Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P17694 | NDUS2_BOVIN | MAALRALCRLRGAAAQVLRPGAGVRLPIQPSRGARQWQPDVEWAEQYGGAVMYPTKETAHWKPPPWNDVDPPKDTLVSNLTLNFGPQHPAAHGVLRLVMELSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSLAVEKLLNIQPPPRAQWIRVLFGEITRLLNHIMAVTTHALDIGAMTPFFWMFEEREKMFEFYERVSGARMHAAYVRPGGVHQDLPLGLMDDIYEFSKNFSLRIDELEEMLTNNRIWRNRTVDIGIVTAEDALNYGFSGVMLRGSGIQWDLRKTQPYDVYDQVEFDVPI... | 7.1.1.2 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster.; | cellular response to oxygen levels [GO:0071453]; gliogenesis [GO:0042063]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; neural precursor cell proliferation [GO:0061351]; neurogenesis [GO:0022008]; response to oxidative stress [GO:000... | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; oxygen sensor activity [GO:0019826]; quinone binding [GO:0048038]; ubiquitin protein ligase binding [GO:0031625] | PF00346; | 1.10.645.10; | Complex I 49 kDa subunit family | PTM: Dimethylation at Arg-118 by NDUFAF7 takes place after NDUFS2 assembles into the complex I, leading to stabilize the early intermediate complex. {ECO:0000250|UniProtKB:O75306}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Peripheral membrane protein {ECO:0000305|PubMed:25209663}; Matrix side {ECO:0000305|PubMed:25209663}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:Q91WD5}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:10852722, PubMed:18721790). Essential for the catalytic activity and assembly of complex I (By... | Bos taurus (Bovine) |
P17695 | GLRX2_YEAST | METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTYCPYCKATLSTLFQELNVPKSKALVLELDEMSNGSEIQDALEEISGQKTVPNVYINGKHIGGNSDLETLKKNGKLAEILKPVFQ | 1.11.1.9; 2.5.1.18 | null | cellular response to oxidative stress [GO:0034599]; glutathione metabolic process [GO:0006749] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | disulfide oxidoreductase activity [GO:0015036]; glutathione disulfide oxidoreductase activity [GO:0015038]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364] | PF00462; | 3.40.30.10; | Glutaredoxin family | null | SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:11958675, ECO:0000269|PubMed:16606613}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:11958675, ECO:0000269|PubMed:16606613}. | CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000269|PubMed:11875065}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitroph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for H(2)O(2) {ECO:0000269|PubMed:12684511}; KM=2.2 mM for tert-butyl hydroperoxide {ECO:0000269|PubMed:12684511}; KM=0.87 mM for cumene hydroperoxide {ECO:0000269|PubMed:12684511}; KM=0.17 mM for 1-chloro-2,4-dinitrobenzene {ECO:0000269|PubMed:12684511}; KM=0.... | null | null | null | FUNCTION: Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed:11875065, PubMed:12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17697 | CLUS_BOVIN | MKTLLLLMGLLLSWESGWAISDKELQEMSTEGSKYVNKEIKNALKEVKQIKTQIEQTNEERKLLLSSLEEAKKKKEDALNDTRDSENKLKASQGVCNETMTALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDSLMENDREQSHVMDVMEDSFTRASSIMDELFQDRFFLRRPQDTQYYSPFSSFPRGSLFFNPKSRFARNVMPFPLLEPFNFHDVFQPFYDMIHQAQQAMDAHLQRTPYHFPTMEFTENNDRTVCKEIRHNSTGCLRMKDQCEKCQEILEVDCSASNPTQTLLRQQLN... | null | null | chaperone-mediated protein folding [GO:0061077]; immune complex clearance [GO:0002434]; intrinsic apoptotic signaling pathway [GO:0097193]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulati... | chromaffin granule [GO:0042583]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum lumen [GO:0099020]; perin... | misfolded protein binding [GO:0051787]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082] | PF01093; | null | Clusterin family | PTM: Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen. Proteolytic cleavage is not necessary for its chaperone activity. All non-secreted forms are not proteolytically cleaved. Chaperone activity of uncleaved forms is dependent on a non-reducing environment. {ECO:0000250|... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, ... | null | null | null | null | null | FUNCTION: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partia... | Bos taurus (Bovine) |
P17706 | PTN2_HUMAN | MPTTIEREFEELDTQRRWQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCIKGDSSIQKRWKELSKEDLSPAFDHSPNKIMTEKYNGNRIGL... | 3.1.3.48 | null | B cell differentiation [GO:0030183]; erythrocyte differentiation [GO:0030218]; glucose homeostasis [GO:0042593]; insulin receptor recycling [GO:0038020]; insulin receptor signaling pathway [GO:0008286]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chemotaxis [GO:0050922]; ne... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome lumen [GO:0031904]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | integrin binding [GO:0005178]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]; receptor tyrosine kinase binding [GO:0030971]; STAT family protein binding [GO:0097677]; syntaxin binding [GO:0019905] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class 1 subfamily | PTM: [Isoform 2]: Specifically phosphorylated in a cell cycle-dependent manner by cyclin-dependent kinases CDK1 and CDK2. Probably activated through phosphorylation by PKR. {ECO:0000269|PubMed:15030318, ECO:0000269|PubMed:16431927}. | SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:7593185}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:7593185}. Note=Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region. {ECO:0000269|PubMed:7593185}.; SUBCELLULAR LOCATION: [Isoform 2]: Nuc... | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.48 mM for p-nitrophenyl phosphate (at pH 6.5 and 25 degrees Celsius) {ECO:0000269|PubMed:11907034}; | null | null | null | FUNCTION: Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Nega... | Homo sapiens (Human) |
P17707 | DCAM_HUMAN | MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNF... | 4.1.1.50 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000269|PubMed:11583147}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000269|PubMed:11583147}; | polyamine metabolic process [GO:0006595]; spermidine biosynthetic process [GO:0008295]; spermine biosynthetic process [GO:0006597] | cytosol [GO:0005829] | adenosylmethionine decarboxylase activity [GO:0004014]; identical protein binding [GO:0042802]; putrescine binding [GO:0019810] | PF01536; | 3.60.90.10; | Eukaryotic AdoMetDC family | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... | null | CATALYTIC ACTIVITY: Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50; Evidence={ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:10574985, ECO:0000269|PubMed:11583147, EC... | null | PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. {ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:10574985, ECO:0000269|PubMed:11583147, ECO:0000269|PubMed:1917972, ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270}. | null | null | FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. {ECO:0000250|UniProtKB:P0DMN7}. | Homo sapiens (Human) |
P17708 | DCAM_RAT | MEAAHFFEGTEKLLEVWFSRQQSDASQGSGDLRTIPRSEWDVLLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDLPESRVINQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATLFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLSSPQKIDGFKRLDCQSAMFNDYNF... | 4.1.1.50 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.; | polyamine metabolic process [GO:0006595]; S-adenosylmethionine metabolic process [GO:0046500]; spermidine biosynthetic process [GO:0008295]; spermine biosynthetic process [GO:0006597] | cytosol [GO:0005829] | adenosylmethionine decarboxylase activity [GO:0004014]; identical protein binding [GO:0042802]; putrescine binding [GO:0019810] | PF01536; | 3.60.90.10; | Eukaryotic AdoMetDC family | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... | null | CATALYTIC ACTIVITY: Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50; Evidence={ECO:0000250|UniProtKB:P17707}; | null | PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. | null | null | FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. {ECO:0000250|UniProtKB:P0DMN7}. | Rattus norvegicus (Rat) |
P17709 | HXKG_YEAST | MSFDDLHKATERAVIQAVDQICDDFEVTPEKLDELTAYFIEQMEKGLAPPKEGHTLASDKGLPMIPAFVTGSPNGTERGVLLAADLGGTNFRICSVNLHGDHTFSMEQMKSKIPDDLLDDENVTSDDLFGFLARRTLAFMKKYHPDELAKGKDAKPMKLGFTFSYPVDQTSLNSGTLIRWTKGFRIADTVGKDVVQLYQEQLSAQGMPMIKVVALTNDTVGTYLSHCYTSDNTDSMTSGEISEPVIGCIFGTGTNGCYMEEINKITKLPQELRDKLIKEGKTHMIINVEWGSFDNELKHLPTTKYDVVIDQKLSTNPGFH... | 2.7.1.2 | null | carbohydrate phosphorylation [GO:0046835]; glucose 6-phosphate metabolic process [GO:0051156]; glucose import [GO:0046323]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeostasis [GO:0001678]; mannose metabolic process [GO:0006013] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536] | PF00349;PF03727; | 3.30.420.40;3.40.367.20; | Hexokinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2; Evidence={ECO:0000305|PubMed:3072253}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence=... | null | PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000269|PubMed:3072253}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000269|PubMed:3072253}. | null | null | FUNCTION: Two isoenzymes, hexokinase-1 and hexokinase-2, can phosphorylate keto- and aldohexoses in yeast, whereas a third isoenzyme, GLK, is specific for aldohexoses. All glucose phosphorylating enzymes are involved in glucose uptake. {ECO:0000269|PubMed:3072253}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17710 | HXK1_MOUSE | MGWGAPLLSRMLHGPGQAGETSPVPERQSGSENPASEDRRPLEKQCSHHLYTMGQNCQRGQAVDVEPKIRPPLTEEKIDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKSQNVSMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAF... | 2.7.1.1 | null | canonical glycolysis [GO:0061621]; carbohydrate phosphorylation [GO:0046835]; establishment of protein localization to mitochondrion [GO:0072655]; fructose 6-phosphate metabolic process [GO:0006002]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycolytic process [GO:00060... | caveola [GO:0005901]; cytosol [GO:0005829]; membrane raft [GO:0045121]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucosamine kinase activity [GO:0047931]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]; identical protein binding [GO:0042802]; mannokinase activity [GO:0019158]; peptidoglycan binding [GO:0042834]; protei... | PF00349;PF03727; | 3.30.420.40;3.40.367.20; | Hexokinase family | PTM: [Isoform HK1-SC]: Tyrosine-phosphorylated. {ECO:0000269|PubMed:9450953}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:27374331}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19367}. Cytoplasm, cytosol {ECO:0000269|PubMed:27374331}. Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane (By similarity). ... | CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000250|UniProtKB:P19367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evid... | null | PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000250|UniProtKB:P19367}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000250|UniProtKB:P05708}. | null | null | FUNCTION: Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively). Does not pho... | Mus musculus (Mouse) |
P17712 | HXK4_RAT | MLDDRARMEATKKEKVEQILAEFQLQEEDLKKVMSRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDLDKGILLNWTKGFKASGAEGNNIVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRMVDESSANPGQQLYEKIIGGKYMGELVRLVLLKLVDENLLFHGEA... | 2.7.1.1 | null | calcium ion import [GO:0070509]; carbohydrate phosphorylation [GO:0046835]; cellular response to glucose starvation [GO:0042149]; cellular response to insulin stimulus [GO:0032869]; cellular response to leptin stimulus [GO:0044320]; fructose 2,6-bisphosphate metabolic process [GO:0006003]; fructose 6-phosphate metaboli... | basal cortex [GO:0045180]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; secretory granule [GO:0030141] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; glucose sensor activity [GO:0141089]; hexokinase activity [GO:0004396]; magnesium ion binding [GO:0000287]; mannokinase activity [GO:0019158]; protein phosphatase bind... | PF00349;PF03727; | 3.30.420.40;3.40.367.20; | Hexokinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10456334, ECO:0000269|PubMed:16542652}. Nucleus {ECO:0000269|PubMed:10456334}. Mitochondrion {ECO:0000269|PubMed:16542652}. Note=Under low glucose concentrations, associates with GCKR and the inactive complex is recruited to the hepatocyte nucleus. {ECO:0000269|PubMed... | CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:12513690, ECO:0000269|PubMed:6477520}; PhysiologicalDirection=left-to-right;... | null | PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305|PubMed:12513690, ECO:0000305|PubMed:6477520}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000305|PubMed:12513690, ECO:0000305|PubMed:6477520}. | null | null | FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose, D-fructose and D-mannose, to hexose 6-phosphate (D-glucose 6-phosphate, D-fructose 6-phosphate and D-mannose 6-phosphate, respectively) (PubMed:12513690, PubMed:24187134, PubMed:6477520). Compared to other hexokinases, has a weak affinity for D-gluco... | Rattus norvegicus (Rat) |
P17715 | INS_OCTDE | MAPWMHLLTVLALLALWGPNSVQAYSSQHLCGSNLVEALYMTCGRSGFYRPHDRRELEDLQVEQAELGLEAGGLQPSALEMILQKRGIVDQCCNNICTFNQLQNYCNVP | null | null | acute-phase response [GO:0006953]; alpha-beta T cell activation [GO:0046631]; fatty acid homeostasis [GO:0055089]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin receptor signaling pathway [GO:0008286]; negative regulation of ... | extracellular space [GO:0005615] | hormone activity [GO:0005179]; identical protein binding [GO:0042802]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; protease binding [GO:0002020] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. | Octodon degus (Degu) (Sciurus degus) |
P17721 | G3P_THEMA | MARVAINGFGRIGRLVYRIIYERKNPDIEVVAINDLTDTKTLAHLLKYDSVHKKFPGKVEYTENSLIVDGKEIKVFAEPDPSKLPWKDLGVDFVIESTGVFRNREKAELHLQAGAKKVIITAPAKGEDITVVIGCNEDQLKPEHTIISCASCTTNSIAPIVKVLHEKFGIVSGMLTTVHSYTNDQRVLDLPHKDLRRARAAAVNIIPTTTGAAKAVALVVPEVKGKLDGMAIRVPTPDGSITDLTVLVEKETTVEEVNAVMKEATEGRLKGIIGYNDEPIVSSDIIGTTFSGIFDATITNVIGGKLVKVASWYDNEYGYS... | 1.2.1.12 | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8508805}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000269|PubMed:2271518, EC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=440 uM for glyceraldehyde-3-phosphate (at pH 8.0 and 40 degrees Celsius) {ECO:0000269|PubMed:2271518}; KM=360 uM for glyceraldehyde-3-phosphate (at pH 8.0 and 50 degrees Celsius) {ECO:0000269|PubMed:2271518}; KM=400 uM for glyceraldehyde-3-phosphate (at pH 8.0 and ... | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD (PubMed:2271518). The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidize... | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
P17727 | TXL1_PHONI | MKLLGIFLVASFAFVLSFGEEMIEGENPLEDQRAELTSCFPVGHECDGDASNCNCCGDDVYCGCGWGRWNCKCKVADQSYAYGICKDKVNCPNRHLWPAKVCKKPCRRNCGG | null | null | null | extracellular region [GO:0005576] | sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF08396; | null | Neurotoxin 04 (omega-agtx) family, 02 (Tx1) subfamily | PTM: Contains 7 disulfide bonds. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16278100}. | null | null | null | null | null | FUNCTION: Reversible inhibitor of neuronal sodium channels (Nav1.2/ SCN2A) that binds in proximity to site 1 and displays increasing affinity as the membrane potential is depolarized. Induces excitatory symptoms and spastic paralysis in mice. {ECO:0000269|PubMed:16505156, ECO:0000269|PubMed:16908187, ECO:0000269|PubMed... | Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer) |
P17728 | SCXA_LEIHE | MNHLVMISLALLLLLGVESVRDAYIAKNYNCVYECFRDAYCNELCTKNGASSGYCQWAGKYGNACWCYALPDNVPIRVPGKCHRK | 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. | 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. The dissociation is voltage-dependent. This toxin is active on insects. It is also highly toxic to crustaceans and has a measurable but low... | Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus hebraeus) |
P17735 | ATTY_HUMAN | MDPYMIQMSSKGNLPSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIVDNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSREEIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMGIEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQCVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDIFGNEIRDGLVKLSQRILGPC... | 2.6.1.5 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|Ref.8}; | 2-oxoglutarate metabolic process [GO:0006103]; biosynthetic process [GO:0009058]; glutamate metabolic process [GO:0006536]; L-phenylalanine catabolic process [GO:0006559]; response to dexamethasone [GO:0071548]; response to mercury ion [GO:0046689]; response to oxidative stress [GO:0006979]; tyrosine catabolic process ... | cytosol [GO:0005829] | amino acid binding [GO:0016597]; identical protein binding [GO:0042802]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; pyridoxal phosphate binding [GO:0030170] | PF00155;PF07706; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5; Evidence={ECO:0000269|PubMed:16640556, ECO:0000269|PubMed:7999802}; | null | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 2/6. | null | null | FUNCTION: Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine. {ECO:0000269|PubMed:16640556, ECO:0000269|P... | Homo sapiens (Human) |
P17741 | HMGB2_PIG | MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKGEAGKKGPGRPTGSKKKNEPEDEEEEEEEEEDEDEEEEDEDEE | null | null | chemotaxis [GO:0006935]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; DNA topological change [GO:0006265]; double-strand break repair via nonhomologous end joining [GO:0006303]; infl... | chromatin [GO:0000785]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; non-sequence-specific DNA binding, bending [GO:0044378]; protein domain specific binding [GO:0019904]; sing... | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P26583, ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000250|UniProtKB:P26583}. Cytoplasm {ECO:0000250|UniProtKB:P26583, ECO:0000250|UniProtKB:P30681}. Secreted {ECO:0000250|UniProtKB:P26583}. | null | null | null | null | null | FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes (By similarity). Binds... | Sus scrofa (Pig) |
P17742 | PPIA_MOUSE | MVNPTVFFDITADDEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCGQL | 5.2.1.8 | null | activation of protein kinase B activity [GO:0032148]; apoptotic process [GO:0006915]; cell adhesion molecule production [GO:0060352]; cellular response to oxidative stress [GO:0034599]; endothelial cell activation [GO:0042118]; leukocyte chemotaxis [GO:0030595]; lipid droplet organization [GO:0034389]; negative regulat... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | cyclosporin A binding [GO:0016018]; heparan sulfate binding [GO:1904399]; integrin binding [GO:0005178]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF00160; | 2.40.100.10; | Cyclophilin-type PPIase family, PPIase A subfamily | PTM: Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization (By similarity). PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (By similarity). Acetylation at Lys-125 favors the ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62937}. Secreted {ECO:0000250|UniProtKB:P62937}. Nucleus {ECO:0000250|UniProtKB:P62937}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, ... | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:24429998, ECO:0000305|PubMed:25678563}; | null | null | null | null | FUNCTION: Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:24429998). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (By similarity)... | Mus musculus (Mouse) |
P17745 | EFTU_ARATH | MAISAPAACSSSSRILCSYSSPSPSLCPAISTSGKLKTLTLSSSFLPSYSLTTTSASQSTRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASIGSSVAKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPDMVVFLNKEDQVDDAELLELVELEVRELLSSYEFNGDDIPIISGSALLAVETLTENPKVKRGDNKWVDKIYELMDAVDDYIPIPQRQTELPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV... | null | null | chloroplast organization [GO:0009658]; leaf development [GO:0048366]; mitochondrial translational elongation [GO:0070125] | apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast nucleoid [GO:0042644]; chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plastid [GO:0... | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; mRNA binding [GO:0003729]; translation elongation factor activity [GO:0003746] | PF00009;PF03144;PF03143; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | null | null | null | null | null | FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Arabidopsis thaliana (Mouse-ear cress) |
P17751 | TPIS_MOUSE | MAPTRKFFVGGNWKMNGRKKCLGELICTLNAANVPAGTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDLGATWVVLGHSERRHVFGESDELIGQKVSHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVNDGVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ | 4.2.3.3; 5.3.1.1 | null | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glyceraldehyde-3-phosphate metabolic process [GO:0019682]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]; methylglyoxal biosyn... | cytosol [GO:0005829] | isomerase activity [GO:0016853]; methylglyoxal synthase activity [GO:0008929]; protein homodimerization activity [GO:0042803]; triose-phosphate isomerase activity [GO:0004807]; ubiquitin protein ligase binding [GO:0031625] | PF00121; | 3.20.20.70; | Triosephosphate isomerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}. | CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000250|UniProtKB:P00939}; CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:... | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-ProRule:PRU10127}.; PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|PROSITE-ProRule:PRU10127}. | null | null | FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.; FUNCTION: It is also responsible for the non-negligible p... | Mus musculus (Mouse) |
P17752 | TPH1_HUMAN | MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGL... | 1.14.16.4 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:12379098}; | aromatic amino acid metabolic process [GO:0009072]; 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]; regulatio... | cytosol [GO:0005829]; neuron projection [GO:0043005] | iron ion binding [GO:0005506]; tryptophan 5-monooxygenase activity [GO:0004510] | 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:0000250|UniProtKB:P09810}.; PTM: Phosphorylated; triggering degradation by the proteasome. {ECO:0000250|UniProtKB:P09810}. | 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:0000250|UniProtKB:P17532}. | null | null | FUNCTION: Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis. {ECO:0000250|UniProtKB:P17532}. | Homo sapiens (Human) |
P17755 | ENV_HV2D1 | MEPGRNQLLVAILLTSACLIYCKQYVTVFYGIPAWRNASIPLFCATKNRDTWGTIQCLPDNDDYQEITLNVTEAFDAWDNTVTEQAIEDVWRLFETSIKPCVKLTPLCVAMNCNITSGTTATPSPPNITIIDENSTCIGDNNCTGLGKEEVVECEFNMTGLEQDKKRKYNDAWYSRDVVCDKTNGTGTCYMRHCNTSVIKESCDKHYWDAMKFRYCAPPGFALLRCNDTNYSGFEPKCSKVVAASCTRMMETQTSTWFGFNGTRAENRTYIYWHGKDNRTIISLNKYYNLTMHCKRPGNKTVVPITLMSGRRFHSRPVYN... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy a... | Human immunodeficiency virus type 2 subtype A (isolate D194) (HIV-2) |
P17756 | GAG_HV2D1 | MGARNSVLRGKKADELEKVRLRPNGKKRYRLKHVVWAANELDRFGLAESLLESKEGCQKILKVLEPLVPTGSENLKSLFNTVCVIWCLHAEEKVKDTEEAKKLAQRHLVAETGTAEKMPNISRPTAPPSGKGGNFPVQQAGGNYIHVPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDAQHPIPGPLPAGQLRDPRGSDIAGTTSTVDEQIQWMYRQPNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKESFQSYVDRFYKSLRAEQTDPAVKNWMT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate D194) (HIV-2) |
P17757 | POL_HV2D1 | MGARNSVLRGKKADELEKVRLRPNGKKRYRLKHVVWAANELDRFGLAESLLESKEGCQKILKVLEPLVPTGSENLKSLFNTVCVIWCLHAEEKVKDTEEAKKLAQRHLVAETGTAEKMPNISRPTAPPSGKGGNFPVQQAGGNYIHVPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDAQHPIPGPLPAGQLRDPRGSDIAGTTSTVDEQIQWMYRQPNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKESFQSYVDRFYKSLRAEQTDPAVKNWMT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immun... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate D194) (HIV-2) |
P17763 | POLG_DEN1W | MNNQRKKTGRPSFNMLKRARNRVSTVSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWGSFKKNGAIKVLRGFKKEISNMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPHMIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCEDTMTYKCPRITETEPDDVDCWCNATETWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETWALRHPGFTVIALFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKDKPT... | 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: [RNA-directed RNA polymerase NS5]: Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication. {ECO:0000250|UniProtKB:P29990}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reti... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion. Host nucleus {ECO:0000269|PubMed:18420804}. Host cytoplasm {ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:19889084}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000269|PubMed:19759134}.; SUBCELLULAR LOCATION: [Small en... | 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; Evidence={ECO:0000269|PubMed:15917225}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=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 (PubMed:11893341). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface ... | Dengue virus type 1 (strain Nauru/West Pac/1974) (DENV-1) |
P17764 | THIL_RAT | MAALAVLHGVVRRPLLRGLLQEVRCLGRSYASKPTLNDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPI... | 2.3.1.9 | null | acetyl-CoA biosynthetic process [GO:0006085]; acetyl-CoA catabolic process [GO:0046356]; adipose tissue development [GO:0060612]; coenzyme A biosynthetic process [GO:0015937]; coenzyme A metabolic process [GO:0015936]; fatty acid beta-oxidation [GO:0006635]; isoleucine catabolic process [GO:0006550]; ketone body catabo... | endoplasmic reticulum [GO:0005783]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | acetyl-CoA C-acetyltransferase activity [GO:0003985]; C-acetyltransferase activity [GO:0016453]; cholesterol O-acyltransferase activity [GO:0034736]; coenzyme A binding [GO:0120225]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; potassium ion binding [GO:0030955] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | PTM: Succinylation at Lys-265, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P24752}. | CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037; Evidence={ECO:0000250|UniProtKB:P24752}; Physiologica... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:P24752}. | null | null | FUNCTION: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened ... | Rattus norvegicus (Rat) |
P17765 | POLG_BYMV | MTTINIGTIPVVINQNADTQMGEGTKNIFPIVKDFVDPFADLEMRCAERVKRMGELCFSKKGRYITMIPKPDYIKAREKEQREEELNFQNSEHVLNSLDTTCTPEHHSSRNNGMQVSFKTQHYKRTFRKPRIQAKKRDLKGQHTIHYVAKELLSIVKKRDMVLEVVDKRKHANFATFRRYGKTYGMHITLNHMVRKRRRVDVTLNKLMTEIAMHCAIPFECLNTLTLRKGHSGLVLQTETVPNVHKIKSKITIVRGVVNEGNIPVLIDARKKLSGRDMSTIREFSAGDLFWKGYNQTFIDNRPTDLNHQCTSDLNVTQCG... | 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 (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Potyviral RNA is expressed as ... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate ... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Hydrolyz... | 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... | Bean yellow mosaic virus |
P17766 | POLG_PPVNA | MSTIVFGSFTCHLDAAIHQDNADRLAKAWTRPENRQVSNAHLLCRRAAESLINTYESATASAWKGLEEKLQPMFAKREFSKTVTKRKGLRCFKESSEKFIEKKLRKQYQEERERLQFLNGPDAIVNQISVDKCEASVRVPSPHIIEKPSFVTPSMKKKVVFKKVRMSEASLQLFMRRVAANAKANGQKVEIIGRKRVVGNYTTKSRLTYFRTHVRHLDGSKPRYDLVLDEATKKILQLFANTSGFHHVHKKGEVTPGMSGFVVNPMNLSDPMQVYDTDLFIVRGKHNSILVDSRCKVSKKQSNEIIHYSDPGKQFSDGFT... | 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 (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Potyviral RNA is expressed as ... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate ... | CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but oth... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. 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... | Plum pox potyvirus (isolate NAT) (PPV) |
P17767 | POLG_PPVRA | MSTIVFGSFTCHLDAAIHQDNADRLAKAWTRPENRQVSNVHLLCRRAAKSLINTYESATASAWKGLEEKLQPMFAKREFSKTVTKRKGLRCFKESSEKFIEKKLRKQYQEERERFQFLNGPDAIVNQISVDKCEASVRVPFPHIIEKPSFATPSMKKKVVFTKVRMSEASLQLFMRRVAANAKANGQKVEIIGRKRVVGNYTTKSRLTYFRTHVRHLDGSKPRYDLVLDEATKKILQLFANTSGFHHVHKKGEVTPGMSGFVVNPMNLSDPMQVYDTDLFIVRGKHNSILVDSRCKVSKEQSNEIIHYSDPGKQFWDGFT... | 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 (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Genome polyprotein of potyviru... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate ... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Hydrolyz... | 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... | Plum pox potyvirus (strain Rankovic) (PPV) |
P17770 | TDC_CATRO | MGSIDSTNVAMSNSPVGEFKPLEAEEFRKQAHRMVDFIADYYKNVETYPVLSEVEPGYLRKRIPETAPYLPEPLDDIMKDIQKDIIPGMTNWMSPNFYAFFPATVSSAAFLGEMLSTALNSVGFTWVSSPAATELEMIVMDWLAQILKLPKSFMFSGTGGGVIQNTTSESILCTIIAARERALEKLGPDSIGKLVCYGSDQTHTMFPKTCKLAGIYPNNIRLIPTTVETDFGISPQVLRKMVEDDVAAGYVPLFLCATLGTTSTTATDPVDSLSEIANEFGIWIHVDAAYAGSACICPEFRHYLDGIERVDSLSLSPHKW... | 4.1.1.28 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:23204519}; | amino acid metabolic process [GO:0006520]; carboxylic acid metabolic process [GO:0019752] | cytoplasm [GO:0005737] | 5-hydroxy-L-tryptophan decarboxylase activity [GO:0036467]; L-tryptophan decarboxylase activity [GO:0036469]; pyridoxal phosphate binding [GO:0030170] | PF00282; | 3.90.1150.10;1.20.1340.10;3.40.640.10; | Group II decarboxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-tryptophan = CO2 + tryptamine; Xref=Rhea:RHEA:30339, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57887, ChEBI:CHEBI:57912; EC=4.1.1.28; Evidence={ECO:0000269|PubMed:23204519}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30340; Evidence={ECO:0000269|PubMed:23204519}; ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 mM for L-tryptophan {ECO:0000269|PubMed:23204519}; Vmax=2710 nmol/min/mg enzyme with L-tryptophan as substrate {ECO:0000269|PubMed:23204519}; | null | null | null | FUNCTION: Catalyzes the decarboxylation of L-tryptophan to tryptamine and L-5-hydroxytryptophan to serotonin, respectively. {ECO:0000269|PubMed:23204519, ECO:0000269|PubMed:25107664}. | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
P17773 | IFNG_SHEEP | MKYTSSFLALLLCVLLGFSGSYGQGPFFKEIENLKEYFNASNPDVAKGGPLFSEILKNWKEESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKRLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRASM | null | null | adaptive immune response [GO:0002250]; astrocyte activation [GO:0048143]; defense response to virus [GO:0051607]; extrinsic apoptotic signaling pathway [GO:0097191]; humoral immune response [GO:0006959]; macrophage activation involved in immune response [GO:0002281]; macrophage differentiation [GO:0030225]; microglial ... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; type II interferon receptor binding [GO:0005133] | PF00714; | 1.20.1250.10; | Type II (or gamma) interferon family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01579}. | null | null | null | null | null | FUNCTION: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNG... | Ovis aries (Sheep) |
P17777 | LIF_RAT | MKVLAAGIVPLLLILHWKHGAGSPLPITPVNATCAIRHPCHGNLMNQIKSQLAQLNGSANALFISYYTAQGEPFPNNVDKLCAPNMTDFPPFHANGTEKTKLVELYRMVTYLGASLTNITWDQKNLNPTAVSLQIKLNATTDVMRGLLSSVLCRLCNKYHVGHVDVPCVPDNSSKEAFQRKKLGCQLLGTYKQVISVLAQAF | null | null | animal organ regeneration [GO:0031100]; astrocyte differentiation [GO:0048708]; blood vessel remodeling [GO:0001974]; cell morphogenesis [GO:0000902]; cell population proliferation [GO:0008283]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; fibroblast proliferation [GO:0048144]; gene expression [GO:00... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; leukemia inhibitory factor receptor binding [GO:0005146]; signaling receptor binding [GO:0005102] | PF01291; | 1.20.1250.10; | LIF/OSM family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes. | Rattus norvegicus (Rat) |
P17785 | ANXA2_CHICK | MSTVHEILSKLSLEGDHSLPPSAYATVKAYSNFDADRDAAALEAAIKTKGVDEVTIINILTNRSNEQRQDIAFAYQRRTKKELSAALKSALSGHLEAVILGLLKTPSQYDASELKAAMKGLGTDEDTLIEIICSRTNQELNEINRVYREMYKTELEKDIISDTSGDFRKLMVALAKGKRCEDTSVIDYELIDQDARELYDAGVKRKGTDVPKWINIMTERSVPHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKQLYFADRLYDSMKGKGTRDKVLIRIMVSRCEVDMLKIKSEFKRKYGKSLYYFIQ... | null | null | bone mineralization [GO:0030282]; calcium ion homeostasis [GO:0055074]; endocardial cell differentiation [GO:0060956]; growth plate cartilage development [GO:0003417]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of recep... | basement membrane [GO:0005604]; calcium channel complex [GO:0034704]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; vesicle [GO:0031982] | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; cytoskeletal protein binding [GO:0008092]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [G... | PF00191; | 1.10.220.10; | Annexin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=In the lamina beneath the plasma membrane. | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. | Gallus gallus (Chicken) |
P17787 | ACHB2_HUMAN | MARRCGPVALLLGFGLLRLCSGVWGTDTEERLVEHLLDPSRYNKLIRPATNGSELVTVQLMVSLAQLISVHEREQIMTTNVWLTQEWEDYRLTWKPEEFDNMKKVRLPSKHIWLPDVVLYNNADGMYEVSFYSNAVVSYDGSIFWLPPAIYKSACKIEVKHFPFDQQNCTMKFRSWTYDRTEIDLVLKSEVASLDDFTPSGEWDIVALPGRRNENPDDSTYVDITYDFIIRRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLDVPLVGKYLMFTMVLVTFSIVTSVCVLN... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; associative learning [GO:0008306]; B cell activation [GO:0042113]; behavioral response to nicotine [GO:0035095]; calcium ion transport [GO:0006816]; central nervous system projection neuron axonogenesis [GO:0021952]; cognition [GO:0050890]; lateral geniculate nucle... | acetylcholine-gated channel complex [GO:0005892]; cholinergic synapse [GO:0098981]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; postsynaptic specialization membrane [GO:0099634]; presynaptic membra... | acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; heterocyclic compound binding [GO:1901363]; ligand-gated monoatomic ion channel activity [GO:0015276]; protein-containing complex binding [GO:0044877]; quatern... | 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-2/CHRNB2 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | null | 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 permeable to sodiun ions. {ECO:0000269|PubMed:22361591}. | Homo sapiens (Human) |
P17789 | TTKB_DROME | MKMASQRFCLRWNNHQSNLLSVFDQLLHAETFTDVTLAVEGQHLKAHKMVLSACSPYFNTLFVSHPEKHPIVILKDVPYSDMKSLLDFMYRGEVSVDQERLTAFLRVAESLRIKGLTEVNDDKPSPAAAAAGAGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSDGNDSDGEGLDTSYMEPQLMLDEYDEPVEFKY... | null | null | branch fusion, open tracheal system [GO:0035147]; branching involved in open tracheal system development [GO:0060446]; chitin-based cuticle development [GO:0040003]; compound eye cone cell differentiation [GO:0042675]; compound eye corneal lens morphogenesis [GO:0048750]; dorsal appendage formation [GO:0046843]; dorsal... | nucleus [GO:0005634]; polytene chromosome [GO:0005700]; transcription repressor complex [GO:0017053] | chromatin binding [GO:0003682]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [... | PF00651;PF00096; | 3.30.160.60; | null | PTM: Polyubiquitinated by sina. Polyubiquitin linkage is mainly through 'Lys-48', but linkage through 'Lys-63' also occurs. Deubiquitination by Usp47 leads to its stabilization. {ECO:0000269|PubMed:18160715}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Binds to a number of sites in the transcriptional regulatory region of ftz (PubMed:2104801). Isoform beta is required to repress inappropriate segmentation gene transcription and repress genes incompatible with development of photoreceptor cell fates (PubMed:12384587, PubMed:18160715). Probable repressor of t... | Drosophila melanogaster (Fruit fly) |
P17790 | BASI_CHICK | MAAGADVPCAVLALLVLGSLAAGGDATAGFIKSPLSQRRLTQDSVELHCEAVGSPIPEIQWWFEGNEPNETSAQLWDGAWQDRVQINATYNLHSTSTIYIANLTSDDSGTYECRASNDPDRNHLSKSPKVKWIRSQANVLVIERPVITGQYSSSADKVVLSCNISAPPTLIKGHKWMLGDKVLKTDESDASSYISYTIEGKVEDHSGVYECIYNTNPVAKGNVSIEVEPQVVAYKKSEHGNEGDVGVLTCKSPSYPPVDHWAWYKSGQTVPLESSAGIYNISRTGNKTELRILKLNIEQDMGDYSCNGTNMKGSGSATVN... | null | null | angiogenesis [GO:0001525]; axon guidance [GO:0007411]; dendrite self-avoidance [GO:0070593]; endothelial tube morphogenesis [GO:0061154]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neural retina development [GO:0003407]; neutrophil chemotaxis [GO:0030593]; photoreceptor cell maintenan... | acrosomal membrane [GO:0002080]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; endoplasmic reticulum membrane [GO:0005789]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886] | cell-cell adhesion mediator activity [GO:0098632]; signaling receptor activity [GO:0038023] | PF13927; | 2.60.40.10; | null | PTM: [Isoform 2]: N-glycosylated. {ECO:0000269|PubMed:2357963}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:25957687}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P18572}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P18572}.; SUBCELLULAR LOCATION: [Iso... | null | null | null | null | null | FUNCTION: [Isoform 1]: Essential for normal retinal maturation and development (By similarity). Acts as a retinal cell surface receptor for NXNL1 and plays an important role in NXNL1-mediated survival of retinal cone photoreceptors (PubMed:25957687). In association with glucose transporter SLC16A1/GLUT1 and NXNL1, prom... | Gallus gallus (Chicken) |
P17809 | GTR1_MOUSE | MDPSSKKVTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWNHRYGEPIPSTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVAAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNADLWPLLLSVIFIPALLQCILLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQEMKEEGRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAF... | null | null | cellular hyperosmotic response [GO:0071474]; cellular response to glucose starvation [GO:0042149]; cellular response to mechanical stimulus [GO:0071260]; cerebral cortex development [GO:0021987]; dehydroascorbic acid transport [GO:0070837]; female pregnancy [GO:0007565]; glucose import [GO:0046323]; glucose import acro... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; female germ cell nucleus [GO:0001674]; female pronucleus [GO:0001939]; glucose transporter complex... | D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; glucose transmembrane transporter activity [GO:0005355]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; long-chain fatty acid transporter activity [GO:0005324]; protein ... | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | PTM: Phosphorylation at Ser-226 by PKC promotes glucose uptake by increasing cell membrane localization. {ECO:0000250|UniProtKB:P11166}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17320047, ECO:0000269|PubMed:30197081, ECO:0000269|PubMed:35810171}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000269|PubMed:25957687}. | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11166}; | null | null | null | null | FUNCTION: Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake (PubMed:17320047, PubMed:35810171). Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses (By similarity). Most important energy carrier of the brain: pre... | Mus musculus (Mouse) |
P17810 | PRPH2_BOVIN | MALLKVKFDQKKRVKLAQGLWLMNWFSVLAGIIIFGLGLFLKIELRKRSDVMNNSESHFVPNSLIGVGVLSCVFNSLAGKICYDALDPAKYAKWKPWLKPYLAVCVLFNVVLFLVALCCFLLRGSLESTLAHGLKNGMKFYRDTDTPGRCFMKKTIDMLQIEFKCCGNNGFRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRYLVDGVPFSCCNPNSPRPCIQYQLTNNSAHYSYDHQTEELNLWLRGCRAALLSYYSNLMNTTGAVTLLVWLFEVTITVGLRYLHTALEGMANPEDPECESEGWLLEKSVPETWKAFL... | null | null | cell adhesion [GO:0007155]; detection of light stimulus involved in visual perception [GO:0050908]; photoreceptor cell outer segment organization [GO:0035845]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; protein localization to plasma membrane [GO:0072659]; protein maturation [... | cytoplasm [GO:0005737]; membrane [GO:0016020]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF00335; | 1.10.1450.10; | PRPH2/ROM1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:2372552}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:10681511}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P15499}. | null | null | null | null | null | FUNCTION: Essential for retina photoreceptor outer segment disk morphogenesis, may also play a role with ROM1 in the maintenance of outer segment disk structure (PubMed:24196967). Required for the maintenance of retinal outer nuclear layer thickness (By similarity). Required for the correct development and organization... | Bos taurus (Bovine) |
P17811 | PLA_YERPE | MKKSSIVATIITILSGSANAASSQLIPNISPDSFTVAASTGMLSGKSHEMLYDAETGRKISQLDWKIKNVAILKGDISWDPYSFLTLNARGWTSLASGSGNMDDYDWMNENQSEWTDHSSHPATNVNHANEYDLNVKGWLLQDENYKAGITAGYQETRFSWTATGGSYSYNNGAYTGNFPKGVRVIGYNQRFSMPYIGLAGQYRINDFELNALFKFSDWVRAHDNDEHYMRDLTFREKTSGSRYYGTVINAGYYVTPNAKVFAEFTYSKYDEGKGGTQTIDKNSGDSVSIGGDAAGISNKNYTVTAGLQYRF | 3.4.23.48 | null | proteolysis [GO:0006508] | cell outer membrane [GO:0009279] | aspartic-type endopeptidase activity [GO:0004190] | PF01278; | 2.40.128.90; | Peptidase A26 family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:20637417, ECO:0000305|PubMed:2526282}; Multi-pass membrane protein {ECO:0000269|PubMed:20637417, ECO:0000269|PubMed:22645135}. | CATALYTIC ACTIVITY: Reaction=Converts human Glu-plasminogen to plasmin by cleaving the 560-Arg-|-Val-561 peptide bond that is also hydrolyzed by the mammalian u-plasminogen activator and t-plasminogen activator. Also cleaves arginyl bonds in other proteins.; EC=3.4.23.48; Evidence={ECO:0000269|PubMed:22645135}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7 for plasminogen cleavage (PubMed:20637417). {ECO:0000269|PubMed:20637417}; | null | FUNCTION: In the mammalian host activates (cleaves) plasminogen to generate the serine protease plasmin. Plasmin degrades fibrin clots (fibrinolysis) and facilitates bacterial cell migration, enabling rapid dissemination of bacteria from the initial site of infection (Probable). Cleaves host plasminogen to generate pla... | Yersinia pestis |
P17812 | PYRG1_HUMAN | MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA... | 6.3.4.2 | null | 'de novo' CTP biosynthetic process [GO:0044210]; B cell proliferation [GO:0042100]; CTP biosynthetic process [GO:0006241]; glutamine metabolic process [GO:0006541]; nucleobase-containing compound metabolic process [GO:0006139]; pyrimidine nucleobase biosynthetic process [GO:0019856]; response to xenobiotic stimulus [GO... | cytoophidium [GO:0097268]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | ATP binding [GO:0005524]; CTP synthase activity [GO:0003883]; identical protein binding [GO:0042802] | PF06418;PF00117; | 3.40.50.880;3.40.50.300; | CTP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25223282}. Note=Mainly cytosolic but when active detected in long filamentous structures (PubMed:25223282). Co-localizes with TNK2 in the cytosolic filaments (By similarity). {ECO:0000250|UniProtKB:P70698, ECO:0000269|PubMed:25223282}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; Evidenc... | null | PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000269|PubMed:16179339, ECO:0000269|PubMed:24870241}. | null | null | FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocyte... | Homo sapiens (Human) |
P17813 | EGLN_HUMAN | MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTYTTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVLSVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPITSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLEGVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLIDANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPLA... | null | null | artery morphogenesis [GO:0048844]; atrial cardiac muscle tissue morphogenesis [GO:0055009]; atrioventricular canal morphogenesis [GO:1905222]; BMP signaling pathway [GO:0030509]; bone development [GO:0060348]; branching involved in blood vessel morphogenesis [GO:0001569]; cardiac atrium morphogenesis [GO:0003209]; card... | cell surface [GO:0009986]; endothelial microparticle [GO:0072563]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | activin binding [GO:0048185]; coreceptor activity [GO:0015026]; galactose binding [GO:0005534]; glycosaminoglycan binding [GO:0005539]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; signaling receptor activator activity [GO:0030546]; transforming growth factor beta binding [GO:... | null | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10545596, ECO:0000269|PubMed:1326540, ECO:0000269|PubMed:1692830, ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:8370410}; Single-pass type I membrane protein {ECO:0000305|PubMed:1692830, ECO:0000305|PubMed:8370410}. | null | null | null | null | null | FUNCTION: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis (PubMed:21737454, PubMed:23300529). Required for normal structure and integrity of adult vasculature (PubMed:7894484). Regulates the migration of vascular endothelial cells (PubMed:17540773). Required for normal e... | Homo sapiens (Human) |
P17814 | 4CL1_ORYSJ | MGSMEQQQPESAAPATEASPEIIFRSKLQDIAITNTLPLHRYCFERLPEVAARPCLIDGATGGVLTYADVDRLSRRLAAALRRAPLGLRRGGVVMSLLRNSPEFVLSFFAASRVGAAVTTANPMSTPHEIESQLAAAGATVVITESMAADKLPSHSHGALTVVLIDERRDGCLHFWDDLMSEDEASPLAGDEDDEKVFDPDDVVALPYSSGTTGLPKGVMLTHRSLSTSVAQQVDGENPNIGLHAGDVILCALPMFHIYSLNTIMMCGLRVGAAIVVMRRFDLAAMMDLVERHRVTIAPLVPPIVVAVAKSEAAAARDLS... | 6.2.1.12; 6.2.1.34 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O24146}; | phenylpropanoid metabolic process [GO:0009698] | null | (E)-caffeate-CoA ligase activity [GO:0106286]; 4-coumarate-CoA ligase activity [GO:0016207]; ATP binding [GO:0005524]; CoA-ligase activity [GO:0016405]; trans-cinnamate-CoA ligase activity [GO:0106290] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36251, ChEBI:CHEBI:29749, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:87305, ChEBI:CHEBI:456215; EC=6.2.1.34; Evidence={ECO:0000269|PubMed:21807887, ECO:0000269|PubMed:23246835}; Physiol... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.4 uM for cinnamate {ECO:0000269|PubMed:21807887}; KM=11.9 uM for 4-coumarate {ECO:0000269|PubMed:21807887}; KM=29.3 uM for caffeate {ECO:0000269|PubMed:21807887}; KM=8.3 uM for ferulate {ECO:0000269|PubMed:21807887}; Vmax=100 pmol/sec/mg enzyme with cinnamate as ... | PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step 1/2. {ECO:0000305}. | null | null | FUNCTION: Involved in the phenylpropanoid metabolism by mediating the activation of a number of hydroxycinnamates for the biosynthesis of monolignols and other phenolic secondary metabolites (PubMed:21807887, PubMed:23246835). Catalyzes the formation of CoA esters of cinnamate, 4-coumarate, caffeate and ferulate (PubMe... | Oryza sativa subsp. japonica (Rice) |
P17839 | AG_ARATH | MAYQSELGGDSSPLRKSGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSSRGRLYEYSNNSVKGTIERYKKAISDNSNTGSVAEINAQYYQQESAKLRQQIISIQNSNRQLMGETIGSMSPKELRNLEGRLERSITRIRSKKNELLFSEIDYMQKREVDLHNDNQILRAKIAENERNNPSISLMPGGSNYEQLMPPPQTQSQPFDSRNYFQVAALQPNNHHYSSAGRQDQTALQLV | null | null | cell differentiation [GO:0030154]; flower development [GO:0009908]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF01486;PF00319; | 3.40.1810.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Probable transcription factor involved in the control of organ identity during the early development of flowers. Is required for normal development of stamens and carpels in the wild-type flower. Plays a role in maintaining the determinacy of the floral meristem. Acts as C class cadastral protein by repressin... | Arabidopsis thaliana (Mouse-ear cress) |
P17844 | DDX5_HUMAN | MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVC... | 3.6.4.13 | null | alternative mRNA splicing, via spliceosome [GO:0000380]; androgen receptor signaling pathway [GO:0030521]; BMP signaling pathway [GO:0030509]; epithelial to mesenchymal transition [GO:0001837]; intracellular estrogen receptor signaling pathway [GO:0030520]; intrinsic apoptotic signaling pathway by p53 class mediator [G... | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium-dependent protein binding [GO:0048306]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; MH2 domain binding [GO:0035500]; mRNA 3'-UTR binding [GO:0003730]; nuclear androgen receptor binding [GO:0050681]; pre-mRNA binding [GO:0036002]; ... | PF00270;PF00271;PF08061; | 3.40.50.300; | DEAD box helicase family, DDX5/DBP2 subfamily | PTM: Arg-502 is dimethylated, probably to asymmetric dimethylarginine.; PTM: Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination. {ECO:0000269|PubMed:17369852, ECO:0000269|... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22034099}. Nucleus, nucleolus {ECO:0000269|PubMed:10837141, ECO:0000269|PubMed:1996094}. Nucleus speckle {ECO:0000269|PubMed:24644279}. Cytoplasm {ECO:0000269|PubMed:22034099}. Note=During the G0 phase, predominantly located in the nucleus. Cytoplasmic levels increase d... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-str... | Homo sapiens (Human) |
P17846 | CYSI_ECOLI | MSEKHPGPLVVEGKLTDAERMKHESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMLLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPRTRAYAEIWLDQEKVATTDEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFK... | 1.8.1.2 | COFACTOR: Name=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000255|HAMAP-Rule:MF_01540, ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848}; Note=Binds 1 siroheme per subunit. {ECO:0000255|HAMAP-Rule:MF_01540, ECO:0000269|PubMed:7569952, ECO:0000269|PubMed:9315848}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:C... | cysteine biosynthetic process [GO:0019344]; hydrogen sulfide biosynthetic process [GO:0070814]; sulfate assimilation [GO:0000103] | sulfite reductase complex (NADPH) [GO:0009337] | 4 iron, 4 sulfur cluster binding [GO:0051539]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; sulfite reductase (ferredoxin) activity [GO:0050311]; sulfite reductase (NADPH) activity [GO:0004783]; sulfite reductase activity [GO:0016002] | PF01077;PF03460; | 3.30.413.10; | Nitrite and sulfite reductase 4Fe-4S domain family | null | null | CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01540}; | null | PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01540}. | null | null | FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. {ECO:0000255|HAMAP-Rule:MF_01540}. | Escherichia coli (strain K12) |
P17852 | ITA3_CRIGR | MGPGPRCAPGDPGWMLGALALMVAASGRFAFAFNLDTRFLVVKEAVNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLSVADGYTNRTGAVYLCPLTALKDDCERMDISEKSDPDHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGMEDQRRMVGKCYVRGNDLQLDPGDDWQTYHNEMCNSNTDYLQTGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYKGSEDQGNLYIGYTVQVGSAVLHPTYITVVAGAPRHQHMGAVFLLSQESGGDLKRKQVLEGTQVGAYFGSAIALADLNNDG... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]; leukocyte migration [GO:0050900]; positive regulation of protein localization to plasma membrane [GO:1903078] | anchoring junction [GO:0070161]; external side of plasma membrane [GO:0009897]; filopodium membrane [GO:0031527]; integrin complex [GO:0008305] | integrin binding [GO:0005178]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982] | PF01839;PF08441;PF20805;PF20806; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | PTM: Isoform 1, but not isoform 2, is phosphorylated on serine residues. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P26006}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, filopodium membrane {ECO:0000250|UniProtKB:P26006}... | null | null | null | null | null | FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia an... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P17854 | CYSH_ECOLI | MSKLDLNALNELPKVDRILALAETNAELEKLDAEGRVAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWEPGMAEEETRFFGLKRECGLHEG | 1.8.4.8 | null | hydrogen sulfide biosynthetic process [GO:0070814]; sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) [GO:0019379]; sulfur compound metabolic process [GO:0006790] | cytoplasm [GO:0005737] | phosphoadenylyl-sulfate reductase (thioredoxin) activity [GO:0004604] | PF01507; | 3.40.50.620; | PAPS reductase family, CysH subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol; Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:58339, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for phosphoadenosine 5'-phosphosulfate {ECO:0000269|PubMed:7588765}; KM=23 uM for thioredoxin {ECO:0000269|PubMed:7588765}; Vmax=94 umol/min/mg enzyme {ECO:0000269|PubMed:7588765}; | PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00063}. | null | null | FUNCTION: Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor. {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:7588765}. | Escherichia coli (strain K12) |
P17858 | PFKAL_HUMAN | MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDGSLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEA... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glycolytic process [GO:0006096]; negative regulation of insulin secretion [GO:0046676]; response to glucose [GO:0009749] | 6-phosphofructokinase complex [GO:0005945]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; secretory granule lumen [GO:0034774] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose binding [GO:0070061]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | PTM: GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation. {ECO:0000269|PubMed:22923583}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:22923583}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (PubMed:22923583). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived rea... | Homo sapiens (Human) |
P17861 | XBP1_HUMAN | MVVVAAAPNPADGTPKVLLLSGQPASAAGAPAGQALPLMVPAQRGASPEAASGGLPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENQKLLLENQLLREKTHGLVVENQELRQRLGMDALVAEEEAEAKGNEVRPVAGSAESAALRLRAPLQQVQAQLSPLQNISPWILAVLTLQIQSLISCWAFWTTWTQSCSSNALPQSLPAWRSSQRSTQKDPVPYQPPFLCQWGRHQPSWKPLMN | null | null | adipose tissue development [GO:0060612]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; ATF6-mediated unfolded protein response [GO:0036500]; autophagy [GO:0006914]; cellular response to amino acid stimulus [GO:0071230]; cellular response to fluid shear stress [GO:0071498]; cellular response to fructose sti... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin DNA binding [GO:0031490]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; nuclear estr... | PF07716; | 1.20.5.170; | BZIP family | PTM: [Isoform 2]: Acetylated by EP300; acetylation positively regulates the transcriptional activity of XBP1 isoform 2 (PubMed:20955178). Isoform 2 is deacetylated by SIRT1; deacetylation negatively regulates the transcriptional activity of XBP1 isoform 2 (PubMed:20955178). {ECO:0000269|PubMed:20955178, ECO:0000305|Pub... | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:23529610}. Note=Colocalizes with ERN1 and KDR in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (PubMed:23529610). {ECO:0000269|PubMed:23529610}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {E... | null | null | null | null | null | FUNCTION: Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland (By similarity).... | Homo sapiens (Human) |
P17865 | FTSZ_BACSU | MLEFETNIDGLASIKVIGVGGGGNNAVNRMIENEVQGVEYIAVNTDAQALNLSKAEVKMQIGAKLTRGLGAGANPEVGKKAAEESKEQIEEALKGADMVFVTAGMGGGTGTGAAPVIAQIAKDLGALTVGVVTRPFTFEGRKRQLQAAGGISAMKEAVDTLIVIPNDRILEIVDKNTPMLEAFREADNVLRQGVQGISDLIATPGLINLDFADVKTIMSNKGSALMGIGIATGENRAAEAAKKAISSPLLEAAIDGAQGVLMNITGGTNLSLYEVQEAADIVASASDQDVNMIFGSVINENLKDEIVVTVIATGFIEQEK... | null | null | cell division [GO:0051301]; chloroplast fission [GO:0010020]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; protein polymerization [GO:0051258] | cell division site [GO:0032153]; cell septum [GO:0030428]; cytoplasm [GO:0005737] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802] | PF12327;PF00091; | 3.30.1330.20;3.40.50.1440; | FtsZ family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00909}. | null | null | null | null | null | FUNCTION: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produc... | Bacillus subtilis (strain 168) |
P17870 | ARRB1_BOVIN | MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVEPVDGVVLVDPEYLKERRVYVTLTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVS... | null | null | clathrin-dependent endocytosis [GO:0072583]; desensitization of G protein-coupled receptor signaling pathway [GO:0002029]; G protein-coupled receptor internalization [GO:0002031]; negative regulation of Notch signaling pathway [GO:0045746]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation ... | clathrin coat of coated pit [GO:0030132]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143] | acetylcholine receptor binding [GO:0033130]; AP-2 adaptor complex binding [GO:0035612]; clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; G protein-coupled receptor binding [GO:0001664]; inositol hexakisphosphate binding [GO:0000822]; molecular adaptor activity [GO:0060090]; phosphatidylinositol... | PF02752;PF00339; | 2.60.40.640;2.60.40.840; | Arrestin family | PTM: Constitutively phosphorylated at Ser-412 in the cytoplasm. At the plasma membrane, is rapidly dephosphorylated, a process that is required for clathrin binding and ADRB2 endocytosis but not for ADRB2 binding and desensitization. Once internalized, is rephosphorylated.; PTM: The ubiquitination status appears to reg... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Membrane, clathrin-coated pit {ECO:0000305}. Cell projection, pseudopodium {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. The monomeric form is predominantly located in ... | null | null | null | null | null | FUNCTION: Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protei... | Bos taurus (Bovine) |
P17871 | TBP_SCHPO | MDFALPTTASQASAFMNNSSLTFPVLPNANNEATNETADSGDAEVSKNEGVSGIVPTLQNIVATVNLDCRLDLKTIALHARNAEYNPKRFAAVIMRIREPKSTALIFASGKMVVLGGKSEDDSKLASRKYARIIQKLGFNAKFTDFKIQNIVGSCDVKFPIRLEGLAYSHGTFSSYEPELFPGLIYRMVKPKVVLLIFVSGKIVLTGAKVREEIYQAFEAIYPVLSEFRKH | null | null | DNA-templated transcription initiation [GO:0006352]; transcription initiation at RNA polymerase I promoter [GO:0006361]; transcription initiation at RNA polymerase II promoter [GO:0006367]; transcription initiation at RNA polymerase III promoter [GO:0006384] | nucleus [GO:0005634]; RNA polymerase I transcription regulator complex [GO:0000120]; transcription factor TFIID complex [GO:0005669]; transcription factor TFIIIB complex [GO:0000126] | RNA polymerase I general transcription initiation factor activity [GO:0001181]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; RNA polymerase III general transcription initiation factor activity [GO:0000995]; R... | PF00352; | 3.30.310.10; | TBP family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P17879 | HS71B_MOUSE | MAKNTAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDAVVQSDMKHWPFQVVNDGDKPKVQVNYKGESRSFFPEEISSMVLTKMKEIAEAYLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRGTLEPVEKA... | null | null | binding of sperm to zona pellucida [GO:0007339]; chaperone cofactor-dependent protein refolding [GO:0051085]; negative regulation of apoptotic process [GO:0043066]; positive regulation of microtubule nucleation [GO:0090063]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; ... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; blood microparticle [GO:0072562]; cell body [GO:0044297]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane raft [GO:0045121]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634];... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; NF-kappaB binding [GO:0051059]; protease binding [GO:0002020]; protein folding chaperone [GO:0044183]; ubiquitin protein ligase binding [GO:0031625] | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and S... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DMV9}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P0DMV9}. | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Mus musculus (Mouse) |
P17880 | GP_SEOUS | MWSLLLLAALVGQGFALKNVFDMRIQLPHSVNFGETSVSGYTEFPPLSLQEAEQLVPESSCNMDNHQSLSTINKLTKVIWRKKANQESANQNSFEVVESEVSFKGLCMLKHRMVEESYRNRRSVICYDLACNSTFCKPTVYMIVPIHACNMMKSCLIGLGPYRIQVVYERTYCTTGILTEGKCFVPDKAVVSALKRGMYAIASIETICFFIHQKGNTYKIVTAITSAMGSKCNNTDTKVQGYYICIIGGNSAPVYAPAGEDFRAMEVFSGIITSPHGEDHDLPGEEIATYQISGQIEAKIPHTVSSKNLKLTAFAGIPSY... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; signal transduction [GO:0007165]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host TRAF-mediated signal transduction [GO:0039527]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense ... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; host cell surface [GO:0044228]; membrane [GO:0016020]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF20682;PF01561;PF20679;PF01567;PF10538; | 1.10.8.1320; | Hantavirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is quickly cleaved in vivo just after synthesis, presumably by host signal peptidase. {ECO:0000250|UniProtKB:P08668}. | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein. Host cell surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum memb... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at the surface of the virion (By similarity). Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (By similarity). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity)... | Seoul virus (strain SR-11) (Sapporo rat virus) |
P17883 | SKI3_YEAST | MSDIKQLLKEAKQELTNRDYEETIEISEKVLKLDPDNYFAHIFLGKALSSLPASNNVSSNRNLERATNHYVSAAKLVPDNLLAWKGLFLLFRTTEVVPDILSYDEYFDLCGQYADALLKQEQSQVELINDIKLLKKTHPDCQKAFYQHLKPGSLMAETIGRHLSTPQDALLNLIKILSNIETTEIGKTLSQNRLKLKASDPDYQIKLNSFSWEIIKNSEIDQLYNQLVNILADDQKRSEIENQWLEYRIKVLKSMPLDVKKDFFTKVKEMVEDMVLVNHQSLLAWQKYFEWTDYEDLDNMDAPLIIKYFKKFPKDPLAMI... | null | null | defense response to virus [GO:0051607]; mRNA catabolic process [GO:0006402]; nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay [GO:0070478]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; nuclear-transcribed mRNA catabolic process, non-stop decay [... | nucleus [GO:0005634]; Ski complex [GO:0055087] | null | PF18833;PF13181; | 1.25.40.10; | SKI3 family | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | null | null | null | null | null | FUNCTION: Component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon. {ECO:0000269|PubMed:10744028, ECO:00002... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17886 | CRN_DROME | MERPQKMPKVAKVKNKAPAEVQITAEQLLREAKERDLEILPPPPKQKISDPAELADYQQRKRKTFEDNLRKNRMVVSHWIKYAQWEEQQQEIQRARSIWERALDNEHRNVTLWLKYAEMEMKNKQVNHARNLWDRAVTIMPRVNQFWYKYTYMEEMLENVAGARQVFERWMEWQPEEQAWQTYVNFELRYKEIDRAREIYERFVYVHPDVKNWIKFARFEESHGFIHGSRRVFERAVEFFGDDYIEERLFIAFARFEEGQKEHDRARIIYKYALDHLPKDRTQELFKAYTKHEKKYGDRAGIEDVIVSKRKYQYEQEVAA... | null | null | axon ensheathment [GO:0008366]; glial cell migration [GO:0008347]; Malpighian tubule morphogenesis [GO:0007443]; mRNA splicing, via spliceosome [GO:0000398]; oenocyte development [GO:0007438]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; spliceosomal complex assembly [GO:0000245] | catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; precatalytic spliceosome [GO:0071011]; Prp19 complex [GO:0000974]; U2-type catalytic step 2 spliceosome [GO:0071007] | RNA binding [GO:0003723] | PF02184; | 1.25.40.10; | Crooked-neck family | null | SUBCELLULAR LOCATION: Nucleus speckle. Note=Concentrated in nuclear speckles. | null | null | null | null | null | FUNCTION: May be involved in pre-mRNA splicing process (PubMed:12163015, PubMed:2044955). Involved in embryonic neurogenesis and cell rearrangement during Malpighian tubule morphogenesis (PubMed:10502111, PubMed:2044955). {ECO:0000269|PubMed:10502111, ECO:0000269|PubMed:12163015, ECO:0000269|PubMed:2044955}. | Drosophila melanogaster (Fruit fly) |
P17888 | PRIA_ECOLI | MPVAHVALPVPLPRTFDYLLPEGMTVKAGCRVRVPFGKQQERIGIVVSVSDASELPLNELKAVVEVLDSEPVFTHSVWRLLLWAADYYHHPIGDVLFHALPILLRQGRPAANAPMWYWFATEQGQAVDLNSLKRSPKQQQALAALRQGKIWRDQVATLEFNDAALQALRKKGLCDLASETPEFSDWRTNYAVSGERLRLNTEQATAVGAIHSAADTFSAWLLAGVTGSGKTEVYLSVLENVLAQGKQALVMVPEIGLTPQTIARFRERFNAPVEVLHSGLNDSERLSAWLKAKNGEAAIVIGTRSALFTPFKNLGVIVID... | 3.6.4.- | null | DNA recombination [GO:0006310]; DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA replication, synthesis of RNA primer [GO:0006269]; DNA unwinding involved in DNA replication [GO:0006268]; DNA-templated DNA replication [GO:0006261]; double-strand break repair [GO:0006302]; plasmid maintenance [... | DnaB-DnaC-DnaT-PriA-PriB complex [GO:1990158]; DnaB-DnaC-DnaT-PriA-PriC complex [GO:1990159]; primosome complex [GO:1990077] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]; zinc ion binding [GO:0008270] | PF00270;PF00271;PF21213;PF17764;PF18074;PF18319; | 3.40.50.300;3.40.1440.60; | Helicase family, PriA subfamily | null | null | null | null | null | null | null | FUNCTION: Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. Is also involved in ... | Escherichia coli (strain K12) |
P17890 | RPC7_YEAST | MSSYRGGSRGGGSNYMSNLPFGLGYGDVGKNHITEFPSIPLPINGPITNKERSLAVKYINFGKTVKDGPFYTGSMSLIIDQQENSKSGKRKPNIILDEDDTNDGIERYSDKYLKKRKIGISIDDHPYNLNLFPNELYNVMGINKKKLLAISKFNNADDVFTGTGLQDENIGLSMLAKLKELAEDVDDASTGDGAAKGSKTGEGEDDDLADDDFEEDEDEEDDDDYNAEKYFNNGDDDDYGDEEDPNEEAAF | null | null | termination of RNA polymerase III transcription [GO:0006386]; transcription by RNA polymerase III [GO:0006383]; transcription initiation at RNA polymerase III promoter [GO:0006384]; tRNA transcription by RNA polymerase III [GO:0042797] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase III complex [GO:0005666] | DNA binding [GO:0003677]; nucleotidyltransferase activity [GO:0016779] | PF11705; | null | Eukaryotic RPC7 RNA polymerase subunit family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. C31 is involved in the formation of the initiation complex. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17891 | CLC1_YEAST | MSEKFPPLEDQNIDFTPNDKKDDDTDFLKREAEILGDEFKTEQDDILETEASPAKDDDEIRDFEEQFPDINSANGAVSSDQNGSATVSSGNDNGEADDDFSTFEGANQSTESVKEDRSEVVDQWKQRRAVEIHEKDLKDEELKKELQDEAIKHIDDFYDSYNKKKEQQLEDAAKEAEAFLKKRDEFFGQDNTTWDRALQLINQDDADIIGGRDRSKLKEILLRLKGNAKAPGA | null | null | clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; endocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; positive regulation of endocytosis [GO:0045807]; protein-containing complex assembly [GO:0065003] | clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin complex [GO:0071439]; clathrin vesicle coat [GO:0030125]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | calmodulin binding [GO:0005516]; clathrin heavy chain binding [GO:0032050]; structural molecule activity [GO:0005198] | PF01086; | null | Clathrin light chain family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles. | null | null | null | null | null | FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. The yeast light chain is important for cell growth. The light chain may help to properly orient the asse... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17892 | LIPR2_MOUSE | MPMDVRGCLFPSVQMLLCWLVSLLLATVGGKEVCYGHLGCFSNDKPWAGMIQRPSKIFPWSPEDIDTRFLLYTNENPNNYQIISATDPATINASNFQLDRKTRFIIHGFIDKGEEGWLLDMCKKMFQVEKVNCICVDWKRGSRTEYTQASYNTRVVGAEIAFLVQVLSTEMGYSPENVHLIGHSLGSHVAGEAGRRLEGHVGRITGLDPAEPCFQGLPEEVRLDPSDAMFVDVIHTDSAPIIPYLGFGMSQKVGHLDFFPNGGKEMPGCQKNILSTIVDINGIWEGTRNFAACNHLRSYKYYASSILNPDGFLGYPCSSY... | 3.1.1.26; 3.1.1.3 | null | cellular defense response [GO:0006968]; galactolipid catabolic process [GO:0019376]; intestinal lipid catabolic process [GO:0044258]; phosphatidylcholine catabolic process [GO:0034638]; phospholipid catabolic process [GO:0009395]; phospholipid metabolic process [GO:0006644]; response to bacterium [GO:0009617]; triglyce... | extracellular space [GO:0005615]; neuron projection [GO:0043005]; zymogen granule membrane [GO:0042589] | 1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity [GO:0102549]; acylglycerol lipase activity [GO:0047372]; calcium ion binding [GO:0005509]; galactolipase activity [GO:0047714]; lipase activity [GO:0016298]; phospholipase activity [GO:0004620]; triglyceride lipase activity [GO:0004806] | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:... | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:21382969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:120... | null | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000250|UniProtKB:P54317}.; PATHWAY: Glycolipid metabolism. {ECO:0000250|UniProtKB:P54317}. | null | null | FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:21382969, PubMed:9813028). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (PubMed:9813028). Hydrolyzes short-, medium- and long-chain fatty... | Mus musculus (Mouse) |
P17896 | SP4B_BACSU | MPDNIRKAVGLILLVSLLSVGLCKPLKEYLLIPTQMRVFETQTQAIETSLSVNAQTSESSEAFTVKKDPHEIKVTGKKSGESELVYDLAGFPIKKTKVHVLPDLKVIPGGQSIGVKLHSVGVLVVGFHQINTSEGKKSPGETAGIEAGDIIIEMNGQKIEKMNDVAPFIQKAGKTGESLDLLIKRDKQKIKTKLIPEKDEGEGKYRIGLYIRDSAAGIGTMTFYEPKTKKYGALGHVISDMDTKKPIVVENGEIVKSTVTSIEKGTGGNPGEKLARFSSERKTIGDINRNSPFGIFGTLHQPIQNNISDQALPVAFSTEV... | 3.4.21.116 | null | proteolysis [GO:0006508]; sporulation resulting in formation of a cellular spore [GO:0030435] | null | serine-type peptidase activity [GO:0008236] | PF17820;PF05580; | 2.30.42.10; | null | null | SUBCELLULAR LOCATION: Forespore intermembrane space. | CATALYTIC ACTIVITY: Reaction=Self-cleaves 52-Val-|-Asn-53, 62-Ala-|-Phe-63 and 74-Val-|-Thr-75 at the N-terminus of SpoIVB.; EC=3.4.21.116; | null | null | null | null | FUNCTION: Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. Th... | Bacillus subtilis (strain 168) |
P17897 | LYZ1_MOUSE | MKALLTLGLLLLSVTAQAKVYNRCELARILKRNGMDGYRGVKLADWVCLAQHESNYNTRATNYNRGDRSTDYGIFQINSRYWCNDGKTPRSKNACGINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRTQCQNRDLSQYIRNCGV | 3.2.1.17 | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; Golgi cis cisterna [GO:0000137]; Golgi stack [GO:0005795]; microvillus [GO:0005902]; rough endoplasmic reticulum lumen [GO:0048237]; secretory granule [GO:0030141]; trans-Golgi network transport vesicle [GO:0030140] | hydrolase activity, acting on glycosyl bonds [GO:0016798]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; | null | null | null | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lyz1 is active against a range of Gram-positive and Gram-negative bacteria. Less effective than Lyz2 in killing Gram-negative bacteri... | Mus musculus (Mouse) |
P17898 | CPT1_YEAST | MGFFIPQSSLGNLKLYKYQSDDRSFLSNHVLRPFWRKFATIFPLWMAPNLVTLLGFCFIIFNVLTTLYYDPYFDQESPRWTYFSYAIGLFLYQTFDACDGMHARRTGQQGPLGELFDHCIDSINTTLSMIPVCSMTGMGYTYMTIFSQFAILCSFYLSTWEEYHTHKLYLAEFCGPVEGIIVLCISFIAVGIYGPQTIWHTKVAQFSWQDFVFDVETVHLMYAFCTGALIFNIVTAHTNVVRYYESQSTKSATPSKTAENISKAVNGLLPFFAYFSSIFTLVLIQPSFISLALILSIGFSVAFVVGRMIIAHLTMQPFPM... | 2.7.8.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1847919}; | CDP-choline pathway [GO:0006657] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; mitochondrial outer membrane [GO:0005741] | diacylglycerol cholinephosphotransferase activity [GO:0004142]; metal ion binding [GO:0046872] | PF01066; | 1.20.120.1760; | CDP-alcohol phosphatidyltransferase class-I family | null | SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:32939, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2; Evidence={ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919}... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for CDP-choline {ECO:0000269|PubMed:1847919}; KM=137 uM for CDP-dimethylethanolamine {ECO:0000269|PubMed:1847919}; Vmax=0.2 nmol/min/mg enzyme for CDP-choline {ECO:0000269|PubMed:1847919}; Vmax=0.07 nmol/min/mg enzyme for CDP-dimethylethanolamine {ECO:000026... | PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2. | null | null | FUNCTION: Catalyzes the final step in the CDP-choline route leading to phosphatidylcholin (PC). Preferentially uses CDP-monomethylethanolamine as aminoalcohol substrate. Shows highest activity toward di- and mono-unsaturated diacylglycerol species as lipid substrates. The CDP-choline pathway only contributes to net PC ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17900 | SAP3_HUMAN | MQSLMQAPLLIALGLLLAAPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKRLGCIKIAASLKGI | null | null | ganglioside catabolic process [GO:0006689]; glycosphingolipid catabolic process [GO:0046479]; learning or memory [GO:0007611]; lipid storage [GO:0019915]; lipid transport [GO:0006869]; maintenance of location in cell [GO:0051651]; neuromuscular process controlling balance [GO:0050885]; oligosaccharide catabolic process... | apical plasma membrane [GO:0016324]; azurophil granule lumen [GO:0035578]; basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; lysos... | beta-N-acetylgalactosaminidase activity [GO:0032428]; lipid transporter activity [GO:0005319]; phospholipase activator activity [GO:0016004]; sphingolipid activator protein activity [GO:0030290] | PF02221; | 2.70.220.10; | null | PTM: The serines in positions 32 and 33 are absent in 80% of the sequenced protein. | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:17552909}; | null | null | null | null | FUNCTION: The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2... | Homo sapiens (Human) |
P17904 | RSBW_BACSU | MKNNADYIEMKVPAQPEYVGIIRLTLSGVASRMGYTYDEIEDLKIAVSEACTNAVQHAYKEDKNGEVSIRFGVFEDRLEVIVADEGDSFDFDQKQQDLGPYTPSHTVDQLSEGGLGLYLMETLMDEVRVQNHSGVTVAMTKYLNGERVDHDTTIKNYETN | 2.7.11.1 | null | phosphorylation [GO:0016310] | null | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; sigma factor antagonist activity [GO:0016989] | PF13581; | 3.30.565.10; | Anti-sigma-factor family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). {ECO:0000269|PubMed:1592822, ECO:0000269|PubMed:8144... | Bacillus subtilis (strain 168) |
P17917 | PCNA_DROME | MFEARLGQATILKKILDAIKDLLNEATFDCSDSGIQLQAMDNSHVSLVSLTLRSDGFDKFRCDRNLSMGMNLGSMAKILKCANNEDNVTMKAQDNADTVTIMFESANQEKVSDYEMKLMNLDQEHLGIPETDFSCVVRMPAMEFARICRDLAQFSESVVICCTKEGVKFSASGDVGTANIKLAQTGSVDKEEEAVIIEMQEPVTLTFACRYLNAFTKATPLSTQVQLSMCADVPLVVEYAIKDLGHIRYYLAPKIEDNET | null | null | DNA damage response [GO:0006974]; DNA replication [GO:0006260]; DNA-templated DNA replication [GO:0006261]; eggshell chorion gene amplification [GO:0007307]; leading strand elongation [GO:0006272]; mismatch repair [GO:0006298]; mitotic spindle organization [GO:0007052]; nucleotide-excision repair [GO:0006289]; positive... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]; PCNA complex [GO:0043626] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA polymerase processivity factor activity [GO:0030337] | PF02747;PF00705; | 3.70.10.10; | PCNA family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17087725, ECO:0000269|PubMed:9310333}. Chromosome {ECO:0000269|PubMed:17087725}. Cytoplasm {ECO:0000269|PubMed:17087725}. Note=Colocalizes with crm in polytene nuclei during embryogenesis (PubMed:9310333). Increased association with chromatin in response to DNA damage c... | null | null | null | null | null | FUNCTION: Likely to be an auxiliary protein of DNA polymerase delta complex and is probably involved in the control of DNA replication and repair by increasing the polymerase's processibility. {ECO:0000269|PubMed:1360647}. | Drosophila melanogaster (Fruit fly) |
P17918 | PCNA_MOUSE | MFEARLIQGSILKKVLEALKDLINEACWDVSSGGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVIKMPSGEFARICRDLSHIGDAVVISCAKNGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVHLTFALRYLNFFTKATPLSPTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEAS | null | null | base-excision repair, gap-filling [GO:0006287]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to UV [GO:0034644]; cellular response to xenobiotic stimulus [GO:0071466]; epithelial cell differentiation [GO:0030855]; estrous cycle [GO:0044849]; heart development [GO:0007507]; leading strand elong... | centrosome [GO:0005813]; chromatin [GO:0000785]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; male germ cell nucleus [GO:0001673]; nuclear body [GO:0016604]; nuclear lamina [GO:0005652]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]; PCNA complex [GO:0043626]; PCNA-p21 complex [GO:0070... | chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; dinucleotide insertion or deletion binding [GO:0032139]; DNA polymerase binding [GO:0070182]; DNA polymerase processivity factor activity [GO:0030337]; enzyme binding [GO:0019899]; histone acetyltransferase binding [GO:0035035]; identical protein binding... | PF02747;PF00705; | 3.70.10.10; | PCNA family | PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to U... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24115439}. Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (By similarity). Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear ... | null | null | null | null | null | FUNCTION: Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimi... | Mus musculus (Mouse) |
P17919 | HXB1_MOUSE | MDYNRMSSFLEYPLCNRGPSAYSAPTSFPPCSAPAVDSYAGESRYGGGLPSSALQQNSGYPVQQPPSSLGVSFPSPAPSGYAPAACNPSYGPSQYYSVGQSEGDGSYFHPSSYGAQLGGLPDSYGAGGVGSGPYPPPQPPYGTEQTATFASAYDLLSEDKESPCSSEPSTLTPRTFDWMKVKRNPPKTAKVSELGLGAPGGLRTNFTTRQLTELEKEFHFNKYLSRARRVEIAATLELNETQVKIWFQNRRMKQKKREREGGRMPAGPPGCPKEAAGDASDQSACTSPEASPSSITS | null | null | anatomical structure formation involved in morphogenesis [GO:0048646]; anatomical structure morphogenesis [GO:0009653]; anterior/posterior pattern specification [GO:0009952]; embryonic skeletal system morphogenesis [GO:0048704]; facial nerve structural organization [GO:0021612]; facial nucleus development [GO:0021754];... | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein domain specific binding [GO:0019904]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:000... | PF00046; | 1.10.10.60; | Antp homeobox family, Labial subfamily | 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. Acts on the anterior body structures. | Mus musculus (Mouse) |
P17920 | MYOG_CHICK | MELFETNPYFFPEQRFYDGENFLGSRLQGYEAAAFPERPEVTLCPESRGALEEKDSTLPEHCPGQCLPWACKICKRKTVSIDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQSLLSSLNQQEREQRELRYRPAAPQPAAPSECGSGSSSCSPEWSTQLEFGTNPADHLLSDDQAEDRNLHSLSSIVESIAVEDVAVTFPEERVQN | null | null | cellular response to estradiol stimulus [GO:0071392]; muscle cell fate commitment [GO:0042693]; myoblast differentiation [GO:0045445]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of muscle atrophy [GO:0014737]; positive regulation of myoblast differentiation [GO:0045663]; posi... | nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription regulator complex [GO:0005667] | bHLH transcription factor binding [GO:0043425]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; identical protein binding [GO:0042802]; prote... | PF01586;PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein (By similarity). {ECO:0000250}. | Gallus gallus (Chicken) |
P17924 | NFIB_CHICK | MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEFREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQPGSPSHNDPAKNPPVYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGELPSQPYYHDMNSGINLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPNSPAAGSRTWHERDQDMSSPTMKKPEK... | null | null | anterior commissure morphogenesis [GO:0021960]; chondrocyte differentiation [GO:0002062]; club cell differentiation [GO:0060486]; commissural neuron axon guidance [GO:0071679]; DNA replication [GO:0006260]; glial cell differentiation [GO:0010001]; lung ciliated cell differentiation [GO:0061141]; negative regulation of ... | cerebellar mossy fiber [GO:0044300]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00859;PF03165;PF10524; | null | CTF/NF-I family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. | Gallus gallus (Chicken) |
P17927 | CR1_HUMAN | MGASSPRSPEPVGPPAPGLPFCCGGSLLAVVVLLALPVAWGQCNAPEWLPFARPTNLTDEFEFPIGTYLNYECRPGYSGRPFSIICLKNSVWTGAKDRCRRKSCRNPPDPVNGMVHVIKGIQFGSQIKYSCTKGYRLIGSSSATCIISGDTVIWDNETPICDRIPCGLPPTITNGDFISTNRENFHYGSVVTYRCNPGSGGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPDVLHAERTQRDKDNFSPGQ... | null | null | ATP export [GO:1904669]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; complement receptor mediated signaling pathway [GO:0002430]; immune complex clearance by erythrocytes [GO:0002435]; negative regulation of activation of membrane attack complex [GO:00... | cell surface [GO:0009986]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; ficolin-1-rich granule membrane [GO:0101003]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; secretory granule membrane [GO:0030667] | complement component C3b binding [GO:0001851]; complement component C3b receptor activity [GO:0004877]; complement component C4b binding [GO:0001855]; complement component C4b receptor activity [GO:0001861]; virus receptor activity [GO:0001618] | PF00084; | 2.10.70.10; | Receptors of complement activation (RCA) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1385479}; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Membrane immune adherence receptor that plays a critical role in the capture and clearance of complement-opsonized pathogens by erythrocytes and monocytes/macrophages (PubMed:2963069). Mediates the binding by these cells of particles and immune complexes that have activated complement to eliminate them from t... | Homo sapiens (Human) |
P17931 | LEG3_HUMAN | MADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYPGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSATGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI | null | null | eosinophil chemotaxis [GO:0048245]; epithelial cell differentiation [GO:0030855]; innate immune response [GO:0045087]; macrophage chemotaxis [GO:0048246]; monocyte chemotaxis [GO:0002548]; mononuclear cell migration [GO:0071674]; mRNA processing [GO:0006397]; negative regulation of endocytosis [GO:0045806]; negative re... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule membrane [GO:0101003]; immunological synapse [GO:0001772]; membr... | carbohydrate binding [GO:0030246]; chemoattractant activity [GO:0042056]; disaccharide binding [GO:0048030]; IgE binding [GO:0019863]; laminin binding [GO:0043236]; molecular condensate scaffold activity [GO:0140693]; protein phosphatase binding [GO:0019903]; protein phosphatase inhibitor activity [GO:0004864]; RNA bin... | PF00337; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32272059}. Nucleus. Secreted {ECO:0000269|PubMed:32272059}. Note=Secreted by a non-classical secretory pathway and associates with the cell surface. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it resul... | null | null | null | null | null | FUNCTION: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mR... | Homo sapiens (Human) |
P17935 | PA2HL_VIPAA | MRILWIVAVCLIGVEGSVIEFGKMIQEETDKNPLTSYSFYGCHCGLGNKGKPKDATDRCCFVHSCCYAKLPDCSPKTNRYEYHRENGAIVCGSSTPCKKQICECDRAAAICFRENLKTYNKKYKVYLRFKCKGVSEKC | null | null | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, S49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1765075, ECO:0000269|PubMed:2101000}. | null | null | null | null | null | FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic activity.Snake venom phospholipase A2 homolog that Is very active in inducing myonecrosis in vivo and shows a potent calcium-independent membrane-damaging activity in vitro, most probably by binding and incorporating in the membrane. Also acts as a pre... | Vipera ammodytes ammodytes (Western sand viper) |
P17936 | IBP3_HUMAN | MQRARPTLWAAALTLLVLLRGPPVARAGASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPLHSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHCYSMQSK | null | null | apoptotic process [GO:0006915]; MAPK cascade [GO:0000165]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of signal transduction [GO:0009968]; negative regulation of smooth muscle cell migration [GO:0014912]; negative r... | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; insulin-like growth factor binding protein complex [GO:0016942]; insulin-like growth factor ternary complex [GO:0042567]; nucleus [GO:0005634] | fibronectin binding [GO:0001968]; insulin-like growth factor binding [GO:0005520]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]; metal ion binding [GO:0046872]; protein tyrosine phosphatase activator activity [GO:0008160] | PF00219;PF00086; | 4.10.40.20;4.10.800.10; | null | PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20353938}. | null | null | null | null | null | FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediat... | Homo sapiens (Human) |
P17945 | HGF_RAT | MMWGTKLLPVLLLQHVLLHLLLLPVTIPYAEGQKKRRNTLHEFKKSAKTTLTKEDPLVKIKTKKVNSADECANRCIRNKGFPFTCKAFVFDKSRKRCYWYPFNSMSSGVKKGFGHEFDLYENKDYIRNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQCSEVECMTCNGESYRGPMDHTESGKTCQRWDQQTPHRHKFLPERYPDKGFDDNYCRNPDGKPRPWCYTLDPDTPWEYCAIKMCAHSAVNETDVPMETTECIKGQGEGYRGTTNT... | null | null | animal organ regeneration [GO:0031100]; cell chemotaxis [GO:0060326]; cell morphogenesis [GO:0000902]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; epithelial cell proliferation [GO:0050673]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; liver development [GO:0001889]; myobla... | extracellular space [GO:0005615] | chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF00051;PF00024;PF00089; | 3.50.4.10;2.40.20.10;2.40.10.10; | Peptidase S1 family, Plasminogen subfamily | PTM: The single-chain precursor undergoes proteolytic processing by TMPRSS13 resulting in an active two-chain form. {ECO:0000250|UniProtKB:P14210}. | null | null | null | null | null | null | FUNCTION: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types (By similarity). Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization (By similarity). Activa... | Rattus norvegicus (Rat) |
P17947 | SPI1_HUMAN | MLQACKMEGFPLVPPPSEDLVPYDTDLYQRQTHEYYPYLSSDGESHSDHYWDFHPHHVHSEFESFAENNFTELQSVQPPQLQQLYRHMELEQMHVLDTPMVPPHPSLGHQVSYLPRMCLQYPSLSPAQPSSDEEEGERQSPPLEVSDGEADGLEPGPGLLPGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRHPPH | null | null | defense response to tumor cell [GO:0002357]; endothelial to hematopoietic transition [GO:0098508]; interleukin-6-mediated signaling pathway [GO:0070102]; myeloid leukocyte differentiation [GO:0002573]; negative regulation of adipose tissue development [GO:1904178]; negative regulation of DNA-templated transcription [GO... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcripti... | PF00178; | 1.10.10.10; | ETS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:33951726}. | null | null | null | null | null | FUNCTION: Pioneer transcription factor, which controls hematopoietic cell fate by decompacting stem cell heterochromatin and allowing other transcription factors to enter otherwise inaccessible genomic sites. Once in open chromatin, can directly control gene expression by binding genetic regulatory elements and can als... | Homo sapiens (Human) |
P17948 | VGFR1_HUMAN | MVSYWDTGVLLCALLSCLLLTGSSSGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFK... | 2.7.10.1 | null | angiogenesis [GO:0001525]; blood vessel morphogenesis [GO:0048514]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; embryonic morphogenesis [GO:0048598]; hyaloid vascular plexus regression [GO:1990384]; monocyte chemotaxis [G... | actin cytoskeleton [GO:0015629]; endosome [GO:0005768]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; growth factor binding [GO:0019838]; placental growth factor receptor activity [GO:0036332]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; vascular endothelial growth factor receptor activity [GO:0005021] | PF07679;PF00047;PF13927;PF07714;PF21339;PF17988; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:10471394, ECO:0000269|PubMed:11513746}.; PTM: Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation. {ECO:0000269|PubMed:15001553}.; PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. o... | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. Endosome. Note=Autophosphorylation promotes ubiquitination and endocytosis.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:8248162}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted.; SUBCELLULAR LOCATION: [Isoform 4]: ... | 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 VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. Acts as a positive regulator... | Homo sapiens (Human) |
P17952 | MURC_ECOLI | MNTQQLAKLRSIVPEMRRVRHIHFVGIGGAGMGGIAEVLANEGYQISGSDLAPNPVTQQLMNLGATIYFNHRPENVRDASVVVVSSAISADNPEIVAAHEARIPVIRRAEMLAELMRFRHGIAIAGTHGKTTTTAMVSSIYAEAGLDPTFVNGGLVKAAGVHARLGHGRYLIAEADESDASFLHLQPMVAIVTNIEADHMDTYQGDFENLKQTFINFLHNLPFYGRAVMCVDDPVIRELLPRVGRQTTTYGFSEDADVRVEDYQQIGPQGHFTLLRQDKEPMRVTLNAPGRHNALNAAAAVAVATEEGIDDEAILRALES... | 6.3.2.8 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; UDP-N-acetylmuramate-L-alanine ligase activity [GO:0008763] | PF01225;PF02875;PF08245; | 3.90.190.20;3.40.1190.10;3.40.50.720; | MurCDEF family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidenc... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for UDP-N-acetyl-alpha-D-muramate {ECO:0000269|PubMed:7601127}; KM=20 uM for L-alanine {ECO:0000269|PubMed:7601127}; KM=450 uM for ATP {ECO:0000269|PubMed:7601127}; Vmax=17.3 umol/min/mg enzyme {ECO:0000269|PubMed:7601127}; | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.6. {ECO:0000269|PubMed:7601127}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:7601127}; | FUNCTION: Cell wall formation. {ECO:0000269|PubMed:7601127}. | Escherichia coli (strain K12) |
P17955 | NUP62_RAT | MSGFNFGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLATQTSTTQTPGFNFGTTPASGGTGFSLGISTPKLSLSSTAATPATANTGSFGLGSSTLTNAISGASTSSQGTAPTGFVFGSSTTSAPSTGTTGFSFTSGSASQPGASGFNIGSVGSLAQPTALSGSPFTPATLATTTAGATQPAAATPTAATTSAGSTLFASIAAAPASSSTTVLSLSAPATTAATPTAGTLGFSLKAPGAAPGASTTSTTTTTTTTTTTASTSSSTTTTGFALSLKPLVPAGPSSVAATALPASS... | null | null | cell surface receptor signaling pathway [GO:0007166]; cellular senescence [GO:0090398]; centriole assembly [GO:0098534]; centrosome cycle [GO:0007098]; mitotic centrosome separation [GO:0007100]; mitotic metaphase chromosome alignment [GO:0007080]; mRNA transport [GO:0051028]; negative regulation of apoptotic process [... | annulate lamellae [GO:0005642]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; Flemming body [GO:0090543]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore central transport channel [GO:0044613]; protein-containing complex [GO:0032991]... | Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; kinesin binding [GO:0019894]; nuclear thyroid hormone receptor binding [GO:0046966]; phospholipid binding [GO:0005543]; protein-containing complex binding [GO:0044877]; PTB domain binding [GO:0051425]; SH2 domain binding [GO:0042169]; signaling rec... | PF05064; | 1.20.5.170; | Nucleoporin NSP1/NUP62 family | PTM: The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:8707840}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Nucleus envelope {ECO:0000269|PubMed:2190987}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of... | null | null | null | null | null | FUNCTION: Essential component of the nuclear pore complex (PubMed:2190987, PubMed:8707840). The N-terminal is probably involved in nucleocytoplasmic transport (By similarity). The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may ... | Rattus norvegicus (Rat) |
P17967 | PDI_YEAST | MKFSAGAVLSWSSLLLASSVFAQQEAVAPEDSAVVKLATDSFNEYIQSHDLVLAEFFAPWCGHCKNMAPEYVKAAETLVEKNITLAQIDCTENQDLCMEHNIPGFPSLKIFKNSDVNNSIDYEGPRTAEAIVQFMIKQSQPAVAVVADLPAYLANETFVTPVIVQSGKIDADFNATFYSMANKHFNDYDFVSAENADDDFKLSIYLPSAMDEPVVYNGKKADIADADVFEKWLQVEALPYFGEIDGSVFAQYVESGLPLGYLFYNDEEELEEYKPLFTELAKKNRGLMNFVSIDARKFGRHAGNLNMKEQFPLFAIHDMT... | 5.3.4.1 | null | mannose trimming involved in glycoprotein ERAD pathway [GO:1904382]; positive regulation of endoplasmic reticulum unfolded protein response [GO:1900103]; protein alpha-1,2-demannosylation [GO:0036508]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976] | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; mannosyl-oligosaccharide 1,2-alpha-mannosidase complex [GO:0106055] | protein disulfide isomerase activity [GO:0003756]; protein-disulfide reductase activity [GO:0015035]; unfolded protein binding [GO:0051082] | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; | null | null | null | null | FUNCTION: Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17970 | KCNAB_DROME | MVGQLQGGQAAGQQQQQQQATQQQQHSKQQQQQQQQQQQQLQLKQHQQQQQDILYQQHNEAIAIARGLQAATPADIGDNQPYYDTSGNVDWERAMGAGGAGAYGGIGIGSLPAAGGAAYHLGPANPAGLVSRHLDYGDGGHLAGPSAGLPAGAVGSGAGAGAGAGASVTGSGSGAGTGTGTGAGSGSGSGAAGKEVRYAPFPVASPTHSIPTTSQQIVGSVGGVGVGGASSQSISGGVPTHSQSNTTGALQRTHSRSMSSIPPPEPFMIAQSKAVNSRVSINVGGVRHEVLWRTLERLPHTRLGRLRECTTHEAIVELCD... | null | null | action potential [GO:0001508]; chemical synaptic transmission [GO:0007268]; larval locomotory behavior [GO:0008345]; positive regulation of circadian sleep/wake cycle, sleep [GO:0045938]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; ... | plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251]; voltage-gated potassium channel activity [GO:0005249] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, B (Shab) (TC 1.A.1.2) subfamily, Shab sub-subfamily | null | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gr... | Drosophila melanogaster (Fruit fly) |
P17971 | KCNAL_DROME | MASVAAWLPFARAAAIGWVPIATHPLPPPPMPKDRRKTDDEKLLINVSGRRFETWRNTLEKYPDTLLGSNEREFFYDEDCKEYFFDRDPDIFRHILNYYRTGKLHYPKHECLTSYDEELAFFGIMPDVIGDCCYEDYRDRKRENAERLMDDKLSENGDQNLQQLTNMRQKMWRAFENPHTSTSALVFYYVTGFFIAVSVMANVVETVPCGHRPGRAGTLPCGERYKIVFFCLDTACVMIFTAEYLLRLFAAPDRCKFVRSVMSIIDVVAIMPYYIGLGITDNDDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSC... | null | null | associative learning [GO:0008306]; chemical synaptic transmission [GO:0007268]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260] | dendritic spine [GO:0043197]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; voltage-gated potassium channel complex [GO:0008076] | A-type (transient outward) potassium channel activity [GO:0005250]; voltage-gated potassium channel activity [GO:0005249] | PF02214;PF11879;PF00520;PF11601; | 1.10.287.70;1.20.120.350; | Potassium channel family, D (Shal) (TC 1.A.1.2) subfamily, Shal sub-subfamily | null | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell projection, dendrite. Perikaryon. | null | null | null | null | null | FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gr... | Drosophila melanogaster (Fruit fly) |
P17977 | CATG_RAT | MQPLLFLLIFVLFQEDEAGKIIGGREARPNSHPYMAFLLIQSPEGLSACGGFLVREDFVLTAGHCFGSSINVTLGAHNIRRQEGTQQHITVLRAIRHPDYNPPPVIQNDIMLLQLRSRARRSRAVKPVALPQATKRVQPGALCTVAGWGLVSQRRGTNVLQEVKLRVQTDQTCANRFQFYNSQTQICVGNPRERKSAFKGDSGGPLVCNNVAQGIVSYGSSSGNPPAVFTRIQSFMPWIKRTMRRLSSRY | 3.4.21.20 | null | biofilm matrix disassembly [GO:0098786]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; monocyte chemotaxis [GO:0002548]; negative regulation of T cell activation [GO:0050868]; neutrophil activation [GO:0042119... | cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; extracellular space [GO:0005615]; lysosome [GO:0005764]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; secretory granule [GO:0030141] | caspase binding [GO:0089720]; heparin binding [GO:0008201]; peptidase activity [GO:0008233]; receptor ligand activity [GO:0048018]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08311}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic granule {ECO:0000250|UniProtKB:P08311}. Secreted {ECO:0000250|UniProtKB:P08311}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P08311}. Lysosome {ECO:0000250|UniProtKB:P08311}. Nucleus {ECO:0000250|Uni... | CATALYTIC ACTIVITY: Reaction=Specificity similar to chymotrypsin C.; EC=3.4.21.20; Evidence={ECO:0000250|UniProtKB:P08311}; | null | null | null | null | FUNCTION: Serine protease with trypsin- and chymotrypsin-like specificity. Also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity. Prefers Phe and Tyr residues in the P1 position of substrates but also cleaves efficiently after Trp and Leu. Shows a pre... | Rattus norvegicus (Rat) |
P17978 | VGB_STAAU | MEFKLQELNLTNQDTGPYGITVSDKGKVWITQHKANMISCINLDGKITEYPLPTPDAKVMCLTISSDGEVWFTENAANKIGRITKKGIIKEYTLPNPDSAPYGITEGPNGDIWFTEMNGNRIGRITDDGKIREYELPNKGSYPSFITLGSDNALWFTENQNNAIGRITESGDITEFKIPTPASGPVGITKGNDDALWFVEIIGNKIGRITPLGEITEFKIPTPNARPHAITAGAGIDLWFTEWGANKIGRLTSNNIIEEYPIQIKSGEPHGICFDGETIWFAMECDKIGKLTLIKDNME | 4.2.99.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11467949}; | antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677] | outer membrane-bounded periplasmic space [GO:0030288] | carbon-oxygen lyase activity [GO:0016835]; magnesium ion binding [GO:0000287] | null | 2.130.10.10; | Vgb family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for quinupristin {ECO:0000269|PubMed:11467949, ECO:0000269|PubMed:17563376}; KM=19 uM for pristinamycin IA {ECO:0000269|PubMed:11467949, ECO:0000269|PubMed:17563376}; KM=0.19 mM for magnesium {ECO:0000269|PubMed:11467949, ECO:0000269|PubMed:17563376}; | null | null | null | FUNCTION: Inactivates the type B streptogramin antibiotics by linearizing the lactone ring at the ester linkage, generating a free phenylglycine carboxylate and converting the threonyl moiety into 2-amino-butenoic acid. {ECO:0000269|PubMed:11467949}. | Staphylococcus aureus |
P17980 | PRS6A_HUMAN | MNLLPNIESPVTRQEKMATVWDEAEQDGIGEEVLKMSTEEIIQRTRLLDSEIKIMKSEVLRVTHELQAMKDKIKENSEKIKVNKTLPYLVSNVIELLDVDPNDQEEDGANIDLDSQRKGKCAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGF... | null | null | modulation by host of viral transcription [GO:0043921]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161] | cytosol [GO:0005829]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; proteasome-activating activity [GO:0036402] | PF00004;PF17862;PF16450; | 1.10.8.60;2.40.50.140;3.40.50.300; | AAA ATPase family | PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli. {ECO:0000269|PubMed:17709345}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Colocalizes with TRIM5 in the cytoplasmic bodies. {ECO:0000250|UniProtKB:O88685}. | null | null | null | null | null | FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose ... | Homo sapiens (Human) |
P17981 | NAR2A_MOUSE | MPSNNFKFFLTWWLTQQVTGLAVPFMLDMAPNAFDDQYEGCVEDMEKKAPQLLQEDFNMNEELKLEWEKAEIKWKEIKNCMSYPAGFHDFHGTALVAYTGNIHRSLNEATREFKINPGNFHYKAFHYYLTRALQLLSDQGCRSVYRGTNVRFRYTGKGSVRFGHFASSSLNRSVATSSPFFNGQGTLFIIKTCLGAHIKHCSYYTHEEEVLIPGYEVFHKVKTQSVERYIQISLDSPKRKKSNFNCFYSGSTQAANVSSLGSRESCVSLFLVVLLGLLVQQLTLAEP | 2.4.2.31; 3.2.2.5 | null | NAD catabolic process [GO:0019677] | external side of plasma membrane [GO:0009897] | hydrolase activity, acting on glycosyl bonds [GO:0016798]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; nucleotidyltransferase activity [GO:001... | PF01129; | null | Arg-specific ADP-ribosyltransferase family | PTM: It is proposed that in the absence of reducing agents, a disulfide bond is formed between Cys-80 and Cys-201, leading to a conformational change that reduces the catalytic rate of NAD glycohydrolysis. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; EC=2.4.2.31; Evidence={ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 mM for NAD for the NADase activity (in the presence of 0.03 mM DTT) {ECO:0000269|PubMed:11011142}; KM=0.41 mM for NAD for the NADase activity (in the presence of 2 mM DTT) {ECO:0000269|PubMed:11011142}; KM=0.5 mM for NAD for the ADP-ribosyltransferase activity... | null | null | null | FUNCTION: Has both ADP-ribosyltransferase activity and thiol-dependent NAD(+) glycohydrolase activity. {ECO:0000269|PubMed:11011142, ECO:0000269|PubMed:9300695}. | Mus musculus (Mouse) |
P17982 | NAR2A_RAT | MPSNICKFFLTWWLIQQVTGLTGPLMLDTAPNAFDDQYEGCVNKMEEKAPLLLKEDFNKSEKLKVAWEEAKKRWNNIKPSMSYPKGFNDFHGTALVAYTGSIGVDFNRAVREFKENPGQFHYKAFHYYLTRALQLLSNGDCHSVYRGTKTRFHYTGAGSVRFGQFTSSSLSKTVAQSPEFFSDDGTLFIIKTCLGVYIKEFSFYPDQEEVLIPGYEVYQKVRTQGYNEIFLDSPKRKKSNYNCLYSSAGTRESCVSLFLVVLTSLLVQLLCLAEP | 2.4.2.31; 3.2.2.5 | null | NAD catabolic process [GO:0019677] | external side of plasma membrane [GO:0009897] | hydrolase activity, acting on glycosyl bonds [GO:0016798]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; nucleotidyltransferase activity [GO:001... | PF01129; | null | Arg-specific ADP-ribosyltransferase family | null | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; EC=2.4.2.31; Evidence={ECO:000... | null | null | null | null | FUNCTION: Has NAD(+) glycohydrolase activity and extremely low ADP-ribosyltransferase activity. | Rattus norvegicus (Rat) |
P17987 | TCPA_HUMAN | MEGPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIA... | null | null | binding of sperm to zona pellucida [GO:0007339]; chaperone-mediated protein folding [GO:0061077]; positive regulation of establishment of protein localization to telomere [GO:1904851]; positive regulation of protein localization to Cajal body [GO:1904871]; positive regulation of telomerase activity [GO:0051973]; positi... | acrosomal vesicle [GO:0001669]; cell body [GO:0044297]; centrosome [GO:0005813]; chaperonin-containing T-complex [GO:0005832]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; heterochromatin [GO:0000792]; microtubule [GO:0005874]; pericentriolar material [GO:0000242]; zona pelluc... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; protein folding chaperone [GO:0044183]; RNA binding [GO:0003723]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | TCP-1 chaperonin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1630492}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. | null | null | null | null | null | FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may p... | Homo sapiens (Human) |
P17988 | ST1A1_RAT | MEFSRPPLVHVKGIPLIKYFAETIGPLQNFTAWPDDLLISTYPKSGTTWMSEILDMIYQGGKLEKCGRAPIYARVPFLEFKCPGVPSGLETLEETPAPRLLKTHLPLSLLPQSLLDQKVKVIYIARNAKDVVVSYYNFYNMAKLHPDPGTWDSFLENFMDGEVSYGSWYQHVKEWWELRHTHPVLYLFYEDIKENPKREIKKILEFLGRSLPEETVDSIVHHTSFKKMKENCMTNYTTIPTEIMDHNVSPFMRKGTTGDWKNTFTVAQNERFDAHYAKTMTDCDFKFRCEL | 2.8.2.1 | null | 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; 4-nitrophenol metabolic process [GO:0018960]; catecholamine metabolic process [GO:0006584]; estrogen metabolic process [GO:0008210]; ethanol catabolic process [GO:0006068]; flavonoid metabolic process [GO:0009812]; regulation of blood pressure [GO:00... | cytoplasm [GO:0005737] | 3'-phosphoadenosine 5'-phosphosulfate binding [GO:0050656]; aryl sulfotransferase activity [GO:0004062]; flavonol 3-sulfotransferase activity [GO:0047894]; identical protein binding [GO:0042802]; steroid sulfotransferase activity [GO:0050294]; sulfotransferase activity [GO:0008146] | PF00685; | 3.40.50.300; | Sulfotransferase 1 family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1513323}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; Evidence={ECO:0000269|PubMed:1513323, ECO:0000269|PubMed:7889867, ... | null | null | null | null | FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it c... | Rattus norvegicus (Rat) |
P17993 | UBIG_ECOLI | MNAEKSPVNHNVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMAVVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNYMLHTQNK | 2.1.1.222; 2.1.1.64 | null | hyperosmotic salinity response [GO:0042538]; methylation [GO:0032259]; ubiquinone biosynthetic process [GO:0006744] | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; ubiquinone biosynthesis complex [GO:0110142] | 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase activity [GO:0043431]; 2-polyprenyl-6-hydroxyphenol methylase activity [GO:0102208]; 2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity [GO:0008425]; 3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity [GO:00104... | PF13489; | 3.40.50.150; | Methyltransferase superfamily, UbiG/COQ3 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30686758}. | CATALYTIC ACTIVITY: Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378, ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:000025... | null | PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00472}. | null | null | FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-Rule:MF_00472, ECO:0000269|PubMed:10419476}. | Escherichia coli (strain K12) |
P18011 | SCTE_SHIFL | MHNVSTTTTGFPLAKILTSTELGDNTIQAANDAANKLFSLTIADLTANQNINTTNAHSTSNILIPELKAPKSLNASSQLTLLIGNLIQILGEKSLTALTNKITAWKSQQQARQQKNLEFSDKINTLLSETEGLTRDYEKQINKLKNADSKIKDLENKINQIQTRLSELDPESPEKKKLSREEIQLTIKKDAAVKDRTLIEQKTLSIHSKLTDKSMQLEKEIDSFSAFSNTASAEQLSTQQKSLTGLASVTQLMATFIQLVGKNNEESLKNDLALFQSLQESRKTEMERKSDEYAAEVRKAEELNRVMGCVGKILGALLTI... | null | null | null | extracellular region [GO:0005576]; host cell [GO:0043657]; host cell membrane [GO:0033644]; host cell nucleus [GO:0042025]; membrane [GO:0016020] | null | PF04888;PF16535; | 1.20.120.330; | SctE/SipB/YopB family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10545510, ECO:0000269|PubMed:17719540, ECO:0000269|PubMed:7954817, ECO:0000269|PubMed:9009343}. Host membrane {ECO:0000269|PubMed:10545510, ECO:0000269|PubMed:34809452}; Multi-pass membrane protein {ECO:0000269|PubMed:34809452}. Host cell {ECO:0000269|PubMed:9009343}. ... | null | null | null | null | null | FUNCTION: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:10545510, PubMed:17367391). IpaB/SctE and IpaC/SctB are inserted into the host membrane where they form a pore and allow the translocation of effec... | Shigella flexneri |
P18012 | SCTB_SHIFL | MEIQNTKPTQTLYTDISTKQTQSSSETQKSQNYQQIAAHIPLNVGKNPVLTTTLNDDQLLKLSEQVQHDSEIIARLTDKKMKDLSEMSHTLTPENTLDISSLSSNAVSLIISVAVLLSALRTAETKLGSQLSLIAFDATKSAAENIVRQGLAALSSSITGAVTQVGITGIGAKKTHSGISDQKGALRKNLATAQSLEKELAGSKLGLNKQIDTNITSPQTNSSTKFLGKNKLAPDNISLSTEHKTSLSSPDISLQDKIDTQRRTYELNTLSAQQKQNIGRATMETSAVAGNISTSGGRYASALEEEEQLISQASSKQAEE... | null | null | null | extracellular region [GO:0005576]; host cell membrane [GO:0033644]; membrane [GO:0016020] | null | PF09599; | null | SctB/SipC family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10545510, ECO:0000269|PubMed:7954817, ECO:0000269|PubMed:9001387}. Host membrane {ECO:0000269|PubMed:10545510, ECO:0000305|PubMed:9001387}; Single-pass membrane protein {ECO:0000255}. Note=Secreted via the type III secretion system (T3SS) (PubMed:10545510). Localizes a... | null | null | null | null | null | FUNCTION: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:10545510, PubMed:17367391). IpaB/SctE and IpaC/SctB are inserted into the host membrane where they form a pore and allow the translocation of effec... | Shigella flexneri |
P18014 | IPA7_SHIFL | MFSVNNTHSSVSCSPSINSNSTSNEHYLRILTEWEKNSSPGEERGIAFNRLSQCFQNQEAVLNLSDLNLTSLPELPKHISALIVENNKLTSLPKLPAFLKELNADNNRLSVIPELPESLTTLSVRSNQLENLPVLPNHLTSLFVENNRLYNLPALPEKLKFLHVYYNRLTTLPDLPDKLEILCAQRNNLVTFPQFSDRNNIRQKEYYFHFNQITTLPESFSQLDSSYRINISGNPLSTRVLQSLQRLTSSPDYHGPQIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSAR... | 2.3.2.27 | null | effector-mediated activation of programmed cell death in host [GO:0034055]; protein ubiquitination [GO:0016567]; symbiont-mediated suppression of host programmed cell death [GO:0052041]; ubiquitin-dependent protein catabolic process [GO:0006511] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430] | ubiquitin protein ligase activity [GO:0061630] | PF14496;PF12468; | 1.20.58.90;3.80.10.10;1.20.58.360;1.20.1270.130; | LRR-containing bacterial E3 ligase family | PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin. {ECO:0000250|UniProtKB:D0ZPH9}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:D0ZVG2}. Host cytoplasm {ECO:0000250|UniProtKB:D0ZVG2}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000250|UniProtKB:D0ZVG2}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:30872533, ECO:0000269|PubMed:34022140, ECO:0000269|PubMed:344922... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:30872533, ECO:0000269|PubMed:34022140, ECO:0000269|PubMed:34492225, ECO:0000269|PubMed:36599845, ECO:0000269|PubMed:36991122, ECO:0000269|PubMed:36991125}. | null | null | FUNCTION: E3 ubiquitin ligase effector protein that interferes with host's innate immunity (PubMed:30872533, PubMed:34022140, PubMed:34492225, PubMed:36599845, PubMed:36991122, PubMed:36991125). Functions to alter host cell physiology and promote bacterial survival in host tissues (PubMed:30872533, PubMed:34022140, Pub... | Shigella flexneri |
P18031 | PTN1_HUMAN | MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPH... | 3.1.3.48 | null | actin cytoskeleton organization [GO:0030036]; cellular response to unfolded protein [GO:0034620]; endoplasmic reticulum unfolded protein response [GO:0030968]; growth hormone receptor signaling pathway via JAK-STAT [GO:0060397]; insulin receptor recycling [GO:0038020]; insulin receptor signaling pathway [GO:0008286]; I... | cytoplasm [GO:0005737]; cytoplasmic side of endoplasmic reticulum membrane [GO:0098554]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endosome lumen [GO:0031904]; mitochondrial crista [GO:0030061]; mitochondrial matrix [GO:0005759]; protein-containing complex [GO:0032991]; sort... | cadherin binding [GO:0045296]; enzyme binding [GO:0019899]; ephrin receptor binding [GO:0046875]; insulin receptor binding [GO:0005158]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; protein kinase binding [GO:0019901]; protein phosphatase 2A binding [GO:0051721]; protein tyrosine phosphatas... | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class 1 subfamily | PTM: Oxidized on Cys-215; the Cys-SOH formed in response to redox signaling reacts with the alpha-amido of the following residue to form a sulfenamide cross-link, triggering a conformational change that inhibits substrate binding and activity. The active site can be restored by reduction. {ECO:0000269|PubMed:12802338, ... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1739967, ECO:0000269|PubMed:21135139}; Peripheral membrane protein {ECO:0000269|PubMed:1739967, ECO:0000269|PubMed:21135139}; Cytoplasmic side {ECO:0000269|PubMed:1739967, ECO:0000269|PubMed:21135139}. Note=Interacts with EPHA3 at the cell membran... | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate t... | Homo sapiens (Human) |
P18040 | ENV_HV2G1 | MCGKSLLCVASLLASAYLVYCTQYVTVFYGVPVWRNASIPLFCATKNRDTWGTIQCKPDNDDYQEITLNVTEAFDAWDNTVTEQAVEDVWSLFETSIKPCVKLTPLCVAMSCNSTTNNTTTTGSTTGMSEINETSPSYSDNCTGLGKEEIVNCQFYMTGLERDKKKQYNETWYSKDVVCESNNTKDGKNRCYMNHCNTSVITESCDKHYWDAIKFRYCAPPGYALLRCNDTNYSGFEPKCSKVVASTCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLSIHCKRPGNKTVVPITLMSGLVFHSQPI... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy a... | Human immunodeficiency virus type 2 subtype A (isolate Ghana-1) (HIV-2) |
P18041 | GAG_HV2G1 | MGARNSVLRGKKADELEKIRLRPSGKKKYRLKHIVWAANELDKFGLAESLLESKEGCQKILTVLDPLVPTGSENLKSLFNTVCVIWCLHAEEKVKDTEEAKKLVQRHLGAETGTAEKMPSTSRPTAPPSGRGRNFPVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADWDAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWM... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate Ghana-1) (HIV-2) |
P18042 | POL_HV2G1 | MGARNSVLRGKKADELEKIRLRPSGKKKYRLKHIVWAANELDKFGLAESLLESKEGCQKILTVLDPLVPTGSENLKSLFNTVCVIWCLHAEEKVKDTEEAKKLVQRHLGAETGTAEKMPSTSRPTAPPSGRGRNFPVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADWDAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWM... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immun... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate Ghana-1) (HIV-2) |
P18052 | PTPRA_MOUSE | MDSWFILVLFGSGLIHVSANNATTVSPSLGTTRLIKTSTTELAKEENKTSNSTSSVISLSVAPTFSPNLTLEPTYVTTVNSSHSDNGTRRAASTESGGTTISPNGSWLIENQFTDAITEPWEGNSSTAATTPETFPPADETPIIAVMVALSSLLVIVFIIIVLYMLRFKKYKQAGSHSNSFRLSNGRTEDVEPQSVPLLARSPSTNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPFLSLAVSKDAVKALNKTTPLLERRFIGKSNSRGCLSDDHSRVHLTPVEGVPDS... | 3.1.3.48 | null | dephosphorylation [GO:0016311]; insulin receptor signaling pathway [GO:0008286]; integrin-mediated signaling pathway [GO:0007229]; modulation of chemical synaptic transmission [GO:0050804]; positive regulation of oligodendrocyte differentiation [GO:0048714]; regulation of focal adhesion assembly [GO:0051893] | focal adhesion [GO:0005925]; membrane [GO:0016020]; receptor complex [GO:0043235]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic membrane [GO:0097060] | protein tyrosine phosphatase activity [GO:0004725]; protein-containing complex binding [GO:0044877] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 4 subfamily | PTM: Integrin binding to extracellular matrix induces phosphorylation at Tyr-825 which induces PTPRA localization and recruitment of BCAR3, BCAR1 and CRK to focal adhesions. {ECO:0000269|PubMed:22801373}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22801373}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000269|PubMed:22801373}. Note=Localizes to focal adhesion sites following integrin engagement. {ECO:0000269|PubMed:22801373}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Tyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation (PubMed:22801373). Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GT... | Mus musculus (Mouse) |
P18054 | LOX12_HUMAN | MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQP... | 1.13.11.-; 1.13.11.31; 1.13.11.33; 3.3.2.- | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 1 Fe cation per subunit.; | arachidonic acid metabolic process [GO:0019369]; establishment of skin barrier [GO:0061436]; fatty acid oxidation [GO:0019395]; hepoxilin biosynthetic process [GO:0051122]; leukotriene A4 metabolic process [GO:1901751]; linoleic acid metabolic process [GO:0043651]; lipid metabolic process [GO:0006629]; lipid oxidation ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; sarcolemma [GO:0042383] | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; hepoxilin-epoxide hydrolase activity [GO:0047977]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane. Note=Membrane association is stimulated by EGF. | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444; EC=1.13.11.31; Evidence={ECO:0000269|PubMed:17493578, ECO:0000269|PubMed:22984144, ECO:0000269|PubMed:24282679, ECO:00... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for arachidonate (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:1851637}; KM=10 uM for arachidonate (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:8319693}; KM=6.2 uM for arachidonate (at pH 7.4) {ECO:0000269|PubMed:8250832}; KM=9 uM for linole... | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:1851637}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0 (for arachidonate 12-lipoxygenase activity). {ECO:0000269|PubMed:8250832, ECO:0000269|PubMed:8319693}; | null | FUNCTION: Catalyzes the regio and stereo-specific incorporation of molecular oxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:17493578, PubMed:18311922, PubMed:1851637, PubMed:32404334, PubMed:8319693, Pu... | Homo sapiens (Human) |
P18064 | GPA1_ARATH | MGLLCSRSRHHTEDTDENTQAAEIERRIEQEAKAEKHIRKLLLLGAGESGKSTIFKQIKLLFQTGFDEGELKSYVPVIHANVYQTIKLLHDGTKEFAQNETDSAKYMLSSESIAIGEKLSEIGGRLDYPRLTKDIAEGIETLWKDPAIQETCARGNELQVPDCTKYLMENLKRLSDINYIPTKEDVLYARVRTTGVVEIQFSPVGENKKSGEVYRLFDVGGQRNERRKWIHLFEGVTAVIFCAAISEYDQTLFEDEQKNRMMETKELFDWVLKQPCFEKTSFMLFLNKFDIFEKKVLDVPLNVCEWFRDYQPVSSGKQEI... | null | null | abscisic acid-activated signaling pathway [GO:0009738]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; blue light signaling pathway [GO:0009785]; cell death [GO:0008219]; G protein-coupled receptor signaling pathway [GO:0007186]; gibberellic acid mediated signaling pathway [GO:0... | endoplasmic reticulum membrane [GO:0005789]; heterotrimeric G-protein complex [GO:0005834]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506] | channel regulator activity [GO:0016247]; G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; GTPase binding [GO:0051020]; GTPase inhibitor activity [GO:0005095]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14500984, ECO:0000269|PubMed:17158913}. | null | null | null | null | null | FUNCTION: Exhibits a fast rate of basal nucleotide exchange. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Together with GCR1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipas... | Arabidopsis thaliana (Mouse-ear cress) |
P18065 | IBP2_HUMAN | MLPRVGCPALPLPPPPLLPLLLLLLGASGGGGGARAEVLFRCPPCTPERLAACGPPPVAPPAAVAAVAGGARMPCAELVREPGCGCCSVCARLEGEACGVYTPRCGQGLRCYPHPGSELPLQALVMGEGTCEKRRDAEYGASPEQVADNGDDHSEGGLVENHVDSTMNMLGGGGSAGRKPLKSGMKELAVFREKVTEQHRQMGKGGKHHLGLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDERGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKLIQGAPTIRGDPECHLFYNEQQEARGVH... | null | null | cellular response to hormone stimulus [GO:0032870]; female pregnancy [GO:0007565]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of activated T cell proliferation [GO:0042104]; regulation of insulin-like growth factor receptor signaling pathway [GO:0043567]; response to estrad... | apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]; signaling receptor binding [GO:0005102] | PF00219;PF00086; | 4.10.40.20;4.10.800.10; | null | PTM: O-glycosylated. {ECO:0000269|PubMed:1726837}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibits IGF-mediated growth and developmental rates. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. {ECO:0000269|PubMed:19... | Homo sapiens (Human) |
P18066 | RAB5A_CANLF | MANRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFARAKNWVKELQRQASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTSMNVNEIFMAIAKKLPKNEPQNPGANSARGRGVDLTEPTQPTRSQCCSN | 3.6.5.2 | null | amyloid-beta clearance by transcytosis [GO:0150093]; canonical Wnt signaling pathway [GO:0060070]; early endosome to late endosome transport [GO:0045022]; endocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; modulation by host of viral process [GO:0044788]; phagocytosis [GO:0006909]; positive regulat... | actin cytoskeleton [GO:0015629]; axon [GO:0030424]; cytoplasmic side of early endosome membrane [GO:0098559]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome [GO:0005769]; early phagosome [GO:0032009]; endomembrane system [GO:0012505]; exocytic vesicle [GO:0070382]; Golgi apparatus [GO:0005794]; lipid dropl... | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including RAB GDP dissociation inhibitors GDI1 and GDI2. {ECO:0000250|UniProtKB:P20339}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2115402}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:2115402}. Early endosome membrane {ECO:0000269|PubMed:2115402}; Lipid-anchor {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:P20339}. Cytoplasmic vesicle {ECO:0000269|PubMed:2115402}. Cell... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P20339}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Active GTP-bound... | Canis lupus familiaris (Dog) (Canis familiaris) |
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