRKGDEVDGTDEVAKKKSRKETDKYSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTK... | 2.4.2.-; 2.4.2.30 | null | apoptotic process [GO:0006915]; ATP generation from poly-ADP-D-ribose [GO:1990966]; base-excision repair [GO:0006284]; behavioral response to cocaine [GO:0048148]; carbohydrate biosynthetic process [GO:0016051]; cellular response to amyloid-beta [GO:1904646]; cellular response to nerve growth factor stimulus [GO:199009... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear replication fork [GO:0043596]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; site of DNA damage [GO:0090734]; site of double-strand break [GO:00358... | chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; NAD binding [GO:0051287]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+- protein-aspartate ADP-ribosyltransferase activity [GO:0140806]; NAD+-histone H2BE35 glutamate ADP-ri... | PF00533;PF21728;PF08063;PF00644;PF02877;PF05406;PF00645; | 1.10.20.130;2.20.25.630;3.90.228.10;3.40.50.10190;1.20.142.10;3.30.1740.10; | ARTD/PARP family | PTM: Poly-ADP-ribosylated on serine, glutamate and aspartate residues by autocatalysis. Auto-ADP-ribosylation on serine takes place following interaction with HPF1. Auto poly-ADP-ribosylation on serine residues promotes its dissociation from chromatin. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the r... | SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:P09874}. Nucleus {ECO:0000250|UniProtKB:P09874}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P09874}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage. Recognizes (via PARP-type zinc-fingers) and binds DNA strand breaks. Also ... | CATALYTIC ACTIVITY: Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30; Evidence={ECO:0000250|UniProtKB:P09874}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA... | null | null | null | null | FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:21680843). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target... | Mus musculus (Mouse) |
P11116 | LEG1_BOVIN | MACGLVASNLNLKPGECLRVRGEVAADAKSFLLNLGKDDNNLCLHFNPRFNAHGDVNTIVCNSKDAGAWGAEQRESAFPFQPGSVVEVCISFNQTDLTIKLPDGYEFKFPNRLNLEAINYLSAGGDFKIKCVAFE | null | null | apoptotic process [GO:0006915] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615] | galactoside binding [GO:0016936]; lactose binding [GO:0030395]; laminin binding [GO:0043236] | PF00337; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09382}. Cytoplasm {ECO:0000250|UniProtKB:P09382}. Secreted {ECO:0000250|UniProtKB:P09382}. Note=Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in p... | null | null | null | null | null | FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates (PubMed:1900835, PubMed:7773775, PubMed:8108426). Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong... | Bos taurus (Bovine) |
P11117 | PPAL_HUMAN | MAGKRSGWSRAALLQLLLGVNLVVMPPTRARSLRFVTLLYRHGDRSPVKTYPKDPYQEEEWPQGFGQLTKEGMLQHWELGQALRQRYHGFLNTSYHRQEVYVRSTDFDRTLMSAEANLAGLFPPNGMQRFNPNISWQPIPVHTVPITEDRLLKFPLGPCPRYEQLQNETRQTPEYQNESSRNAQFLDMVANETGLTDLTLETVWNVYDTLFCEQTHGLRLPPWASPQTMQRLSRLKDFSFRFLFGIYQQAEKARLQGGVLLAQIRKNLTLMATTSQLPKLLVYSAHDTTLVALQMALDVYNGEQAPYASCHIFELYQEDS... | 3.1.3.2 | null | dephosphorylation [GO:0016311]; lysosome organization [GO:0007040] | extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020] | acid phosphatase activity [GO:0003993] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | PTM: The membrane-bound form is converted to the soluble form by sequential proteolytic processing. First, the C-terminal cytoplasmic tail is removed. Cleavage by a lysosomal protease releases the soluble form in the lysosome lumen. {ECO:0000269|PubMed:2684640, ECO:0000269|PubMed:3056714}.; PTM: N-glycosylated. The int... | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:2684640, ECO:0000269|PubMed:3056714}; Single-pass membrane protein {ECO:0000255}; Lumenal side {ECO:0000305|PubMed:2684640, ECO:0000305|PubMed:3056714}. Lysosome lumen. Note=The soluble form arises by proteolytic processing of the membrane-bound form. {ECO:000... | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; | null | null | null | null | null | Homo sapiens (Human) |
P11124 | RDRP_BPPH6 | MPRRAPAFPLSDIKAQMLFANNIKAQQASKRSFKEGAIETYEGLLSVDPRFLSFKNELSRYLTDHFPANVDEYGRVYGNGVRTNFFGMRHMNGFPMIPATWPLASNLKKRADADLADGPVSERDNLLFRAAVRLMFSDLEPVPLKIRKGSSTCIPYFSNDMGTKIEIAERALEKAEEAGNLMLQGKFDDAYQLHQMGGAYYVVYRAQSTDAITLDPKTGKFVSKDRMVADFEYAVTGGEQGSLFAASKDASRLKEQYGIDVPDGFFCERRRTAMGGPFALNAPIMAVAQPVRNKIYSKYAYTFHHTTRLNKEEKVKEWSL... | 2.7.7.48 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; | DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694] | virion component [GO:0044423] | metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA uridylyltransferase activity [GO:0050265]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00680; | 3.30.70.1600;6.20.410.10;1.10.490.60; | null | null | SUBCELLULAR LOCATION: Virion. Note=Found in the capsid (12 copies). Prior to RNA packaging, localizes on the inner procapsid surface near the three-fold axis of symmetry. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; | null | null | null | null | FUNCTION: Rna-dependent RNA polymerase part of the packaging complex that packages the viral RNA segments, replicate them into a double-stranded form and transcribe them. | Pseudomonas phage phi6 (Bacteriophage phi-6) |
P11132 | HEMA_I83A3 | MEEIVLLFAIVSLARSDQICIGYHANNSTKQVDTIMEKNVTVTHAQDILEKTHNGKLCSLNGVKPLILRDCSVAGWLLGNPMCDEFLNVPEWSYIVEKDNPVNGLCYPGDFNDYEELKHLLSCTKHFEKIRIIPRDSWPNHEASLGVSSACPYNGRSSFFRNVVWLIKKDNAYPTIKRSYNNTNKEDLLILWGIHHPNDAAEQTKLYQNPTTYVSVGTSTLNQRSIPKIATRPKLNGQSGRMEFFWTILKPSDTINFESNGNFIAPEYAYKIVKKGDSAIMKSGLEYGNCNTKCQTPIGAINSSMPFHNIHPLTIGECPK... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789] | PF00509; | 3.90.20.10;3.90.209.20;2.10.77.10; | Influenza viruses hemagglutinin family | PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.; PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in ... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Note=Targeted to the apical plasma membrane ... | null | null | null | null | null | FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... | Influenza A virus (strain A/Duck/Ireland/113/1983 H5N8) |
P11137 | MTAP2_HUMAN | MADERKDEAKAPHWTSAPLTEASAHSHPPEIKDQGGAGEGLVRSANGFPYREDEEGAFGEHGSQGTYSNTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQTAALPLAAEETANLPPSPPPSPASEQTVTVEEDLLTASKMEFHDQQELTPSTAEPSDQKEKESEKQSKPGEDLKHAALVSQPETTKTYPDKKDMQGTEEEKAPLALFGHTLVASLEDMKQKTEPSLVVPGIDLPKEPPTPKEQKDWFIEMPTEAKKDEWGLVAPISPGPLTPMREKDVFDDIPKWEGKQFDSPMPSPFQGG... | null | null | central nervous system neuron development [GO:0021954]; dendrite development [GO:0016358]; dendrite morphogenesis [GO:0048813]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of axon extension [GO:0030517]; negative regulation of microtubule binding [GO:1904527]; negative regulation of microtub... | apical distal dendrite [GO:0150014]; axon hillock [GO:0043203]; axon initial segment [GO:0043194]; basal dendrite [GO:0097441]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; dendritic branch [GO:0044307]; dendritic filopodium [GO:1902737]; dendritic growth cone [G... | calmodulin binding [GO:0005516]; dystroglycan binding [GO:0002162]; microtubule binding [GO:0008017]; structural molecule activity [GO:0005198]; tau protein binding [GO:0048156] | PF08377;PF00418; | null | null | PTM: Phosphorylated at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly (By similarity). Isoform 2 is probably phosphorylated by PKA at Ser-323, Ser-354 and Ser-386 and by FYN at Tyr-67. The interaction with KND... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:P20357}. | null | null | null | null | null | FUNCTION: The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules. | Homo sapiens (Human) |
P11139 | TBA1_ARATH | MREIISIHIGQAGIQVGNSCWELYCLEHGIQPDGTMPSDSTVGACHDAFNTFFSETSSGQHVPRAVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTVGREIVDTCLERLRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDFGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVVVLLDNEAIYDICRRSLDIERPTYSNLNRLISQTISSLTTSLRFDGAINVDITEFQTNLVPYPRIHFMLSSYAPVISSAKAYHEQFSVPEITTSVFEPSNMMAKCDPRHGKYMACCLMYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Arabidopsis thaliana (Mouse-ear cress) |
P11140 | ABRA_ABRPR | QDRPIKFSTEGATSQSYKQFIEALRERLRGGLIHDIPVLPDPTTLQERNRYITVELSNSDTESIEVGIDVTNAYVVAYRAGTQSYFLRDAPSSASDYLFTGTDQHSLPFYGTYGDLERWAHQSRQQIPLGLQALTHGISFFRSGGNDNEEKARTLIVIIQMVAEAARFRYISNRVRVSIQTGTAFQPDAAMISLENNWDNLSRGVQESVQDTFPNQVTLTNIRNEPVIVDSLSHPTVAVLALMLFVCNPPNANQSPLLIRSIVEKSKICSSRYEPTVRIGGRDGMCVDVYDNGYHNGNRIIMWKCKDRLEENQLWTLKSD... | 3.2.2.22 | null | defense response [GO:0006952]; negative regulation of translation [GO:0017148]; positive regulation of endocytosis [GO:0045807] | null | galactose binding [GO:0005534]; 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 | FUNCTION: The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. Abrin-a is more toxic than ricin.; FUNCTION: The B chain is a galactose-specific lectin that facilitates the binding of abrin to the cel... | Abrus precatorius (Indian licorice) (Glycine abrus) |
P11142 | HSP7C_HUMAN | MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKA... | 3.6.4.10 | null | ATP metabolic process [GO:0046034]; cellular response to cadmium ion [GO:0071276]; cellular response to heat [GO:0034605]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to starvation [GO:0009267]; cellular response to steroid hormone stimulus [GO:0071383]; cerebellum development [GO:0021549]; c... | autophagosome [GO:0005776]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane [GO:0061202]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; extrac... | A1 adenosine receptor binding [GO:0031686]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; ATP-dependent protein folding chaperone [GO:0140662]; C3HC4-type RING finger domain binding [GO:0055131]; cadherin binding [GO:0... | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | PTM: Acetylated. {ECO:0000269|Ref.5, ECO:0000269|Ref.6}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798, ECO:0000269|PubMed:16815975}.; PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}. Melanosome {ECO:0000269|PubMed:17081065}. Nucleus, nucleolus {ECO:0000269|PubMed:1586970}. Cell membrane. Lysosome membrane {ECO:0000269|PubMed:11559757}; Peripheral membrane protein {ECO:0000269|PubMed:11559757}; Cytoplasmic side {ECO:0000269|PubMed:115597... | 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:0000269|PubMed:12526792}; | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and... | Homo sapiens (Human) |
P11147 | HSP7D_DROME | MSKAPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTQTIFDAKRLIGRKFDDAAVQSDMKHWPFEVVSADGKPKIEVTYKDEKKTFFPEEISSMVLTKMKETAEAYLGKTVTNAVITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKAVGERNVLIFDLGGGTFDVSILSIDDGIFEVKSTAGDTHLGGEDFDNRLVTHFVQEFKRKHKKDLTTNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGTDFYTSITRARFEELNADLFRSTMDPVEKA... | null | null | axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; cellular response to topologically incorrect protein [GO:0035967]; chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated protein folding [GO:0061077]; follicle cell of egg chamber development [GO:0030707]; late endosomal microautop... | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; precatalytic spliceosome [GO:0071011]; presynapse [GO:0098793] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087] | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus. Note=Localized to a meshwork of cytoplasmic fibers around the nucleus. Translocates to the nucleus after thermal stress. | null | null | null | null | null | null | Drosophila melanogaster (Fruit fly) |
P11150 | LIPC_HUMAN | MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQGCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLVDWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAYPCGDMNSFSQGLCLSCKKGR... | 3.1.1.3; 3.1.1.32; 3.1.1.5 | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance [GO:0034382]; fatty acid biosynthetic process [GO:0006633]; high-density lipoprotein particle remodeling [GO:0034375]; intermediate-density lipoprotein particle remodeling [GO:0034373]; low-density lipoprotei... | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; apolipoprotein binding [GO:0034185]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; low-density lipoprotein particle binding [GO:0030169]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102... | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2828141}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:26193433, ECO:0000269|PubMed:7592706, ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 mM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol {ECO:0000269|PubMed:8798474}; Vmax=1.4 umol/min/ug enzyme with 1,2,3-tri-(9Z-octadecenoyl)-glycerol as substrate {ECO:0000269|PubMed:8798474}; | null | null | null | FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein pa... | Homo sapiens (Human) |
P11151 | LIPL_BOVIN | MESKALLLLALSVCLQSLTVSRGGLVAADRITGGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEI... | 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]; high-density lipoprotein particle remodeling [GO:0034375]; low-density lipoprotein particle mediated signalin... | catalytic complex [GO:1902494]; cell surface [GO:0009986]; chylomicron [GO:0042627]; 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:0000269|PubMed:2142941}; Peripheral membrane protein {ECO:0000269|PubMed:2142941}; Extracellular side {ECO:0000269|PubMed:2142941}. Secreted {ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:2142941, ECO:0000269|PubMed:2674142, ECO:0000269|PubMed:2885834, ECO:0000269|PubMed:29899... | 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:10727238, ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:27929370... | null | null | null | null | FUNCTION: Key enzyme in triglyceride metabolism (PubMed:10727238, PubMed:16179346, PubMed:9188470). 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 storag... | Bos taurus (Bovine) |
P11152 | LIPL_MOUSE | MESKALLLVVLGVWLQSLTAFRGGVAAADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKV... | 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]; lipid c... | catalytic complex [GO:1902494]; cell surface [GO:0009986]; chylomicron [GO:0042627]; 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}.; PTM: N-glycosylated. {ECO:0000269|PubMed:25066055}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}; Peripheral membrane protein {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}; Extracellular side {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ... | 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:8675619}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-p... | 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:8675619). Although it has both phospholip... | Mus musculus (Mouse) |
P11153 | LIPL_CAVPO | MNIDRKILNKALAKEKVANCQKDYTDIESKFARRTPENTVEDTCHLIPGVTESVANCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLRRAQHHYPESADYTKLVGEDVARFINWMEDEFKYSVDNVHLLGYSLGAHAAGVAGSRTNTKVSRITGLDPAGPNFEYAEATSRLSPDDAQFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGSFQPGCNIQDALRVISQKGFGDMDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKVRAKRSSKMYL... | 3.1.1.32; 3.1.1.34 | null | chylomicron remodeling [GO:0034371]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; triglyceride catabolic process [GO:0019433]; very-low-density lipoprotein particle remodeling [GO:0034372] | chylomicron [GO:0042627]; 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]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; lipoprotein particle binding [GO:0071813]; metal ion binding [GO:0046872]; phosphatidylseri... | 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:0000250|UniProtKB:P11151}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11151}. Note=Newly synth... | 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:0000250|UniProtKB:P11151}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3... | null | null | null | null | FUNCTION: Key enzyme in triglyceride metabolism (By similarity). 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 (By similarity). Although it has ... | Cavia porcellus (Guinea pig) |
P11154 | PYC1_YEAST | MSQRKFAGLRDNFNLLGEKNKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVGQYTPVGAYLAIDEIISIAQKHQVDFIHPGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTIT... | 6.4.1.1 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; | gluconeogenesis [GO:0006094]; pyruvate metabolic process [GO:0006090] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; pyruvate carboxylase activity [GO:0004736] | PF02785;PF00289;PF00364;PF02786;PF00682;PF02436; | 2.40.50.100;3.20.20.70;3.30.470.20;1.10.472.90;1.10.10.60;3.10.600.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1; | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. | null | null | FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11155 | PPDK1_MAIZE | MAASVSRAICVQKPGSKCTRDREATSFARRSVAAPRPPHAKAAGVIRSDSGAGRGQHCSPLRAVVDAAPIQTTKKRVFHFGKGKSEGNKTMKELLGGKGANLAEMASIGLSVPPGFTVSTEACQQYQDAGCALPAGLWAEIVDGLQWVEEYMGATLGDPQRPLLLSVRSGAAVSMPGMMDTVLNLGLNDEVAAGLAAKSGERFAYDSFRRFLDMFGNVVMDIPRSLFEEKLEHMKESKGLKNDTDLTASDLKELVGQYKEVYLSAKGEPFPSDPKKQLELAVLAVFNSWESPRAKKYRSINQITGLRGTAVNVQCMVFGN... | 2.7.9.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15667207, ECO:0000305|PubMed:9287137}; | phosphorylation [GO:0016310]; photosynthesis [GO:0015979]; pyruvate metabolic process [GO:0006090] | chloroplast [GO:0009507] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; pyruvate, phosphate dikinase activity [GO:0050242] | PF00391;PF02896;PF01326; | 1.20.80.30;3.30.1490.20;3.30.470.20;3.20.20.60;3.50.30.10;1.10.189.10; | PEP-utilizing enzyme family | PTM: Phosphorylation of Thr-527 in the dark inactivates the enzyme, dephosphorylation upon light stimulation reactivates the enzyme (PubMed:2834385). More highly phosphorylated when grown under high rather than low light regimes (70 vs 900 umol photons/m-2/s). the degree of phosphorylation is strictly regulated by ligh... | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:22833285}. Cytoplasm {ECO:0000269|PubMed:1668653}. Note=Isoform C4PPDKZM1 is targeted to the chloroplast while isoform CYPPDKZM1 is found in the cytoplasm. Can be found associated with the thylakoid membrane. | CATALYTIC ACTIVITY: Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1; Evidence={ECO:0000269|PubMed:10683263, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=158 uM for pyruvate {ECO:0000269|PubMed:9038349}; KM=178 uM for pyruvate {ECO:0000269|PubMed:21414960}; KM=95 uM for ATP {ECO:0000269|PubMed:9038349}; KM=194 uM for phosphoenolpyruvate {ECO:0000269|PubMed:21414960}; KM=408 uM for phosphate {ECO:0000269|PubMed:90383... | PATHWAY: Photosynthesis; C4 acid pathway. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Loss of activity below 10 degrees Celsius. {ECO:0000269|PubMed:9038349}; | FUNCTION: Formation of phosphoenolpyruvate, which is the primary acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants. {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:21414960}. | Zea mays (Maize) |
P11157 | RIR2_MOUSE | MLSVRTPLATIADQQQLQLSPLKRLTLADKENTPPTLSSTRVLASKAARRIFQDSAELESKAPTNPSVEDEPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREYLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPAEQRVREIITNAVRIEQEFLTEALPVKLIGMNCTL... | 1.17.4.1 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 2 iron ions per subunit.; | 2'-deoxyribonucleotide biosynthetic process [GO:0009265]; blastocyst development [GO:0001824]; deoxyribonucleotide biosynthetic process [GO:0009263]; deoxyribonucleotide metabolic process [GO:0009262]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; protein heterotetramerization [GO:0051290];... | cytosol [GO:0005829]; nuclear envelope [GO:0005635]; ribonucleoside-diphosphate reductase complex [GO:0005971] | ferric iron binding [GO:0008199]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748] | PF00268; | 1.10.620.20; | Ribonucleoside diphosphate reductase small chain family | PTM: Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling (By similarity). Phosphorylated on Thr-33 by CDK1 and CDK2; predominantly in G2 and M phase (By similarity). {ECO:0000250|UniProtKB:P31350}.; PTM: Ubiquitinated by the SCF(CCNF) E3 ubiquitin-protein ligase complex; leading to its degradation... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31350}. Nucleus {ECO:0000250|UniProtKB:P31350}. Note=Localized to the cytoplasm in S phase cells. May localize to the nucleus in G2 phase cells. {ECO:0000250|UniProtKB:P31350}. | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316;... | null | null | null | null | FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P11161 | EGR2_HUMAN | MMTAKAVDKIPVTLSGFVHQLSDNIYPVEDLAATSVTIFPNAELGGPFDQMNGVAGDGMINIDMTGEKRSLDLPYPSSFAPVSAPRNQTFTYMGKFSIDPQYPGASCYPEGIINIVSAGILQGVTSPASTTASSSVTSASPNPLATGPLGVCTMSQTQPDLDHLYSPPPPPPPYSGCAGDLYQDPSAFLSAATTSTSSSLAYPPPPSYPSPKPATDPGLFPMIPDYPGFFPSQCQRDLHGTAGPDRKPFPCPLDTLRVPPPLTPLSTIRNFTLGGPSAGVTGPGASGGSEGPRLPGSSSAAAAAAAAAAYNPHHLPLRPI... | 2.3.2.- | null | aorta development [GO:0035904]; brain development [GO:0007420]; brain segmentation [GO:0035284]; cellular response to organic substance [GO:0071310]; facial nerve structural organization [GO:0021612]; fat cell differentiation [GO:0045444]; gene expression [GO:0010467]; learning or memory [GO:0007611]; motor neuron axon... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; 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]; HMG box domain binding [GO:0071837]; metal ion binding [GO:00... | PF11928;PF00096; | 3.30.160.60; | EGR C2H2-type zinc-finger protein family | PTM: Ubiquitinated by WWP2 leading to proteasomal degradation. {ECO:0000250|UniProtKB:P08152}.; PTM: Acetylated at Lys-247. May be deacetylated by HDAC6, HDAC10 or SIRT1. {ECO:0000250|UniProtKB:P08152}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P08152}. | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: Sequence-specific DNA-binding transcription factor (PubMed:17717711). Plays a role in hindbrain segmentation by regulating the expression of a subset of homeobox containing genes and in Schwann cell myelination by regulating the expression of genes involved in the formation and maintenance of myelin (By simil... | Homo sapiens (Human) |
P11166 | GTR1_HUMAN | MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAF... | null | null | cellular hyperosmotic response [GO:0071474]; cellular response to glucose starvation [GO:0042149]; cellular response to mechanical stimulus [GO:0071260]; central nervous system development [GO:0007417]; cerebral cortex development [GO:0021987]; dehydroascorbic acid transport [GO:0070837]; female pregnancy [GO:0007565];... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; blood microparticle [GO:0072562]; caveola [GO:0005901]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; female germ cell nucleus [GO:0001674]; female pronucleus [GO:0001939]; glucose transp... | D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; glucose transmembrane transporter activity [GO:0005355]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; long-chain fatty acid transporter activity [GO:0005324]; protein ... | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | PTM: Phosphorylation at Ser-226 by PKC promotes glucose uptake by increasing cell membrane localization. {ECO:0000269|PubMed:25982116}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18245775, ECO:0000269|PubMed:19449892, ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:24847886, ECO:0000269|PubMed:25982116, ECO:0000269|PubMed:30197081}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000269|PubMed:17081065}. Photoreceptor inner seg... | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:10227690, ECO:0000269|PubMed:10954735, ECO:0000269|PubMed:25982116, ECO:0000269|PubMed:27078104, ECO:0000269|PubMed:32860739}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25.6 mM for glucose {ECO:0000269|PubMed:25982116}; KM=50.1 mM for glucose (in presence of TPA) {ECO:0000269|PubMed:25982116}; KM=2.5 mM for glucose {ECO:0000269|PubMed:10954735}; | PATHWAY: Carbohydrate degradation. | null | null | FUNCTION: Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake (PubMed:10227690, PubMed:10954735, PubMed:18245775, PubMed:19449892, PubMed:25982116, PubMed:27078104, PubMed:32860739). Has a very broad substrate specificity; can transport a wide range of aldoses including both ... | Homo sapiens (Human) |
P11167 | GTR1_RAT | MEPSSKKVTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWNHRYGESIPSTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNADLWPLLLSVIFIPALLQCILLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQEMKEEGRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAF... | null | null | cellular hyperosmotic response [GO:0071474]; cellular response to glucose starvation [GO:0042149]; cellular response to mechanical stimulus [GO:0071260]; central nervous system development [GO:0007417]; cerebral cortex development [GO:0021987]; dehydroascorbic acid transport [GO:0070837]; female pregnancy [GO:0007565];... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; female germ cell nucleus [GO:0001674]; female pronucleus [GO:0001939]; glucose transporter complex... | D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; glucose transmembrane transporter activity [GO:0005355]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; long-chain fatty acid transporter activity [GO:0005324]; protein ... | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | PTM: Phosphorylation at Ser-226 by PKC promotes glucose uptake by increasing cell membrane localization. {ECO:0000250|UniProtKB:P11166}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2211693}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P17809}. | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:2211693}; | null | null | null | null | FUNCTION: Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake (PubMed:2211693). Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses (By similarity). Most important energy carrier of the brain: present at the blood-... | Rattus norvegicus (Rat) |
P11168 | GTR2_HUMAN | MTEDKVTGTLVFTVITAVLGSFQFGYDIGVINAPQQVIISHYRHVLGVPLDDRKAINNYVINSTDELPTISYSMNPKPTPWAEEETVAAAQLITMLWSLSVSSFAVGGMTASFFGGWLGDTLGRIKAMLVANILSLVGALLMGFSKLGPSHILIIAGRSISGLYCGLISGLVPMYIGEIAPTALRGALGTFHQLAIVTGILISQIIGLEFILGNYDLWHILLGLSGVRAILQSLLLFFCPESPRYLYIKLDEEVKAKQSLKRLRGYDDVTKDINEMRKEREEASSEQKVSIIQLFTNSSYRQPILVALMLHVAQQFSGIN... | null | null | carbohydrate metabolic process [GO:0005975]; dehydroascorbic acid transport [GO:0070837]; fructose transmembrane transport [GO:0015755]; galactose transmembrane transport [GO:0015757]; glucose import [GO:0046323]; glucose transmembrane transport [GO:1904659]; positive regulation of insulin secretion involved in cellula... | apical plasma membrane [GO:0016324]; brush border [GO:0005903]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; membrane [GO:0016020]; plasma membrane [GO:0005886] | D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; fructose transmembrane transporter activity [GO:0005353]; galactose transmembrane transporter activity [GO:0005354]; glucose transmembrane transporter activity [GO:0005355]; hexose transmembr... | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | PTM: N-glycosylated; required for stability and retention at the cell surface of pancreatic beta cells. {ECO:0000250|UniProtKB:P14246}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28083649}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:23396969, ECO:0000269|PubMed:28083649, ECO:0000269|PubMed:29548810, ECO:0000269|PubMed:8457197}; CATALYTIC ACTIVITY: Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.23 mM for dehydroascorbate {ECO:0000269|PubMed:23396969}; KM=11.2 mM for deoxyglucose {ECO:0000269|PubMed:8457197}; KM=85.5 mM for D-galactose {ECO:0000269|PubMed:8457197}; KM=66.7 mM for D-fructose {ECO:0000269|PubMed:8457197}; | null | null | null | FUNCTION: Facilitative hexose transporter that mediates the transport of glucose, fructose and galactose (PubMed:16186102, PubMed:23396969, PubMed:28083649, PubMed:8027028, PubMed:8457197). Likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of g... | Homo sapiens (Human) |
P11169 | GTR3_HUMAN | MGTQKVTPALIFAITVATIGSFQFGYNTGVINAPEKIIKEFINKTLTDKGNAPPSEVLLTSLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLIVNLLAVTGGCFMGLCKVAKSVEMLILGRLVIGLFCGLCTGFVPMYIGEISPTALRGAFGTLNQLGIVVGILVAQIFGLEFILGSEELWPLLLGFTILPAILQSAALPFCPESPRFLLINRKEEENAKQILQRLWGTQDVSQDIQEMKDESARMSQEKQVTVLELFRVSSYRQPIIISIVLQLSQQLSGINAVFYYSTGIFKDAGVQEPIYATIGAGVVNTIFTV... | null | null | carbohydrate metabolic process [GO:0005975]; dehydroascorbic acid transport [GO:0070837]; galactose transmembrane transport [GO:0015757]; glucose import [GO:0046323]; glucose import across plasma membrane [GO:0098708]; glucose transmembrane transport [GO:1904659]; L-ascorbic acid metabolic process [GO:0019852]; transpo... | aggresome [GO:0016235]; cell projection [GO:0042995]; extracellular exosome [GO:0070062]; ficolin-1-rich granule membrane [GO:0101003]; membrane [GO:0016020]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]; specific granule membrane [GO:0035579]; tertiary granule membrane... | D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; galactose transmembrane transporter activity [GO:0005354]; glucose binding [GO:0005536]; glucose transmembrane transporter activity [GO:0005355] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9477959, ECO:0000305|PubMed:26176916}; Multi-pass membrane protein {ECO:0000269|PubMed:26176916}. Perikaryon {ECO:0000250|UniProtKB:Q07647}. Cell projection {ECO:0000250|UniProtKB:Q07647}. Note=Localized to densely spaced patches along neuronal processes. {ECO:000... | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:26176916, ECO:0000269|PubMed:32860739, ECO:0000269|PubMed:8457197, ECO:0000269|PubMed:9477959}; CATALYTIC ACTIVITY: Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for deoxyglucose {ECO:0000269|PubMed:8457197, ECO:0000269|PubMed:9477959}; KM=8.5 mM for D-galactose {ECO:0000269|PubMed:8457197}; | null | null | null | FUNCTION: Facilitative glucose transporter (PubMed:26176916, PubMed:32860739, PubMed:9477959). Can also mediate the uptake of various other monosaccharides across the cell membrane (PubMed:26176916, PubMed:9477959). Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also... | Homo sapiens (Human) |
P11170 | SC5A1_RABIT | MDSSTLSPLTTSTAAPLESYERIRNAADISVIVIYFLVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAASGIATGGFEWNALIMVVVLGWVFVPIYIRAGVVTMPEYLQKRFGGKRIQIYLSILSLLLYIFTKISADIFSGAIFIQLTLGLDIYVAIIILLVITGLYTITGGLAAVIYTDTLQTAIMMVGSVILTGFAFHEVGGYEAFTEKYMRAIPSQISYGNTSIPQKCYTPREDAFHIFRDAITGDIPWPGLVFGMSILTLWYWCTDQVIVQRCLSAKNLSHVKAGCILCGYL... | null | null | alpha-glucoside transport [GO:0000017]; fucose transmembrane transport [GO:0015756]; galactose transmembrane transport [GO:0015757]; glucose transmembrane transport [GO:1904659]; intestinal D-glucose absorption [GO:0001951]; myo-inositol transport [GO:0015798]; pentose transmembrane transport [GO:0015750]; renal glucos... | apical plasma membrane [GO:0016324] | alpha-glucoside transmembrane transporter activity [GO:0015151]; fucose transmembrane transporter activity [GO:0015150]; galactose transmembrane transporter activity [GO:0005354]; galactose:sodium symporter activity [GO:0015371]; glucose:sodium symporter activity [GO:0005412]; myo-inositol:sodium symporter activity [GO... | PF00474; | 1.20.1730.10; | Sodium:solute symporter (SSF) (TC 2.A.21) family | PTM: N-glycosylation is not necessary for the cotransporter function. {ECO:0000250|UniProtKB:P13866}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q8C3K6}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=D-glucose(out) + 2 Na(+)(out) = D-glucose(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70495, ChEBI:CHEBI:4167, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P13866}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70496; Evidence={ECO:0000250|UniProtKB:P13866}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: Electrogenic Na(+)-coupled sugar symporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (By similarity). Has a primary role in t... | Oryctolagus cuniculus (Rabbit) |
P11171 | EPB41_HUMAN | MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRPKSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECSKIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPC... | null | null | actin cytoskeleton organization [GO:0030036]; actomyosin structure organization [GO:0031032]; cell cycle [GO:0007049]; cell division [GO:0051301]; cortical actin cytoskeleton organization [GO:0030866]; positive regulation of protein binding [GO:0032092]; positive regulation of protein localization to cell cortex [GO:19... | basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cortical cytoskeleton [GO:0030863]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; mitotic spindle [GO:0072686]; nuclear body [GO:0016604... | 1-phosphatidylinositol binding [GO:0005545]; actin binding [GO:0003779]; calmodulin binding [GO:0005516]; phosphoprotein binding [GO:0051219]; spectrin binding [GO:0030507]; structural constituent of cytoskeleton [GO:0005200] | PF05902;PF08736;PF09380;PF00373;PF09379;PF04382; | 1.20.80.10;2.30.29.30; | null | PTM: Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions.; PTM: Phosphorylation on Tyr-660 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex. {ECO:0000269|PubMed:1647028}.; PTM: O-glycosylat... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12427749}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12427749, ECO:0000269|PubMed:23870127}. Nucleus {ECO:0000269|PubMed:12427749}. | null | null | null | null | null | FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruit... | Homo sapiens (Human) |
P11172 | UMPS_HUMAN | MAVARAALGPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCTLSKMLEILEQQKKVDAETVGRVKRFIQENVFVAANHNGSPLSIKEAPKELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKCHEFLIFEDRKFADIGN... | 2.4.2.10; 4.1.1.23 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; cellular response to xenobiotic stimulus [GO:0071466]; female pregnancy [GO:0007565]; lactation [GO:0007595]; pyrimidine nucleobase biosynthetic process [GO:0019856]; UDP biosynthetic process [GO:0006225]... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; orotate phosphoribosyltransferase activity [GO:0004588]; orotidine-5'-phosphate decarboxylase activity [GO:0004590] | PF00215;PF00156; | 3.40.50.2020;3.20.20.70; | Purine/pyrimidine phosphoribosyltransferase family; OMP decarboxylase family | null | null | CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000269|PubMed:9042911}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.6 uM for orotidine 5'-phosphate {ECO:0000269|PubMed:18184586}; Note=kcat is 0.75 sec(-1) with orotidine 5'-phosphate as substrate. {ECO:0000269|PubMed:18184586}; | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. {ECO:0000269|PubMed:9042911}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. {ECO:0000269|PubMed:9042911}. | null | null | FUNCTION: Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine mon... | Homo sapiens (Human) |
P11177 | ODPB_HUMAN | MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDA... | 1.2.4.1 | COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:12651851, ECO:0000269|PubMed:19081061}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; glucose metabolic process [GO:0006006]; tricarboxylic acid cycle [GO:0006099] | mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pyruvate dehydrogenase complex [GO:0045254] | pyruvate dehydrogenase (acetyl-transferring) activity [GO:0004739] | PF02779;PF02780; | 3.40.50.920;3.40.50.970; | null | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:1... | null | null | null | null | FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061}. | Homo sapiens (Human) |
P11179 | ODO2_BOVIN | MLSRSRCASRAFSRSLSAFQKGNCPLVRRSLPGISLCQGPGYPDSRKTVINSSNIFSVRFFRTTAVCKDDVITVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAAAPAAAAPKAEPTVSAVPPPPAAPIPTQMPPVPSPSQPLTSKPVSAVKPTAAPPRAEAGAGVGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDIS... | 2.3.1.61 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000269|PubMed:3115829}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000269|PubMed:3115829}; | 2-oxoglutarate metabolic process [GO:0006103]; histone succinylation [GO:0106077]; L-lysine catabolic process to acetyl-CoA via saccharopine [GO:0033512]; succinyl-CoA metabolic process [GO:0006104]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; oxoglutarate dehydrogenase complex [GO:0045252] | acyltransferase activity [GO:0016746]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149] | PF00198;PF00364; | 2.40.50.100;3.30.559.10; | 2-oxoacid dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P36957}. Nucleus {ECO:0000250|UniProtKB:P36957}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:P36957}. | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287,... | null | PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. {ECO:0000250|UniProtKB:P36957}. | null | null | FUNCTION: Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in t... | Bos taurus (Bovine) |
P11180 | ODP2_BOVIN | MWRVCARRAQNAAPRAGFGARWTAFREEPGAPCVTPQAGSALARCSSKTPGYGRVRALCGWSPVSRATPRNRVLLQLWGSPSRRWYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGEKINEGELIAEVETDKATVGFESVEECYMAKILVAEGTRDVPVGAIICITVDKPEDVEAFKNYTLDSSAAPAPPAAPAPTPAAPAPSPTPSAQAPGSSYPTHMQVLLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILIPEGTRDVPLGTPLCIIVEKEADIPAFADYRPAEVTDLKPPAPP... | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000269|PubMed:3117054}; Note=Binds 2 lipoyl cofactors covalently. {ECO:0000305|PubMed:3117054}; | carboxylic acid metabolic process [GO:0019752]; glucose metabolic process [GO:0006006]; tricarboxylic acid cycle [GO:0006099] | mitochondrial matrix [GO:0005759] | dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | PTM: Delipoylated at Lys-132 and Lys-259 by SIRT4, delipoylation decreases the PHD complex activity. {ECO:0000250|UniProtKB:P10515}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P08461}. | 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; Evidence={ECO:000... | null | null | null | null | FUNCTION: As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety (PubMed:3117054). The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarbox... | Bos taurus (Bovine) |
P11181 | ODB2_BOVIN | MAAALVLRTWSRAAGQLICVRYFQTCGNVHVLKPKYVCFFGYPPFKYSHPYQWLKTTAALQGQIVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDTAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVIGSGKDGRILKEDILNYLEKQTGAILPPSPKAEIMPPPPKPKDRTIPIPISKPPVFIGKDRTEPVKGFHKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLL... | 2.3.1.168 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000269|PubMed:3245861}; | carboxylic acid metabolic process [GO:0019752] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | acetyltransferase activity [GO:0016407]; dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity [GO:0043754]; 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 | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:283398}. | CATALYTIC ACTIVITY: Reaction=2-methylpropanoyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1... | null | null | null | null | FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within ... | Bos taurus (Bovine) |
P11182 | ODB2_HUMAN | MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPILVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLL... | 2.3.1.168 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250|UniProtKB:P11181}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250|UniProtKB:P11181}; | branched-chain amino acid catabolic process [GO:0009083] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrial oxoglutarate dehydrogenase complex [GO:0009353]; mitochondrion [GO:0005739] | acetyltransferase activity [GO:0016407]; dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity [GO:0043754]; lipoic acid binding [GO:0031405]; ubiquitin protein ligase binding [GO:0031625] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P11181}. | CATALYTIC ACTIVITY: Reaction=2-methylpropanoyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1... | null | null | null | null | FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within ... | Homo sapiens (Human) |
P11193 | VP4_ROTHW | MASLIYRQLLTNSYSVDLHDEIEQIGSEKTQNVTINPSPFAQTRYAPVNWGHGEINDSTTVEPILDGPYQPTTFTPPNDYWILINSNTNGVVYESTNNSDFWTAVVAIEPHVNPVDRQYTIFGESKQFNVSNDSNKWKFLEMFRSSSQNEFYNRRTLTSDTRFVGILKYGGRVWTFHGETPRATTDSSSTANLNNISITIHSEFYIIPRSQESKCNEYINNGLPPIQNTRNVVPLPLSSRSIQYKRAQVNEDIIVSKTSLWKEMQYNRDIIIRFKFGNSIVKMGGLGYKWSEISYKAANYQYNYLRDGEQVTAHTTCSVN... | null | null | permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell plasma membrane [GO:0020002]; host cell rough endoplasmic reticulum [GO:0044168]; host cytoskeleton [GO:0044163]; membrane [GO:0016020]; viral outer capsid [GO:0039624] | null | PF17477;PF00426;PF17478; | 1.20.5.170;2.60.120.200; | Rotavirus VP4 family | PTM: [Outer capsid protein VP4]: Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion. Cleavage of VP4 by tryps... | SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04132}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04132}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04132}. Host cytoplasm, host cytoskeleton {ECO:0000255|HAMAP-Rule:MF_04132}. Host endoplasmic reticulum-Golgi inte... | null | null | null | null | null | FUNCTION: [Outer capsid protein VP4]: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential con... | Rotavirus A (strain RVA/Human/United States/Wa/1974/G1P1A[8]) (RV-A) |
P11204 | POL_EIAV9 | TAWTFLKAMQKCSKKREARGSREAPETNFPDTTEESAQQICCTRDSSDSKSVPRSERNKKGIQCQGEGSSRGSQPGQFVGVTYNLEKRPTTIVLINDTPLNVLLDTGADTSVLTTAHYNRLKYRGRKYQGTGIIGVGGNVETFSTPVTIKKKGRHIKTRMLVADIPVTILGRDILQDLGAKLVLAQLSKEIKFRKIELKEGTMGPKIPQWPLTKEKLEGAKEIVQRLLSEGKISEASDNNPYNSPIFVIKKRSGKWRLLQDLRELNKTVQVGTEISRGLPHPGGLIKCKHMTVLDIGDAYFTIPLDPEFRPYTAFTIPSI... | 2.7.7.-; 2.7.7.49; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; dUMP biosynthetic process [GO:0006226]; dUTP catabolic process [GO:0046081]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | null | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; dUTP diphosphatase activity [GO:0004170]; exoribonuclease H activity [GO:0004533]; magnesium ion binding [GO:0000287]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; UTP binding [GO:000213... | PF00692;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817; | 1.10.10.200;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;2.30.30.10;3.30.420.10; | Retroviral Pol polyprotein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end... | null | null | null | null | FUNCTION: During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. | Equine infectious anemia virus (isolate 1369) (EIAV) |
P11205 | L_NDVB | MASSGPERAEHQIILPESHLSSPLVKHKLLYYWKLTGLPLPDECDFDHLILSRQWKKILESASPDTERMIKLGRAVHQTLNHNSRITGVLHPRCLEELASIEVPDSTNKFRKIEKKIQIHNTRYGELFTRLCTHIEKKLLGSSWSNNVPRSEEFNSIRTDPAFWFHSKWSTAKFAWLHIKQIQRHLIVAARTRSAANKLVMLTHKVGQVFVTPELVIVTHTNENKFTCLTQELVLMYADMMEGRDMVNIISTTAVHLRSLSEKIDDILQLIDALAKDLGNQVYDVVSLMEGFAYGAVQLLEPSGRFAGHFFAFNLQELKD... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | negative stranded viral RNA transcription [GO:0039697] | 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... | Newcastle disease virus (strain Beaudette C/45) (NDV) |
P11207 | V_PIV5 | MDPTDLSFSPDEINKLIETGLNTVEYFTSQQVTGTSSLGKNTIPPGVTGLLTNAAEAKIQESTNHQKGSVGGGAKPKKPRPKIAIVPADDKTVPGKPIPNPLLGLDSTPSTQTVLDLSGKTLPSGSYKGVKLAKFGKENLMTRFIEEPRENPIATSSPIDFKRGRDTGGFHRREYSIGWVGDEVKVTEWCNPSCSPITAAARRFECTCHQCPVTCSECERDT | null | null | symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity [GO:0039554]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of S... | host cell cytoplasm [GO:0030430] | metal ion binding [GO:0046872]; RNA binding [GO:0003723]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF14313;PF13008; | 4.10.80.340; | Paramyxoviruses V protein family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activ... | Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5) |
P11209 | FUS_HRSVR | MELPILKTNAITAILAAVTLCFASSQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKSAVTELQLLMQSTPATNNRARRELPRFMNYTLNNTKNTNVTLSKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSP... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of syncytium formation by virus [GO:0060141]; symbiont entry into host cell [GO:0046718] | host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00523; | 1.10.287.2480;6.10.250.1160;6.20.370.50; | Paramyxoviruses fusion glycoprotein family | PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed at two sites by a host furin-like protease probably in the Golgi. The cleavage site between p27 and F1 may occur after endocytosis to yield the mature F1 and F2 proteins. Both cleavag... | SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03420}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane {ECO:0000250|UniProtKB:P03420}; Single-pass type I membrane protein {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. {ECO:0000250|UniProtKB:P03420}.; FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein. Under the current model, the protein has at least 3 c... | Human respiratory syncytial virus A (strain RSS-2) |
P11213 | L_RABVP | MLDPGEVYDDPIDPIELEAEPRGTPTVPNILRNSDYNLNSPLIEDPARLMLEWLKTGNRPYRMTLTDNCSRSFRVLKDYFKKVDLGSLKVGGMAAQSMISLWLYGAHSESNRSRRCITDLAHFYSKSSPIEKLLNLTLGNRGLRIPPEGVLSCLERVDYDNAFGRYLANTYSSYLFFHVITLYMNALDWDEEKTILALWKDLTSVDIGKDLVKFKDQIWGLLIVTKDFVYSQSSNCLFDRNYTLMLKDLFLSRFNSLMVLLSPPEPRYSDDLISQLCQLYIAGDQVLSMCGNSGYEVIKILEPYVVNSLVQRAEKFRPLI... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | negative stranded viral RNA replication [GO:0039689] | 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] | PF21080;PF14314;PF21081;PF14318;PF00946; | null | Rhabdoviruses protein L family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged asymmetrically towards the blunt end of the virus. {ECO:0000250|UniProtKB:P03523}. | 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... | Rabies virus (strain Pasteur vaccins / PV) (RABV) |
P11214 | TPA_MOUSE | MKRELLCVLLLCGLAFPLPDQGIHGRFRRGARSYRATCRDEPTQTTYQQHQSWLRPMLRSSRVEYCRCNSGLVQCHSVPVRSCSEPRCFNGGTCQQALYFSDFVCQCPDGFVGKRCDIDTRATCFEEQGITYRGTWSTAESGAECINWNSSVLSLKPYNARRPNAIKLGLGNHNYCRNPDRDLKPWCYVFKAGKYTTEFCSTPACPKGKSEDCYVGKGVTYRGTHSLTTSQASCLPWNSIVLMGKSYTAWRTNSQALGLGRHNYCRNPDGDARPWCHVMKDRKLTWEYCDMSPCSTCGLRQYKRPQFRIKGGLYTDITSH... | 3.4.21.68 | null | negative regulation of fibrinolysis [GO:0051918]; negative regulation of plasminogen activation [GO:0010757]; plasminogen activation [GO:0031639]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; prevention of polyspermy [GO:0060468]; proteolysis [GO:0006508]; response to hypoxia [GO:0001666]; sm... | apical part of cell [GO:0045177]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; neuronal dense core vesicle [GO:0098992]; perisynaptic space [GO:0099544]; postsynapse [GO:0098794]; Schaffer collateral - CA1 synapse [GO:0098685]; secretory granul... | phosphoprotein binding [GO:0051219]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102] | PF00008;PF00039;PF00051;PF00089; | 2.10.70.10;2.10.25.10;2.40.20.10;2.40.10.10; | Peptidase S1 family | PTM: The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-308 catalyzed by plasmin, tissue kallikrein or factor Xa. | SUBCELLULAR LOCATION: Secreted, extracellular space. | CATALYTIC ACTIVITY: Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.68; | null | null | null | null | FUNCTION: Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activ... | Mus musculus (Mouse) |
P11215 | ITAM_HUMAN | MALRVLLLTALTLCHGFNLDTENAMTFQENARGFGQSVVQLQGSRVVVGAPQEIVAANQRGSLYQCDYSTGSCEPIRLQVPVEAVNMSLGLSLAATTSPPQLLACGPTVHQTCSENTYVKGLCFLFGSNLRQQPQKFPEALRGCPQEDSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVNNFEA... | null | null | amyloid-beta clearance [GO:0097242]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cell-matrix adhesion [GO:0007160]; complement receptor mediated signaling pathway [GO:0002430]; compl... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integrin alphaM-beta2 complex [GO:0034688]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; specific granule membrane [GO:003557... | amyloid-beta binding [GO:0001540]; cargo receptor activity [GO:0038024]; complement component C3b binding [GO:0001851]; heat shock protein binding [GO:0031072]; integrin binding [GO:0005178]; metal ion binding [GO:0046872] | PF01839;PF08441;PF20805;PF00357;PF21520;PF00092; | 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 {ECO:0000269|PubMed:21193407}; Single-pass type I membrane protein {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:21193407}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens (PubMed:20008295, PubMed:9558116). It is identical with CR-3, the receptor for the iC3b fragment of the third complemen... | Homo sapiens (Human) |
P11216 | PYGB_HUMAN | MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCR... | 2.4.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | glycogen catabolic process [GO:0005980] | azurophil granule lumen [GO:0035578]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020] | 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 | PTM: Phosphorylated (PubMed:27402852). Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A (By similarity). {ECO:0000250|UniProtKB:P11217, ECO:0000269|PubMed:27402852}. | null | 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:27402852}; | null | null | null | null | FUNCTION: Glycogen phosphorylase that regulates glycogen mobilization (PubMed:27402852). Phosphorylase is an important allosteric enzyme in carbohydrate metabolism (PubMed:3346228). Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates (PubMed:3346228). However, all known ... | Homo sapiens (Human) |
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