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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P06214 | HEM2_RAT | MHHQSVLHSGYFHPLLRAWQTTPSTVSATNLIYPIFVTDVPDDVQPIASLPGVARYGVNQLEEMLRPLVEAGLRCVLIFGVPSRVPKDEQGSAADSEDSPTIEAVRLLRKTFPTLLVACDVCLCPYTSHGHCGLLSENGAFLAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKAALLKHGLGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVARDIQEGADILMVKPGLPYLDMVQEVKDKHPELPLAVYQVSGEFAMLWHGAKAGAFDLRTAVLESMTAFRRAGADIIITYFA... | 4.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 8 zinc ions per octamer. Requires four zinc ions per octamer for full catalytic activity. Can bind up to 2 zinc ions per subunit. {ECO:0000250}; | cellular response to interleukin-4 [GO:0071353]; cellular response to lead ion [GO:0071284]; heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; negative regulation of proteasomal protein catabolic process ... | cytosol [GO:0005829]; extracellular space [GO:0005615] | identical protein binding [GO:0042802]; porphobilinogen synthase activity [GO:0004655]; proteasome core complex binding [GO:1904854]; zinc ion binding [GO:0008270] | PF00490; | 3.20.20.70; | ALAD family | null | null | CATALYTIC ACTIVITY: Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. | null | null | FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
P06229 | FEN_BPT5 | MSKSWGKFIEEEEAEMASRRNLMIVDGTNLGFRFKHNNSKKPFASSYVSTIQSLAKSYSARTTIVLGDKGKSVFRLEHLPEYKGNRDEKYAQRTEEEKALDEQFFEYLKDAFELCKTTFPTFTIRGVEADDMAAYIVKLIGHLYDHVWLISTDGDWDTLLTDKVSRFSFTTRREYHLRDMYEHHNVDDVEQFISLKAIMGDLGDNIRGVEGIGAKRGYNIIREFGNVLDIIDQLPLPGKQKYIQNLNASEELLFRNLILVDLPTYCVDAIAAVGQDVLDKFTKDILEIAEQ | 3.1.11.-; 3.1.11.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:12606565, ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516}; Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:27273516}; Note=Binds divalent metal cations,... | DNA replication, Okazaki fragment processing [GO:0033567]; late viral transcription [GO:0019086]; viral DNA genome replication [GO:0039693] | viral replication complex [GO:0019034] | 5'-3' DNA exonuclease activity [GO:0035312]; 5'-3' exonuclease activity [GO:0008409]; 5'-flap endonuclease activity [GO:0017108]; DNA binding [GO:0003677]; DNA exonuclease activity [GO:0004529]; double-stranded DNA 5'-3' DNA exonuclease activity [GO:0051908]; double-stranded DNA endonuclease activity [GO:1990238]; meta... | PF01367;PF02739; | 1.10.150.20;3.40.50.1010; | null | null | null | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.3; Evidence={ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:10364212, ECO:0000269|PubMed:17559871, ECO:0000269|PubMed:2211703, ECO:0000269|PubMed:27273516, ECO:0000269|PubMed:9380501, ECO:0... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.3 for the exonuclease activity, 5.5 for endonuclease activity. High pH favors the exonuclease activity whereas low pH favors the endonuclease activity. {ECO:0000269|PubMed:10364212, ECO:0000269|PubMed:9874768}; | null | FUNCTION: Catalyzes both the 5'-exonucleolytic and structure-specific endonucleolytic hydrolysis of DNA branched nucleic acid molecules and probably plays a role in viral genome replication (PubMed:10364212, PubMed:15077103, PubMed:9874768). Active on flap (branched duplex DNA containing a free single-stranded 5'-end),... | Escherichia phage T5 (Enterobacteria phage T5) |
P06238 | A2MG_RAT | MGKHRLRSLALLPLLLRLLLLLLPTDASAPQKPIYMVMVPSLLHAGTPEKACFLFSHLNETVAVRVSLESVRGNQSLFTDLVVDKDLFHCTSFTVPQSSSDEVMFFTVQVKGATHEFRRRSTVLVKKKESLVFAQTDKPIYKPGQTVRFRVVSLDESFHPLNELIPLLYIQDPKNNRIAQWQNFNLEGGLKQLSFPLSSEPTQGSYKVVIRTESGRTVEHPFSVEEFVLPKFEVRVTVPETITILEEEMNVSVCGIYTYGKPVPGRVTVNICRKYSNPSNCFGEESVAFCEKLSQQLDGRGCFSQLVKTKSFQLKRQEYE... | null | null | acute inflammatory response to antigenic stimulus [GO:0002438]; acute-phase response [GO:0006953]; embryonic liver development [GO:1990402]; luteinization [GO:0001553]; negative regulation of complement activation, lectin pathway [GO:0001869]; response to carbon dioxide [GO:0010037]; response to glucocorticoid [GO:0051... | extracellular space [GO:0005615] | brain-derived neurotrophic factor binding [GO:0048403]; calcium-dependent protein binding [GO:0048306]; endopeptidase inhibitor activity [GO:0004866]; enzyme binding [GO:0019899]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; interleukin-1 binding [GO:0019966]; interleukin-8 binding [GO:00... | PF00207;PF07703;PF07677;PF01835;PF17791;PF17789;PF07678; | 1.50.10.20;2.20.130.20;2.60.120.1540;2.60.40.1930;2.60.40.1940;2.60.40.690;2.60.40.10; | Protease inhibitor I39 (alpha-2-macroglobulin) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which... | Rattus norvegicus (Rat) |
P06239 | LCK_HUMAN | MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYME... | 2.7.10.2 | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; B cell receptor signaling pathway [GO:0050853]; Fc-gamma receptor signaling pathway [GO:0038094]; hemopoiesis [GO:0030097]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; intracellular zi... | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; immunological synapse [GO:0001772]; membrane raft [GO:0045121]; pericentriolar material [GO:0000242]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATPase binding [GO:0051117]; CD4 receptor binding [GO:0042609]; CD8 receptor binding [GO:0042610]; identical protein binding [GO:0042802]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol 3-kinase binding [GO:0043548]; phospholipase activator activity [... | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cell receptor signaling. {ECO:0000269|PubMed:1639064, ECO:0000269... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:22034844}; Lipid-anchor {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:22034844}; Cytoplasmic side {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:22034844}. Cytoplasm, cytosol {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:220348... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic por... | Homo sapiens (Human) |
P06240 | LCK_MOUSE | MGCVCSSNPEDDWMENIDVCENCHYPIVPLDSKISLPIRNGSEVRDPLVTYEGSLPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHDLVRHYTNASDGLCTKLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHPRLVRLYAVVTQEPIYIITEYME... | 2.7.10.2 | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; B cell receptor signaling pathway [GO:0050853]; cell surface receptor signaling pathway [GO:0007166]; gamma-delta T cell differentiation [GO:0042492]; innate immune response [GO:0045087]; intracellular zinc ion homeostasis [G... | cell-cell junction [GO:0005911]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; glutamatergic synapse [GO:0098978]; immunological synapse [GO:0001772]; membrane raft [GO:0045121]; pericentriolar material [GO:0000242]; postsynaptic specializ... | antigen binding [GO:0003823]; ATP binding [GO:0005524]; CD4 receptor binding [GO:0042609]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein antigen binding [GO:1990405]; protein phosphatase binding [GO:0019903]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine kin... | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cells differentiation (By similarity). {ECO:0000250}.; PTM: Myris... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12218089}; Lipid-anchor {ECO:0000269|PubMed:12218089}; Cytoplasmic side {ECO:0000269|PubMed:12218089}. Cytoplasm, cytosol {ECO:0000269|PubMed:12218089}. Note=Present in lipid rafts in an inactive form. {ECO:0000250|UniProtKB:P06239}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic por... | Mus musculus (Mouse) |
P06241 | FYN_HUMAN | MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKK... | 2.7.10.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; | activated T cell proliferation [GO:0050798]; adaptive immune response [GO:0002250]; axon guidance [GO:0007411]; calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; cellular response to amyloid-beta [GO:1904646]; cellular response to glycine [GO:1905430]; cellular response to hydrogen peroxide [GO:007... | actin filament [GO:0005884]; cell body [GO:0044297]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; glial cell projection [GO:0097386]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perikaryon [... | alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; disordered domain specific binding [GO:0097718]; enzyme binding [GO:0019899]; ephrin receptor binding [GO:0046875]; growth factor receptor binding [GO:0070851]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; non-membrane spanning pro... | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state (PubMed:1699196). PTPRC/CD45 dephosphorylates Tyr-531 leading to activation (PubMed:1533589). Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15537652, ECO:0000269|PubMed:8206991}. Nucleus {ECO:0000269|PubMed:15537652}. Cell membrane {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:8206991}. Perikaryon {ECO:0000250|UniProtKB:Q62844}. Note=Present and active in lipid rafts (PubMed:12218089). Palmitoylation i... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail wit... | Homo sapiens (Human) |
P06242 | KIN28_YEAST | MKVNMEYTKEKKVGEGTYAVVYLGCQHSTGRKIAIKEIKTSEFKDGLDMSAIREVKYLQEMQHPNVIELIDIFMAYDNLNLVLEFLPTDLEVVIKDKSILFTPADIKAWMLMTLRGVYHCHRNFILHRDLKPNNLLFSPDGQIKVADFGLARAIPAPHEILTSNVVTRWYRAPELLFGAKHYTSAIDIWSVGVIFAELMLRIPYLPGQNDVDQMEVTFRALGTPTDRDWPEVSSFMTYNKLQIYPPPSRDELRKRFIAASEYALDFMCGMLTMNPQKRWTAVQCLESDYFKELPPPSDPSSIKIRN | 2.7.11.23 | null | 7-methylguanosine mRNA capping [GO:0006370]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to nitrogen starvation [GO:0006995]; nucleotide-excision repair [GO:0006289]; positive regulation of Atg1/ULK1 kinase complex assembly [GO:1905866]; positive regulation of autophagy [GO:0010508]; positive... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; transcription factor TFIIH holo complex [GO:0005675]; transcription factor TFIIK complex [GO:0070985] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase activity [GO:0004672]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation of Thr-162 regulates the affinity of interaction between CCL1, KIN28 and TFB3. Thr-162 phosphorylation does not vary through the cell cycle and is necessary for full kinase activity. {ECO:0000269|PubMed:10373527, ECO:0000269|PubMed:11839796, ECO:0000269|PubMed:9774652}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; | null | null | null | null | FUNCTION: Catalytic component of the TFIIK complex (KIN28-CCL1 dimer) which is the protein kinase component of transcription factor IIH (TFIIH) and phosphorylates the C-terminal domain of RNA polymerase II during transition from transcription to elongation after preinitiation complex (PIC) formation, thereby positively... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06243 | CDC7_YEAST | MTSKTKNIDDIPPEIKEEMIQLYHDLPGIENEYKLIDKIGEGTFSSVYKAKDITGKITKKFASHFWNYGSNYVALKKIYVTSSPQRIYNELNLLYIMTGSSRVAPLCDAKRVRDQVIAVLPYYPHEEFRTFYRDLPIKGIKKYIWELLRALKFVHSKGIIHRDIKPTNFLFNLELGRGVLVDFGLAEAQMDYKSMISSQNDYDNYANTNHDGGYSMRNHEQFCPCIMRNQYSPNSHNQTPPMVTIQNGKVVHLNNVNGVDLTKGYPKNETRRIKRANRAGTRGFRAPEVLMKCGAQSTKIDIWSVGVILLSLLGRRFPMF... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cell division [GO:0051301]; DNA replication initiation [GO:0006270]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic DNA replication checkpoint signaling [GO:0033314]; mitotic DNA replication preinitiation complex assembly [GO:1902977]... | centrosome [GO:0005813]; chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; Dbf4-dependent protein kinase complex [GO:0031431]; nucleus [GO:0005634] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC7 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase. Needed for the initiation of DNA synthesis during mitosis as well as for synaptonemal complex formation and commitment to recombination during meiosis. Required for HTA1-HTB1 locus transcription repression. {ECO:0000269|PubMed:1865880}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06244 | KAPA_YEAST | MSTEEQNGGGQKSLDDRQGEESQKGETSERETTATESGNESKSVEKEGGETQEKPKQPHVTYYNEEQYKQFIAQARVTSGKYSLQDFQILRTLGTGSFGRVHLIRSRHNGRYYAMKVLKKEIVVRLKQVEHTNDERLMLSIVTHPFIIRMWGTFQDAQQIFMIMDYIEGGELFSLLRKSQRFPNPVAKFYAAEVCLALEYLHSKDIIYRDLKPENILLDKNGHIKITDFGFAKYVPDVTYTLCGTPDYIAPEVVSTKPYNKSIDWWSFGILIYEMLAGYTPFYDSNTMKTYEKILNAELRFPPFFNEDVKDLLSRLITRD... | 2.7.11.11 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; phosphorylation [GO:0016310]; protein kinase A signaling [GO:0010737]; Ras protein signal transduction [GO:0007265]; regulation of macroautophagy [GO:0016241] | cAMP-dependent protein kinase complex [GO:0005952]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. | 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=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06245 | KAPB_YEAST | MEFVAERAQPVGQTIQQQNVNTYGQGVLQPHHDLQQRQQQQQQRQHQQLLTSQLPQKSLVSKGKYTLHDFQIMRTLGTGSFGRVHLVRSVHNGRYYAIKVLKKQQVVKMKQVEHTNDERRMLKLVEHPFLIRMWGTFQDARNIFMVMDYIEGGELFSLLRKSQRFPNPVAKFYAAEVILALEYLHAHNIIYRDLKPENILLDRNGHIKITDFGFAKEVQTVTWTLCGTPDYIAPEVITTKPYNKSVDWWSLGVLIYEMLAGYTPFYDTTPMKTYEKILQGKVVYPPYFHPDVVDLLSKLITADLTRRIGNLQSGSRDIKA... | 2.7.11.11 | null | invasive growth in response to glucose limitation [GO:0001403]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; negative regulation of cytoplasmic translation [GO:2000766]; phosphorylation [GO:0016310]; protein kinase A signaling [GO:0010737]; Ras protein signal transduction [GO:0007265] | cAMP-dependent protein kinase complex [GO:0005952]; chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932] | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06276 | CHLE_HUMAN | MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGP... | 3.1.1.8 | null | acetylcholine catabolic process [GO:0006581]; choline metabolic process [GO:0019695]; cocaine metabolic process [GO:0050783]; learning [GO:0007612]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of synaptic transmission [GO:0050805]; neuroblast differentiation [GO:0014016]; pept... | blood microparticle [GO:0072562]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nuclear envelope lumen [GO:0005641]; plasma membrane [GO:0005886] | acetylcholinesterase activity [GO:0003990]; amyloid-beta binding [GO:0001540]; catalytic activity [GO:0003824]; choline binding [GO:0033265]; cholinesterase activity [GO:0004104]; enzyme binding [GO:0019899]; hydrolase activity, acting on ester bonds [GO:0016788]; identical protein binding [GO:0042802] | PF08674;PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | PTM: N-glycosylated. No other PTM detected (PubMed:20946535). The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid molecules (Neu5Ac) making up approximately 33% and 47% of the total N-glycans, respectively. Only low amounts of fucosylated diantennary N-glycans are dete... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19542320}. | CATALYTIC ACTIVITY: Reaction=an acylcholine + H2O = a carboxylate + choline + H(+); Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8; Evidence={ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19452557}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for butyrylthiocholine (at 25 degrees Celsius) {ECO:0000269|PubMed:25054547}; | null | null | null | FUNCTION: Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. {ECO:0000269|PubMed:19452557, ECO:0000269|PubMed:19542320}. | Homo sapiens (Human) |
P06278 | AMY_BACLI | MKQQKRLYARLLTLLFALIFLLPHSAAAAANLNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDPADRNRVISGEHRIKAWTHFHFPGRGSTYSDFKWHWYHFDGTDWDESRKLNRIYKFQGKAWDWEVSNENGNYDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKTGKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQ... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551}; COFACTOR: Name=Na(+); Xref=ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551... | carbohydrate metabolic process [GO:0005975] | extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509] | PF09154;PF00128; | 2.40.30.140;3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14632998}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:11997021, ECO:0000269|PubMed:12915728, ECO:0000269|PubMed:14632998}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active up to pH 11.; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active up to 100 degrees Celsius.; | null | Bacillus licheniformis |
P06280 | AGAL_HUMAN | MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAIN... | 3.2.1.22 | null | glycoside catabolic process [GO:0016139]; glycosphingolipid catabolic process [GO:0046479]; glycosylceramide catabolic process [GO:0046477]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of nitric-oxide synthase activity [GO:0051001]; oligosaccharide metabolic process [GO:00... | azurophil granule lumen [GO:0035578]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764] | alpha-galactosidase activity [GO:0004557]; catalytic activity [GO:0003824]; galactoside binding [GO:0016936]; hydrolase activity [GO:0016787]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102] | PF16499;PF17450; | 3.20.20.70;2.60.40.1180; | Glycosyl hydrolase 27 family | null | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22; Evidence={ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27211852}; CATALYTIC ACTIVITY: Reaction=a globoside Gb3Cer... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of glycosphingolipids and participates in their degradation in the lysosome. {ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}. | Homo sapiens (Human) |
P06281 | RENI1_MOUSE | MDRRRMPLWALLLLWSPCTFSLPTRTATFERIPLKKMPSVREILEERGVDMTRLSAEWGVFTKRPSLTNLTSPVVLTNYLNTQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSRLYLACGIHSLYESSDSSSYMENGSDFTIHYGSGRVKGFLSQDSVTVGGITVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEEVFSVYYNRGSHLLGGEVVLGGSDPQHYQGNFHYVSISKTDSWQITMKGVSVGSSTLLCEEGCAVVVDTGSSFISAPTSSLKLIMQALGAKEKRIEEYVVN... | 3.4.23.15 | null | amyloid-beta metabolic process [GO:0050435]; angiotensin maturation [GO:0002003]; cell maturation [GO:0048469]; cellular response to xenobiotic stimulus [GO:0071466]; drinking behavior [GO:0042756]; hormone-mediated signaling pathway [GO:0009755]; juxtaglomerular apparatus development [GO:0072051]; male gonad developme... | apical part of cell [GO:0045177]; extracellular space [GO:0005615]; membrane [GO:0016020] | aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]; insulin-like growth factor receptor binding [GO:0005159]; signaling receptor binding [GO:0005102] | PF07966;PF00026; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9030738}. Membrane {ECO:0000250|UniProtKB:P00797}. Note=Associated to membranes via binding to ATP6AP2. {ECO:0000250|UniProtKB:P00797}. | CATALYTIC ACTIVITY: Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.; EC=3.4.23.15; Evidence={ECO:0000250|UniProtKB:P00797}; | null | null | null | null | FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. {ECO:0000269|PubMed:6370686}. | Mus musculus (Mouse) |
P06292 | RBL_MARPO | MSPQTETKAGVGFKAGVKDYRLTYYTPDYETKDTDILAAFRMTPQPGVPAEEAGNAVAAESSTGTWTTVWTDGLTNLDRYKGRCYDIDPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEAIYKSQAETGEIKGHYLNATAGTCEEMLKRAACARELGVPIVMHDYLTGGFTANTSLAFYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRM... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; | photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253] | chloroplast [GO:0009507] | magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type I subfamily | PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000250}. | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglyce... | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Marchantia polymorpha (Common liverwort) (Marchantia aquatica) |
P06298 | COLI1_XENLA | MFRPLWGCFLAILGICIFHIGEVQSQCWESSRCADLSSEDGVLECIKACKTDLSAESPVFPGNGHLQPLSESIRKYVMTHFRWNKFGRRNSTGNDGSNTGYKREDISSYPVFSLFPLSDQNAPGDNMEEEPLDRQENKRAYSMEHFRWGKPVGRKRRPIKVYPNGVEEESAESYPMELRRELSLELDYPEIDLDEDIEDNEVESALTKKNGNYRMHHFRWGSPPKDKRYGGFMTPERSQTPLMTLFKNAIIKNSHKKGQ | null | null | neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852] | extracellular space [GO:0005615]; secretory granule [GO:0030141] | G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184] | PF00976;PF08384;PF08035; | null | POMC family | PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}. | null | null | null | null | null | FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin ... | Xenopus laevis (African clawed frog) |
P06299 | COLI2_XENLA | MFRPTGGCSLAILGVFIFHIGEVQSQCWESSRCADLSSEDGILECIKACKMDLSAESPVFPGNGHLQPLSESIRKYVMTHFRWNKFGRRNNTGNDGSSGGYKREDISNYPVLNLFPSSDNQNAQGDNMEEEPMDRQENKRAYSMEHFRWGKPVGRKRRPIKVYPNGVEEESAESFPMELRRELSLELDYPEIDLDEDIEDNEVERALTKKNGNYRMHHFRWGSPPKDKRYGGFMTPERSQTPLMTLFKNAIIKNTHKKGL | null | null | neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852] | extracellular space [GO:0005615]; secretory granule [GO:0030141] | G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184] | PF00976;PF08384;PF08035; | null | POMC family | PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}. | null | null | null | null | null | FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin ... | Xenopus laevis (African clawed frog) |
P06300 | PDYN_RAT | MAWSRLMLAACLLVIPSEVAADCLSLCSLCAVRTQDGPHPINPLICSLECQDLVPPSEEWETCRGFWSFLTLTASGLHGKDDLENEVALEEGYTALTKLLEPLLKELEKGQLLTSVSEEKLRGLSSRFGNGRESELLGTDLMNDEAAQAGTLHFNEEDLRKQAKRYGGFLRKYPKRSSEMTGDEDRGQDGDQVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQENPNTYSEDLDV | null | null | chemical synaptic transmission [GO:0007268]; neuropeptide signaling pathway [GO:0007218]; response to immobilization stress [GO:0035902]; response to nicotine [GO:0035094]; sensory perception [GO:0007600] | axon terminus [GO:0043679]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dense core granule [GO:0031045]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; neuronal dense core vesicle [GO:0098992]; neuronal dense... | opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628] | PF01160; | null | Opioid neuropeptide precursor family | PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). {ECO:0000250}.; FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a ... | Rattus norvegicus (Rat) |
P06302 | PTMA_RAT | MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD | null | null | cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; negative regulation of apoptotic process [GO:0043066]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleus [GO:0005634] | DNA-binding transcription factor binding [GO:0140297]; histone binding [GO:0042393]; histone chaperone activity [GO:0140713]; ion binding [GO:0043167] | PF03247; | null | Pro/parathymosin family | PTM: Covalently linked to a small RNA of about 20 nucleotides. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. | Rattus norvegicus (Rat) |
P06307 | CCKN_HUMAN | MNSGVCLCVLMAVLAAGALTQPVPPADPAGSGLQRAEEAPRRQLRVSQRTDGESRAHLGALLARYIQQARKAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDFGRRSAEEYEYPS | null | null | axonogenesis [GO:0007409]; digestion [GO:0007586]; eating behavior [GO:0042755]; neuron migration [GO:0001764]; signal transduction [GO:0007165] | axon [GO:0030424]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428] | PF00918; | null | Gastrin/cholecystokinin family | PTM: The precursor is cleaved by proteases to produce a number of active cholecystokinins.; PTM: [Cholecystokinin-5]: The precursor is cleaved by ACE, which removes the Gly-Arg-Arg peptide at the C-terminus, leading to mature hormone. {ECO:0000269|PubMed:10336644, ECO:0000269|PubMed:9371719}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:37453717}. | null | null | null | null | null | FUNCTION: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. {ECO:0000250|UniProtKB:Q9TS44}. | Homo sapiens (Human) |
P06312 | KV401_HUMAN | MVLQTQVFISLLLWISGAYGDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTP | null | null | adaptive immune response [GO:0002250]; immune response [GO:0006955] | blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886] | antigen binding [GO:0003823] | PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. | null | null | null | null | null | FUNCTION: V segment of the variable domain of immunoglobulins light chain that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound im... | Homo sapiens (Human) |
P06332 | CD4_MOUSE | MCRAISLRRLLLLLLQLSQLLAVTQGKTLVLGKEGESAELPCESSQKKITVFTWKFSDQRKILGQHGKGVLIRGGSPSQFDRFDSKKGAWEKGSFPLIINKLKMEDSQTYICELENRKEEVELWVFKVTFSPGTSLLQGQSLTLTLDSNSKVSNPLTECKHKKGKVVSGSKVLSMSNLRVQDSDFWNCTVTLDQKKNWFGMTLSVLGFQSTAITAYKSEGESAEFSFPLNFAEENGWGELMWKAEKDSFFQPWISFSIKNKEVSVQKSTKDLKLQLKETLPLTLKIPQVSLQFAGSGNLTLTLDKGTLHQEVNLVVMKVA... | null | null | adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; defense response to Gram-negative bacterium [GO:0050829]; helper ... | cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | coreceptor activity [GO:0015026]; immunoglobulin binding [GO:0019865]; interleukin-16 binding [GO:0042011]; interleukin-16 receptor activity [GO:0042012]; MHC class II protein binding [GO:0042289]; MHC class II protein complex binding [GO:0023026]; protein homodimerization activity [GO:0042803]; protein kinase binding ... | PF05790;PF09191;PF00047;PF12104; | 2.60.40.10;1.20.5.900; | null | PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. {ECO:0000250|UniProtKB:P01730}.; PTM: Phosphorylated by PKC; phosphorylation plays an important role for CD4 internalization. {ECO:0000269|PubMed:2512251}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01730}. | null | null | null | null | null | FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are ... | Mus musculus (Mouse) |
P06339 | HA15_MOUSE | MLLFAHLLQLLVSATVPTQSSPHSLRYFTTAVSRPGLGEPRFIIVGYVDDTQFVRFDSDAENPRMEPRARWIEQEGPEYWERETWKARDMGRNFRVNLRTLLGYYNQSNDESHTLQWMYGCDVGPDGRLLRGYCQEAYDGQDYISLNEDLRSWTANDIASQISKHKSEAVDEAHQQRAYLQGPCVEWLHRYLRLGNETLQRSDPPKAHVTHHPRSEDEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWAAVVVPLGKEQYYTCHVYHEGLPEPLTLRWEPPPSTVSNMVIIAVLVVLGAVIILG... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathw... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P06340 | DOA_HUMAN | MALRAGLVLGFHTLMTLLSPQEAGATKADHMGSYGPAFYQSYGASGQFTHEFDEEQLFSVDLKKSEAVWRLPEFGDFARFDPQGGLAGIAAIKAHLDILVERSNRSRAINVPPRVTVLPKSRVELGQPNILICIVDNIFPPVINITWLRNGQTVTEGVAQTSFYSQPDHLFRKFHYLPFVPSAEDVYDCQVEHWGLDAPLLRHWELQVPIPPPDAMETLVCALGLAIGLVGFLVGTVLIIMGTYVSSVPR | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; negative regulation of antigen processing and presentation of peptide antigen via MHC class II [GO:0002587]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; pos... | late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=Complexes with HLA-DM molecule during intracellular transport and in endosomal/lysosomal compartments. Heterotetramerization is necessary to exit the ER. | null | null | null | null | null | FUNCTION: Important modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B-cells. Modifies peptide exchange activity of HLA-DM. | Homo sapiens (Human) |
P06342 | HB2Q_MOUSE | MALQIPSLLLSAAVVVLMVLSSPRTEGGNSERHFVAQLKGECYFTNGTQRIRSVNRYIYNREEWVRFDSDVGEYRAVTELGRPDAEYWNSQPEILERTRAEVDTVCRHNYEGVETHTSLRRLEQPNVAISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPHQGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC cl... | cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [... | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P06343 | HB2K_MOUSE | MALQIPSLLLLAAVVVLTVLSSPGTEGGNSERHFVHQFQPFCYFTNGTQRIRLVIRYIYNREEYVRFDSDVGEYRAVTELGRPDAEYWNKQYLERTRAELDTVCRHNYEKTETPTSLRRLEQPSVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC cl... | cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [... | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P06345 | HB2S_MOUSE | MALQIPSLLLSAAVVVLMVLSSPGTEGGDSERHFVFQFKGECYFTNGTQRIRSVDRYIYNREEYLRFDSDVGEYRAVTELGRPDAEYYNKQYLEQTRAELDTVCRHNYEGVETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLISNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC cl... | cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [... | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P06346 | HB2F_MOUSE | AAVVVLMVLSSPGTEGGNSERHFVSQFKGECYFTNGTQRIRSVDRYIYNREEYLRFDSDVGEYRAVTELGRSDAEYYNKQYLERTRAELDTVCRHNYEGVETPTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMAPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRYRSQKGPRGPPPAGLLQ | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC cl... | cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [... | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P06349 | H1T_RAT | MSETAPAASSTLVPAPVEKPATKRRGKKPGMATARKPRGFSVSKLIPEALSMSQERAGMSLAALKKALAAAGYDVEKNNSRIKLALKRLVNKGVLVQTKGTGASGSFKLSKKAASGNDKGKGKKSASAKAKKLGLSRASRSPKSSKTKVVKKPKATPTKGSGSRRKTKGAKGLQQRKSPAKARATNSNSGKSKMVMQKTDLRKAAGRK | null | null | binding of sperm to zona pellucida [GO:0007339]; cell differentiation [GO:0030154]; chromosome condensation [GO:0030261]; flagellated sperm motility [GO:0030317]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]; spermatogenesis [GO:0007283] | condensed nuclear chromosome [GO:0000794]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: Phosphorylated in early spermatids. {ECO:0000269|PubMed:19043117}.; PTM: Citrullination at Arg-56 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:00002... | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}. | null | null | null | null | null | FUNCTION: Testis-specific histone H1 that forms less compacted chromatin compared to other H1 histone subtypes. Formation of more relaxed chromatin may be required to promote chromatin architecture required for proper chromosome regulation during meiosis, such as homologous recombination. Histones H1 act as linkers tha... | Rattus norvegicus (Rat) |
P06350 | H1_ONCMY | MAEVAPAPAAAAPAKAPKKKAAAKPKKAGPSVGELIVKAVSASKERSGVSLAALKKSLAAGGYDVEKNNSRVKIAVKSLVTKGTLVQTKGTGASGSFKLNKKAVEAKKPAKKAAAPKAKKVAAKKPAAAKKPKKVAAKKAVAAKKSPKKAKKPATPKKAAKSPKKVKKPAAAAKKAAKSPKKATKAAKPKAAKPKAAKAKKAAPKKK | null | null | defense response to bacterium [GO:0042742]; nucleosome assembly [GO:0006334] | extracellular region [GO:0005576]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | null | SUBCELLULAR LOCATION: Nucleus. Chromosome.; SUBCELLULAR LOCATION: [Oncorhyncin II]: Secreted. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable up to 80 degrees Celsius.; | FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. {ECO:0000269|PubMed:12969798}.; FUNCTION: Oncorhyncin II has antibacterial activity against Gram-positive and Gram-negative bacteria at submicromolar concentrations. Potentially important role in mucosal defense.... | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) |
P06367 | RS14A_YEAST | MSNVVQARDNSQVFGVARIYASFNDTFVHVTDLSGKETIARVTGGMKVKADRDESSPYAAMLAAQDVAAKCKEVGITAVHVKIRATGGTRTKTPGPGGQAALRALARSGLRIGRIEDVTPVPSDSTRKKGGRRGRRL | null | null | cytoplasmic translation [GO:0002181]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412] | 90S preribosome [GO:0030686]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040] | mRNA binding [GO:0003729]; structural constituent of ribosome [GO:0003735] | PF00411; | 3.30.420.80; | Universal ribosomal protein uS11 family | PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:1544921}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06394 | K1C10_BOVIN | MSVRYSSSKQYSSSRSGGGGGGGSSLRISSSKGSLGGGYSSGGFSGGSFSRGSSAGGCFGGSSSIYGGGLGSGFGGGYGSSFGGSYGGSFGGGYGGGGFGGGSFGGGSFGGGLGGGFGDGGLISGNQKITMQNLNDRLASYLDKVRALEESNYELEVKIKEWYEKYGNSRQREPRDYSKYYQTIDDLKNQIFNLTTDNANILIQVDNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLTKTDLEMQIESLTEELAYLKKNHEEEMRDLQNVSTGDVNVEMNAAPGVDLTELLNNMRSQYEQLAEKNRRDAEAW... | null | null | epidermis development [GO:0008544]; epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; positive regulation of epidermis development [GO:0045684]; protein heterotetramerization [GO:0051290] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular region [GO:0005576]; keratin filament [GO:0045095] | protein heterodimerization activity [GO:0046982]; structural constituent of skin epidermis [GO:0030280] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:P13645}. Cell surface {ECO:0000250|UniProtKB:P13645}. Cytoplasm {ECO:0000250|UniProtKB:P02535}. | null | null | null | null | null | FUNCTION: Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity). Involved in the maintenance of cell layer development and keratin filament bundles in suprabasal cells of the epithelium (By similarity). {ECO:0000250|UniProtKB:P02535}. | Bos taurus (Bovine) |
P06396 | GELS_HUMAN | MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENP... | null | null | actin filament capping [GO:0051693]; actin filament depolymerization [GO:0030042]; actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; amyloid fibril formation [GO:1990000]; barbed-end actin fi... | actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; blood microparticle [GO:0072562]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:190... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; myosin II binding [GO:0045159]; phosphatidylinositol 3-kinase catalytic subunit binding [GO:0036313]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00626; | 3.40.20.10; | Villin/gelsolin family | PTM: Phosphorylation on Tyr-86, Tyr-409, Tyr-465, Tyr-603 and Tyr-651 in vitro is induced in presence of phospholipids. {ECO:0000269|PubMed:10210201}. | SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: [Isoform 1]: Secreted. | null | null | null | null | null | FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (PubMed:19666512). Plays a ro... | Homo sapiens (Human) |
P06399 | FIBA_RAT | MLSLRVACLILSLASTVWTADTGTTSEFIEAGGDIRGPRIVERQPSQCKETDWPFCSDEDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQKNNKDSNSLTRNIMEYLRGDFANANNFDNTFGQVSEDLRRRIQILKRKVIEKAQQIQVLQKDVRDQLIDMKRLEVDIDIKIRSCKGSCSRSVSREINLKDYEGQQKQLEQVIAKDLLPAKDRQYLPAIKMSPVPDLVPGSFKSQLQEGPPEWKALTEMRQMRMELERPGKDGASRGDLPGDSRGDSATRGPGSKIENPMTPGHGGSGYWRPGSSGSGSDGNWG... | null | null | acute-phase response [GO:0006953]; adaptive immune response [GO:0002250]; blood coagulation [GO:0007596]; blood coagulation, common pathway [GO:0072377]; blood coagulation, fibrin clot formation [GO:0072378]; cell-matrix adhesion [GO:0007160]; cellular response to granulocyte colony-stimulating factor [GO:1990643]; cel... | blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; platelet alpha granule [GO:0031091]; synapse [GO:0045202] | extracellular matrix structural constituent [GO:0005201]; metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102]; structural molecule activity [GO:0005198] | PF08702;PF12160;PF00147; | 1.20.5.50;3.90.215.10;4.10.530.10; | null | PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsil... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02671}. | null | null | null | null | null | FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of ... | Rattus norvegicus (Rat) |
P06400 | RB_HUMAN | MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKR... | null | null | aortic valve morphogenesis [GO:0003180]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cell morphogenesis involved in neuron differentiation [GO:0048667]; cellular response to insulin stimulus [GO:0032869]; cellular response to xenobiotic stimulus [GO:0071466]; chondrocyte differentiation [GO:0002062];... | chromatin [GO:0000785]; chromatin lock complex [GO:0061793]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; Rb-E2F complex [GO:0035189]; spindle [GO:0005819]; SWI/SNF complex [GO:0016514] | disordered domain specific binding [GO:0097718]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; importin-alpha family protein binding [GO:0061676]; kinase binding [GO:0019900]; molecular adaptor activity [GO:0060090]; phosphoprotein binding [GO:0051219]; RNA polymerase II... | PF11934;PF01858;PF01857;PF08934; | 1.10.472.140;6.10.140.1380;6.10.250.530;1.10.472.10; | Retinoblastoma protein (RB) family | PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-567 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. SV40 large T antigen, HPV E7 and adenovirus E1A bind to the underphosphorylated, active form of pRb. Phosphorylation at Thr-821 and Th... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940255}. Note=During keratinocyte differentiation, acetylation by KAT2B/PCAF is required for nuclear localization. {ECO:0000269|PubMed:20940255}. | null | null | null | null | null | FUNCTION: Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:10499802). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes (PubMed:10499802). Both physically blocks E2Fs transactivating domain and recruits... | Homo sapiens (Human) |
P06401 | PRGR_HUMAN | MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAART... | null | null | cell-cell signaling [GO:0007267]; glandular epithelial cell maturation [GO:0002071]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; lung alveolus development [GO:0048286]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of gene expression [GO:0010629]; negative regul... | chromatin [GO:0000785]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | ATPase binding [GO:0051117]; 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]; enzyme binding [GO:0019899]; estrogen response element binding [GO:0034056]; G protein-coupled... | PF00104;PF02161;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases.; SUBCELLULAR LOCATION: [Isoform A]: Nucleus. Cytoplasm. Note=Mainly nuclear.; SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrio... | null | null | null | null | null | FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Depending on the isoform, progesterone receptor functions as a transcriptional activator or repressor. {ECO:0000269|PubMed:10757795, EC... | Homo sapiens (Human) |
P06437 | GB_HHV1K | MHQGAPSWGRRWFVVWALLGLTLGVLVASAAPTSPGTPGVAAATQAANGGPATPAPPPLGAAPTGDPKPKKNKKPKNPTPPRPAGDNATVAAGHATLREHLRDIKAENTDANFYVCPPPTGATVVQFEQPRRCPTRPEGQNYTEGIAVVFKENIAPYKFKATMYYKDVTVSQVWFGHRYSQFMGIFEDRAPVPFEEVIDKINAKGVCRSTAKYVRNNLETTAFHRDDHETDMELKPANAATRTSRGWHTTDLKYNPSRVEAFHRYGTTVNCIVEEVDARSVYPYDEFVLATGDFVYMSPFYGYREGSHTEHTTYAADRFK... | null | null | symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | identical protein binding [GO:0042802] | PF17416;PF17417;PF00606; | 1.20.5.1890;2.30.29.100;2.30.30.1230;6.10.250.3280; | Herpesviridae glycoprotein B family | PTM: The cytoplasmic tail is phosphorylated by the viral kinase US3. Phosphorylation may be linked to a down-regulation of gB expression on cell surface. {ECO:0000269|PubMed:18945776, ECO:0000269|PubMed:19158241}.; PTM: ubiquitinated. {ECO:0000250}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its hos... | Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1) |
P06441 | POLG_HAVLA | MNMSKQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQIEPLKTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQ... | 2.7.7.48; 3.4.22.28; 3.6.1.15 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; viral RNA genome re... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell mitochondrial outer membrane [GO:0044193]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF20758;PF12944;PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | Picornaviridae polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precu... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:000025... | 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:0000250|UniProtKB:P08617, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a d... | Human hepatitis A virus genotype IA (isolate LA) (HHAV) (Human hepatitis A virus (isolate Human/Northern California/LA/1974)) |
P06442 | POLG_HAVCR | MNMSKQGIFQTVGSGLDHILSLADIEEEQMIQSVVRTAVTGASYFTSVDQSSVHTAEVGLHQIEPLKTSVDKPSSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPSDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQ... | null | null | protein complex oligomerization [GO:0051259]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell membrane [GO:0033644]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | monoatomic ion channel activity [GO:0005216]; structural molecule activity [GO:0005198] | PF12944;PF00073; | 2.60.120.20; | Picornaviridae polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precu... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:000025... | null | null | null | null | null | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a d... | Human hepatitis A virus genotype IA (isolate CR326) (HHAV) (Human hepatitis A virus (isolate Human/Costa Rica/CR326/1960)) |
P06445 | ENV_RMCFV | MACSTFSKPLKDKINPWGPLIILGILIRAGVSVQHDSPHKVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLVGDYWDDPEPDIGDGCRTPGGRRRTRLYDFYVCPGHTVPIGCGGPGEGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDQGPCYDSSVSSDIKGATPGGRCNPLVLEFTDAGKKASWDGPKVWGLRLYRSTGTDPVTRFSLTRRVLNIGPRVPIGPNPVIIDQLPPSRPVQIMLPRPPQPPPPGAASIVPETAPPSQQPGTGDRLLNLVDGAYQALNLTSPDKTQECWLCLVAEPPY... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Rauscher mink cell focus-inducing virus |
P06446 | MATRX_SENDZ | MADIYRFPKFSYEDNGTVEPLPLRTGPDKKAIPHIRIVKVGDPPKHGVRYLDLLLLGFFETPKQTTNLGSVSDLTEPTSYSICGSGSLPIGVAKYYGTDQELLKACTDLRITVRRTVRAGEMIVYMVDSIGAPLLPWSGRLRQGMIFNANKVALAPQCLPVDKDIRLRVVFVNGTSLGAITIAKIPKTLADLALPNSISVNLLVTLKTGISTEQKGVLPVLDDQGEKKLNFMVHLGLIRRKVGKIYSVEYCKSKIERMRLIFSLGLIGGISFHVQVNGTLSKTFMSQLAWKRAVCFPLMDVNPHMNMVIWAASVEITGVD... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | structural constituent of virion [GO:0039660] | PF00661; | 2.70.20.60;2.70.20.50; | Morbillivirus/respirovirus/rubulavirus M protein family | PTM: A large portion is phosphorylated in the cytoplasm, but not in virion. However, this phosphorylation is not essential for virus replication. {ECO:0000269|PubMed:9281516}. | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:6285608}. Host cell membrane {ECO:0000269|PubMed:6285608}; Peripheral membrane protein {ECO:0000269|PubMed:6285608}; Cytoplasmic side {ECO:0000269|PubMed:6285608}. Note=During bud formation, associates at the inner side of the plasma membran... | null | null | null | null | null | FUNCTION: Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane and concentrates the HN and F glycoproteins. Acts as a negative regulator for transcription and replication by sticking to the nucleocapsid. This effect might be regulated by the cytoplasmic interaction... | Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)) |
P06447 | L_SENDZ | MDGQESSQNPSDILYPECHLNSPIVRGKIAQLHVLLDVNQPYRLKDDSIINITKHKIRNGGLSPRQIKIRSLGKALQRTIKDLDRYTFEPYPTYSQELLRLDIPEICDKIRSVFAVSDRLTRELSSGFQDLWLNIFKQLGNIEGREGYDPLQDIGTIPEITDKYSRNRWYRPFLTWFSIKYDMRWMQKTRPGGPLDTSNSHNLLECKSYTLVTYGDLVMILNKLTLTGYILTPELVLMYCDVVEGRWNMSAAGHLDKKSIGITSKGEELWELVDSLFSSLGEEIYNVIALLEPLSLALIQLNDPVIPLRGAFMRHVLTEL... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | null | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF14318;PF00946; | null | Paramyxovirus L protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a 5'-end... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 for mRNA (guanine-N(7)-)-methyltransferase activity.; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius.; | FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all vir... | Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)) |
P06454 | PTMA_HUMAN | MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAENEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAESATGKRAAEDDEDDDVDTKKQKTDEDD | null | null | DNA-templated transcription [GO:0006351]; negative regulation of apoptotic process [GO:0043066]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor binding [GO:0140297]; histone binding [GO:0042393]; ion binding [GO:0043167] | PF03247; | null | Pro/parathymosin family | PTM: Covalently linked to a small RNA of about 20 nucleotides. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. | Homo sapiens (Human) |
P06463 | VE6_HPV18 | MARFEDPTRRPYKLPDLCTELNTSLQDIEITCVYCKTVLELTEVFEFAFKDLFVVYRDSIPHAACHKCIDFYSRIRELRHYSDSVYGDTLEKLTNTGLYNLLIRCLRCQKPLNPAEKLRHLNEKRRFHNIAGHYRGQCHSCCNRARQERLQRRRETQV | null | null | DNA-templated transcription [GO:0006351]; negative regulation of DNA-templated transcription [GO:0045892]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity [GO:0039... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | DNA binding [GO:0003677]; PDZ domain binding [GO:0030165]; zinc ion binding [GO:0008270] | PF00518; | 3.30.240.40; | Papillomaviridae E6 protein family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}. | null | null | null | null | null | FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting the... | Human papillomavirus type 18 |
P06467 | HBAZ_MOUSE | MSLMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQLRAHGFKIMTAVGDAVKSIDNLSSALTKLSELHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEKYR | null | null | carbon dioxide transport [GO:0015670]; erythrocyte maturation [GO:0043249]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oxygen transport [GO:0015671] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin. {ECO:0000250}. | Mus musculus (Mouse) |
P06473 | GB_HCMVA | MESRIWCLVVCVNLCIVCLGAAVSSSSTSHATSSTHNGSHTSRTTSAQTRSVYSQHVTSSEAVSHRANETIYNTTLKYGDVVGVNTTKYPYRVCSMAQGTDLIRFERNIICTSMKPINEDLDEGIMVVYKRNIVAHTFKVRVYQKVLTFRRSYAYIYTTYLLGSNTEYVAPPMWEIHHINKFAQCYSSYSRVIGGTVFVAYHRDSYENKTMQLIPDDYSNTHSTRYVTVKDQWHSRGSTWLYRETCNLNCMLTITTARSKYPYHFFATSTGDVVYISPFYNGTNRNASYFGENADKFFIFPNYTIVSDFGRPNAAPETHR... | null | null | symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF17416;PF17417;PF00606;PF12154; | 1.20.5.1890;2.30.29.100;2.30.30.1230;6.10.250.3280; | Herpesviridae glycoprotein B family | PTM: A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds. {ECO:0000250}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Envelope glycoprotein that plays a role in host cell entry, cell to-cell virus transmission, and fusion of infected cells. May be involved in the initial attachment via binding to heparan sulfate together with the gM/gN complex that binds heparin with higher affinity. Interacts with host integrin ITGB1, PDGFR... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P06487 | GI_HHV11 | MPCRPLQGLVLVGLWVCATSLVVRGPTVSLVSNSFVDAGALGPDGVVEEDLLILGELRFVGDQVPHTTYYDGGVELWHYPMGHKCPRVVHVVTVTACPRRPAVAFALCRATDSTHSPAYPTLELNLAQQPLLRVQRATRDYAGVYVLRVWVGDAPNASLFVLGMAIAAEGTLAYNGSAYGSCDPKLLPSSAPRLAPASVYQPAPNQASTPSTTTSTPSTTIPAPSTTIPAPQASTTPFPTGDPKPQPPGVNHEPPSNATRATRDSRYALTVTQIIQIAIPASIIALVFLGSCICFIHRCQRRYRRSRRPIYSPQMPTGIS... | null | null | virus-mediated perturbation of host defense response [GO:0019049] | host cell [GO:0043657]; host cell Golgi apparatus [GO:0044177]; host cell junction [GO:0044156]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF01688; | null | Alphaherpesvirinae glycoprotein I family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:18596102}; Single-pass membrane protein {ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:16537585}; Single-pass type I membrane protein {ECO:0000255}. Host cell junction {ECO:0000269|PubMed:11134295, ECO:0000269|PubMed:16537585}. Host Golgi apparatus, host ... | null | null | null | null | null | FUNCTION: In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate ... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P06492 | VP16_HHV11 | MDLLVDELFADMNADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERTQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLT... | null | null | biological process involved in interaction with host [GO:0051701]; DNA-templated viral transcription [GO:0039695]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-containing complex assembly [GO:0065003]; regulation of vira... | host cell cytoplasm [GO:0030430]; host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; replication compartment [GO:0046809]; transcription regulator complex [GO:0005667]; viral tegument [GO:0019033] | core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor binding [GO:0140297]; molecular function activator activity [GO:0140677]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO... | PF02232;PF12149; | 1.10.1290.10; | Herpesviridae tegument protein VP16 protein family | null | SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P04486}. Host nucleus {ECO:0000250|UniProtKB:P04486}. | null | null | null | null | null | FUNCTION: In the early stage of viral replication, acts as a transcriptional activator of immediate-early (IE) gene products (alpha-genes), which is released by invading virions (PubMed:12826401, PubMed:23029222). Recruits P-TEFb to the viral alpha-gene promoters and overcomes transcriptional inhibition by ICP22 to pro... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P06493 | CDK1_HUMAN | MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM | 2.7.11.22; 2.7.11.23 | null | animal organ regeneration [GO:0031100]; apoptotic process [GO:0006915]; cell division [GO:0051301]; cell migration [GO:0016477]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to organic cyclic compound [GO:0071407]; centrosome cycle [GO:0007098]; chromosome condensation [GO:0030261]; DNA repair... | centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; cyclin A2-CDK1 complex [GO:0097122]; cyclin B1-CDK1 complex [GO:0097125]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome ... | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; cyclin binding [GO:0030332]; cyclin-dependent protein kinase activity [GO:0097472]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; histone kinase activity [GO:0035173]; Hsp70 protein binding [GO:0030544]; kinase activity [GO:0016301]; pr... | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity (PubMed:20360007). Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation (PubMed:7569953). Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts as a negative regulator of entry into mitosis ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11440}. Cytoplasm {ECO:0000250|UniProtKB:P11440}. Mitochondrion {ECO:0000269|PubMed:19917720}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, spindle. Note=Cytoplasmic during the interphase.... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000269|PubMed:19202191, ECO:00002... | null | null | null | null | FUNCTION: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition via association with multiple interphase cyclins (PubMed:16407259, PubMed:16933150, PubMed:17459720, PubMed:18356527, PubMed:19509060, PubMed:19917720, PubMed:2017... | Homo sapiens (Human) |
P06494 | ERBB2_RAT | MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNRDPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQLAPVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPPNN... | 2.7.10.1 | null | cell surface receptor signaling pathway [GO:0007166]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to growth factor stimulus [GO:0071363]; ERBB2-EGFR signaling pathway [GO:0038134]; ERBB2-ERBB3 signaling pathway [GO:0038133]; ERBB2-ERBB4 signaling pathway [GO:0038135]; estrous c... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; ERBB3:ERBB2 complex [GO:0038143]; lateral loop [GO:0043219]; microvillus [GO:0005902];... | ATP binding [GO:0005524]; coreceptor activity [GO:0015026]; DNA binding [GO:0003677]; ErbB-3 class receptor binding [GO:0043125]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein tyrosine kinase activity [GO:0004713]; protein-containin... | PF00757;PF14843;PF07714;PF01030;PF21314; | 1.20.5.100;4.10.1140.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily | PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Ligand-binding increases phosphorylation on tyrosine residues. Signaling via SEMA4C promotes phosphorylation at Tyr-1250. Dephosphorylated by PTPN12. {ECO:0000250... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cyto... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowt... | Rattus norvegicus (Rat) |
P06525 | ADH1_ARATH | MSTTGQIIRCKAAVAWEAGKPLVIEEVEVAPPQKHEVRIKILFTSLCHTDVYFWEAKGQTPLFPRIFGHEAGGIVESVGEGVTDLQPGDHVLPIFTGECGECRHCHSEESNMCDLLRINTERGGMIHDGESRFSINGKPIYHFLGTSTFSEYTVVHSGQVAKINPDAPLDKVCIVSCGLSTGLGATLNVAKPKKGQSVAIFGLGAVGLGAAEGARIAGASRIIGVDFNSKRFDQAKEFGVTECVNPKDHDKPIQQVIAEMTDGGVDRSVECTGSVQAMIQAFECVHDGWGVAVLVGVPSKDDAFKTHPMNFLNERTLKGT... | 1.1.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:25447145}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:25447145}; | cellular response to hypoxia [GO:0071456]; formaldehyde catabolic process [GO:0046294]; positive regulation of cellular response to hypoxia [GO:1900039]; response to abscisic acid [GO:0009737]; response to caffeine [GO:0031000]; response to cold [GO:0009409]; response to estradiol [GO:0032355]; response to flooding [GO... | cytosol [GO:0005829]; plasma membrane [GO:0005886] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; nucleotide binding [GO:0000166]; protein homodimerization activity [GO:0042803]; S-(hydroxymethyl)glutathione dehydrogenase activity [GO:0051903]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Class-P subfamily | PTM: Glutathionylated. {ECO:0000269|PubMed:16055689}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7851777}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754}; CATALYTIC ACTIVITY: Reaction=a seconda... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.65 mM for NAD(+) (at pH 10.5 and 25 degrees Celsius) {ECO:0000269|PubMed:23707506}; KM=5.1 mM for ethanol (at pH 10.5 and 25 degrees Celsius) {ECO:0000269|PubMed:23707506}; Vmax=7.9 umol/min/mg enzyme with NAD(+) as substrate (at pH 10.5 and 25 degrees Celsius) {... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.5 (at 25 degrees Celsius). {ECO:0000269|PubMed:23707506}; | null | FUNCTION: Alcohol dehydrogenase mostly active on ethanol (EtOH), but exhibits broad substrates selectivity for primary and secondary alcohols (e.g. butanol, propyl alcohol, pentanol, isopentanol, ethylene glycol, isopropanol, methanol and tertiary butyl alcohol) (PubMed:23707506). Converts allyl alcohol to highly toxic... | Arabidopsis thaliana (Mouse-ear cress) |
P06534 | SP0A_BACSU | MEKIKVCVADDNRELVSLLSEYIEGQEDMEVIGVAYNGQECLSLFKEKDPDVLVLDIIMPHLDGLAVLERLRESDLKKQPNVIMLTAFGQEDVTKKAVDLGASYFILKPFDMENLVGHIRQVSGNASSVTHRAPSSQSSIIRSSQPEPKKKNLDASITSIIHEIGVPAHIKGYLYLREAISMVYNDIELLGSITKVLYPDIAKKFNTTASRVERAIRHAIEVAWSRGNIDSISSLFGYTVSMTKAKPTNSEFIAMVADKLRLEHKAS | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | asymmetric cell division [GO:0008356]; cell septum assembly [GO:0090529]; detection of stimulus [GO:0051606]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of sporulation resulting in formation of a cellular spore [GO:0045881]; single-species surface biofilm formation [GO:0090606]... | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | calcium ion binding [GO:0005509]; DNA-binding transcription factor activity [GO:0003700]; phosphorelay response regulator activity [GO:0000156]; transcription cis-regulatory region binding [GO:0000976] | PF00072;PF08769; | 3.40.50.2300;1.10.10.10; | null | PTM: Phosphorylated by KinA and KinB. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... | Bacillus subtilis (strain 168) |
P06536 | GCR_RAT | MDSKESLAPPGRDEVPGSLLGQGRGSVMDFYKSLRGGATVKVSASSPSVAAASQADSKQQRILLDFSKGSTSNVQQRQQQQQQQQQQQQQQQQQQQPDLSKAVSLSMGLYMGETETKVMGNDLGYPQQGQLGLSSGETDFRLLEESIANLNRSTSVPENPKSSTSATGCATPTEKEFPKTHSDASSEQQNRKSQTGTNGGSVKLYPTDQSTFDLLKDLEFSAGSPSKDTNESPWRSDLLIDENLLSPLAGEDDPFLLEGNTNEDCKPLILPDTKPKIKDTGDTILSSPSSVALPQVKTEKDDFIELCTPGVIKQEKLGPV... | null | null | adrenal gland development [GO:0030325]; androgen metabolic process [GO:0008209]; astrocyte differentiation [GO:0048708]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to magnesium ion [GO:0071286]; cellular response to steroid horm... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; postsynaptic density, intracellular component [GO:0099092]; protein-containing com... | chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase ... | PF02155;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000250}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids. {ECO:0000250|UniProtKB:P04150}.; PTM: Phosphorylated in the absence of hormone; becomes hyperphosphorylated i... | SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000269|PubMed:21730050}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04... | null | null | null | null | null | FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in... | Rattus norvegicus (Rat) |
P06537 | GCR_MOUSE | MDSKESLAPPGRDEVPSSLLGRGRGSVMDLYKTLRGGATVKVSASSPSVAAASQADSKQQRILLDFSKGSASNAQQQQQQQQQQQQQQQQQPQPDLSKAVSLSMGLYMGETETKVMGNDLGYPQQGQLGLSSGETDFRLLEESIANLNRSTSRPENPKSSTPAAGCATPTEKEFPQTHSDPSSEQQNRKSQPGTNGGSVKLYTTDQSTFDILQDLEFSAGSPGKETNESPWRSDLLIDENLLSPLAGEDDPFLLEGDVNEDCKPLILPDTKPKIQDTGDTILSSPSSVALPQVKTEKDDFIELCTPGVIKQEKLGPVYCQ... | null | null | adrenal gland development [GO:0030325]; astrocyte differentiation [GO:0048708]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chromatin remodeling [GO:0006338]; gene expression [GO:0010467]; glucocorticoid metabolic process [GO:0008... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic density, intracellular component [GO:009909... | chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase ... | PF02155;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000250|UniProtKB:P04150}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids. {ECO:0000269|PubMed:11555652}.; PTM: Phosphorylated in the absence of hormone; becomes hyper... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:25676786, ECO:0000269|PubMed:27686098}. Nucleus {ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:25676786, ECO:0000269|PubMed:27686098}. Note=Cytoplasmic in the absence of ligand, nuclear after ligand-binding (... | null | null | null | null | null | FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in... | Mus musculus (Mouse) |
P06575 | BINA1_LYSSH | MRNLDFIDSFIPTEGKYIRVMDFYNSEYPFCIHAPSAPNGDIMTEICSRENNQYFIFFPTDDGRVIIANRHNGSVFTGEATSVVSDIYTGSPLQFFREVKRTMATYYLAIQNPESATDVRALEPHSHELPSRLYYTNNIENNSNILISNKEQIYLTLPSLPENEQYPKTPVLSGIDDIGPNQSEKSIIGSTLIPCIMVSDFISLGERMKTTPYYYVKHTQYWQSMWSALFPPGSKETKTEKSGITDTSQISMTDGINVSIGADFGLRFGNKTFGIKGGFTYDTKTQITNTSQLLIETTYTREYTNTENFPVRYTGYVLAS... | null | null | sporulation resulting in formation of a cellular spore [GO:0030435] | null | toxin activity [GO:0090729] | PF05431; | null | Toxin_10 family | PTM: Processed by proteases extracted from C.pipiens larval gut; 6 amino acids are removed from the N-terminus while it is estimated about 20 residues are removed from the C-terminus to yield the 40 kDa toxin form that is seen in insects. The 40 kDa form is 50-fold more lethal against tissue culture cells than the prec... | SUBCELLULAR LOCATION: Spore, perispore {ECO:0000305|PubMed:3926751}. | null | null | null | null | null | FUNCTION: Component of a binary toxin active against Culex and some Aedes mosquito larvae; about 1000-fold more toxic against C.quinquefasciatus than A.aegypti (Probable) (PubMed:8419297, Ref.10). This subunit alone is active against C.quinquefasciatus, Anopheles gambiae, A.stephensi and Aedes aegypti mosquito cell lin... | Lysinibacillus sphaericus (Bacillus sphaericus) |
P06576 | ATPB_HUMAN | MLGFVGRVAAAPASGALRRLTPSASLPPAQLLLRAAPTAVHPVRDYAAQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSA... | 7.1.2.2 | null | angiogenesis [GO:0001525]; ATP biosynthetic process [GO:0006754]; cellular response to interleukin-7 [GO:0098761]; generation of precursor metabolites and energy [GO:0006091]; lipid metabolic process [GO:0006629]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; osteoblast d... | cell surface [GO:0009986]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrial nucleoid [GO:0042645]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial... | angiostatin binding [GO:0043532]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; MHC class I protein binding [GO:0042288]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00006;PF02874; | 2.40.10.170;3.40.50.300; | ATPase alpha/beta chains family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:25168243}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829, ECO:0000269|PubMed:25168243}. | CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000305|PubMed:25168243}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57722; Evide... | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Homo sapiens (Human) |
P06583 | AT1B1_CANLF | MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEEYVRNIVRFLEKYKDSAQKDEMIFEDCGNMPSEIKERGEFNNERGERKVCRFKLEWLGNCSGINDETYGYRDGKPCVLIKLNRVLGFKPKPPKNESLEAYPVMKYSPYVLPVQCTGKRDEDKDRIGNVEYFGLGGYPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS | null | null | cell adhesion [GO:0007155]; innate immune response [GO:0045087]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; potassium ion import across plasma membrane [GO:1990573]; sodium ion export across plasma membrane [GO:0036376] | apical plasma membrane [GO:0016324]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890] | ATPase activator activity [GO:0001671] | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | PTM: Glutathionylated (By similarity). N-glycosylated (By similarity). {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the intercalated disk a... | null | null | null | null | null | FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane (P... | Canis lupus familiaris (Dog) (Canis familiaris) |
P06585 | PSBA_PEA | MTAILERRDSENLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADI... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster o... | photosynthetic electron transport in photosystem II [GO:0009772]; response to herbicide [GO:0009635] | chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxygen evolv... | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}.; PTM: C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}. | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:1499553, ECO:0000269|PubMed:9407103}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}. | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379}; | null | null | null | null | FUNCTION: This is one of the two reaction center proteins of photosystem II.; FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core ant... | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
P06596 | PA21B_CANLF | MKFLVLAALLTVAAAEGGISPRAVWQFRNMIKCTIPESDPLKDYNDYGCYCGLGGSGTPVDELDKCCQTHDHCYSEAKKLDSCKFLLDNPYTKIYSYSCSGSEITCSSKNKDCQAFICNCDRSAAICFSKAPYNKEHKNLDTKKYC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593}; | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; arachidonic acid secretion [GO:0050482]; defense response to Gram-positive bacterium [GO:0050830]; fatty acid biosynthetic process [GO:0006633]; innate immune response in mucosa [GO:0002227... | cell surface [GO:0009986]; extracellular space [GO:0005615] | bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|U... | null | null | null | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols ov... | Canis lupus familiaris (Dog) (Canis familiaris) |
P06602 | EVE_DROME | MHGYRTYNMESHHAHHDASPVDQKPLVVDLLATQYGKPQTPPPSPNECLSSPDNSLNGSRGSEIPADPSVRRYRTAFTRDQLGRLEKEFYKENYVSRPRRCELAAQLNLPESTIKVWFQNRRMKDKRQRIAVAWPYAAVYSDPAFAASILQAAANSVGMPYPPYAPAAAAAAAAAAAVATNPMMATGMPPMGMPQMPTMQMPGHSGHAGHPSPYGQYRYTPYHIPARPAPPHPAGPHMHHPHMMGSSATGSSYSAGAAGLLGALPSATCYTGLGVGVPKTQTPPLDLQSSSSPHSSTLSLSPVGSDHAKVFDRSPVAQSA... | null | null | adult heart development [GO:0007512]; blastoderm segmentation [GO:0007350]; cephalic furrow formation [GO:0007376]; germ-band extension [GO:0007377]; heart morphogenesis [GO:0003007]; motor neuron axon guidance [GO:0008045]; negative regulation of cardioblast cell fate specification [GO:0009997]; negative regulation of... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Even-skipped homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: May play a role in determining neuronal identity. May be directly involved in specifying identity of individual neurons. Pair-rule protein required for segmentation; involved in transforming the broad, spatial, aperiodic expression patterns of the gap genes into a system of precise periodic expression pattern... | Drosophila melanogaster (Fruit fly) |
P06603 | TBA1_DROME | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTVGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADQCTGLQGFLIFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | lysosome localization [GO:0032418]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | astral microtubule [GO:0000235]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects ... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Drosophila melanogaster (Fruit fly) |
P06604 | TBA2_DROME | MRECISVHIGQAGVQIGNACWELYCLEHGIQPDGHMPSDKTVGGGDDSFSTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDVVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYMNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISVEKAYHEQLTVAEITNACFEPANQMVKCDPRRGKYMACCMLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; unidimensional cell growth [GO:0009826] | cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; microtubule [GO:0005874]; spindle microtubule [GO:0005876] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects ... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Drosophila melanogaster (Fruit fly) |
P06605 | TBA3_DROME | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTVGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADQCTGLQGFLIFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFAVYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPVISAEKAYHEQLSVAEITNACFEPANQMVKVDPRHGKYMACCMLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; sperm axoneme assembly [GO:0007288]; spermatogenesis [GO:0007283] | cytoplasm [GO:0005737]; microtubule [GO:0005874]; perinuclear region of cytoplasm [GO:0048471] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; myosin binding [GO:0017022]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects ... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Drosophila melanogaster (Fruit fly) |
P06606 | TBA4_DROME | MREVVSIQIGQCGIQIGNACWELYLLEHGINLDGSLKTKEELTASGSSASVGHDTSANDARTFFTETGNGKQVPRSIFVDLEPTVIDDVRNGCMRELYHPEQLISGKEDAANNYARGRYSIGKEVIDRVTSRLQKIAEQCDSLQGFLIFHSLGGGTGSGFTSLLVERLSTDYSKKCKLDFAVYPSPKVSTAVVEPYNALLTTHSTMDHSDCVFMVDNEAIYDICNNSLGVDRPAYRNLNRLIAQIVSSTTASLRFSGSMNVDLNEFQTNLVPFPRIHFPLVAYAPLMSAERSAHEQHAITTLTNACFESSNMMVKCDPRA... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | central nervous system development [GO:0007417]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic cleavage [GO:0040016]; female pronucleus assembly [GO:0035038]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; mitotic spindle organization [GO:0007052]; mRNA... | cortical microtubule [GO:0055028]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; spindle [GO:0005819] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Drosophila melanogaster (Fruit fly) |
P06607 | VIT3_DROME | MMSLRICLLATCLLVAAHASKDASNDRLKPTKWLTATELENVPSLNDITWERLENQPLEQGAKVIEKIYHVGQIKHDLTPSFVPSPSNVPVWIIKSNGQKVECKLNNYVETAKAQPGFGEDEVTIVLTGLPKTSPAQQKAMRRLIQAYVQKYNLQQLQKNAQEQQQQLKSSDYDYTSSEEAADQWKSAKAASGDLIIIDLGSTLTNFKRYAMLDVLNTGAMIGQTLIDLTNKGVPQEIIHLIGQGISAHVAGAAGNKYTAQTGHKLRRITGLDPAKVLSKRPQILGGLSRGDADFVDAIHTSTFAMGTPIRCGDVDFYPN... | null | null | embryo development ending in birth or egg hatching [GO:0009792]; lipid catabolic process [GO:0016042]; regulation of embryonic development [GO:0045995]; response to bacterium [GO:0009617]; sex differentiation [GO:0007548] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; P granule [GO:0043186] | serine hydrolase activity [GO:0017171] | PF00151; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | PTM: Tyrosine sulfation occurs in the female only and plays an essential functional role. {ECO:0000269|PubMed:3922974}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Vitellogenin is the major yolk protein of eggs where it is used as a food source during embryogenesis. Vitellogenins and their receptor yl/yolkless are required for maintenance of microtubule plus-end orientation towards the posterior pole of oocytes (PubMed:33891588). Involved in polarized localization of ge... | Drosophila melanogaster (Fruit fly) |
P06609 | BTUC_ECOLI | MLTLARQQQRQNIRWLLCLSVLMLLALLLSLCAGEQWISPGDWFTPRGELFVWQIRLPRTLAVLLVGAALAISGAVMQALFENPLAEPGLLGVSNGAGVGLIAAVLLGQGQLPNWALGLCAIAGALIITLILLRFARRHLSTSRLLLAGVALGIICSALMTWAIYFSTSVDLRQLMYWMMGGFGGVDWRQSWLMLALIPVLLWICCQSRPMNMLALGEISARQLGLPLWFWRNVLVAATGWMVGVSVALAGAIGFIGLVIPHILRLCGLTDHRVLLPGCALAGASALLLADIVARLALAAAELPIGVVTATLGAPVFIWL... | null | null | cobalamin transport [GO:0015889] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; BtuCD complex [GO:1990193]; cobalamin transport complex [GO:1990191]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ABC-type vitamin B12 transporter activity [GO:0015420]; identical protein binding [GO:0042802]; transmembrane transporter activity [GO:0022857] | PF01032; | 1.10.3470.10; | Binding-protein-dependent transport system permease family, FecCD subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane. | Escherichia coli (strain K12) |
P06611 | BTUD_ECOLI | MSIVMQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFATPVWHYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPQANPAGQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNFRRLDIEGHRMLISTI | 7.6.2.8 | null | cobalamin transport [GO:0015889] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; BtuCD complex [GO:1990193]; cobalamin transport complex [GO:1990191]; extrinsic component of membrane [GO:0019898]; membrane [GO:0016020] | ABC-type vitamin B12 transporter activity [GO:0015420]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626] | PF00005; | 3.40.50.300; | ABC transporter superfamily, Vitamin B12 importer (TC 3.A.1.13.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate; Xref=Rhea:RHEA:17873, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:140785, ChEBI:CHEBI:456216; EC=7.6.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01005}; | null | null | null | null | FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01005}. | Escherichia coli (strain K12) |
P06612 | TOP1_ECOLI | MGKALVIVESPAKAKTINKYLGSDYVVKSSVGHIRDLPTSGSAAKKSADSTSTKTAKKPKKDERGALVNRMGVDPWHNWEAHYEVLPGKEKVVSELKQLAEKADHIYLATDLDREGEAIAWHLREVIGGDDARYSRVVFNEITKNAIRQAFNKPGELNIDRVNAQQARRFMDRVVGYMVSPLLWKKIARGLSAGRVQSVAVRLVVEREREIKAFVPEEFWEVDASTTTPSGEALALQVTHQNDKPFRPVNKEQTQAAVSLLEKARYSVLEREDKPTTSKPGAPFITSTLQQAASTRLGFGVKKTMMMAQRLYEAGYITYM... | 5.6.2.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796}; Note=Binds two Mg(2+) ions per subunit. The magnesium ions form salt bridges with both the protein... | DNA topological change [GO:0006265] | chromosome [GO:0005694]; cytosol [GO:0005829] | DNA binding [GO:0003677]; DNA topoisomerase activity [GO:0003916]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; metal ion binding [GO:0046872] | PF21372;PF08272;PF01131;PF01751;PF01396; | 2.20.25.10;3.40.50.140;3.30.65.10;1.10.460.10;2.70.20.10;1.10.290.10; | Type IA topoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00952, ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:14604525, ECO:0000269|PubMed:21482796, ECO:0000269|PubMed:9497321}; | null | null | null | null | FUNCTION: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... | Escherichia coli (strain K12) |
P06616 | ERA_ECOLI | MSIDKSYCGFIAIVGRPNVGKSTLLNKLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRAINRLMNKAASSSIGDVELVIFVVEGTRWTPDDEMVLNKLREGKAPVILAVNKVDNVQEKADLLPHLQFLASQMNFLDIVPISAETGLNVDTIAAIVRKHLPEATHHFPEDYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFVSNERGGYDINGLILVEREGQKKMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWVKVKSGWADDERALRSLGYVDDL | null | null | protein phosphorylation [GO:0006468]; ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; rRNA binding [GO:0019843]; small ribosomal subunit rRNA binding [GO:0070181] | PF07650;PF01926; | 3.30.300.20;3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Era GTPase family | PTM: Autophosphorylated. {ECO:0000269|PubMed:8919456}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8282709}. Cell inner membrane {ECO:0000269|PubMed:8282709}; Peripheral membrane protein {ECO:0000269|PubMed:8282709}; Cytoplasmic side {ECO:0000269|PubMed:8282709}. Note=Binding is GDP or GTP-dependent, slightly more protein is bound in the presence of GTP than GDP. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.4 uM for GTP (for His-tagged protein at pH 8.0, 5 mM MgCl(2)) {ECO:0000269|PubMed:2105934, ECO:0000269|PubMed:8919456}; KM=9 uM for GTP (for overexpressed protein at pH 8.0, 5 mM MgCl(2)) {ECO:0000269|PubMed:2105934, ECO:0000269|PubMed:8919456}; | null | null | null | FUNCTION: An essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring on the order of seconds whereas hydrolysis occurs on the order of minutes. Plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing and 30S ribosomal subuni... | Escherichia coli (strain K12) |
P06621 | CBPG_PSES6 | MRPSIHRTAIAAVLATAFVAGTALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIV... | 3.4.17.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:9083113}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:9083113}; | proteolysis [GO:0006508] | null | carboxypeptidase activity [GO:0004180]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237] | PF07687;PF01546; | 3.30.70.360;3.40.630.10; | Peptidase M20A family | null | null | CATALYTIC ACTIVITY: Reaction=Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups.; EC=3.4.17.11; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity. | Pseudomonas sp. (strain RS-16) |
P06623 | CN37_BOVIN | MSSSGAKDKPELQFPFLQDEETVATLQECKTLFILRGLPGSGKSTLARFIVDKYRDGTKMVSADSYKITPGARGSFSEEYKQLDEDLAACCRRDFRVLVLDDTNHERERLEQLFELADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSAALWKTGQTFLEELGNHKAFKKELRHFVSGDEPREKIELVTYFGKRPPGVLHCTTKFCDYGKAAGAEEYAQQDVVKKSYCKAFTLTISALFVTPKTTGARVELSEQQLALWPNDVDKLSPSDNLPRGSRAHITLGCAGDVEA... | 3.1.4.37 | null | cyclic nucleotide catabolic process [GO:0009214] | cytoplasm [GO:0005737]; melanosome [GO:0042470]; membrane [GO:0016020] | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity [GO:0004113]; RNA binding [GO:0003723] | PF13671;PF05881; | 3.90.1740.10;3.40.50.300; | 2H phosphoesterase superfamily, CNPase family | PTM: Met-1 may be removed after translation. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P16330}; Lipid-anchor {ECO:0000250|UniProtKB:P16330}. Melanosome {ECO:0000250|UniProtKB:P09543}. Note=Firmly bound to membrane structures of brain white matter. {ECO:0000250|UniProtKB:P16330}. | CATALYTIC ACTIVITY: Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37; Evidence={ECO:0000269|PubMed:6272743}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for AMP {ECO:0000269|PubMed:6272743}; KM=0.4 mM for GMP {ECO:0000269|PubMed:6272743}; KM=6.3 mM for CMP {ECO:0000269|PubMed:6272743}; KM=7.1 mM for UMP {ECO:0000269|PubMed:6272743}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 (in the presence of both hexadecyltrimethylammonium bromide and serum albumin). {ECO:0000269|PubMed:6272743}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:6272743}; | FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (PubMed:6272743). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). {ECO:0000250|UniProtKB:P16330, ECO:0000269|PubMed:6272743}. | Bos taurus (Bovine) |
P06624 | MIP_BOVIN | MWELRSASFWRAICAEFFASLFYVFFGLGASLRWAPGPLHVLQVALAFGLALATLVQAVGHISGAHVNPAVTFAFLVGSQMSLLRAICYMVAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHPGVSVGQATIVEIFLTLQFVLCIFATYDERRNGRLGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFTNHWVYWVGPVIGAGLGSLLYDFLLFPRLKSVSERLSILKGSRPSESNGQPEVTGEPVELKTQAL | null | null | gap junction-mediated intercellular transport [GO:1990349]; lens development in camera-type eye [GO:0002088]; positive regulation of cell adhesion [GO:0045785]; protein homotetramerization [GO:0051289]; visual perception [GO:0007601]; water transport [GO:0006833] | apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; gap junction [GO:0005921]; plasma membrane [GO:0005886] | calmodulin binding [GO:0005516]; structural constituent of eye lens [GO:0005212]; water channel activity [GO:0015250] | PF00230; | 1.20.1080.10; | MIP/aquaporin (TC 1.A.8) family | PTM: Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes (By similarity). {ECO:0000250}.; PTM: Fatty acylated at Met-1 and Lys-238. The acyl modifications, in decreasing order of ion abundance, are: oleoyl (C18:1) > palmitoyl... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell junction, gap junction {ECO:0000250|UniProtKB:P30301}. | null | null | null | null | null | FUNCTION: Water channel (PubMed:23893133). Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core (By similarity).... | Bos taurus (Bovine) |
P06632 | DKGA_CORSC | MTVPSIVLNDGNSIPQLGYGVFKVPPADTQRAVEEALEVGYRHIDTAAIYGNEEGVGAAIAASGIARDDLFITTKLWNDRHDGDEPAAAIAESLAKLALDQVDLYLVHWPTPAADNYVHAWEKMIELRAAGLTRSIGVSNHLVPHLERIVAATGVVPAVNQIELHPAYQQREITDWAAAHDVKIESWGPLGQGKYDLFGAEPVTAAAAAHGKTPAQAVLRWHLQKGFVVFPKSVRRERLEENLDVFDFDLTDTEIAAIDAMDPGDGSGRVSAHPDEVD | 1.1.1.346 | null | L-ascorbic acid biosynthetic process [GO:0019853] | cytoplasm [GO:0005737] | oxidoreductase activity [GO:0016491] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2-dehydro-L-idonate + NADP(+) = 2,5-didehydro-D-gluconate + H(+) + NADPH; Xref=Rhea:RHEA:35111, ChEBI:CHEBI:11449, ChEBI:CHEBI:15378, ChEBI:CHEBI:36602, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.346; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 mM for 2,5-diketo-D-gluconate {ECO:0000269|PubMed:3597405}; KM=10 uM for NADPH {ECO:0000269|PubMed:3597405}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.4. Active over a broad pH range. {ECO:0000269|PubMed:3597405}; | null | FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B. | Corynebacterium sp. (strain ATCC 31090) |
P06634 | DED1_YEAST | MAELSEQVQNLSINDNNENGYVPPHLRGKPRSARNNSSNYNNNNGGYNGGRGGGSFFSNNRRGGYGNGGFFGGNNGGSRSNGRSGGRWIDGKHVPAPRNEKAEIAIFGVPEDPNFQSSGINFDNYDDIPVDASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLMACAQTGSGKTGGFLFPVLSESFKTGPSPQPESQGSFYQRKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQI... | 3.6.4.13 | null | cell differentiation [GO:0030154]; positive regulation of formation of translation preinitiation complex [GO:1901195]; spliceosomal complex disassembly [GO:0000390]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; eukaryotic initiation factor 4G binding [GO:0031370]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724]; RNA strand annealing activity [GO:0033592]; translation initiation factor activity [GO:0003743] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX3/DED1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | 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; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 mM for ATP {ECO:0000269|PubMed:15201868, ECO:0000269|PubMed:18332124}; | null | null | null | FUNCTION: ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes. Has weak ATP-dependent affinity for dsRNA, but strong ATP-dependent affinity for ssRNA. Acts as a virus host factor involved in th... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06636 | HBA3_XENLA | MTLTDSDKAAVVALWGKIAPQANAIGAEALERLFLSYPQTKTYFSHFDLSHGSADLANHGGKVVNALGEAAKHIDDLDAALSTLSDLHAYNLRVDPGNFKLLSHTIQVTLAIHFHKEFDAATQAAWDKFLAEVATVLTSKYR | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: This is a larval (tadpole) alpha-globin. | Xenopus laevis (African clawed frog) |
P06637 | HBA4_XENLA | MTLTDSDKAAIVALWGKIAPQASAIGAEALERLFLSYPQTKTYFSHFDVSHGSADLSNHGGKVVNALGEAAKHIDDLDSALSTLSDLHAYNLRIDPGNFKLLSHTIQVTLAIHFHKEFDAATQAAWDKFLAEVATVLTSKYR | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: This is a larval (tadpole) alpha-globin. | Xenopus laevis (African clawed frog) |
P06652 | MPIP_SCHPO | MDSPLSSLSFTNTLSGKRNVLRPAARELKLMSDRNANQELDFFFPKSKHIASTLVDPFGKTCSTASPASSLAADMSMNMHIDESPALPTPRRTLFRSLSCTVETPLANKTIVSPLPESPSNDALTESYFFRQPASKYSITQDSPRVSSTIAYSFKPKASIALNTTKSEATRSSLSSSSFDSYLRPNVSRSRSSGNAPPFLRSRSSSSYSINKKKGTSGGQATRHLTYALSRTCSQSSNTTSLLESCLTDDTDDFELMSDHEDTFTMGKVADLPESSVELVEDAASIQRPNSDFGACNDNSLDDLFQASPIKPIDMLPKIN... | 3.1.3.48 | null | cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic G2 cell size control checkpoint signaling [GO:0031569]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of G2/MI transition... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | phosphoprotein phosphatase activity [GO:0004721]; protein tyrosine phosphatase activity [GO:0004725] | PF00581; | 3.40.250.10; | MPI phosphatase family | PTM: Phosphorylated by srk1 in the N-terminus; phosphorylation promotes nuclear exclusion. {ECO:0000269|PubMed:15629716}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15629716}. Nucleus {ECO:0000269|PubMed:15629716}. Note=Accumulates in the nucleus in cycling cells; nuclear localization is the highest in G2. {ECO:0000269|PubMed:15629716}. | 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:0000250|UniProtKB:P30303}; | null | null | null | null | FUNCTION: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic and meiotic progression (PubMed:3955656, PubMed:7498766, Ref.3). Directly dephosphorylates cdc2 and stimulates its kinase activity (By similarity). Required for the G2/M transition of the cell cycle (PubMed:15629716). Requir... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P06681 | CO2_HUMAN | MGPLMVLFCLLFLYPGLADSAPSCPQNVNISGGTFTLSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQWQTPGATRSLSKAVCKPVRCPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVCDNGAGHCPNPGISLGAVRTGFRFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICRQPYSYDFPEDVAPALGTSFSHMLGATNPTQKTKESLGRKIQIQRSGHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVI... | 3.4.21.43 | null | complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; positive regulation of apoptotic cell clearance [GO:2000427]; proteolysis [GO:0006508]; response to bacterium [GO:0009617]; response to lipopolysaccharide [GO:0032496]; response to nutrient [G... | classical-complement-pathway C3/C5 convertase complex [GO:0005601]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | PF00084;PF00089;PF00092; | 2.10.70.10;2.40.10.10;3.40.50.410; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.; EC=3.4.21.43; | null | null | null | null | FUNCTION: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase. | Homo sapiens (Human) |
P06683 | CO9_MOUSE | MASGMAITLALAIFALGVNAQMPIPVSREEQEQHYPIPIDCRMSPWSNWSECDPCLKQRFRSRSILAFGQFNGKSCVDVLGDRQGCEPTQECEEIQENCGNDFQCETGRCIKRRLLCNGDNDCGDYSDENDCDDDPRTPCRDRVAEESELGLTAGYGINILGMEPLRTPFDNEFYNGLCDRVRDEKTYYRKPWNVVSLIYETKADKSFRTENYDEHLEVFKAINREKTSNFNADFALKFSATEVPEKGAGEVSPAEHSSKPTNISAKFKFSYFMGKNFRRLSSYFSQSKKMFVHLRGVVQLGRFVMRNRDVVLRSTFLDD... | null | null | cell killing [GO:0001906]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778]; protein homooligomerization [GO:0051260] | extracellular space [GO:0005615]; membrane attack complex [GO:0005579]; other organism cell membrane [GO:0044218]; plasma membrane [GO:0005886] | null | PF00057;PF01823;PF00090; | 2.10.25.10;4.10.400.10;2.20.100.10; | Complement C6/C7/C8/C9 family | PTM: Initially, positions and connectivity of disulfide bonds were based on peptide sequencing done for the human protein. The high-resolution crystal structure for the mouse protein corrected the positions and connectivities of some disulfide bonds (PubMed:30111885). The distance between Cys-55 and Cys-92 in the monom... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02748}. Target cell membrane {ECO:0000250|UniProtKB:P02748}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02748}. Note=Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 1... | null | null | null | null | null | FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC. {ECO:0000250|UniProtKB:P02748}. | Mus musculus (Mouse) |
P06684 | CO5_MOUSE | MGLWGILCLLIFLDKTWGQEQTYVISAPKILRVGSSENVVIQVHGYTEAFDATLSLKSYPDKKVTFSSGYVNLSPENKFQNAALLTLQPNQVPREESPVSHVYLEVVSKHFSKSKKIPITYNNGILFIHTDKPVYTPDQSVKIRVYSLGDDLKPAKRETVLTFIDPEGSEVDIVEENDYTGIISFPDFKIPSNPKYGVWTIKANYKKDFTTTGTAYFEIKEYVLPRFSVSIELERTFIGYKNFKNFEITVKARYFYNKVVPDAEVYAFFGLREDIKDEEKQMMHKATQAAKLVDGVAQISFDSETAVKELSYNSLEDLNN... | null | null | complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; in utero embryonic development [GO:0001701]; inflammatory response [GO:0006954]; killing of cells of another organism [GO:0031640]; positive regulation of angiogenesis [GO:0045766] | extracellular space [GO:0005615]; membrane attack complex [GO:0005579] | endopeptidase inhibitor activity [GO:0004866] | PF00207;PF07703;PF07677;PF01821;PF21309;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678; | 1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled.; FUNCTION: [C5a anaphylatoxin]: Derived fr... | Mus musculus (Mouse) |
P06685 | AT1A1_RAT | MGKGVGRDKYEPAAVSEHGDKKSKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSATEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEA... | 7.2.2.13 | null | cardiac muscle contraction [GO:0060048]; cellular response to mechanical stimulus [GO:0071260]; cellular response to steroid hormone stimulus [GO:0071383]; energy coupled proton transmembrane transport, against electrochemical gradient [GO:0015988]; establishment or maintenance of transmembrane electrochemical gradient... | apical plasma membrane [GO:0016324]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; melanosome [GO:0042470]; membrane [GO:001... | ADP binding [GO:0043531]; ankyrin binding [GO:0030506]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type potassium transmembrane transporter activity [GO:0008556]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; phosphatase activity [GO:0016791]; phosphatidylinositol 3-kinase... | PF13246;PF00689;PF00690;PF00122; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | PTM: Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity. {ECO:0000269|PubMed:10473631, ECO:0000269|PubMed:1... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VDN2}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:16914892}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein {ECO:0000255}. Cell pro... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; Evidence={ECO:0000269|PubMed:17939993,... | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... | Rattus norvegicus (Rat) |
P06686 | AT1A2_RAT | MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGALLCFLAYGILAAMEDEPSNDNLYLGIVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGQTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVI... | 7.2.2.13 | null | adult locomotory behavior [GO:0008344]; amygdala development [GO:0021764]; ATP metabolic process [GO:0046034]; behavioral fear response [GO:0001662]; cardiac muscle contraction [GO:0060048]; cellular response to mechanical stimulus [GO:0071260]; cellular response to steroid hormone stimulus [GO:0071383]; energy coupled... | caveola [GO:0005901]; cell projection [GO:0042995]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; intercalated disc [GO:0014704]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; organelle membrane [GO:0031090]; plasma ... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled monoatomic cation transmembrane transporter activity [GO:0019829]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; potassium ion binding [GO:0030955]; protein heterodimerization activity [GO:0046982]; protein-folding ch... | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... | Rattus norvegicus (Rat) |
P06687 | AT1A3_RAT | MGDKKDDKSSPKKSKAKERRDLDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTHSKAQEILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNLYLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDLVEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCVEGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILSLILGYTWLEAVIFLIGIIVA... | 7.2.2.13 | null | adult locomotory behavior [GO:0008344]; cardiac muscle contraction [GO:0060048]; cellular response to amyloid-beta [GO:1904646]; cellular response to retinoic acid [GO:0071300]; cellular response to thyroid hormone stimulus [GO:0097067]; cerebral cortex development [GO:0021987]; intracellular potassium ion homeostasis ... | axon [GO:0030424]; calyx of Held [GO:0044305]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendritic spine head [GO:0044327]; dendritic spine neck [GO:0044326]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; myelin sheath [GO:0043209]; neuron to neuron synapse [GO:009898... | amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; D1 dopamine receptor binding [GO:0031748]; heparan sulfate proteoglycan binding [GO:0043395]; metal ion binding [GO:0046872]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; P-type sodium:potassium-e... | PF13246;PF00689;PF00690;PF00122; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... | Rattus norvegicus (Rat) |
P06700 | SIR2_YEAST | MTIPHMKYAVSKTSENKVSNTVSPTQDKDAIRKQPDDIINNDEPSHKKIKVAQPDSLRETNTTDPLGHTKAALGEVASMELKPTNDMDPLAVSAASVVSMSNDVLKPETPKGPIIISKNPSNGIFYGPSFTKRESLNARMFLKYYGAHKFLDTYLPEDLNSLYIYYLIKLLGFEVKDQALIGTINSIVHINSQERVQDLGSAISVTNVEDPLAKKQTVRLIKDLQRAINKVLCTRLRLSNFFTIDHFIQKLHTARKILVLTGAGVSTSLGIPDFRSSEGFYSKIKHLGLDDPQDVFNYNIFMHDPSVFYNIANMVLPPEK... | 2.3.1.286 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23307867}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23307867}; | chromatin organization [GO:0006325]; double-strand break repair via nonhomologous end joining [GO:0006303]; establishment of protein-containing complex localization to telomere [GO:0097695]; heterochromatin formation [GO:0031507]; negative regulation of DNA amplification [GO:1904524]; negative regulation of DNA recombi... | chromatin silencing complex [GO:0005677]; chromosome, telomeric region [GO:0000781]; heterochromatin [GO:0000792]; nuclear inner membrane [GO:0005637]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; rDNA heterochromatin [GO:0033553]; RENT complex [GO:0030869] | metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent histone H3K14 deacetylase activity [GO:0032041]; NAD-dependent histone H3K9 deacetylase activity [GO:0046969]; NAD-dependent histone H4K16 deacetylase activity [GO:0046970]; transcription co... | PF04574;PF02146; | 1.20.120.1710;3.30.1600.10;3.40.50.1220; | Sirtuin family, Class I subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9214640}. Note=Associated with nucleolar chromatin. Preferentially bound to the spacer regions of the rDNA repeats through its interaction with NET1. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29.3 uM for NAD(+) {ECO:0000269|PubMed:15274642}; KM=239 uM for a synthetic histone H3K9 acetyllysine peptide {ECO:0000269|PubMed:15274642}; KM=420 uM for a synthetic histone H3K14 acetyllysine peptide {ECO:0000269|PubMed:15274642}; KM=140 uM for a synthetic histon... | null | null | null | FUNCTION: NAD-dependent deacetylase, which participates in a wide range of cellular events including chromosome silencing, chromosome segregation, DNA recombination and the determination of life span. Involved in transcriptional repression of the silent mating-type loci HML and HMR and telomeric silencing via its assoc... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06701 | SIR3_YEAST | MAKTLKDLDGWQVIITDDQGRVIDDNNRRRSRKRGGENVFLKRISDGLSFGKGESVIFNDNVTETYSVYLIHEIRLNTLNNVVEIWVFSYLRWFELKPKLYYEQFRPDLIKEDHPLEFYKDKFFNEVNKSELYLTAELSEIWLKDFIAVGQILPESQWNDSSIDKIEDRDFLVRYACEPTAEKFVPIDIFQIIRRVKEMEPKQSDEYLKRVSVPVSGQKTNRQVMHKMGVERSSKRLAKKPSMKKIKIEPSADDDVNNGNIPSQRGTSTTHGSISPQEESVSPNISSASPSALTSPTDSSKILQKRSISKELIVSEEIPI... | null | null | DNA replication initiation [GO:0006270]; double-strand break repair via nonhomologous end joining [GO:0006303]; establishment of protein-containing complex localization to telomere [GO:0097695]; heterochromatin formation [GO:0031507]; mitotic DNA replication checkpoint signaling [GO:0033314]; nuclear-transcribed mRNA c... | chromatin silencing complex [GO:0005677]; chromosome, telomeric region [GO:0000781]; heterochromatin [GO:0000792]; mitochondrion [GO:0005739]; nuclear origin of replication recognition complex [GO:0005664]; nucleolus [GO:0005730] | chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; nucleic acid binding [GO:0003676]; nucleosome binding [GO:0031491]; single-stranded DNA binding [GO:0003697] | PF17872;PF01426; | 1.10.10.2450;1.10.8.60;2.30.30.490;3.40.50.300; | null | PTM: N-terminal acetylation by NatA is important for transcriptional silencing activity. {ECO:0000269|PubMed:15454564}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06702 | S10A9_HUMAN | MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; apoptotic process [GO:0006915]; astrocyte development [GO:0014002]; autocrine signaling [GO:0035425]; autophagy [GO:0006914]; cell-cell sig... | calprotectin complex [GO:1990660]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ... | antioxidant activity [GO:0016209]; arachidonic acid binding [GO:0050544]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; microtubule binding [GO:0008017]; RAGE receptor binding [GO:0050786]; Toll-like receptor 4 binding [GO:0035662]; zinc ion binding [GO:0008270] | PF01023; | 1.10.238.10; | S-100 family | PTM: Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization. {ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:15905572, ECO:0000269|PubMed:2478889}.; PTM: S-nitrosylation of Cys-3 is implicated in LDL(ox)-induced S-nitrosylation of GAPDH at 'Cys-247' through a transnitrosylase mechanism involving... | SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:8423249}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22489132, ECO:0000269|PubMed:9083090}. Cell membrane {ECO:0000269|PubMed:18786929}; Peripheral membrane protein {ECO:0000305|PubMed:18786929}. Note=Predominantly localized in ... | null | null | null | null | null | FUNCTION: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response (PubMed:12626582, PubMed:15331440, PubMed:16258195, PubMed:19122197, PubMed:20103766, PubMed:21325622, PubMed:8423249). It can induce neutrophil chemotaxis, adhesion, can ... | Homo sapiens (Human) |
P06703 | S10A6_HUMAN | MACPLDQAIGLLVAIFHKYSGREGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMEDLDRNKDQEVNFQEYVTFLGALALIYNEALKG | null | null | axonogenesis [GO:0007409]; positive regulation of fibroblast proliferation [GO:0048146]; signal transduction [GO:0007165] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471];... | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; monoatomic ion transmembrane transporter activity [GO:0015075]; protein homodimerization activity [GO:0042803]; S100 protein binding [GO:0044548]; tropomyosin binding [GO:0005523]; zinc ion binding [GO:0008270] | PF01023; | 1.10.238.10; | S-100 family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Nucleus envelope. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. | null | null | null | null | null | FUNCTION: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Bind... | Homo sapiens (Human) |
P06704 | CDC31_YEAST | MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS | null | null | cell division [GO:0051301]; Golgi vesicle transport [GO:0048193]; mRNA export from nucleus [GO:0006406]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; spindle pole body duplication [GO:0030474] | cytoplasm [GO:0005737]; half bridge of spindle pole body [GO:0005825]; mitotic spindle pole body [GO:0044732]; nuclear envelope [GO:0005635]; transcription export complex 2 [GO:0070390] | calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017] | PF13499; | 1.10.238.10; | Centrin family | null | SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:10684247}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:8188750}. Note=Spindle pole body, SPB half- bridge (PubMed:8188750). Interacts with the nuclear pore complex (NPCs) at the nucleus envelope (PubMed:10684247... | null | null | null | null | null | FUNCTION: Functions as a component of the spindle pole body (SPB) half-bridge (PubMed:10684247, PubMed:11156974, PubMed:12486115, PubMed:14504268, PubMed:8070654). At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication (PubMed:11156974, PubMed:12486115, ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06709 | BIRA_ECOLI | MKDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSVAVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAE... | 6.3.4.15 | null | biotin biosynthetic process [GO:0009102]; biotin metabolic process [GO:0006768]; protein modification process [GO:0036211]; regulation of DNA-templated transcription [GO:0006355] | cytoplasm [GO:0005737]; transcription repressor complex [GO:0017053] | ATP binding [GO:0005524]; biotin binding [GO:0009374]; biotin-[acetyl-CoA-carboxylase] ligase activity [GO:0004077]; DNA binding [GO:0003677]; nucleic acid binding [GO:0003676]; protein homodimerization activity [GO:0042803]; transcription cis-regulatory region binding [GO:0000976] | PF02237;PF03099;PF08279; | 2.30.30.100;1.10.10.10; | Biotin--protein ligase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:45621... | null | null | null | null | FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subun... | Escherichia coli (strain K12) |
P06710 | DPO3X_ECOLI | MSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARLLAKGLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPARGRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKALDVEQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVSTQAVSAMLGTLDDDQALSLVEAMVEANGERVMALINEAAARGIEWEALLVEMLGLLHRIAMVQLSPAALGNDMAAIELRMRELARTI... | 2.7.7.7 | null | DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA-templated DNA replication [GO:0006261] | DNA polymerase III complex [GO:0009360]; DNA polymerase III, clamp loader complex [GO:0043846]; replisome [GO:0030894] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; DNA polymerase processivity factor activity [GO:0030337]; DNA-directed DNA polymerase activity [GO:0003887]; identical protein binding [GO:0042802]; ribonucleoside triphosphate phosphatase a... | PF13177;PF12169;PF12168;PF12170; | 1.10.8.60;1.20.272.10;3.30.300.150;3.40.50.300; | DnaX/STICHEL family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; | null | null | null | null | FUNCTION: Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex (PubMed:2040637). DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase... | Escherichia coli (strain K12) |
P06715 | GSHR_ECOLI | MTKHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVEYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDGSLTLELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRR... | 1.8.1.7 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.; | cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; glutathione metabolic process [GO:0006749] | cytosol [GO:0005829]; membrane [GO:0016020] | FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; glutathione-disulfide reductase (NADP) activity [GO:0004362]; NADP binding [GO:0050661] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7; | null | null | null | null | FUNCTION: Maintains high levels of reduced glutathione in the cytosol. | Escherichia coli (strain K12) |
P06717 | ELAP_ECOLX | MKNITFIFFILLASPLYANGDRLYRADSRPPDEIKRSGGLMPRGHNEYFDRGTQMNINLYDHARGTQTGFVRYDDGYVSTSLSLRSAHLAGQSILSGYSTYYIYVIATAPNMFNVNDVLGVYSPHPYEQEVSALGGIPYSQIYGWYRVNFGVIDERLHRNREYRDRYYRNLNIAPAEDGYRLAGFPPDHQAWREEPWIHHAPQGCGNSSRTITGDTCNEETQNLSTIYLREYQSKVKRQIFSDYQSEVDIYNRIRDEL | null | null | null | extracellular space [GO:0005615] | toxin activity [GO:0090729] | PF01375; | 1.20.5.240;3.90.210.10; | Enterotoxin A family | null | null | null | null | null | null | null | FUNCTION: The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. | Escherichia coli |
P06721 | METC_ECOLI | MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLKKKLN... | 4.4.1.13; 4.4.1.28 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:3307782, ECO:0000269|PubMed:7049234, ECO:0000269|PubMed:8566238}; | L-cysteine catabolic process to pyruvate [GO:0019450]; methionine biosynthetic process [GO:0009086]; protein homotetramerization [GO:0051289]; transsulfuration [GO:0019346] | cytoplasm [GO:0005737]; protein-containing complex [GO:0032991] | alanine racemase activity [GO:0008784]; cystathionine beta-lyase activity [GO:0004121]; cysteine-S-conjugate beta-lyase activity [GO:0047804]; identical protein binding [GO:0042802]; L-cysteine desulfhydrase activity [GO:0080146]; pyridoxal phosphate binding [GO:0030170] | PF01053; | 3.90.1150.10;3.40.640.10; | Trans-sulfuration enzymes family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate; Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; Evidence={ECO:0000269|PubMed:7049234}; CATALYTIC ACTIVITY: Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide +... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for L-cystathionine {ECO:0000269|PubMed:7049234}; KM=0.25 mM for L-cystine {ECO:0000269|PubMed:7049234}; Vmax=249 umol/min/mg enzyme with L-cystathionine as substrate {ECO:0000269|PubMed:7049234}; Vmax=263 umol/min/mg enzyme with L-cystine as substrate {ECO... | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:7049234}; | null | FUNCTION: Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis (PubMed:7049234). Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine (PubMed:12883870). In addition, under certain growth conditions, exhibits significant alanine ... | Escherichia coli (strain K12) |
P06722 | MUTH_ECOLI | MSQPRPLLSPPETEEQLLAQAQQLSGYTLGELAALVGLVTPENLKRDKGWIGVLLEIWLGASAGSKPEQDFAALGVELKTIPVDSLGRPLETTFVCVAPLTGNSGVTWETSHVRHKLKRVLWIPVEGERSIPLAQRRVGSPLLWSPNEEEDRQLREDWEELMDMIVLGQVERITARHGEYLQIRPKAANAKALTEAIGARGERILTLPRGFYLKKNFTSALLARHFLIQ | null | null | DNA modification [GO:0006304]; mismatch repair [GO:0006298]; regulation of DNA recombination [GO:0000018] | cytoplasm [GO:0005737]; mismatch repair complex [GO:0032300] | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; T/G mismatch-specific endonuclease activity [GO:0043765] | PF02976; | 3.40.600.10; | MutH family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair. | Escherichia coli (strain K12) |
P06726 | PP71_HCMVA | MSQASSSPGEGPSSEAAAISEAEAASGSFGRLHCQVLRLITNVEGGSLEAGRLRLLDLRTNIEVSRPSVLCCFQENKSPHDTVDLTDLNIKGRCVVGEQDRLLVDLNNFGPRRLTPGSENNTVSVLAFALPLDRVPVSGLHLFQSQRRGGEENRPRMEARAIIRRTAHHWAVRLTVTPNWRRRTDSSLEAGQIFVSQFAFRAGAIPLTLVDALEQLACSDPNTYIHKTETDERGQWIMLFLHHDSPHPPTSVFLHFSVYTHRAEVVARHNPYPHLRRLPDNGFQLLIPKSFTLTRIHPEYIVQIQNAFETNQTHDTIFFP... | null | null | DNA-templated viral transcription [GO:0039695]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; virus-mediated perturbation of host defense response [GO:0019049] | host cell endoplasmic reticulum [GO:0044165]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | null | PF05784; | null | Herpesviridae pp71 family | PTM: S-nitrosylation limits ability to undermine the cGAS/STING antiviral pathway. {ECO:0000269|PubMed:32581105}. | SUBCELLULAR LOCATION: Virion tegument {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:19369322, ECO:0000269|PubMed:9000101}. Host endoplasmic reticulum {ECO:0000269|PubMed:28132838}. Note=Present in the nucleus shortly after infection as well as during the late phase of viral morphogenesis. Detected at nuclear domain 1... | null | null | null | null | null | FUNCTION: Stimulates viral immediate-early (IE) transcription. Plays a role in the inhibition of the host innate repsonse by targeting STING1 and thus the cGAS-STING pathway (PubMed:28132838, PubMed:32581105). Counteracts also host DAXX-mediated repression of viral transcription. Displaces a DAXX-binding protein, ATRX,... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P06727 | APOA4_HUMAN | MFLKAVVLTLALVAVAGARAEVSADQVATVMWDYFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYADQLRTQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYGENFNKALVQ... | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron assembly [GO:0034378]; chylomicron remodeling [GO:0034371]; high-density lipoprotein particle remodeling [GO:0034375]; hydrogen peroxide catabolic process... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extrace... | antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator ac... | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Phosphorylation sites are present in the extracellular medium. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. | Homo sapiens (Human) |
P06728 | APOA4_MOUSE | MFLKAAVLTLALVAITGTRAEVTSDQVANVVWDYFTQLSNNAKEAVEQFQKTDVTQQLSTLFQDKLGDASTYADGVHNKLVPFVVQLSGHLAQETERVKEEIKKELEDLRDRMMPHANKVTQTFGENMQKLQEHLKPYAVDLQDQINTQTQEMKLQLTPYIQRMQTTIKENVDNLHTSMMPLATNLKDKFNRNMEELKGHLTPRANELKATIDQNLEDLRRSLAPLTVGVQEKLNHQMEGLAFQMKKNAEELQTKVSAKIDQLQKNLAPLVEDVQSKVKGNTEGLQKSLEDLNRQLEQQVEEFRRTVEPMGEMFNKALVQ... | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; high-density lipoprotein particle remodeling [GO:0034375]; hydrogen peroxide catabolic process [GO:0042744]; innate immune response in mucosa [GO:0002227]; leukocyte ... | blood microparticle [GO:0072562]; cell surface [GO:0009986]; chylomicron [GO:0042627]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; synapse [GO... | antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; copper ion binding [GO:0005507]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. | Mus musculus (Mouse) |
P06729 | CD2_HUMAN | MSFPCKFVASFLLIFNVSSKGAVSKEITNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTYKLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQERVSKPKISWTCINTTLTCEVMNGTDPELNLYQDGKHLKLSQRVITHKWTTSLSAKFKCTAGNKVSKESSVEPVSCPEKGLDIYLIIGICGGGSLLMVFVALLVFYITKRKKQRSRRNDEELETRAHRVATEERGRKPHQIPASTPQNPATSQHPPPPPGHRSQAPSHRPPPPGHRVQHQPQKRPPAPSGTQV... | null | null | apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cell-cell adhesion [GO:0098609]; heterotypic cell-cell adhesion [GO:0034113]; membrane raft polarization [GO:0001766]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]; positive regul... | cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; protein self-association [GO:0043621]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor activity [GO:0038023]; signaling receptor binding [GO:0005102] | PF05790;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:2437578}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function. | Homo sapiens (Human) |
P06730 | IF4E_HUMAN | MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV | null | null | behavioral fear response [GO:0001662]; cellular response to dexamethasone stimulus [GO:0071549]; G1/S transition of mitotic cell cycle [GO:0000082]; mRNA export from nucleus [GO:0006406]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of translation [GO:0017148]; neuron differentiation ... | chromatoid body [GO:0033391]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; nuclear speck... | DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; eukaryotic initiation factor 4G binding [GO:0031370]; mRNA cap binding [GO:0098808]; RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; RNA cap binding [GO:0000339]; translation initiation factor activity [GO:0003... | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex (PubMed:11154262, PubMed:3112145, PubMed:7590282, PubMed:7665584, PubMed:7782323, PubMed:8505316, PubMed:9878069). Phosphorylation also enhances its mRNA transport function (By similarity). Phosphorylation at Se... | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:25923732}. Cytoplasm {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:12554669, ECO:0000269|PubMed:1384058, ECO:0000269|PubMed:15657436, ECO:0000269|PubMed:21883093, ECO:000... | null | null | null | null | null | FUNCTION: Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:11606200, PubMed:22578813, PubMed:22684010, PubMed:24335285, PubMed:29... | Homo sapiens (Human) |
P06731 | CEAM5_HUMAN | MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYA... | null | null | apoptotic process [GO:0006915]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; homotypic cell-cell adhesion [GO:0034109]; negative regulation of anoikis [GO:2000811]; negative regulation of apoptotic... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | GPI anchor binding [GO:0034235]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase binding [GO:1990782] | PF13895;PF13927;PF07686; | 2.60.40.10; | Immunoglobulin superfamily, CEA family | PTM: Complex immunoreactive glycoprotein with a MW of 180 kDa comprising 60% carbohydrate. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:18086185, ECO:0000269|PubMed:2317824}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:18086185, ECO:0000269|PubMed:2317824}. Apical cell membrane {ECO:0000269|PubMed:10436421}. Cell surface {ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression (PubMed:10864933, PubMed:10910050, PubMed:2803308). Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:280330... | Homo sapiens (Human) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.