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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P09610 | HMDH_MESAU | MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASALAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTTEHSKVSLGLDEDVSKRIEPSVSLWQFYLSKMISMDI... | 1.1.1.34 | null | cholesterol biosynthetic process [GO:0006695]; coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; isoprenoid biosynthetic process [GO:0008299] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]; NADP binding [GO:0050661] | PF00368;PF12349; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | PTM: Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD). Accumulation of sterols in the endoplasmic reticulum (ER) membrane, triggers binding of the reductase to the ER membrane protein INSIG1 or INSIG2. The INSIG1 binding leads to the recruitment of the ubiquitin ligase, AMFR/gp78, RNF139 or... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. Peroxisome membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000269|PubMed:8288583, ECO:0000269|Pub... | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. | null | null | FUNCTION: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis. {ECO:0000269|PubMed:8288583, ECO:0000269|PubMed:8473286}. | Mesocricetus auratus (Golden hamster) |
P09613 | GP_UUKS | MVRTYLLLLLLCGPATPFFNHLMDVTRRLLDSSNATWQRDQPDTHRLSRLDAHVMSMLGVGSHIDEVSVNHSQHLHNFRSYNCEEGRRTLTMMDPKSGKFKRLKCNENQTLSKDCASCIEKKSSIMKSEHLVYDDAICQSDYSSPEAMPDHETHLCRIGPLHIQHCTHEAKRVQHVSWFWIDGKLRVYDDFSVSWTEGKFLSLFDCLNETSKDHNCNKAVCLEGRCSGDLQFCTEFTCSYAKADCNCKRNQVSGVAVVHTKHGSFMPECMGQSLWSVRKPLSKRSVTVQQPCMDCESDCKVDHILVIVRHFYPDHYQACL... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host endosome membrane [GO:0039654]; symbiont entry into host cell [GO:0046718]; viral budding from Golgi membrane [GO:0046760]; viral budding via host ESCRT complex [GO:0039702] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF19019;PF07243;PF07245; | 2.60.40.3770;2.60.98.50; | Phlebovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins including glycoprotein C and glycoprotein N. {ECO:0000269|PubMed:8985341}.; PTM: [Glycoprotein N]: The cytoplasmic tail is Palmitoylated. {ECO:0000269|PubMed:8985341, ECO:0000269|PubMed:9151865}.; PTM: [Glycoprotein N]: Glycosyla... | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000305|PubMed:1988460}; Single-pass type I membrane protein {ECO:0000269|PubMed:8985341}. Host Golgi apparatus membrane {ECO:0000269|PubMed:17670814, ECO:0000269|PubMed:9151865, ECO:0000269|PubMed:9811692, ECO:0000305|PubMed:1602557, ECO:0000305|PubMed:76251... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (PubMed:1988460). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (Pu... | Uukuniemi virus (strain S23) (UUKV) |
P09615 | WNTG_DROME | MDISYIFVICLMALCSGGSSLSQVEGKQKSGRGRGSMWWGIAKVGEPNNITPIMYMDPAIHSTLRRKQRRLVRDNPGVLGALVKGANLAISECQHQFRNRRWNCSTRNFSRGKNLFGKIVDRGCRETSFIYAITSAAVTHSIARACSEGTIESCTCDYSHQSRSPQANHQAGSVAGVRDWEWGGCSDNIGFGFKFSREFVDTGERGRNLREKMNLHNNEAGRAHVQAEMRQECKCHGMSGSCTVKTCWMRLANFRVIGDNLKARFDGATRVQVTNSLRATNALAPVSPNAAGSNSVGSNGLIIPQSGLVYGEEEERMLND... | null | null | anterior/posterior pattern specification, imaginal disc [GO:0007448]; branch fusion, open tracheal system [GO:0035147]; branching morphogenesis of an epithelial tube [GO:0048754]; canonical Wnt signaling pathway [GO:0060070]; cardioblast differentiation [GO:0010002]; cell elongation involved in imaginal disc-derived wi... | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195] | cytokine activity [GO:0005125]; extracellular matrix binding [GO:0050840]; frizzled binding [GO:0005109]; glycosaminoglycan binding [GO:0005539]; heparan sulfate proteoglycan binding [GO:0043395]; morphogen activity [GO:0016015]; receptor ligand activity [GO:0048018] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylated by porcupine. The lipid group functions as a sorting signal, targeting the ligand to polarized vesicles that transport wg to unique sites at the cell surface. Depalmitoleoylated by notum, leading to inhibit Wnt signaling pathway. {ECO:0000305|PubMed:11821428, ECO:0000305|PubMed:15166250, ECO:00003... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15166250, ECO:0000269|PubMed:18193037, ECO:0000269|PubMed:26974662, ECO:0000269|PubMed:8262072}. Synapse {ECO:0000269|PubMed:19837038}. Membrane; Lipid-anchor. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:15166250}. Note=Palmitoleoylation con... | null | null | null | null | null | FUNCTION: Binds as a ligand to a family of frizzled seven-transmembrane receptors and acts through a cascade of genes on the nucleus. Segment polarity protein. May be a growth factor. Acts on neighboring cells to regulate at least one gene, the homeobox segmentation gene engrailed. Wg signal represses arm phosphorylati... | Drosophila melanogaster (Fruit fly) |
P09616 | HLA_STAAU | MKTRIVSSVTTTLLLGSILMNPVAGAADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGTIAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNSIDTKEYMSTLTYGFNGNVTGDDTGKIGGLIGANVSIGHTLKYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWGPYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASKQQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWTDRSSERYKIDWEKEEMTN | null | null | cytolysis in another organism [GO:0051715] | extracellular region [GO:0005576] | identical protein binding [GO:0042802]; toxin activity [GO:0090729] | PF07968; | 2.70.240.10; | Aerolysin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8943190}. Note=Secreted as a monomer (PubMed:8943190). After oligomerization and pore formation, the complex is translocated across the bilayer, probably via the Gly-rich domain of each strand. {ECO:0000269|PubMed:8943190}. | null | null | null | null | null | FUNCTION: Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis (PubMed:1587866, PubMed:20624979). Human RBCs bind much less alpha-toxin than do rabbit RBCs... | Staphylococcus aureus |
P09619 | PGFRB_HUMAN | MRLPGAMPALALKGELLLLSLLLLLEPQISQGLVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLG... | 2.7.10.1 | null | aorta morphogenesis [GO:0035909]; cardiac myofibril assembly [GO:0055003]; cell chemotaxis [GO:0060326]; cell migration involved in coronary angiogenesis [GO:0060981]; cell migration involved in vasculogenesis [GO:0035441]; metanephric glomerular capillary formation [GO:0072277]; metanephric glomerular mesangial cell p... | apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; recept... | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; platelet activating factor receptor activity [GO:0004992]; platelet-derived growth factor beta-receptor activity [GO:0005019]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor activity [GO:0005017]; platelet-derived growt... | PF00047;PF13927;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-579, and to a lesser degree, at Tyr-581, is important for interaction with SRC family kinases. Pho... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role ... | Homo sapiens (Human) |
P09620 | KEX1_YEAST | MFYNRWLGTWLAMSALIRISVSLPSSEEYKVAYELLPGLSEVPDPSNIPQMHAGHIPLRSEDADEQDSSDLEYFFWKFTNNDSNGNVDRPLIIWLNGGPGCSSMDGALVESGPFRVNSDGKLYLNEGSWISKGDLLFIDQPTGTGFSVEQNKDEGKIDKNKFDEDLEDVTKHFMDFLENYFKIFPEDLTRKIILSGESYAGQYIPFFANAILNHNKFSKIDGDTYDLKALLIGNGWIDPNTQSLSYLPFAMEKKLIDESNPNFKHLTNAHENCQNLINSASTDEAAHFSYQECENILNLLLSYTRESSQKGTADCLNMYN... | 3.4.16.6 | null | apoptotic process [GO:0006915]; proteolysis [GO:0006508] | fungal-type vacuole [GO:0000324]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | serine-type carboxypeptidase activity [GO:0004185] | PF00450; | 3.40.50.1820; | Peptidase S10 family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1469044}; Single-pass type I membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1469044}. | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal arginine or lysine residue.; EC=3.4.16.6; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=284 uM for benzoyl-Phe-Ala-Arg {ECO:0000269|PubMed:8416959}; KM=516 uM for furylacryloyl-Ala-Arg {ECO:0000269|PubMed:8416959}; KM=962 uM for furylacryloyl-Ala-Lys {ECO:0000269|PubMed:8416959}; Vmax=64.25 umol/min/mg enzyme toward benzoyl-Phe-Ala-Arg {ECO:0000269|Pu... | null | null | null | FUNCTION: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09622 | DLDH_HUMAN | MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTK... | 1.8.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15946682, ECO:0000269|PubMed:16442803}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15946682, ECO:0000269|PubMed:16442803}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; branched-chain amino acid catabolic process [GO:0009083]; gastrulation [GO:0007369]; histone succinylation [GO:0106077]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; proteolysis [GO:0006508]; regulation of membrane potential [GO:0042391];... | acetyltransferase complex [GO:1902493]; acrosomal matrix [GO:0043159]; mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; nucleus [GO:0005634]; oxoglutarate dehydrogenase complex [GO:0045252]; pyruvate dehydrogenase compl... | dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:29211711, ECO:0000305|PubMed:3693355}. Nucleus {ECO:0000269|PubMed:29211711}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15888450}. Note=Mainly localizes in the mit... | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence={ECO... | null | null | null | null | FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20... | Homo sapiens (Human) |
P09623 | DLDH_PIG | MQSWSRVYCTLAKRGHFNRIAHGLQGVSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLEKMMEQKSNAVKALTGGIAHLFKQNKVVRVNGYGKITGKNQVTATKADGSTEVINTKNILIATGSEVTPFPGITIDEDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVELLGHVGGIGIDMEVSKNFQRILQKQGFKFKLNTKVIGATKKSDGNIDVSIEAASGGKAEVITCDVLLVCIGRRPFTQ... | 1.8.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P09622}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622}; | histone succinylation [GO:0106077] | acrosomal vesicle [GO:0001669]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; nucleus [GO:0005634]; oxoglutarate dehydrogenase complex [GO:0045252] | dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:3693355}. Nucleus {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P09622}. Note=Mainly localizes in the mitochondrion. A small fractio... | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence={ECO... | null | null | null | null | FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in ... | Sus scrofa (Pig) |
P09624 | DLDH_YEAST | MLRIRSLLNNKRAFSSTVRTLTINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALLNNSHLFHQMHTEAQKRGIDVNGDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILDVKNIIVATGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGL... | 1.8.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:9538259, ECO:0000269|Ref.13}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:9538259, ECO:0000269|Ref.13}; | 2-oxoglutarate metabolic process [GO:0006103]; acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; glycine catabolic process [GO:0006546]; hydrogen peroxide metabolic process [GO:0042743]; isoleucine catabolic process [GO:0006550]; L-serine biosynthetic process [GO:0006564]; leucine catabolic process [GO:000655... | glycine cleavage complex [GO:0005960]; mitochondrial nucleoid [GO:0042645]; mitochondrial oxoglutarate dehydrogenase complex [GO:0009353]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; oxoglutarate dehydrogenase complex [GO:0045252] | dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660]; glycine dehydrogenase (decarboxylating) activity [GO:0004375]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; pyruvate dehydrogenase activity [GO:0004738] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence={ECO... | null | null | null | null | FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and the 2-oxoglutarate dehydrogenase complex, which catalyzes the overall conversion of 2-oxogluta... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09626 | ATP4A_RAT | MGKENYELYSVELGTGPGGDMAAKMSKKKAGGGGGKKKEKLENMKKEMEMNDHQLSVSELEQKYQTSATKGLKASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLALALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILSAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTAQGLVVSTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFVVAM... | 7.2.2.19 | null | gastric acid secretion [GO:0001696]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; pH reduction [GO:0045851]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transmembrane transport [GO:0071805]; proton transmembrane transport [GO:190260... | apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]; potassium:proton exchanging ATPase complex [GO:0005889] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; P-type potassium:proton transporter activity [GO:0008900]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; potassium ion binding [GO:0030955] | PF13246;PF00689;PF00690;PF00122;PF09040;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P20648}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the apical canalicular membrane of parietal cells (By similarity). {ECO:0000250|UniProtKB:P20648}. | CATALYTIC ACTIVITY: Reaction=ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) + K(+)(in) + phosphate; Xref=Rhea:RHEA:22044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.19; Evidence={ECO:0000269|PubMed:20921224, ECO:0000269|PubMed:224482... | null | null | null | null | FUNCTION: The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells (PubMed:20921224, PubMed:22448261). Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into t... | Rattus norvegicus (Rat) |
P09627 | PMA1_SCHPO | MADNAGEYHDAEKHAPEQQAPPPQQPAHAAAPAQDDEPDDDIDALIEELFSEDVQEEQEDNDDAPAAGEAKAVPEELLQTDMNTGLTMSEVEERRKKYGLNQMKEELENPFLKFIMFFVGPIQFVMEMAAALAAGLRDWVDFGVICALLMLNAVVGFVQEYQAGSIVDELKKSLALKAVVIREGQVHELEANEVVPGDILKLDEGTIICADGRVVTPDVHLQVDQSAITGESLAVDKHYGDPTFASSGVKRGEGLMVVTATGDSTFVGRAASLVNAAAGGTGHFTEVLNGIGTILLVLVLLTLFCIYTAAFYRSVRLARL... | 7.1.2.1 | null | proton export across plasma membrane [GO:0120029]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453] | cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type proton-exporting transporter activity [GO:0008553]; proton binding [GO:1901691] | PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIIA subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate; Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1; Evidence={ECO:0000305|PubMed:2891694}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20853; Evidence... | null | null | null | null | FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. {ECO:0000305|PubMed:2891694}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P09629 | HXB7_HUMAN | MSSLYYANTLFSKYPASSSVFATGAFPEQTSCAFASNPQRPGYGAGSGASFAASMQGLYPGGGGMAGQSAAGVYAAGYGLEPSSFNMHCAPFEQNLSGVCPGDSAKAAGAKEQRDSDLAAESNFRIYPWMRSSGTDRKRGRQTYTRYQTLELEKEFHYNRYLTRRRRIEIAHTLCLTERQIKIWFQNRRMKWKKENKTAGPGTTGQDRAEAEEEEEE | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic organ development [GO:0048568]; embryonic skeletal system morphogenesis [GO:0048704]; myeloid cell differentiation [GO:0030099]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of transcription by ... | chromatin [GO:0000785]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-... | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P09631 | HXA9_MOUSE | MATTGALGNYYVDSFLLGADAADELGAGRYAPGTLGQPPRQAAALAEHPDFSPCSFQSKAAVFGASWNPVHAAGANAVPAAVYHHHHHPYVHPQAPVAAAAPDGRYMRSWLEPTPGALSFAGLPSSRPYGIKPEPLSARRGDCPTLDTHTLSLTDYACGSPPVDREKQPSEGAFSENNAENESGGDKPPIDPNNPAANWLHARSTRKKRCPYTKHQTLELEKEFLFNMYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKINKDRAKDE | null | null | anterior/posterior pattern specification [GO:0009952]; definitive hemopoiesis [GO:0060216]; DNA-templated transcription [GO:0006351]; embryonic forelimb morphogenesis [GO:0035115]; embryonic skeletal system development [GO:0048706]; embryonic skeletal system morphogenesis [GO:0048704]; endothelial cell activation [GO:0... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; enzyme binding [GO:0019899]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046;PF04617; | 1.10.10.60; | Abd-B homeobox family | PTM: Methylated on Arg-140 by PRMT5; methylation is critical for E-selectin induction. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P31269}. Cytoplasm {ECO:0000250|UniProtKB:P31269}. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of SELE/E-selectin and VCAM1 on the endothelial cell surface at sites of inflammation (By similarity). Positi... | Mus musculus (Mouse) |
P09632 | HXB8_MOUSE | MSSYFVNSLFSKYKTGESLRPNYYDCGFAQDLGGRPTVVYGPSSGGSFQHPSQIQEFYHGPSSLSTAPYQQNPCAVACHGDPGNFYGYDPLQRQSLFGAQDPDLVQYADCKLAAASGLGEEAEGSEQSPSPTQLFPWMRPQAAAGRRRGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKFPSSKCEQEELEKEKLERAPETAEQGDAQKGDKK | null | null | adult locomotory behavior [GO:0008344]; anterior/posterior pattern specification [GO:0009952]; dorsal spinal cord development [GO:0021516]; embryonic skeletal system morphogenesis [GO:0048704]; grooming behavior [GO:0007625]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of trans... | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Mus musculus (Mouse) |
P09651 | ROA1_HUMAN | MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNN... | null | null | cellular response to glucose starvation [GO:0042149]; cellular response to sodium arsenite [GO:1903936]; import into nucleus [GO:0051170]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; negative regulation of telomere maintenance via telomerase [GO:0032211]; nuclear export [GO:0051168]; posit... | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681] | DNA binding [GO:0003677]; G-rich strand telomeric DNA binding [GO:0098505]; identical protein binding [GO:0042802]; miRNA binding [GO:0035198]; mRNA 3'-UTR binding [GO:0003730]; pre-mRNA binding [GO:0036002]; protein domain specific binding [GO:0019904]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697... | PF11627;PF00076; | 3.30.70.330; | null | PTM: Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine.; PTM: Sumoylated. {ECO:0000269|PubMed:15161980}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27694260}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes (PubMed:... | null | null | null | null | null | FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection (PubMed:17371836). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inc... | Homo sapiens (Human) |
P09655 | ISK1_RAT | MKVAIIFLLSALALLSLAGNPPAEVNGKTPNCPKQIMGCPRIYDPVCGTNGITYPSECSLCFENRKFGTSIHIQRRGTC | null | null | cellular response to peptide hormone stimulus [GO:0071375]; negative regulation of calcium ion import [GO:0090281]; negative regulation of nitric oxide mediated signal transduction [GO:0010751]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; nitric oxide mediated signal transduction [GO:0007263]... | extracellular space [GO:0005615] | peptidase inhibitor activity [GO:0030414]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00050; | 3.30.60.30; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3597401}. | null | null | null | null | null | FUNCTION: Serine protease inhibitor which exhibits anti-trypsin activity (PubMed:3202973, PubMed:3597401). In the pancreas, protects against trypsin-catalyzed premature activation of zymogens (By similarity). {ECO:0000250|UniProtKB:P09036, ECO:0000269|PubMed:3202973, ECO:0000269|PubMed:3597401}.; FUNCTION: In the male ... | Rattus norvegicus (Rat) |
P09660 | ACHE_RAT | MTMALLGTLLLLALFGRSQGKNEELSLYHHLFDNYDPECRPVRRPEDTVTITLKVTLTNLISLNEKEETLTTSVWIGIEWQDYRLNFSKDDFAGVEILRVPSEHVWLPEIVLENNIDGQFGVAYDCNVLVYEGGSVSWLPPAIYRSTCAVEVTYFPFDWQNCSLIFRSQTYNAEEVELIFAVDDDGNAINKIDIDTAAFTENGEWAIDYCPGMIRHYEGGSTEDPGETDVIYTLIIRRKPLFYVINIIVPCVLISGLVLLAYFLPAQAGGQKCTVSINVLLAQTVFLFLIAQKIPETSLSVPLLGRYLIFVMVVATLIVM... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; regulation of membrane potential [GO:0042391]; skeletal muscle contraction [GO:0003009] | acetylcholine-gated channel complex [GO:0005892]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202] | acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Epsilon/CHRNE sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P02715}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P02715}; | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. | Rattus norvegicus (Rat) |
P09661 | RU2A_HUMAN | MVKLTAELIEQAAQYTNAVRDRELDLRGYKIPVIENLGATLDQFDAIDFSDNEIRKLDGFPLLRRLKTLLVNNNRICRIGEGLDQALPCLTELILTNNSLVELGDLDPLASLKSLTYLSILRNPVTNKKHYRLYVIYKVPQVRVLDFQKVKLKERQEAEKMFKGKRGAQLAKDIARRSKTFNPGAGLPTDKKKGGPSPGDVEAIKNAIANASTLAEVERLKGLLQSGQIPGRERRSGPTDDGEEEMEEDTVTNGS | null | null | mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; spermatogenesis [GO:0007283]; U2-type prespliceosome assembly [GO:1903241] | catalytic step 2 spliceosome [GO:0071013]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; small nuclear ribonucleoprotein complex [GO:0030532]; spliceosomal complex [GO:0005681]; U2 snRNP [GO:0005686]; U2-type catalytic step 2 spliceosome [GO:0071007]; U2-type pre... | RNA binding [GO:0003723]; U2 snRNA binding [GO:0030620] | PF14580; | 3.80.10.10; | U2 small nuclear ribonucleoprotein A family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. | null | null | null | null | null | FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:27035939, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA (PubMed:27035939, PubMed:32494006, PubMed:9716128). {... | Homo sapiens (Human) |
P09668 | CATH_HUMAN | MWATLPLLCAGAWLLGVPVCGAAELCVNSLEKFHFKSWMSKHRKTYSTEEYHHRLQTFASNWRKINAHNNGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPPSVDWRKKGNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKN... | 3.4.22.16 | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; bradykinin catabolic process [GO:0010815]; cellular response to thyroid hormone stimulus [GO:0097067]; dichotomous subdivision of terminal units involved in lung branching [GO:0060448]; ERK1 and ERK2 cascade [GO:0070371]; immune re... | alveolar lamellar body [GO:0097208]; collagen-containing extracellular matrix [GO:0062023]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; intrac... | aminopeptidase activity [GO:0004177]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; HLA-A specific activating MHC class I receptor activity ... | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16; | null | null | null | null | FUNCTION: Important for the overall degradation of proteins in lysosomes. | Homo sapiens (Human) |
P09669 | COX6C_HUMAN | MAPEVLPKPRMRGLLARRLRNHMAVAFVLSLGVAALYKFRVADQRKKAYADFYRNYDVMKDFEEMRKAGIFQSVK | null | null | cellular respiration [GO:0045333]; generation of precursor metabolites and energy [GO:0006091]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | null | PF02937; | 4.10.93.10; | Cytochrome c oxidase subunit 6c family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P04038}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Homo sapiens (Human) |
P09670 | SODC_SHEEP | MATKAVCVLKGDGPVQGTIRFEAKGDKVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVKADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGGRLACGVIGIAP | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | action potential initiation [GO:0099610]; anterograde axonal transport [GO:0008089]; apoptotic process [GO:0006915]; auditory receptor cell stereocilium organization [GO:0060088]; determination of adult lifespan [GO:0008340]; ectopic germ cell programmed cell death [GO:0035234]; embryo implantation [GO:0007566]; gene e... | axon cytoplasm [GO:1904115]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]; protein-containing complex... | copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; protein phosphatase 2B binding [GO:0030346]; protein-folding chaperone binding [GO:0051087]; small GTPase binding [GO:0031267]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity. {ECO:0000250}.; PTM: Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity. {ECO:0000250|UniProtKB:P00441}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Ovis aries (Sheep) |
P09671 | SODM_MOUSE | MLCRAACSTGRRLGPVAGAAGSRHKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNATEEKYHEALAKGDVTTQVALQPALKFNGGGHINHTIFWTNLSPKGGGEPKGELLEAIKRDFGSFEKFKEKLTAVSVGVQGSGWGWLGFNKEQGRLQIAACSNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYTACKK | 1.15.1.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P04179}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P04179}; | acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure [GO:0003069]; apoptotic mitochondrial changes [GO:0008637]; cellular response to ethanol [GO:0071361]; cellular response to oxidative stress [GO:0034599]; detection of oxygen [GO:0003032]; erythrophore differentiation [GO:004... | mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209] | DNA binding [GO:0003677]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145]; oxidoreductase activity [GO:0016491]; oxygen binding [GO:0019825]; superoxide dismutase activity [GO:0004784] | PF02777;PF00081; | 1.10.287.990;3.55.40.20; | Iron/manganese superoxide dismutase family | PTM: Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity (By similarity). {ECO:0000250|UniProtKB:P04179}.; PTM: Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting. {ECO:0000269|PubMed:2117265... | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | Mus musculus (Mouse) |
P09678 | SODC_BRAOC | MAKGVAVLNSSEGVKGTIFFTHEGNGATTVTGTVSGLRPGLHGFHVHALGDNTNGCMSTGPHFNPDGKTHGAPEDANRHAGDLGNIIVGDDGTATFTITDSQIPLSGPNSIVGRAIVVHADPDDLGKGGHELSLSTGNAGGRVACGIIGLQG | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Note=Binds 1 copper ion per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | null | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Brassica oleracea var. capitata (Cabbage) |
P09681 | GIP_HUMAN | MVATKTFALLLLSLFLAVGLGEKKEGHFSALPSLPVGSHAKVSSPQPRGPRYAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQREARALELASQANRKEEEAVEPQSSPAKNPSDEDLLRDLLIQELLACLLDQTNLCRLRSR | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adult locomotory behavior [GO:0008344]; digestive system development [GO:0055123]; endocrine pancreas development [GO:0031018]; exploration behavior [GO:0035640]; female pregnancy [GO:0007565]; gastric inhibitory peptide signaling p... | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; secretory granule lumen [GO:0034774] | gastric inhibitory polypeptide receptor binding [GO:0031767]; glucagon receptor binding [GO:0031769]; hormone activity [GO:0005179] | PF00123; | 6.10.250.590; | Glucagon family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion. | Homo sapiens (Human) |
P09683 | SECR_HUMAN | MAPRPLLLLLLLLGGSAARPAPPRARRHSDGTFTSELSRLREGARLQRLLQGLVGKRSEQDAENSMAWTRLSAGLLCPSGSNMPILQAWMPLDGTWSPWLPPGPMVSEPAGAAAEGTLRPR | null | null | brain development [GO:0007420]; diet induced thermogenesis [GO:0002024]; embryonic digestive tract development [GO:0048566]; hippocampus development [GO:0021766]; intracellular water homeostasis [GO:0009992]; negative regulation of gastrin-induced gastric acid secretion [GO:1903640]; pancreatic juice secretion [GO:0030... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | digestive hormone activity [GO:0046659]; G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]; signaling receptor binding [GO:0005102] | PF00123; | null | Glucagon family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}. | null | null | null | null | null | FUNCTION: Hormone involved in different processes, such as regulation of the pH of the duodenal content, food intake and water homeostasis (PubMed:25332973). Exerts its biological effects by binding to secretin receptor (SCTR), a G-protein coupled receptor expressed in the basolateral domain of several cells (PubMed:25... | Homo sapiens (Human) |
P09690 | ACHB_MOUSE | MALGALLLLLGVLGTPLAPGARGSEAEGQLIKKLFSNYDSSVRPAREVGDRVGVSIGLTLAQLISLNEKDEEMSTKVYLDLEWTDYRLSWDPAEHDGIDSLRITAESVWLPDVVLLNNNDGNFDVALDINVVVSFEGSVRWQPPGLYRSSCSIQVTYFPFDWQNCTMVFSSYSYDSSEVSLKTGLDPEGEERQEVYIHEGTFIENGQWEIIHKPSRLIQLPGDQRGGKEGHHEEVIFYLIIRRKPLFYLVNVIAPCILITLLAIFVFYLPPDAGEKMGLSIFALLTLTVFLLLLADKVPETSLAVPIIIKYLMFTMVLVT... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; behavioral response to nicotine [GO:0035095]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; muscle cell development [GO:0055001]; neuromuscular synaptic transmission [GO:0007274]; postsynaptic membrane organization [GO:0001941]; re... | acetylcholine-gated channel complex [GO:0005892]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202] | acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; ligand-gated monoatomic ion channel activity [GO:0015276] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Beta-1/CHRNB1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P04758}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P04758}; | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. | Mus musculus (Mouse) |
P09693 | CD3G_HUMAN | MEQGKGLAVLILAIILLQGTLAQSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKSKPLQVYYRMCQNCIELNAATISGFLFAEIVSIFVLAVGVYFIAGQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLRRN | null | null | adaptive immune response [GO:0002250]; alpha-beta T cell activation [GO:0046631]; cell surface receptor signaling pathway [GO:0007166]; establishment or maintenance of cell polarity [GO:0007163]; gamma-delta T cell activation [GO:0046629]; positive thymic T cell selection [GO:0045059]; protein transport [GO:0015031]; p... | alpha-beta T cell receptor complex [GO:0042105]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; gamma-delta T cell receptor complex [GO:0042106]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; signaling receptor complex adaptor activity [GO:0030159]; T cell receptor binding [GO:0042608]; transmembrane signaling receptor activity [GO:0004888] | PF16680;PF02189; | 2.60.40.10; | null | PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8 (PubMed:2470098). Phosphorylated also by PKC; leading to the TCR complex down-regulation (PubMed:8187769). {ECO:0000269|PubMed:2470098, ECO:0000269|PubMed:8187769}.; PTM: Phosphorylated on Tyr residues after T-cell r... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8636209}; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 cha... | Homo sapiens (Human) |
P09695 | TRS1_HCMVA | MAQRNGMSPRPPPLGRGRGAGGPSGVGSSPPSSCVPMGAPSTAGTGASAAATTTPGHGVHRVEPRGPPGAPPSSGNNSNFWHGPERLLLSQIPVERQALTELEYQAMGAVWRAAFLANSTGRAMRKWSQRDAGTLLPLGRPYGFYARVTPRSQMNGVGATDLRQLSPRDAWIVLVATVVHEVDPAADPTLGDKAGHPEGLCAQDGLYLALGAGFRVFVYDLANNTLILAARDADEWFRHGAGEVVRLYRCNRLGVGTPRATLLPQPALRQTLLRAEEATALGRELRRRWAGTTVALQTPGRRLQPMVLLGAWQELAQYEP... | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host PKR/eIFalpha signaling [GO:0039580]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | protein serine/threonine kinase inhibitor activity [GO:0030291] | PF02393; | null | Herpesviridae US22 family | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8995674}. Host cytoplasm {ECO:0000269|PubMed:8995674}. Host nucleus {ECO:0000269|PubMed:8995674}. | null | null | null | null | null | FUNCTION: Inhibits the establishment of the antiviral state and the integrated stress response (ISR) in the infected cell. Prevents the phosphorylation of the host eukaryotic translation initiation factor eIF-2alpha/EIF2S1 and thus the shutoff of viral and cellular protein synthesis by directly interacting with EIF2AK2... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P09727 | US11_HCMVA | MNLVMLILALWAPVAGSMPELSLTLFDEPPPLVETEPLPPLSDVSEYRVEYSEARCVLRSGGRLEALWTLRGNLSVPTPTPRVYYQTLEGYADRVPTPVEDVSESLVAKRYWLRDYRVPQRTKLVLFYFSPCHQCQTYYVECEPRCLVPWVPLWSSLEDIERLLFEDRRLMAYYALTIKSAQYTLMMVAVIQVFWGLYVKGWLHRHFPWMFSDQW | null | null | symbiont-mediated suppression of host antigen processing and presentation [GO:0039588]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; virus-mediated perturbation of host defense response [GO:0019049] | host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020] | null | PF08001; | null | Cytomegalovirus US6 family | PTM: N-glycosylated. {ECO:0000269|PubMed:11285222}.; PTM: A fraction of newly synthesized molecules retain the signal peptide after the N-linked glycan has been attached and translation of the polypeptide has been completed. Delayed cleavage of the signal peptide is determined by the first four residues, as well as by ... | SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:8625414, ECO:0000269|PubMed:8855296}; Single-pass type I membrane protein {ECO:0000269|PubMed:8625414, ECO:0000269|PubMed:8855296}. | null | null | null | null | null | FUNCTION: Participates in the inhibition of the host immune response. Redirects newly synthesized major histocompatibility complex (MHC) class I heavy chains via the SEC61 translocon to the cytosol where they undergo proteasome-dependent destruction. In consequence, infected cells are masked for immune recognition by c... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P09732 | POLG_STEVM | MSKKPGKPGRNRVVNMLKRGVSRVNPLTGLKRILGSLLDGRGPVRFILAILTFFRFTALQPTEALKRRWRAVDKRTALKHLNGFKRDLGSMLDTINRRPSKKRGGTRSLLGLAALIGLASSLQLSTYQGKVLMSINKTDAQSAINIPSANGANTCIVRALDVGVMCKNDITYLCPVLSAGNDPEDIDCWCDVEEVWVHYGRCTRMGHSRRSRRSISVQHHGDSTLATKNTPWLDTVKTTKYLTKVENWVLRNPGYALVALAIGWMLGSNNTQRVVFVIMLMLIAPAYSFNCLGTSNRDFVEGASGATWIDLVLEGGSCVT... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA he... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | St. louis encephalitis virus (strain MS1-7) |
P09733 | TBA1_YEAST | MREVISINVGQAGCQIGNACWELYSLEHGIKPDGHLEDGLSKPKGGEEGFSTFFHETGYGKFVPRAIYVDLEPNVIDEVRNGPYKDLFHPEQLISGKEDAANNYARGHYTVGREILGDVLDRIRKLADQCDGLQGFLFTHSLGGGTGSGLGSLLLEELSAEYGKKSKLEFAVYPAPQVSTSVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDMCKRNLDIPRPSFANLNNLIAQVVSSVTASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYSPVLSKSKAFHESNSVSEITNACFEPGNQMVKCDPRDGKYMATCLLY... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | homologous chromosome segregation [GO:0045143]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid segregation [GO:0000070]; nuclear division [GO:0000280]; nuclear migration along microtubule [GO:0030473]; nuclear migration by microtubule mediated pushing force... | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nuclear periphery [GO:0034399]; nucleus [GO:0005634]; spindle [GO:0005819]; tubulin complex [GO:0045298] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11739794}. | 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 (PubMed:11739794). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09734 | TBA3_YEAST | MREVISINVGQAGCQIGNACWELYSLEHGIKEDGHLEDGLSKPKGGEEGFSTFFHETGYGKFVPRAIYVDLEPNVIDEVRTGRFKELFHPEQLINGKEDAANNYARGHYTVGREIVDEVEERIRKMADQCDGLQGFLFTHSLGGGTGSGLGSLLLENLSYEYGKKSKLEFAVYPAPQLSTSVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDICKRNLGISRPSFSNLNGLIAQVISSVTASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYAPILSKKRATHESNSVSEITNACFEPGNQMVKCDPTKGKYMANCLLY... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | homologous chromosome segregation [GO:0045143]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid segregation [GO:0000070]; nuclear division [GO:0000280]; nuclear migration along microtubule [GO:0030473]; nuclear migration by microtubule mediated pushing force... | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; spindle [GO:0005819]; tubulin complex [GO:0045298] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09739 | TNNT3_RAT | MSDEETEQVEEQYEEEEEAQEEEVQEEAPEPEEVQEEEKPRPKLTAPKIPEGEKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELIALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEDDLKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDDKLRDKAKELWDTLYQLETDKFEFGEKLKRQKYDITTLRSRIDQAQKHSKKAGATAKGKVGGRWK | null | null | muscle contraction [GO:0006936]; regulation of striated muscle contraction [GO:0006942]; sarcomere organization [GO:0045214]; skeletal muscle contraction [GO:0003009] | troponin complex [GO:0005861] | calcium-dependent protein binding [GO:0048306]; tropomyosin binding [GO:0005523]; troponin C binding [GO:0030172]; troponin I binding [GO:0031013]; troponin T binding [GO:0031014] | PF00992; | 1.20.5.350; | Troponin T family | null | null | null | null | null | null | null | FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. {ECO:0000269|PubMed:16839517}. | Rattus norvegicus (Rat) |
P09741 | TNNT2_RABIT | MSDLEEVVEEYEEEQEAEEAAAEEEDWREDEDEQEAGEEEEAGGGREAEAETEETQAEEDGQEEEDKEDEDGPVEESKPKPRPFMPNLVPPKIPDGERVDFDDIHRKRMEKDLNELQTLIEAHFENRKKEEEELVSLKDRIEKRRADAEQLRIRAEREKERQNRLAEERARREEEESRRKAEDEARKKKALSNMMHFGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSIYNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK | null | null | cardiac muscle contraction [GO:0060048]; muscle filament sliding [GO:0030049]; negative regulation of ATP-dependent activity [GO:0032780]; positive regulation of ATP-dependent activity [GO:0032781]; regulation of heart contraction [GO:0008016]; regulation of muscle contraction [GO:0006937]; response to calcium ion [GO:... | striated muscle thin filament [GO:0005865]; troponin complex [GO:0005861] | actin binding [GO:0003779]; tropomyosin binding [GO:0005523]; troponin C binding [GO:0030172]; troponin I binding [GO:0031013] | PF00992; | 1.20.5.350; | Troponin T family | PTM: Phosphorylation at Thr-216 by PRKCA induces significant reduction in myofilament calcium sensitivity and actomyosin ATPase activity. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. | Oryctolagus cuniculus (Rabbit) |
P09758 | TACD2_HUMAN | MARGPGLAPPPLRLPLLLLVLAAVTGHTAAQDNCTCPTNKMTVCSPDGPGGRCQCRALGSGMAVDCSTLTSKCLLLKARMSAPKNARTLVRPSEHALVDNDGLYDPDCDPEGRFKARQCNQTSVCWCVNSVGVRRTDKGDLSLRCDELVRTHHILIDLRHRPTAGAFNHSDLDAELRRLFRERYRLHPKFVAAVHYEQPTIQIELRQNTSQKAAGDVDIGDAAYYFERDIKGESLFQGRGGLDLRVRGEPLQVERTLIYYLDEIPPKFSMKRLTAGLIAVIVVVVVALVAGMAVLVITNRRKSGKYKKVEIKELGELRKE... | null | null | negative regulation of branching involved in ureteric bud morphogenesis [GO:0090191]; negative regulation of cell motility [GO:2000146]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of ruffle assembly [GO:1900028]; negative regulation of stress fiber assembly [GO:0051497]; negative... | basal plasma membrane [GO:0009925]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; nucleus [GO:0005634] | null | PF21283;PF18635;PF00086; | 4.10.800.10; | EPCAM family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: May function as a growth factor receptor. | Homo sapiens (Human) |
P09759 | EPHB1_RAT | MALDCLLLFLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKAGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPSEASPICTCRTGYYRADFDPPEVACT... | 2.7.10.1 | null | angiogenesis [GO:0001525]; axon guidance [GO:0007411]; camera-type eye morphogenesis [GO:0048593]; cell chemotaxis [GO:0060326]; cell-substrate adhesion [GO:0031589]; central nervous system projection neuron axonogenesis [GO:0021952]; cranial nerve development [GO:0021545]; dendritic spine development [GO:0060996]; den... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; filopodium tip [GO:0032433]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; axon guidance receptor activity [GO:0008046]; protein tyrosine kinase activity [GO:0004713]; protein-containing complex binding [GO:0044877]; transmembrane-ephrin receptor activity [GO:0005005] | PF14575;PF01404;PF00041;PF07714;PF00536; | 2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | PTM: Phosphorylated. Autophosphorylation is stimulated by the ligand EFNB1. Required for interaction with SH2 domain-containing interactors, for activation of the MAPK/ERK and JUN signaling cascades and for ubiquitination by CBL (By similarity). {ECO:0000250|UniProtKB:P54762}.; PTM: Ubiquitinated; (EFNB1)ligand-induced... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54762}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54762}. Early endosome membrane {ECO:0000250|UniProtKB:P54762}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8CBF3}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway dow... | Rattus norvegicus (Rat) |
P09760 | FER_RAT | MGFGSDLKNSQEAVLKLQDWELRLLETVKKFMALRIKSDKEYAYTLQNLCNQVDKDSTVQVNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYVGIHQQIEAEMIKVTKTELEKLKSSYRQLIKEMNSAKEKYKEALAKGKETEKAKERCDKATMKLHMLHNQYVLALKGAQLHQSQYYDTTLPLLLDSVQKMQEEMIKALKGIFDEYSEITSLVTEEIVNVHKEIQMSVDQIDPSTEYNDFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTADSLQVMLKTLAEELTQTQ... | 2.7.10.2 | null | actin cytoskeleton organization [GO:0030036]; adherens junction assembly [GO:0034333]; adherens junction disassembly [GO:0120179]; cell adhesion [GO:0007155]; cell-cell adhesion mediated by cadherin [GO:0044331]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; cellular response to react... | actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; cell cortex [GO:0005938]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; protein-containing c... | ATP binding [GO:0005524]; epidermal growth factor receptor binding [GO:0005154]; lipid binding [GO:0008289]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase activity [GO:0004672]; protein phosphatase 1 binding [GO:0008157]; protein tyrosine kinase activity [GO:0004713] | PF00611;PF07714;PF00017; | 1.20.1270.60;1.10.287.160;3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily | PTM: Autophosphorylated. {ECO:0000250}.; PTM: Polyubiquitinated; this leads to proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}. Cell junction {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cyt... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream o... | Rattus norvegicus (Rat) |
P09769 | FGR_HUMAN | MGCVFCKKLEPVATAKEDAGLEGDFRSYGAADHYGPDPTKARPASSFAHIPNYSNFSSQAINPGFLDSGTIRGVSGIGVTLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSLSSGKTGCIPSNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGAYSLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEVNDGLCNLLIAPCTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWLGTWNGSTKVAVKTLKPGTMSPKAFLEEAQVMKLLRHDKLVQ... | 2.7.10.2 | null | bone mineralization [GO:0030282]; cell differentiation [GO:0030154]; defense response to Gram-positive bacterium [GO:0050830]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; immune response-regulating cell surface receptor signaling pathway [GO:0002768]; innate immune response [GO:0045087]; ... | actin cytoskeleton [GO:0015629]; aggresome [GO:0016235]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; plasma... | ATP binding [GO:0005524]; Fc-gamma receptor I complex binding [GO:0034988]; immunoglobulin receptor binding [GO:0034987]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713];... | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation. {ECO:0000269|PubMed:12435267}.; PTM: Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2A and/or FCGR2B engagement, cell adhesion and signaling by ITGB2. Prior ph... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane. Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Mitochondrion inner membrane {ECO:0000250}. Mitochondrion intermembr... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosi... | Homo sapiens (Human) |
P09774 | AST3_DROME | MTSICSSKFQQQHYQLTNSNIFLLQHQHHHQTQQHQLIAPKIPLGTSQLQNMQQSQQSNVGPMLSSQKKKFNYNNMPYGEQLPSVARRNARERNRVKQVNNGFVNLRQHLPQTVVNSLSNGGRGSSKKLSKVDTLRIAVEYIRGLQDMLDDGTASSTRHIYNSADESSNDGSSYNDYNDSLDSSQQFLTGATQSAQSHSYHSASPTPSYSGSEISGGGYIKQELQEQDLKFDSFDSFSDEQPDDEELLDYISSWQEQ | null | null | central nervous system development [GO:0007417]; epithelial cell proliferation involved in Malpighian tubule morphogenesis [GO:0061331]; Malpighian tubule tip cell differentiation [GO:0061382]; neuroblast fate determination [GO:0007400]; neuron differentiation [GO:0030182]; peripheral nervous system development [GO:000... | RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00010; | 4.10.280.10; | null | null | null | null | null | null | null | null | FUNCTION: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system. | Drosophila melanogaster (Fruit fly) |
P09775 | AST8_DROME | MAALSFSPSPPPKENPKENPNPGIKTTLKPFGKITVHNVLSESGANALQQHIANQNTIIRKIRDFGMLGAVQSAAASTTNTTPISSQRKRPLGESQKQNRHNQQNQQLSKTSVPAKKCKTNKKLAVERPPKAGTISHPHKSQSDQSFGTPGRKGLPLPQAVARRNARERNRVKQVNNGFALLREKIPEEVSEAFEAQGAGRGASKKLSKVETLRMAVEYIRSLEKLLGFDFPPLNSQGNSSGSGDDSFMFIKDEFDCLDEHFDDSLSNYEMDEQQTVQQTLSEDMLNPPQASDLLPSLTTLNGLQYIRIPGTNTYQLLTT... | null | null | central nervous system development [GO:0007417]; chaeta development [GO:0022416]; chaeta morphogenesis [GO:0008407]; epithelial cell proliferation involved in Malpighian tubule morphogenesis [GO:0061331]; Malpighian tubule tip cell differentiation [GO:0061382]; negative regulation of mitotic nuclear division [GO:004583... | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00010; | 4.10.280.10; | null | null | null | null | null | null | null | null | FUNCTION: Involved in the determination of the neuronal precursors of optic lobes in the central nervous system. | Drosophila melanogaster (Fruit fly) |
P09785 | PHNA_PSEAE | MGARRWLVSGVGYRLEESLEYRTLVPEALSIWRMAGANRMLFDCFDVDSKAARRSVAILSSCLRIECWGRDVVLRALNSNGRALLAPLSEDCPAQVTCLRDGDTLHWRFPQEESHADEWRRLHGLSSLEALRRVLGTLGDAEGPVLLGGLFSFDLAEQFEPLPAPAEPARHCPDYLFLVPELLLDIDHLARRTSLQAFVHDPAGHDRLAASLRQCADEFHGAVEEASESPVAGVRAGNYQVDLDDASFARQVERLQAHVRAGDVFQIVPSRSFSMPCADPWRAYRQLCLRNPSPYRFFLDAGDFCLFGASPESALKYDAE... | 4.1.3.27 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00897}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897}; | phenazine biosynthetic process [GO:0002047]; tryptophan biosynthetic process [GO:0000162] | null | anthranilate synthase activity [GO:0004049]; metal ion binding [GO:0046872] | PF04715;PF00425; | 3.60.120.10; | Anthranilate synthase component I family | null | null | CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; Evidence={ECO:0000305|PubMed:2153661}; | null | PATHWAY: Secondary metabolite biosynthesis; pyocyanine biosynthesis. {ECO:0000305|PubMed:2153661}. | null | null | FUNCTION: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, a precursor for Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which is required to induce the genes for the biosynthesis of the virulence factor pyocyanine (PCN), a characteristic blue-... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P09786 | PHNB_PSEAE | MRITLLDNFDSFTYNLVEQFCLLGAEVRVMRNDTPLPTIQAALLADGCELLVLSPGPGRPEDAGCMLELLAWARGRLPVLGVCLGHQALALAAGGAVGEARKPLHGKSTSLRFDQRHPLFDGIADLRVARYHSLVVSRLPEGFDCLADADGEIMAMADPRNRQLGLQFHPESILTTHGQRLLENALLWCGALAVRERLRA | 4.1.3.27 | null | glutamine metabolic process [GO:0006541]; phenazine biosynthetic process [GO:0002047]; tryptophan biosynthetic process [GO:0000162] | cytosol [GO:0005829] | anthranilate phosphoribosyltransferase activity [GO:0004048]; anthranilate synthase activity [GO:0004049] | PF00117; | 3.40.50.880; | null | null | null | CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; Evidence={ECO:0000305|PubMed:2153661}; | null | PATHWAY: Secondary metabolite biosynthesis; pyocyanine biosynthesis. {ECO:0000305|PubMed:2153661}. | null | null | FUNCTION: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, a precursor for Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which is required to induce the genes for the biosynthesis of the virulence factor pyocyanine (PCN), a characteristic blue-... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P09792 | GST28_SCHMA | MAGEHIKVIYFDGRGRAESIRMTLVAAGVDYEDERISFQDWPKIKPTIPGGRLPAVKVTDDHGHVKWMLESLAIARYMAKKHHMMGETDEEYYSVEKLIGQAEDVEHEYHKTLMKPQEEKEKITKEILNGKVPVLLNMICESLKGSTGKLAVGDKVTLADLVLIAVIDHVTDLDKGFLTGKYPEIHKHRENLLASSPRLAKYLSNRPATPF | 2.5.1.18 | null | glutathione metabolic process [GO:0006749] | null | glutathione transferase activity [GO:0004364] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Mu family | null | null | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.; FUNCTION: GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite... | Schistosoma mansoni (Blood fluke) |
P09793 | CTLA4_MOUSE | MACLGLRRYKAQLQLPSRTWPFVALLTLLFIPVFSEAIQVTQPSVVLASSHGVASFPCEYSPSHNTDEVRVTVLRQTNDQMTEVCATTFTEKNTVGFLDYPFCSGTFNESRVNLTIQGLRAVDTGLYLCKVELMYPPPYFVGMGNGTQIYVIDPEPCPDSDFLLWILVAVSLGLFFYSFLVSAVSLSKMLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN | null | null | adaptive immune response [GO:0002250]; B cell receptor signaling pathway [GO:0050853]; negative regulation of regulatory T cell differentiation [GO:0045590]; negative regulation of T cell proliferation [GO:0042130]; T cell receptor signaling pathway [GO:0050852] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; protein complex involved in cell adhesion [GO:0098636] | null | PF07686; | 2.60.40.10; | null | PTM: N-glycosylation is important for dimerization. {ECO:0000250|UniProtKB:P16410}.; PTM: Phosphorylation at Tyr-201 prevents binding to the AP-2 adapter complex, blocks endocytosis, and leads to retention of CTLA4 on the cell surface. {ECO:0000250|UniProtKB:P16410}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16410}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16410}. Note=Exists primarily an intracellular antigen whose surface expression is tightly regulated by restricted trafficking to the cell surface and rapid internalization. {ECO:0000250|UniPr... | null | null | null | null | null | FUNCTION: Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28. {ECO:0000250|UniProtKB:P16410}. | Mus musculus (Mouse) |
P09798 | CDC16_YEAST | MKFCLYCCHCYIVICGKATHYYKSSKATSNLKSSNRVLMRNPMSPSEQHSQHNSTLAASPFVSNVSAARTQQSLPTDAQNDRLQQPWNRTNTATSPYQSLANSPLIQKLQANIMTPHQPSANSNSNSNSITGNVVNDNNLLASMSKNSMFGSTIPSTLRKVSLQREYKDSVDGVVRDEDNDEDVHNNGDAAANANNDRESKLGHNGPLTTTTLTTTTTATQLDVSELSAIERLRLWRFDALMQHMYRTAEYIADKVYNISNDPDDAFWLGQVYYNNNQYVRAVELITRNNLDGVNILCRYLLGLSFVKLQRFDDALDVIG... | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell cycle [GO:0007049]; cell division [GO:0051301]; negative regulation of DNA-templated DNA replication initiation [GO:0032297]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein ubiquitination [GO:0016567]; regulati... | anaphase-promoting complex [GO:0005680]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | null | PF12895;PF13424;PF07719;PF13181; | 1.25.40.10; | APC6/CDC16 family | PTM: Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form. {ECO:0000269|PubMed:10871279}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes,... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09803 | CADH1_MOUSE | MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFT... | null | null | actin cytoskeleton organization [GO:0030036]; adherens junction organization [GO:0034332]; bicellular tight junction assembly [GO:0070830]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; canonical Wnt signaling pathway [GO:0060070]; cell morphogenesis [GO:0000902]; cell-c... | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical part of cell [GO:0045177]; axon [GO:0030424]; axon terminus [GO:0043679]; basolateral plasma membrane [GO:0016323]; catenin complex [GO:0016342]; cell periphery [GO:0071944]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplas... | alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; protein domain specific binding [GO:0019904]; protein phosph... | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (By similarity). Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm (... | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:30639848}. Cell membrane {ECO:0000269|PubMed:27760340}; Single-pass type I membrane protein. Endosome {ECO:0000250|UniProtKB:P12830}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P12830}. Cytoplasm {ECO:0000269|PubMed:27760340}. C... | null | null | null | null | null | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility a... | Mus musculus (Mouse) |
P09809 | APOA1_RABIT | MKAVVLTLAVLFLTGSQARHFWQRDEPRSSWDKIKDFATVYVDTVKDSGREYVAQFEASAFGKQLNLKLLDNWDSLSSTVSKLQEQLGPVTQEFWDNLEKETEGLREEMNKDLQEVRQKVQPYLDEFQKKWQEEVERYRQKVEPLGAELRESARQKLTELQEKLSPLAEELRDSARTHVDTLRTKLAPYSNELQQRLAARLESIKEGGGASLAEYQAKAREHLSVLSEKARPALEDLRQGLLPVLESFKASVQNVLDEATKKLNTQ | null | null | cholesterol metabolic process [GO:0008203]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; peptidyl-methionine modification [GO:0018206]; phosphatidylcholine metabolic process [GO:0046470]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of phagocytosis [GO:0050766... | high-density lipoprotein particle [GO:0034364] | amyloid-beta binding [GO:0001540]; high-density lipoprotein particle receptor binding [GO:0070653]; lipid binding [GO:0008289]; peptide binding [GO:0042277]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. | Oryctolagus cuniculus (Rabbit) |
P09810 | TPH1_RAT | MIEDNKENKDHSSERGRVTLIFSLKNEVGGLIKALKIFQENHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFPLLKSHTTVLSVDSPDQLPEKEDVMETVPWFPKKISDLDFCANRVLLYGSELDADHPGFKDNVYRRRRKYFAELAMNYKHGDPIPKIEFTEEEIKTWGTIFRELNKLYPTHACREYLRNLPLLSKYCGYREDNVPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPLYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEETVQKLATCYFFTVEFGL... | 1.14.16.4 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P17752}; | bone remodeling [GO:0046849]; circadian rhythm [GO:0007623]; mammary gland alveolus development [GO:0060749]; negative regulation of ossification [GO:0030279]; platelet degranulation [GO:0002576]; positive regulation of fat cell differentiation [GO:0045600]; regulation of hemostasis [GO:1900046]; response to immobiliza... | cytoplasm [GO:0005737]; neuron projection [GO:0043005] | iron ion binding [GO:0005506]; tryptophan 5-monooxygenase activity [GO:0004510] | PF01842;PF00351; | 1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitinated is triggered by phosphorylation. {ECO:0000269|PubMed:12354109}.; PTM: Phosphorylated; triggering degradation by the proteasome. {ECO:0000269|PubMed:12354109}. | null | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-hydroxy-L-tryptophan; Xref=Rhea:RHEA:16709, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57912, ChEBI:CHEBI:58266, ChEBI:CHEBI:59560; EC=1.14.16.4; Evidence={E... | null | PATHWAY: Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2. {ECO:0000269|PubMed:12354109}. | null | null | FUNCTION: Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis. {ECO:0000269|PubMed:12354109}. | Rattus norvegicus (Rat) |
P09811 | PYGL_RAT | MAKPLTDQEKRRQISIRGIVGVENVAELKKGFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIREGWQVEEADDWLRHGNPWEKARPEFMLPVHFYGRVEHTQAGTKWVDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLQDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDVIRRFKASKFGSK... | 2.4.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P06737}; | 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; glucose homeostasis [GO:0042593]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; necroptotic process [GO:0070266]; response to bacterium [GO:0009617] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | AMP binding [GO:0016208]; ATP binding [GO:0005524]; bile acid binding [GO:0032052]; carbohydrate binding [GO:0030246]; glucose binding [GO:0005536]; glycogen phosphorylase activity [GO:0008184]; identical protein binding [GO:0042802]; linear malto-oligosaccharide phosphorylase activity [GO:0102250]; purine nucleobase b... | PF00343; | 3.40.50.2000; | Glycogen phosphorylase family | PTM: Acetylation, which is up-regulated by glucose and insulin and down-regulated by glucagon, inhibits the glycogen phosphorylase activity by promoting PPP1R3B-mediated recruitment of phosphatase PP1 and Ser-15 dephosphorylation. {ECO:0000250|UniProtKB:P06737}.; PTM: Phosphorylation at Ser-15 converts inactive phospho... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P06737}. | 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:0000250|UniProtKB:P06737}; Physiologica... | null | null | null | null | FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. {ECO:0000250|UniProtKB:P06737}. | Rattus norvegicus (Rat) |
P09812 | PYGM_RAT | MSRPLSDQDKRKQISVRGLAGVENVSDLKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVDRWIRTQQHYYAKDPKRIYYLSLELYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPPYFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDKFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCR... | 2.4.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P00489}; | glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; intracellular calcium ion homeostasis [GO:0006874]; response to cAMP [GO:0051591]; response to hypoxia [GO:0001666]; response to organic substance [GO:0010033] | cytoplasm [GO:0005737]; sarcoplasmic reticulum [GO:0016529] | AMP binding [GO:0016208]; carbohydrate binding [GO:0030246]; glycogen phosphorylase activity [GO:0008184]; linear malto-oligosaccharide phosphorylase activity [GO:0102250]; organic cyclic compound binding [GO:0097159]; pyridoxal phosphate binding [GO:0030170]; SHG alpha-glucan phosphorylase activity [GO:0102499] | PF00343; | 3.40.50.2000; | Glycogen phosphorylase family | PTM: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000250|UniProtKB:P11217}. | 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:0000250|UniProtKB:P11217}; Physiologica... | null | null | null | null | FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. {ECO:0000250|UniProtKB:P11217}. | Rattus norvegicus (Rat) |
P09813 | APOA2_MOUSE | MKLLAMVALLVTICSLEGALVKRQADGPDMQSLFTQYFQSMTDYGKDLMEKAKTSEIQSQAKAYFEKTHEQLTPLVRSAGTSLVNFFSSLMNLEEKPAPAAK | null | null | animal organ regeneration [GO:0031100]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; diacylglycerol catabolic process [GO:0046340]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein ... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipas... | PF04711; | 6.10.250.100; | Apolipoprotein A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. | null | null | null | null | null | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. | Mus musculus (Mouse) |
P09814 | POLG_TVMV | MAATMIFGSFTHDLLGKAMSTIHSAVTAEKDIFSSIKERLERKRHGKICRMKNGSIYIKAASSTKVEKINAAAKKLADDKAAFLKAQPTIVDKIIVNEKIQVVEAEEVHKREDVQTVFFKKTKKRAPKLRATCSSSGLDNLYNAVANIAKASSLRVEVIHKKRVCGEFKQTRFGRALFIDVAHAKGHRRRIDCRMHRREQRTMHMFMRKTTKTEVRSKHLRKGDSGIVLLTQKIKGHLSGVRDEFFIVRGTCDDSLLEARARFSQSITLRATHFSTGDIFWKGFNASFQEQKAIGLDHTCTSDLPVEACGHVAALMCQSL... | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0... | PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680; | 3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase. {ECO:0000269|PubMed:1702164}.; PTM: [Genome polyprotein]: Potyviral RNA is expressed as two polyproteins w... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000269|PubMed:19906931, ECO:0000269|PubMed:30150314}. Note=6K... | CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but oth... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a m... | Tobacco vein mottling virus (TVMV) |
P09831 | GLTB_ECOLI | MLYDKSLERDNCGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRLAKNYAVGMLFLNKDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLFIARRRIEKRLEADKDFYVCSLSNLVNIYKGLCMPTDLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYLAHNGEINTITGNRQWARARTYKFQTPLIPDLHDAAPFVNETGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDMDPELR... | 1.4.1.13 | COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:4565085}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:4565085}; | ammonia assimilation cycle [GO:0019676]; glutamate biosynthetic process [GO:0006537]; L-glutamate biosynthetic process [GO:0097054] | cytosol [GO:0005829]; glutamate synthase complex (NADPH) [GO:0009342] | 3 iron, 4 sulfur cluster binding [GO:0051538]; glutamate synthase (NADH) activity [GO:0016040]; glutamate synthase (NADPH) activity [GO:0004355]; glutamate synthase activity [GO:0015930]; metal ion binding [GO:0046872] | PF00310;PF04898;PF01645;PF01493; | 3.20.20.70;2.160.20.60;3.60.20.10; | Glutamate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58359; EC=1.4.1.13; Evidence={ECO:0000269|PubMed:4565085}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.3 uM for 2-oxoglutarate {ECO:0000269|PubMed:4565085}; KM=250 uM for L-glutamine {ECO:0000269|PubMed:4565085}; | PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route): step 1/1.; PATHWAY: Energy metabolism; nitrogen metabolism. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6. {ECO:0000269|PubMed:4565085}; | null | FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. {ECO:0000269|PubMed:4565085}. | Escherichia coli (strain K12) |
P09832 | GLTD_ECOLI | MSQNVYQFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPFLIANTKQLMGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRR... | 1.4.1.13 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|PROSITE-ProRule:PRU00711}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711}; | ammonia assimilation cycle [GO:0019676]; glutamate biosynthetic process [GO:0006537]; L-glutamate biosynthetic process [GO:0097054] | cytosol [GO:0005829]; glutamate synthase complex (NADPH) [GO:0009342] | 4 iron, 4 sulfur cluster binding [GO:0051539]; glutamate synthase (NADPH) activity [GO:0004355]; metal ion binding [GO:0046872] | PF14691;PF07992; | 1.10.1060.10;3.50.50.60; | null | null | null | CATALYTIC ACTIVITY: Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58359; EC=1.4.1.13; Evidence={ECO:0000269|PubMed:4565085}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.3 uM for 2-oxoglutarate {ECO:0000269|PubMed:4565085}; KM=250 uM for L-glutamine {ECO:0000269|PubMed:4565085}; | PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route): step 1/1.; PATHWAY: Energy metabolism; nitrogen metabolism. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6. {ECO:0000269|PubMed:4565085}; | null | FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. {ECO:0000269|PubMed:4565085}. | Escherichia coli (strain K12) |
P09835 | UHPB_ECOLI | MKTLFSRLITVIACFFIFSAAWFCLWSISLHLVERPDMAVLLFPFGLRLGLMLQCPRGYWPVLLGAEWLLIYWLTQAVGLTHFPLLMIGSLLTLLPVALISRYRHQRDWRTLLLQGAALTAAALLQSLPWLWHGKESWNALLLTLTGGLTLAPICLVFWHYLANNTWLPLGPSLVSQPINWRGRHLVWYLLLFVISLWLQLGLPDELSRFTPFCLALPIIALAWHYGWQGALIATLMNAIALIASQTWRDHPVDLLLSLLVQSLTGLLLGAGIQRLRELNQSLQKELARNQHLAERLLETEESVRRDVARELHDDIGQTI... | 2.7.13.3; 3.1.3.- | null | signal transduction [GO:0007165] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; protein dimerization activity [GO:0046983] | PF02518;PF07730;PF05231; | 1.20.5.1930;3.30.565.10; | null | PTM: Autophosphorylated. {ECO:0000269|PubMed:11053370, ECO:0000269|PubMed:11739766}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:11053370, ECO:0000269|PubMed:11739766}; | null | null | null | null | FUNCTION: Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. UhpB functions as a membrane-associated protein kinase that autophosphorylates in response to interaction with UhpC, and subsequently transfers its phosphate group to the response regulator UhpA (PubMed... | Escherichia coli (strain K12) |
P09838 | TDT_MOUSE | MDPLQAVHLGPRKKRPRQLGTPVASTPYDIRFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSELELLDISWLIECMGAGKPVEMMGRHQLVVNRNSSPSPVPGSQNVPAPAVKKISQYACQRRTTLNNYNQLFTDALDILAENDELRENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVLNDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVV... | 2.7.7.31; 3.1.11.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23856622}; Note=Can also utilize other divalent cations, such as Mn(2+) and Co(2+) (in vitro). {ECO:0000269|PubMed:23856622, ECO:0000305}; | DNA metabolic process [GO:0006259]; DNA modification [GO:0006304]; double-strand break repair via nonhomologous end joining [GO:0006303]; response to ATP [GO:0033198] | chromatin [GO:0000785]; cytosol [GO:0005829]; euchromatin [GO:0000791]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA nucleotidylexotransferase activity [GO:0003912]; DNA-directed DNA polymerase activity [GO:0003887]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF00533;PF14791;PF10391;PF14716;PF01909; | 1.10.150.20;3.30.460.10;3.40.50.10190;1.10.150.110;3.30.210.10; | DNA polymerase type-X family | null | SUBCELLULAR LOCATION: [Isoform TDT-S]: Nucleus {ECO:0000269|PubMed:7556063}.; SUBCELLULAR LOCATION: [Isoform TDT-L]: Nucleus {ECO:0000269|PubMed:11136823}. Cytoplasm {ECO:0000269|PubMed:7556063}. Note=The subcellular location is controversial. Detected in the nucleus (PubMed:11136823). Found mainly in the cytoplasm (Pu... | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.31; Evidence={ECO:0000269|PubMed:23856622, ECO:0000269|PubMed:23968551}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for dATP (at 35 degrees Celsius) {ECO:0000269|PubMed:10878023}; Note=In assays with isoform TDT-S. {ECO:0000269|PubMed:10878023}; | null | null | null | FUNCTION: [Isoform TDT-S]: Transferase that catalyzes the nontemplated addition of nucleoside triphosphate to coding ends during V(D)J recombination (N addition). Involved in the generation of diversity in the antigen-binding region of immunoglobulin heavy and light chains and T-cell receptors during B- and T-cell deve... | Mus musculus (Mouse) |
P09842 | SSG1_HORVU | MAALATSQLATSGTVLGVTDRFRRPGFQGLRPRNPADAALGMRTIGASAAPKQSRKAHRGSRRCLSVVVSATGSGMNLVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVVSPRYDQYKDAWDTSVISEIKVADEYERVRFFHCYKRGVDRVFIDHPWFLEKVRGKTKEKIYGPDAGTDYEDNQQRFSLLCQAALEAPRILNLNNNPYFSGPYGEDVVFVCNDWHTGLLACYLKSNYQSNGIYRTAKVAFCIHNISYQGRFSFDDFAQLNLPDRFKSSFDFIDGYDKPVEGRKINWMKAGILQADKVLTVSPYYAE... | 2.4.1.242 | null | starch biosynthetic process [GO:0019252] | amyloplast [GO:0009501]; chloroplast [GO:0009507] | ADP-glucose-starch glucosyltransferase activity [GO:0102502]; glycogen (starch) synthase activity [GO:0004373] | PF08323;PF00534; | 3.40.50.2000; | Glycosyltransferase 1 family, Bacterial/plant glycogen synthase subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. Note=Amyloplast or chloroplast, granule-bound. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+); Xref=Rhea:RHEA:15873, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.242; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. | null | null | FUNCTION: Required for the synthesis of amylose in endosperm. | Hordeum vulgare (Barley) |
P09848 | LPH_HUMAN | MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKDMYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKALKTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIKELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQDTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSLFEAINKDQVLTIGFDINEFL... | 3.2.1.108; 3.2.1.62 | null | cellobiose catabolic process [GO:2000892]; glycosylceramide catabolic process [GO:0046477]; lactose catabolic process [GO:0005990]; quercetin catabolic process [GO:1901733] | cytosol [GO:0005829]; external side of apical plasma membrane [GO:0098591]; plasma membrane [GO:0005886] | beta-glucosidase activity [GO:0008422]; cellobiose glucosidase activity [GO:0080079]; galactosylceramidase activity [GO:0004336]; glucosylceramidase activity [GO:0004348]; glycosylceramidase activity [GO:0017042]; lactase activity [GO:0000016]; phlorizin hydrolase activity [GO:0140749]; protein homodimerization activit... | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | PTM: N-glycosylated. {ECO:0000269|PubMed:9593732}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9593732}; Single-pass type I membrane protein {ECO:0000305|PubMed:9593732}. Note=Brush border. {ECO:0000250|UniProtKB:P09849}. | CATALYTIC ACTIVITY: Reaction=H2O + lactose = beta-D-galactose + D-glucose; Xref=Rhea:RHEA:10076, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:27667; EC=3.2.1.108; Evidence={ECO:0000269|PubMed:12594539, ECO:0000269|PubMed:16400612, ECO:0000269|PubMed:3929764, ECO:0000269|PubMed:9762914}; Physiolog... | null | null | null | null | FUNCTION: Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose (PubMed:12594539, PubMed:16400612, PubMed:3929764, PubMed:9762914). The mature protein is composed of two domains that catalyze the hydrolysis o... | Homo sapiens (Human) |
P09849 | LPH_RABIT | MELFWSIVFTVLLSFSCRGSDWESDSNFISAAGPLTTDLLLSLQYPQGNQTSDFAAGGKDLYVCSQPLPAFLPEYFSSLRASEITHYKVFLSWAQLLPAGHSGDPDGNAVRCYRQLLEALRAAQLQPMVVLHHQHLPASSALRSAVFADLFAEYATFAFHAFGDLVGVWLTFSDLEAAIRELPQPESRASRLQLLTEAHRKAYEIYHQKYAAQGGKVSVVLQAEEISELLLESSTSALAKDSIDFLSLDLSYECQSEMSLPEKLSKLQTIEPKVKVFIFTLRLQDCPSSRKSPASLLFSFIEAINKDQVLTLGFDVNAFL... | 3.2.1.108; 3.2.1.62 | null | cellobiose catabolic process [GO:2000892]; glycosylceramide catabolic process [GO:0046477]; lactose catabolic process [GO:0005990]; quercetin catabolic process [GO:1901733] | cytosol [GO:0005829]; external side of apical plasma membrane [GO:0098591] | beta-glucosidase activity [GO:0008422]; cellobiose glucosidase activity [GO:0080079]; galactosylceramidase activity [GO:0004336]; glucosylceramidase activity [GO:0004348]; glycosylceramidase activity [GO:0017042]; lactase activity [GO:0000016]; phlorizin hydrolase activity [GO:0140749]; protein homodimerization activit... | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09848}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:1388157}; Single-pass type I membrane protein {ECO:0000269|PubMed:1388157}. Note=Brush border. {ECO:0000269|PubMed:1388157}. | CATALYTIC ACTIVITY: Reaction=H2O + lactose = beta-D-galactose + D-glucose; Xref=Rhea:RHEA:10076, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:27667; EC=3.2.1.108; Evidence={ECO:0000269|PubMed:1388157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10077; Evidence={ECO:0000269|PubMed:138815... | null | null | null | null | FUNCTION: Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose (PubMed:1388157). The mature protein is composed of two domains that catalyze the hydrolysis of beta-glucopyranosides and beta-galactopyranoside... | Oryctolagus cuniculus (Rabbit) |
P09856 | TRXF_SPIOL | MALHLSLSHQSWTSPAHPITSSDPTRSSVPGTGLSRRVDFLGSCKINGVFVVKRKDRRRMRGGEVRASMEQALGTQEMEAIVGKVTEVNKDTFWPIVKAAGDKPVVLDMFTQWCGPCKAMAPKYEKLAEEYLDVIFLKLDCNQENKTLAKELGIRVVPTFKILKENSVVGEVTGAKYDKLLEAIQAARSS | null | null | null | chloroplast [GO:0009507]; cytosol [GO:0005829] | protein-disulfide reductase activity [GO:0015035] | PF00085; | 3.40.30.10; | Thioredoxin family, Plant F-type subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast. | null | null | null | null | null | FUNCTION: Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The F form is known to activate a number of enzymes of the photosynthetic carbon cycle. | Spinacia oleracea (Spinach) |
P09858 | TGFB2_PIG | MHYCVLSAFLLLHLVTVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVAEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYGLESQQSNRRKKRALDAAYCFRNVQDNCCLR... | null | null | cardiac epithelial to mesenchymal transition [GO:0060317]; cardiac muscle cell proliferation [GO:0060038]; cardioblast differentiation [GO:0010002]; cell migration [GO:0016477]; cell morphogenesis [GO:0000902]; cell-cell junction organization [GO:0045216]; collagen fibril organization [GO:0030199]; dopamine biosyntheti... | axon [GO:0030424]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025] | amyloid-beta binding [GO:0001540]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]; transforming growth factor beta receptor binding [GO:0005160]; type II transforming growth factor beta receptor binding [GO:000... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: [Transforming growth factor beta-2]: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-2 (TGF-beta-2) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-2 inactive. {ECO:0000250|UniProtKB:P01137}. | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: [Transforming growth factor beta-2 proprotein]: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: ... | Sus scrofa (Pig) |
P09866 | POLG_DEN4D | MNQRKKVVRPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKILIGFRKEIGRMLNILNGRKRSTITLLCLIPTVMAFSLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCEDTVTYKCPLLVNTEPEDIDCWCNLTSTWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWILRNPGFALLAGFMAYMIGQTGIQRTVFFVLMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTL... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated suppression of host cytoplasmic pattern recog... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:00550... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; prot... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Dengue virus type 4 (strain Dominica/814669/1981) (DENV-4) |
P09867 | ROA1_BOVIN | MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF | null | null | cellular response to sodium arsenite [GO:1903936]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028] | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | miRNA binding [GO:0035198]; mRNA 3'-UTR binding [GO:0003730] | PF11627;PF00076; | 3.30.70.330; | null | PTM: UP1 is derived from A1 by proteolytic degradation.; PTM: The N-terminus is blocked.; PTM: Sumoylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09651}. Cytoplasm {ECO:0000250|UniProtKB:P09651}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. {ECO:0000250|UniProtKB:P09651}. | null | null | null | null | null | FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulti... | Bos taurus (Bovine) |
P09871 | C1S_HUMAN | MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTPNSVWEPAKAKYVFRDVVQIT... | 3.4.21.42 | null | complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; proteolysis [GO:0006508] | blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252] | PF00431;PF14670;PF00084;PF00089; | 2.10.70.10;2.10.25.10;2.60.120.290;2.40.10.10; | Peptidase S1 family | PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:2141278}. | null | CATALYTIC ACTIVITY: Reaction=Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase.; EC=3.4.21.42; Evidence={ECO:0000269|PubMed:11527969}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.3 uM for complement component C2 (at 37 degrees Celsius) {ECO:0000269|PubMed:11527969}; KM=1.9 uM for complement component C4 (at 37 degrees Celsius) {ECO:0000269|PubMed:11527969}; Note=Less efficient than MASP2 in C4 cleavage.; | null | null | null | FUNCTION: C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4. | Homo sapiens (Human) |
P09872 | VSPCA_AGKCO | VIGGDECNINEHRFLALVYANGSLCGGTLINQEWVLTARHCDRGNMRIYLGMHNLKVLNKDALRRFPKEKYFCLNTRNDTIWDKDIMLIRLNRPVRNSAHIAPLSLPSNPPSVGSVCRIMGWGTITSPNATLPDVPHCANINILDYAVCQAAYKGLAATTLCAGILEGGKDTCKGDSGGPLICNGQFQGILSVGGNPCAQPRKPGIYTKVFDYTDWIQSIISGNTDATCPP | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom serine protease that selectively cleaves the heavy chain of protein C (PROC). This activation is thrombomodulin-independent. {ECO:0000269|PubMed:3624272}. | Agkistrodon contortrix contortrix (Southern copperhead) |
P09874 | PARP1_HUMAN | MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTK... | 2.4.2.-; 2.4.2.30 | null | apoptotic process [GO:0006915]; ATP generation from poly-ADP-D-ribose [GO:1990966]; carbohydrate biosynthetic process [GO:0016051]; cellular response to amyloid-beta [GO:1904646]; cellular response to insulin stimulus [GO:0032869]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to oxi... | chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]; nuclear envelope [GO:0005635]; nuclear replication fork [GO:0043596]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-con... | chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NAD DNA ADP-ribosyltransferase activity [GO:0140294]; NAD+ ADP-ribosyltransferase activity ... | 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 (PubMed:19764761, PubMed:20388712, PubMed:22582261). Auto-ADP-ribosylation on serine takes place following interaction with HPF1 (PubMed:28190768, PubMed:34625544). Auto poly-ADP-ribosylation on serine residues promotes its dissociat... | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:15607977, ECO:0000269|PubMed:22683995, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:26344098, ECO:0000269|PubMed:27568560, ECO:0000269|PubMed:30675909, ECO:0000269|PubMed:32241924, ECO:0000269|PubMed:32358582, ECO:0000269|PubMed:33412112, ECO:0000269|PubMed:346255... | CATALYTIC ACTIVITY: Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30; Evidence={ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19764761, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:26344098, ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:32358582, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=130 uM for NAD(+) {ECO:0000269|PubMed:7852410}; Note=kcat is 390 sec(-1) for NAD(+). {ECO:0000269|PubMed:7852410}; | null | null | null | FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18055453, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:20388712, PubMed:21680843, PubMed:22582261, PubMed:23230272, PubMed:25043379, PubMed:26344098, PubMed:2662... | Homo sapiens (Human) |
P09875 | UD2B1_RAT | MSMKQTSVFLLIQLICYFRPGACGKVLVWPTEYSHWINIKIILNELAQRGHEVTVLVSSASILIEPTKESSINFEIYSVPLSKSDLEYSFAKWIDEWTRDFETLSIWTYYSKMQKVFNEYSDVVENLCKALIWNKSLMKKLQGSQFDVILADAVGPCGELLAELLKTPLVYSLRFCPGYRCEKFSGGLPLPPSYVPVVLSELSDRMTFVERVKNMLQMLYFDFWFQPFKEKSWSQFYSDVLGRPTTLTEMMGKADIWLIRTFWDLEFPHPFLPNFDFVGGLHCKPAKPLPREMEEFVQSSGEHGVVVFSLGSMVKNLTEE... | 2.4.1.17 | null | biphenyl catabolic process [GO:0070980]; cellular glucuronidation [GO:0052695]; cellular response to ethanol [GO:0071361]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to growth hormone stimulus [GO:0071378]; cellular response to testosterone stimulus [GO:0071394]; estrogen metabolic pro... | endoplasmic reticulum membrane [GO:0005789] | glucuronosyltransferase activity [GO:0015020] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:3084479}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; Evidence={ECO:0000269|PubMed:18719240}; PhysiologicalDirection=lef... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.4 uM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:18719240}; Vmax=1630 pmol/min/mg enzyme for the formation of 17beta-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240}; Vmax=55 pmol/min/mg enzy... | null | null | null | FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:18719240). Essential for the elimination ... | Rattus norvegicus (Rat) |
P09880 | TRNL_YEAST | MPSPYDGKRTVTQLVNELEKAEKLSGRGRAYRRVCDLSHSNKKVISWKFNEWDYGKNTITLPCNARGLFISDDTTNPVIVARGYDKFFNVGEVNFTKWNWIEENCTGPYDVTIKANGCIIFISGLEDGTLVVCSKHSTGPRADVDRNHAEAGEKQLLRQLAAMNINRSDFARMLYTHNVTAVAEYCDDSFEEHILEYPLEKAGLYLHGVNVNKAEFETWDMKDVSQMASKYGFRCVQCITSNTLEDLKKFLDNCSATGSFEGQEIEGFVIRCHLKSTEKPFFFKYKFEEPYLMYRQWREVTKDYISNKSRVFKFRKHKFI... | 6.5.1.3 | null | IRE1-mediated unfolded protein response [GO:0036498]; phosphorylation [GO:0016310]; positive regulation of translation in response to stress [GO:0032056]; regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000622]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388] | cytoplasm [GO:0005737]; nuclear inner membrane [GO:0005637]; nucleus [GO:0005634] | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity [GO:0004113]; ATP binding [GO:0005524]; endonuclease activity [GO:0004519]; GTP-dependent polyribonucleotide 5'-hydroxyl-kinase activity [GO:0051730]; RNA ligase (ATP) activity [GO:0003972] | PF09511;PF08302;PF08303; | 3.40.50.300; | TRL1 family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.3; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: One of the two proteins required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09884 | DPOLA_HUMAN | MAPVHGDDSLSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDKRNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMILKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEEEQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSFLPDVSCWDIDQEGDSSFSVQ... | 2.7.7.7 | null | DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA replication, synthesis of RNA primer [GO:0006269]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA synthesis involved in DNA repair [GO:0000731]; double-strand break repair via nonhomologous end joini... | alpha DNA polymerase:primase complex [GO:0005658]; chromatin [GO:0000785]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA replication origin binding [GO:0003688]; DNA-directed DNA polymerase activity [GO:0003887]; nucleotide binding [GO:0000166]; protein kinase binding [GO:0019901]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270] | PF12254;PF00136;PF03104;PF08996; | 2.40.50.730;3.30.70.2820;1.10.3200.20;1.10.132.60;1.10.287.690;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | PTM: A 165 kDa form is probably produced by proteolytic cleavage at Lys-124. {ECO:0000269|PubMed:2243771}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27019227}. Cytoplasm, cytosol {ECO:0000269|PubMed:27019227}. Note=In the cytosol, colocalizes with RNA:DNA hybrids with a speckled pattern. {ECO:0000269|PubMed:27019227}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:26975377, ECO:0000269|PubMed:893425, ECO:0000269|P... | null | null | null | null | FUNCTION: Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, a regulatory subunit P... | Homo sapiens (Human) |
P09889 | PPA5_PIG | MDTWTVLLILQASLVLPGAVGTRTNTRTAPTPILRFVAVGDWGGVPNAPFHTAREMANAKAIATTVKTLGADFILSLGDNFYFTGVHDAKDKRFQETFEDVFSDPSLRNVPWHVLAGNHDHLGNVSAQIAYSKISKRWNFPSPYYRLRFKIPRSNVSVAIFMLDTVTLCGNSDDFVSQQPERPRNLALARTQLAWIKKQLAAAKEDYVLVAGHYPVWSIAEHGPTHCLVKQLLPLLTTHKVTAYLCGHDHNLQYLQDENGLGFVLSGAGNFMDPSKKHLRKVPNGYLRFHFGAENSLGGFAYVEITPKEMSVTYIEASGK... | 3.1.3.2 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 2 iron ions per subunit.; | bone resorption [GO:0045453]; iron ion transport [GO:0006826] | extracellular region [GO:0005576] | acid phosphatase activity [GO:0003993]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198] | PF00149; | 3.60.21.10; | null | null | SUBCELLULAR LOCATION: Secreted. | 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 | FUNCTION: Uteroferrin is a phosphoprotein phosphatase, synthesized in response to progesterone. It appears to function in transplacental transport of iron in pig. | Sus scrofa (Pig) |
P09895 | RL5_RAT | MGFVKVVKNKAYFKRYQVRFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNRFGMDKIYEGQVEVNGDEYNVESIDGQPGAFTCYLDAGLARTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNAEVHRKHIMGQNVADYMRYLMEEDEDAYKKQFSQYIKNNVTPDMMEEMYKKAHAAIRENPVYEKKPKREVKKKRWNRPKMSLAQKKDRVAQKKASFLRAQERAAES | null | null | cellular response to inorganic substance [GO:0071241]; negative regulation of protein neddylation [GO:2000435]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; positive regulation of gene expression [GO:0010628]; positive regulation of translation [GO:0045727]; protein stabilization [... | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991]; ribonuc... | 5S rRNA binding [GO:0008097]; mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729]; structural constituent of ribosome [GO:0003735]; ubiquitin ligase inhibitor activity [GO:1990948]; ubiquitin protein ligase binding [GO:0031625] | PF14204;PF17144; | 3.30.420.100; | Universal ribosomal protein uL18 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46777}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P46777}. Note=Although RP5 is functional within the cytoplasm, the assembly of ribosomal subunits occurs in the nucleus. RPL5 nuclear import is mediated by IPO5/RanBP5, IPO7/RanBP7, KPNB1/importin-beta or TPNO1/Trn... | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Rattus norvegicus (Rat) |
P09905 | HBB_PHYMC | VHLTGEEKSGLTALWAKVNVEEIGGEALGRLLVVYPWTQRFFEHFGDLSTADAVMKNPKVKKHGQKVLASFGEGLKHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVVVLARHFGKEFTPELQTAYQKVVAGVANALAHKYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Physeter macrocephalus (Sperm whale) (Physeter catodon) |
P09912 | IFI6_HUMAN | MRQKAVSLFLCYLLLFTCSGVEAGKKKCSESSDSGSGFWKALTFMAVGGGLAVAGLPALGFTGAGIAANSVAASLMSWSAILNGGGVPAGGLVATLQSLGAGGSSVVIGNIGALMGYATHKYLDSEEDEE | null | null | apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to virus [GO:0098586]; defense response to virus [GO:0051607]; immune response [GO:0006955]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; negative regulation of apoptotic process [GO:0... | endoplasmic reticulum membrane [GO:0005789]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | null | PF06140; | 6.10.110.10; | IFI6/IFI27 family | PTM: Glycosylated. {ECO:0000269|PubMed:15685448}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30224801, ECO:0000269|PubMed:31142663}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:15685448, ECO:0000269|PubMed:17823654, ECO:0000269|PubMed:25757571, ECO:0000269|PubMed:27673746, ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Interferon-stimulated protein that plays an important role in innate immune response against a wide variety of viruses (PubMed:31142663). Inhibits flavivirus replication by preventing the formation of virus-induced endoplasmic reticulum membrane invaginations, which are double-membrane vesicles that flaviviru... | Homo sapiens (Human) |
P09913 | IFIT2_HUMAN | MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAV... | null | null | antiviral innate immune response [GO:0140374]; apoptotic mitochondrial changes [GO:0008637]; defense response to virus [GO:0051607]; negative regulation of protein binding [GO:0032091]; positive regulation of apoptotic process [GO:0043065]; response to virus [GO:0009615] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783] | RNA binding [GO:0003723] | PF13181; | 1.25.40.10; | IFIT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21190939}. Endoplasmic reticulum {ECO:0000269|PubMed:21190939}. | null | null | null | null | null | FUNCTION: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this ... | Homo sapiens (Human) |
P09914 | IFIT1_HUMAN | MSTNGDDHQVKDSLEQLRCHFTWELSIDDDEMPDLENRVLDQIEFLDTKYSVGIHNLLAYVKHLKGQNEEALKSLKEAENLMQEEHDNQANVRSLVTWGNFAWMYYHMGRLAEAQTYLDKVENICKKLSNPFRYRMECPEIDCEEGWALLKCGGKNYERAKACFEKVLEVDPENPESSAGYAISAYRLDGFKLATKNHKPFSLLPLRQAVRLNPDNGYIKVLLALKLQDEGQEAEGEKYIEEALANMSSQTYVFRYAAKFYRRKGSVDKALELLKKALQETPTSVLLHHQIGLCYKAQMIQIKEATKGQPRGQNREKLDK... | null | null | antiviral innate immune response [GO:0140374]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to type I interferon [GO:0071357]; defense response to virus [GO:0051607]; intracellular transport of viral protein in host cell [GO:0019060]; negative regulation of helicase activity [GO:0051097]; negati... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; host cell [GO:0043657] | RNA binding [GO:0003723] | PF13424;PF14559;PF07719;PF13181; | 1.25.40.10; | IFIT family | PTM: Phosphorylated. {ECO:0000269|PubMed:19416887}.; PTM: ISGylated. {ECO:0000269|PubMed:16009940}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:21642987}. | null | null | null | null | null | FUNCTION: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' ca... | Homo sapiens (Human) |
P09916 | SLIB_RAT | MPLWVFFVLLTLTSGSHCSLPPSPPFRVRRHADAIFTSSYRRILGQLYARKLLHEIMNRQQGERNQEQRSRFNRHLDRVWAEDKQMALESILQGFPRMKLSAEA | null | null | adenohypophysis development [GO:0021984]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cellular response to interleukin-6 [GO:0071354]; growth hormone secretion [GO:0030252]; hormone secret... | axon terminus [GO:0043679]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; terminal bouton [GO:0043195] | growth hormone-releasing hormone activity [GO:0016608]; growth hormone-releasing hormone receptor binding [GO:0031770]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428] | PF00123; | null | Glucagon family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone. | Rattus norvegicus (Rat) |
P09917 | LOX5_HUMAN | MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANK... | 1.13.11.-; 1.13.11.34 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:21233389}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:21233389}; | arachidonic acid metabolic process [GO:0019369]; dendritic cell migration [GO:0036336]; glucose homeostasis [GO:0042593]; hepoxilin biosynthetic process [GO:0051122]; humoral immune response [GO:0006959]; leukocyte chemotaxis involved in inflammatory response [GO:0002232]; leukocyte migration involved in inflammatory r... | cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; nuclear envelope [GO:0005635]; nuclear envelope lumen [GO:0005641]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm ... | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 5-lipoxygenase activity [GO:0004051]; arachidonate 8(S)-lipoxygenase activity [GO:0036403]; hydrolase activity [GO:0016787]; iron ion binding [GO:0005506] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | PTM: Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid (PubMed:11844797, PubMed:18978352). Phosphorylation on Ser-524 by PKA has an inhibitory effect (PubMed:15280375). Phosphorylation on Ser-272 prevents export from the nucleus (PubMed:11844797, PubMed:18978352). Phosphorylation at Ser-524 is stimul... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48999, ECO:0000269|PubMed:18978352}. Nucleus matrix {ECO:0000269|PubMed:19233132}. Nucleus membrane {ECO:0000269|PubMed:16275640}; Peripheral membrane protein {ECO:0000269|PubMed:16275640}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19022417}. Cytoplasm, cy... | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = H2O + leukotriene A4; Xref=Rhea:RHEA:32307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57463; EC=1.13.11.34; Evidence={ECO:0000269|PubMed:19022417, ECO:0000269|PubMed:21233389}; PhysiologicalDirection=left-to-right; Xref=Rhe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:8631361}; KM=11 uM for arachidonic acid {ECO:0000269|PubMed:22516296}; KM=1.9 uM for arachidonic acid {ECO:0000269|PubMed:24893149}; KM=14 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicos... | PATHWAY: Lipid metabolism; leukotriene A4 biosynthesis. {ECO:0000269|PubMed:8631361}. | null | null | FUNCTION: Catalyzes the oxygenation of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to 5-hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation (PubMe... | Homo sapiens (Human) |
P09919 | CSF3_HUMAN | MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP | null | null | cellular response to cytokine stimulus [GO:0071345]; cellular response to lipopolysaccharide [GO:0071222]; cytokine-mediated signaling pathway [GO:0019221]; granulocyte colony-stimulating factor signaling pathway [GO:0038158]; granulocyte differentiation [GO:0030851]; immune response [GO:0006955]; positive regulation o... | endocytic vesicle lumen [GO:0071682]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202] | cytokine activity [GO:0005125]; enzyme binding [GO:0019899]; granulocyte colony-stimulating factor receptor binding [GO:0005130]; growth factor activity [GO:0008083] | PF16647; | 1.20.1250.10; | IL-6 superfamily | PTM: O-glycan consists of Gal-GalNAc disaccharide which can be modified with up to two sialic acid residues (done in recombinantly expressed G-CSF from CHO cells). | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes. | Homo sapiens (Human) |
P09920 | CSF3_MOUSE | MAQLSAQRRMKLMALQLLLWQSALWSGREAVPLVTVSALPPSLPLPRSFLLKSLEQVRKIQASGSVLLEQLCATYKLCHPEELVLLGHSLGIPKASLSGCSSQALQQTQCLSQLHSGLCLYQGLLQALSGISPALAPTLDLLQLDVANFATTIWQQMENLGVAPTVQPTQSAMPAFTSAFQRRAGGVLAISYLQGFLETARLALHHLA | null | null | cellular response to lipopolysaccharide [GO:0071222]; granulocyte colony-stimulating factor signaling pathway [GO:0038158]; granulocyte differentiation [GO:0030851]; immune response [GO:0006955]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cell population proliferation [GO:... | endocytic vesicle lumen [GO:0071682]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; enzyme binding [GO:0019899]; granulocyte colony-stimulating factor receptor binding [GO:0005130]; growth factor activity [GO:0008083] | PF16647; | 1.20.1250.10; | IL-6 superfamily | PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes. | Mus musculus (Mouse) |
P09922 | MX1B_MOUSE | MDSVNNLCRHYEEKVRPCIDLIDTLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLRKLKEGEEWRGKVSYDDIEVELSDPSEVEEAINKGQNFIAGVGLGISDKLISLDVSSPNVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIKTYIQKQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGVLTKPDLVDRGAEGKVLDVMRNLVYPLKKGYMIVKCRGQQDIQEQLSLTEAFQKEQVFFKDHSYFSILLEDGKATVPCLAERLTEELTSHICKSLPLLEDQINSSHQSAS... | null | null | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; response to virus [GO:0009615] | endoplasmic reticulum membrane [GO:0005789]; microtubule [GO:0005874]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017] | PF01031;PF00350;PF02212; | 1.20.120.1240;3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | PTM: ISGylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21859714}. Nucleus {ECO:0000269|PubMed:21859714}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: Interferon-induced dynamin-like GTPase with antiviral activity against influenza A virus, (IAV), influenza B virus (IBV) and Thogoto virus (THOV). Inhibits FLUAV by interfering with the process of primary transcription, probably by affecting the viral polymerase function. {ECO:0000269|PubMed:17652381, ECO:000... | Mus musculus (Mouse) |
P09923 | PPBI_HUMAN | MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLGDGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLCGVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADASQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRDPTLDPSLMEMTEAALRLLSR... | 3.1.3.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P15693}; Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P15693}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P15693}; Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P15693}; COFACTOR: Name=Ca(2+); Xref=C... | dephosphorylation [GO:0016311] | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | alkaline phosphatase activity [GO:0004035]; magnesium ion binding [GO:0000287]; protease binding [GO:0002020]; zinc ion binding [GO:0008270] | PF00245; | 3.40.720.10; | Alkaline phosphatase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15693}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15693}. | 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=3.1.3.1; Evidence={ECO:0000250|UniProtKB:P15693, ECO:0000255|PROSITE-ProRule:PRU10042}; | null | null | null | null | FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate compounds. {ECO:0000250|UniProtKB:P15693}. | Homo sapiens (Human) |
P09933 | PERT_PIG | MGARAVLGVTLAVACAGAFFASILRRKDLLGGDTEASGVAGLVEASRLLVDEAIHTTMRRNLRKRGIFSPSQLLSFSKLPEPTSRTASRAAEIMETAVQEVKRRVCRRRDTDQLPTDVLSEELLSTIANLSGCLPHMLPPSCPHTCLANKYRLITGACNNRDHPRWGASNTALARWLPPAYEDGVTEPRGWNPHFLYNGLPLPPVREVTRQVIHVSNEAVTEDGQYSDLLMAWGQYIDHDIAFTPQSTSKAAFAGGADCQLTCENRSPCFPIQLPTNASGAAGATCLPFYRSSAACGSGRQGALVGNLSWAAPRQQMNGL... | 1.11.1.8 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX... | hormone biosynthetic process [GO:0042446]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]; thyroid hormone generation [GO:0006590] | extracellular space [GO:0005615]; membrane [GO:0016020] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; iodide peroxidase activity [GO:0004447]; peroxidase activity [GO:0004601] | PF03098;PF00084; | 2.10.70.10;1.10.640.10;2.10.25.10; | Peroxidase family, XPO subfamily | PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity). {ECO:0000250}.; PTM: Cleaved in its N-terminal part. {ECO:0000250}.; PTM: N-glycosylated; contains mannose and N-acetylglucosamine. {ECO:0000269|... | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O; Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8; Evidence={ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155}; CATALYTIC ACTIVITY: ... | null | PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. | null | null | FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). {ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435}. | Sus scrofa (Pig) |
P09936 | UCHL1_HUMAN | MQLKPMEINPEMLNKVLSRLGVAGQWRFVDVLGLEEESLGSVPAPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVCREFTEREQGEVRFSAVALCKAA | 3.4.19.12 | null | adult walking behavior [GO:0007628]; axon target recognition [GO:0007412]; axonal transport of mitochondrion [GO:0019896]; cellular response to xenobiotic stimulus [GO:0071466]; eating behavior [GO:0042755]; male germ cell proliferation [GO:0002176]; muscle cell development [GO:0055001]; negative regulation of MAP kina... | axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; neuron projection terminus [GO:0044306]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654] | alpha-2A adrenergic receptor binding [GO:0031694]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; omega peptidase activity [GO:0008242]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625] | PF01088; | 3.40.532.10; | Peptidase C12 family | PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19261853}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19261853}; Lipid-anchor {ECO:0000269|PubMed:19261853}. Note=About 30% of total UCHL1 is associated with membranes in brain. Localizes near and/or within mitochondria to potentially interact with mitochondri... | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:12408865, ECO:0000269|PubMed:12705903, ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=122 nM for Ub-AMC {ECO:0000269|PubMed:12705903, ECO:0000269|PubMed:8639624, ECO:0000269|PubMed:9774100}; KM=1.2 uM for ubiquitin ethyl ester {ECO:0000269|PubMed:12705903, ECO:0000269|PubMed:8639624, ECO:0000269|PubMed:9774100}; Vmax=0.47 umol/min/mg enzyme toward U... | null | null | null | FUNCTION: Deubiquitinase that plays a role in the regulation of several processes such as maintenance of synaptic function, cardiac function, inflammatory response or osteoclastogenesis (PubMed:22212137, PubMed:23359680). Abrogates the ubiquitination of multiple proteins including WWTR1/TAZ, EGFR, HIF1A and beta-site a... | Homo sapiens (Human) |
P09938 | RIR2_YEAST | MPKETPSKAAADALSDLEIKDSKSNLNKELETLREENRVKSDMLKEKLSKDAENHKAYLKSHQVHRHKLKEMEKEEPLLNEDKERTVLFPIKYHEIWQAYKRAEASFWTAEEIDLSKDIHDWNNRMNENERFFISRVLAFFAASDGIVNENLVENFSTEVQIPEAKSFYGFQIMIENIHSETYSLLIDTYIKDPKESEFLFNAIHTIPEIGEKAEWALRWIQDADALFGERLVAFASIEGVFFSGSFASIFWLKKRGMMPGLTFSNELICRDEGLHTDFACLLFAHLKNKPDPAIVEKIVTEAVEIEQRYFLDALPVALL... | 1.17.4.1 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 2 iron ions per subunit.; | deoxyribonucleotide biosynthetic process [GO:0009263] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoside-diphosphate reductase complex [GO:0005971] | ferrous iron binding [GO:0008198]; molecular adaptor activity [GO:0060090]; protein heterodimerization activity [GO:0046982]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748]; zinc ion binding [GO:0008270] | PF00268; | 1.10.620.20; | Ribonucleoside diphosphate reductase small chain family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12732713, ECO:0000269|PubMed:18851834}. Note=Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner. Nuclear localization is mediated by DIF1. | 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;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=2250 nmol/min/mg enzyme for cytidine 5'-diphosphate {ECO:0000269|PubMed:10716984}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:10716984}; | FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR2 provides the diiron-tyrosyl radical center. {ECO:0000269|PubMed:10535923}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09950 | HEM1_YEAST | MQRSIFARFGNSSAAVSTLNRLSTTAAPHAKNGYATATGAGAAAATATASSTHAAAAAAAAANHSTQESGFDYEGLIDSELQKKRLDKSYRYFNNINRLAKEFPLAHRQREADKVTVWCSNDYLALSKHPEVLDAMHKTIDKYGCGAGGTRNIAGHNIPTLNLEAELATLHKKEGALVFSSCYVANDAVLSLLGQKMKDLVIFSDELNHASMIVGIKHANVKKHIFKHNDLNELEQLLQSYPKSVPKLIAFESVYSMAGSVADIEKICDLADKYGALTFLDEVHAVGLYGPHGAGVAEHCDFESHRASGIATPKTNDKGG... | 2.3.1.37 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:6381051}; | heme biosynthetic process [GO:0006783]; hemoglobin biosynthetic process [GO:0042541]; positive regulation of organelle assembly [GO:1902117]; protoporphyrinogen IX biosynthetic process [GO:0006782] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | 5-aminolevulinate synthase activity [GO:0003870]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:3023841, ECO:0000269|PubMed:6381051}. | CATALYTIC ACTIVITY: Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305, ChEBI:CHEBI:356416; EC=2.3.1.37; Evidence={ECO:0000269|PubMed:6381051}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 mM for glycine {ECO:0000269|PubMed:6381051}; KM=2 uM for succinyl-CoA {ECO:0000269|PubMed:6381051}; | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. {ECO:0000305|PubMed:6381051}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:6381051}; | null | FUNCTION: Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis. {ECO:0000269|PubMed:6381051}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09951 | SYN1_RAT | MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPSAASPGATPGSAAASAERASTAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAAARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIG... | null | null | neuron development [GO:0048666]; neurotransmitter secretion [GO:0007269]; regulation of synaptic vesicle cycle [GO:0098693]; regulation of synaptic vesicle exocytosis [GO:2000300]; synapse organization [GO:0050808]; synaptic vesicle clustering [GO:0097091]; synaptic vesicle cycle [GO:0099504] | axon [GO:0030424]; cell body [GO:0044297]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; extrinsic component of synaptic vesicle membrane [GO:0098850]; Golgi apparatus [GO:0005794]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; Schaffer collateral - CA1 synapse [G... | actin binding [GO:0003779]; ATP binding [GO:0005524]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901] | PF02078;PF02750;PF10581; | 3.40.50.20;3.30.1490.20;3.30.470.20; | Synapsin family | PTM: Substrate of different protein kinases. Phosphorylation, including phosphorylation at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, regulates its rate of dispersion, and controls the kinetics of vesicle pool turnover (PubMed:10571231, PubMed:11685225). {ECO:0000269|PubMed:10571231, ECO:0000269|Pu... | SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:O88935}. Golgi apparatus {ECO:0000250|UniProtKB:O88935}. Presynapse {ECO:0000269|PubMed:11685225}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:11685225}. Note=Dissociates from synaptic vesicles and redistributes into the axon during a... | null | null | null | null | null | FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (PubMed:11685225). Also involved in the regulation of axon outgrowth and synaptogenesis (B... | Rattus norvegicus (Rat) |
P09956 | ZEST_DROME | MSAQGEGGGAGGSGGGGAGSDGGGNAGQSSTGSGTVAVTNGGNSSAKNQLPLTPRFTAEEKEVLYTLFHLHEEVIDIKHRKKQRNKYSVRETWDKIVKDFNSHPHVSAMRNIKQIQKFWLNSRLRKQYPYRDGSSSNLSSGSAKISSVSVSVASAVPQQQQQQHHQQHDSVKVEPEYQISPDASEHNPQADTFDEIEMDANDVSEIDEDPMEQQQQQQQEAQAQAQAQAQAQAQVQSAAAEMQKMQQVNAVAAAAAANATMINTHQINVDQISAEKLTLNDLLHFKTARPREEIILIKHPEATATQIHTIPTQAQQHPMA... | null | null | heterochromatin formation [GO:0031507]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628] | nucleus [GO:0005634]; polytene chromosome interband [GO:0005705] | sequence-specific DNA binding [GO:0043565] | PF13873; | null | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Involved in transvection phenomena (= synapsis-dependent gene expression), where the synaptic pairing of chromosomes carrying genes with which zeste interacts influences the expression of these genes. Zeste binds to DNA and stimulates transcription from a nearby promoter. | Drosophila melanogaster (Fruit fly) |
P09957 | YELL_DROME | MFQDKGWILVTLITLVTPSWAAYKLQERYSWSQLDFAFPNTRLKDQALASGDYIPQNALPVGVEHFGNRLFVTVPRWRDGIPATLTYINMDRSLTGSPELIPYPDWRSNTAGDCANSITTAYRIKVDECGRLWVLDTGTVGIGNTTTNPCPYAVNVFDLTTDTRIRRYELPGVDTNPNTFIANIAVDIGKNCDDAYAYFADELGYGLIAYSWELNKSWRFSAHSYFFPDPLRGDFNVAGINFQWGEEGIFGMSLSPIRSDGYRTLYFSPLASHRQFAVSTRILRDETRTEDSYHDFVALDERGPNSHTTSRVMSDDGIEL... | null | null | cuticle pigmentation [GO:0048067]; developmental pigmentation [GO:0048066]; male courtship behavior, veined wing extension [GO:0048065]; male mating behavior [GO:0060179]; melanin biosynthetic process [GO:0042438]; melanin biosynthetic process from tyrosine [GO:0006583]; regulation of adult chitin-containing cuticle pi... | cell hair [GO:0070451]; cytoplasm [GO:0005737]; extracellular region [GO:0005576] | null | PF03022; | 2.120.10.30; | Major royal jelly protein family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Controls the pigmentation pattern of the adult cuticle and larval mouth parts. {ECO:0000269|PubMed:16052739, ECO:0000269|PubMed:3096713}. | Drosophila melanogaster (Fruit fly) |
P09958 | FURIN_HUMAN | MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSA... | 3.4.21.75 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:1644824, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:9130696}; Note=Binds 3 calcium ions per subunit. {ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:9130696}; | amyloid fibril formation [GO:1990000]; blastocyst formation [GO:0001825]; collagen catabolic process [GO:0030574]; cytokine precursor processing [GO:0140447]; dibasic protein processing [GO:0090472]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; negative regulation of in... | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; trans-Golgi networ... | endopeptidase activity [GO:0004175]; heparan sulfate binding [GO:1904399]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; nerve growth factor binding [GO:0048406]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; protease binding [GO:0002020]; serine-type endopeptidase activity [GO:0004252]... | PF01483;PF00082;PF16470; | 2.60.120.260;3.30.70.850;3.40.50.200; | Peptidase S8 family, Furin subfamily | PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in prop... | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11331585, ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:8846780, ECO:0000269|PubMed:9130696, ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11799113, ECO:0000269|P... | CATALYTIC ACTIVITY: Reaction=Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.; EC=3.4.21.75; Evidence={ECO:0000269|P... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:9130696}; | null | FUNCTION: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed:11799113, PubMed:1629222, PubMed:1713771, PubMed:2251280, PubMed:24666235, PubMed:25974265, PubMed:7592877, PubMed:7690548, PubMed:9130696). Mediates processing of TGFB1, an essential ste... | Homo sapiens (Human) |
P09959 | SWI6_YEAST | MALEEVVRYLGPHNEIPLTLTRDSETGHFLLKHFLPILQQYHDTGNINETNPDSFPTDEERNKLLAHYGIAVNTDDRGELWIELEKCLQLLNMLNLFGLFQDAFEFEEPETDQDEEDPSHSKLPENKTKSENSKDNISSKRINNLQDMSLDSDAHRELGSPLKKLKIDTSVIDAESDSTPNTARGKPNDDINKGPSGDNENNGTDDNDRTAGPIITFTHDLTSDFLSSPLKIMKALPSPVVNDNEQKMKLEAFLQRLLFPEIQEMPTSLNNDSSNRNSEGGSSNQQQQHVSFDSLLQEVNDAFPNTQLNLNIPVDEHGNT... | null | null | G1/S transition of mitotic cell cycle [GO:0000082]; positive regulation of reciprocal meiotic recombination [GO:0010845]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355] | cytoplasm [GO:0005737]; MBF transcription complex [GO:0030907]; nucleus [GO:0005634]; SBF transcription complex [GO:0033309] | DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713] | PF00023;PF18530; | 3.10.260.30;1.25.40.20; | null | PTM: Phosphorylated by CDC28 and dephosphorylated by CDC14. {ECO:0000269|PubMed:14993267}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. | null | null | null | null | null | FUNCTION: Part of a complex involved in cell-cycle-dependent transcription. SWI4 and SWI6 are required for formation of the cell-cycle box factor-DNA complex. The repeated element in the upstream region of HO (5'-CACGAAAA-3') is called the cell cycle box (CCB). | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P09960 | LKHA4_HUMAN | MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEG... | 3.3.2.6; 3.4.11.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11175901, ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029, ECO:0000269|PubMed:24591641}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:1880... | leukotriene biosynthetic process [GO:0019370]; lipid metabolic process [GO:0006629]; peptide catabolic process [GO:0043171]; protein metabolic process [GO:0019538]; proteolysis [GO:0006508]; response to peptide hormone [GO:0043434]; response to zinc ion [GO:0010043]; type I pneumocyte differentiation [GO:0060509] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; tertiary granule lumen [GO:1904724] | aminopeptidase activity [GO:0004177]; epoxide hydrolase activity [GO:0004301]; leukotriene-A4 hydrolase activity [GO:0004463]; metalloaminopeptidase activity [GO:0070006]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; tripeptide aminopeptidase activity [GO:0045148]; zinc ion binding [GO:0008270] | PF09127;PF01433;PF17900; | 3.30.2010.30;1.10.390.10;1.25.40.320;2.60.40.1730; | Peptidase M1 family | PTM: Phosphorylation at Ser-416 inhibits leukotriene-A4 hydrolase activity. {ECO:0000269|PubMed:9395533}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:6490615}. | CATALYTIC ACTIVITY: Reaction=H2O + leukotriene A4 = leukotriene B4; Xref=Rhea:RHEA:22324, ChEBI:CHEBI:15377, ChEBI:CHEBI:57461, ChEBI:CHEBI:57463; EC=3.3.2.6; Evidence={ECO:0000269|PubMed:11675384, ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029, ECO:00... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.29 mM for Pro-Gly-Pro {ECO:0000269|PubMed:20813919}; | PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis. {ECO:0000269|PubMed:11917124}. | null | null | FUNCTION: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4) (PubMed:11917124, PubMed:12207002, PubMed:15078870, PubMed:18804029, PubMed:1897988, ... | Homo sapiens (Human) |
P09971 | PBAN_BOMMO | MYKTNIVFNVLALALFSIFFASCTDMKDESDRGAHSERGALWFGPRLGKRSMKPSTEDNRQTFLRLLEAADALKFYYDQLPYERQADEPETKVTKKIIFTPKLGRSVAKPQTHESLEFIPRLGRRLSEDMPATPADQEMYQPDPEEMESRTRYFSPRLGRTMSFSPRLGRELSYDYPTKYRVARSVNKTMDN | null | null | neuropeptide signaling pathway [GO:0007218]; pheromone biosynthetic process [GO:0042811] | extracellular region [GO:0005576] | myostimulatory hormone activity [GO:0016084]; neuropeptide hormone activity [GO:0005184] | PF05874; | null | Pyrokinin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8475067}. | null | null | null | null | null | FUNCTION: A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity). Identical to MRCH which is implicated in the formation of both melanin in the cuticle and ommochrome in the epidermis of armyworm species. ... | Bombyx mori (Silk moth) |
P09972 | ALDOC_HUMAN | MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASFNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDN... | 4.1.2.13 | null | epithelial cell differentiation [GO:0030855]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096] | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; secretory granule lumen [GO:0034774]; tertiary granule lumen [GO:1904724] | cytoskeletal protein binding [GO:0008092]; fructose-bisphosphate aldolase activity [GO:0004332] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:15537755}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.7 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:15537755}; KM=16 mM for fructose 1-phosphate {ECO:0000269|PubMed:15537755}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | null | null | Homo sapiens (Human) |
P09980 | REP_ECOLI | MRLNPGQQQAVEFVTGPCLVLAGAGSGKTRVITNKIAHLIRGCGYQARHIAAVTFTNKAAREMKERVGQTLGRKEARGLMISTFHTLGLDIIKREYAALGMKANFSLFDDTDQLALLKELTEGLIEDDKVLLQQLISTISNWKNDLKTPSQAAASAIGERDRIFAHCYGLYDAHLKACNVLDFDDLILLPTLLLQRNEEVRKRWQNKIRYLLVDEYQDTNTSQYELVKLLVGSRARFTVVGDDDQSIYSWRGARPQNLVLLSQDFPALKVIKLEQNYRSSGRILKAANILIANNPHVFEKRLFSELGYGAELKVLSANNE... | 5.6.2.4 | null | bacterial-type DNA replication [GO:0044787]; DNA replication, synthesis of RNA primer [GO:0006269]; DNA unwinding involved in DNA replication [GO:0006268]; recombinational repair [GO:0000725]; replication fork processing [GO:0031297]; response to radiation [GO:0009314] | cytosol [GO:0005829]; DnaB-DnaC-Rep-PriC complex [GO:1990160]; primosome complex [GO:1990077] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; isomerase activity [GO:0016853]; protein homodimerization activity [GO:0042803]; single-stranded DNA binding [GO:0003697] | PF00580;PF13361; | 1.10.10.160;3.40.50.300; | Helicase family, UvrD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01920}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:... | null | null | null | null | FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction. {ECO:0000255|HAMAP-Rule:MF_01920, ECO:0000269|PubMed:221901}. | Escherichia coli (strain K12) |
P09981 | SCX9_MESEU | ARDAYIAKPHNCVYECYNPKGSYCNDLCTENGAESGYCQILGKYGNACWCIQLPDNVPIRIPGKCH | null | null | defense response [GO:0006952] | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Alpha subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6497916}. | null | null | null | null | null | FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active on both mammals and insects, since it inhibits inactivation of rNav1.4/SCN4A, hNav1.5/SCN5A, mNav1.6/SCN8A and insect ... | Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus) |
P09983 | HLYAC_ECOLX | MPTITAAQIKSTLQSAKQSAANKLHSAGQSTKDALKKAAEQTRNAGNRLILLIPKDYKGQGSSLNDLVRTADELGIEVQYDEKNGTAITKQVFGTAEKLIGLTERGVTIFAPQLDKLLQKYQKAGNKLGGSAENIGDNLGKAGSVLSTFQNFLGTALSSMKIDELIKKQKSGGNVSSSELAKASIELINQLVDTAASLNNVNSFSQQLNKLGSVLSNTKHLNGVGNKLQNLPNLDNIGAGLDTVSGILSAISASFILSNADADTGTKAAAGVELTTKVLGNVGKGISQYIIAQRAAQGLSTSAAAAGLIASVVTLAISPL... | null | null | hemolysis in another organism [GO:0044179]; localization [GO:0051179]; protein secretion by the type I secretion system [GO:0030253] | extracellular space [GO:0005615]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | calcium ion binding [GO:0005509]; channel activity [GO:0015267]; lipid binding [GO:0008289]; toxin activity [GO:0090729] | PF00353;PF02382;PF08339; | 2.150.10.10; | RTX prokaryotic toxin (TC 1.C.11) family | PTM: Myristoylated by HlyC; the toxin only becomes active when modified (PubMed:12598051, PubMed:7801126). Mainly myristoylated, while a minor fraction is acylated with pentadecanoyl (C15:0; 26%) and heptadecanoyl (C17:0; 6%) fatty acyl groups (By similarity). Fatty acylation is involved in binding to host membranes an... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3894051}. Host cell membrane {ECO:0000305|PubMed:12598051, ECO:0000305|PubMed:2121650}; Multi-pass membrane protein {ECO:0000305|PubMed:2121650}. | null | null | null | null | null | FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by forming a pore. {ECO:0000269|PubMed:2121650, ECO:0000269|PubMed:3891743, ECO:0000269|PubMed:3894051}. | Escherichia coli |
P09988 | H31_SCHPO | MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS | null | null | DNA damage response [GO:0006974]; heterochromatin boundary formation [GO:0033696]; mitotic sister chromatid biorientation [GO:1990758]; rRNA transcription [GO:0009303] | chromosome, subtelomeric region [GO:0099115]; heterochromatin [GO:0000792]; mating-type region heterochromatin [GO:0031934]; nucleolar peripheral inclusion body [GO:0140602]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | chromatin-protein adaptor activity [GO:0140463]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Phosphorylated by ark1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by ssp2, promotes subsequent H3K14ac formation by gcn5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by sds21.; PTM: ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P09991 | GLYC_LYCVA | MGQIVTMFEALPHIIDEVINIVIIVLIVITGIKAVYNFATCGIFALISFLLLAGRSCGMYGLKGPDIYKGVYQFKSVEFDMSHLNLTMPNACSANNSHHYISMGTSGLELTFTNDSIISHNFCNLTSAFNKKTFDHTLMSIVSSLHLSIRGNSNYKAVSCDFNNGITIQYNLTFSDAQSAQSQCRTFRGRVLDMFRTAFGGKYMRSGWGWTGSDGKTTWCSQTSYQYLIIQNRTWENHCTYAGPFGMSRILLSQEKTKFFTRRLAGTFTWTLSDSSGVENPGGYCLTKWMILAAELKCFGNTAVAKCNVNHDAEFCDMLR... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleava... | SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Go... | null | null | null | null | null | FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glyc... | Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV) |
P09992 | NCAP_LYCVA | MSLSKEVKSFQWTQALRRELQSFTSDVKAAVIKDATNLLNGLDFSEVSNVQRIMRKEKRDDKDLQRLRSLNQTVHSLVDLKSTSKKNVLKVGRLSAEELMSLAADLEKLKAKIMRSERPQASGVYMGNLTTQQLDQRSQILQIVGMRKPQQGASGVVRVWDVKDSSLLNNQFGTMPSLTMACMAKQSQTPLNDVVQALTDLGLLYTVKYPNLNDLERLKDKHPVLGVITEQQSSINISGYNFSLGAAVKAGAALLDGGNMLESILIKPSNSEDLLKAVLGAKRKLNMFVSDQVGDRNPYENILYKVCLSGEGWPYIACRT... | 3.1.13.- | null | negative stranded viral RNA replication [GO:0039689]; RNA-templated viral transcription [GO:0039696]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity [GO:0039724]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasm [GO:0030430]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF17290;PF00843; | 3.30.420.410;1.10.150.550; | Arenaviridae nucleocapsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:3962189}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:3962189}. | null | null | null | null | null | FUNCTION: Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in... | Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV) |
P0A006 | ARSC_STAAU | MDKKTIYFICTGNSCRSQMAEGWGKEILGEGWNVYSAGIETHGVNPKAIEAMKEVDIDISNHTSDLIDNDILKQSDLVVTLCSDADNNCPILPPNVKKEHWGFDDPAGKEWSEFQRVRDEIKLAIEKFKLR | 1.20.4.4 | null | response to arsenic-containing substance [GO:0046685] | cytoplasm [GO:0005737] | arsenate reductase (thioredoxin) activity [GO:0030612]; metal ion binding [GO:0046872]; protein tyrosine phosphatase activity [GO:0004725] | PF01451; | 3.40.50.2300; | Low molecular weight phosphotyrosine protein phosphatase family, Thioredoxin-coupled ArsC subfamily | PTM: Cys-89 performs a nucleophilic attack on a Cys-10-Cys-82 intermediate, forming another disulfide intermediate with Cys-82. {ECO:0000305|PubMed:11573087, ECO:0000305|PubMed:12072565}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000269|PubMed:1409657}. | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-disulfide + arsenite + H2O; Xref=Rhea:RHEA:43848, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29242, ChEBI:CHEBI:29950, ChEBI:CHEBI:48597, ChEBI:CHEBI:50058; EC=1.20.4.4; Evidence={ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for arsenate (below 1 mM arsenate) {ECO:0000269|PubMed:8003493}; KM=2 mM for arsenate (above 1 mM arsenate) {ECO:0000269|PubMed:8003493}; KM=0.066 uM for arsenate {ECO:0000269|PubMed:10606519}; KM=68 uM for arsenate {ECO:0000269|PubMed:11862551}; KM=9 uM for... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:11862551}; | null | FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)] (PubMed:10606519, PubMed:11862551, PubMed:12072565, PubMed:12682056, PubMed:1409657, PubMed:16797027, PubMed:8003493). In vitro, has also low phosphatase activity with para-nitrophenyl phosphate (pNPP) as substrate (PubMed:11573087). {ECO:00002... | Staphylococcus aureus |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.