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Y2296_ARATH
ID   Y2296_ARATH             Reviewed;         494 AA.
AC   Q9SJG2;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Probable receptor-like protein kinase At2g42960;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=At2g42960; ORFNames=F7D19.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AC006580; AAM15294.1; -; Genomic_DNA.
DR   EMBL; AC006931; AAD21713.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10192.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62978.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62979.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62981.1; -; Genomic_DNA.
DR   PIR; D84860; D84860.
DR   RefSeq; NP_001318408.1; NM_001337002.1.
DR   RefSeq; NP_001325098.1; NM_001337005.1.
DR   RefSeq; NP_001325100.1; NM_001337004.1.
DR   RefSeq; NP_181825.1; NM_129858.2.
DR   AlphaFoldDB; Q9SJG2; -.
DR   SMR; Q9SJG2; -.
DR   STRING; 3702.AT2G42960.1; -.
DR   iPTMnet; Q9SJG2; -.
DR   PaxDb; Q9SJG2; -.
DR   PRIDE; Q9SJG2; -.
DR   ProteomicsDB; 242843; -.
DR   EnsemblPlants; AT2G42960.1; AT2G42960.1; AT2G42960.
DR   EnsemblPlants; AT2G42960.3; AT2G42960.3; AT2G42960.
DR   EnsemblPlants; AT2G42960.4; AT2G42960.4; AT2G42960.
DR   EnsemblPlants; AT2G42960.5; AT2G42960.5; AT2G42960.
DR   GeneID; 818898; -.
DR   Gramene; AT2G42960.1; AT2G42960.1; AT2G42960.
DR   Gramene; AT2G42960.3; AT2G42960.3; AT2G42960.
DR   Gramene; AT2G42960.4; AT2G42960.4; AT2G42960.
DR   Gramene; AT2G42960.5; AT2G42960.5; AT2G42960.
DR   KEGG; ath:AT2G42960; -.
DR   Araport; AT2G42960; -.
DR   TAIR; locus:2045620; AT2G42960.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_4_1_1; -.
DR   InParanoid; Q9SJG2; -.
DR   OMA; EGHEPET; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q9SJG2; -.
DR   PRO; PR:Q9SJG2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJG2; baseline and differential.
DR   Genevisible; Q9SJG2; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Receptor; Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..494
FT                   /note="Probable receptor-like protein kinase At2g42960"
FT                   /id="PRO_0000389474"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          183..462
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          442..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        309
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         189..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         172
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         256
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         313
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         343
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         348
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         356
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
SQ   SEQUENCE   494 AA;  55188 MW;  FD7E16AB0CCA05F6 CRC64;
     MPPESSLNAE MSKKISFFGL KGLKLWVWVC LVVGVFIVMI LCILSLWITF RRKSRRSSSK
     FPFNQIPHVS KDIRVDRAGF QNPHPESLYI EMNDKSTGKT MMSHLGRTKS SDNDTLSQCS
     SVNHHERACS SHSGEEGGFG SAGRQYGGGP VTASPLVGLP EISHLGWGHW FTLRDLELAT
     NRFAPVNVLG EGGYGVVYRG KLVNGTEVAV KKLLNNLGQA EKEFRVEVEA IGHVRHKNLV
     RLLGYCIEGV HRMLVYEYVN SGNLEQWLHG AMRQHGNLTW EARMKIITGT AQALAYLHEA
     IEPKVVHRDI KASNILIDDE FNAKLSDFGL AKLLDSGESH ITTRVMGTFG YVAPEYANTG
     LLNEKSDIYS FGVLLLEAIT GRDPVDYGRP ANEVNLVEWL KMMVGTRRAE EVVDPRLEPR
     PSKSALKRAL LVSLRCVDPE AEKRPRMSQV ARMLESDEHP FHKERRNKRS KTAGMEIVET
     KDESLGPSGS ETKP
 
 
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