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YAK1_ARATH
ID   YAK1_ARATH              Reviewed;         956 AA.
AC   Q8RWH3; Q56YT6; Q9FGC1;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Dual specificity protein kinase YAK1 homolog {ECO:0000305};
DE            Short=AtYAK1 {ECO:0000303|PubMed:26452715};
DE            EC=2.7.12.1 {ECO:0000269|PubMed:26452715};
DE   AltName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase YAK1 {ECO:0000305};
GN   Name=YAK1 {ECO:0000303|PubMed:26452715};
GN   OrderedLocusNames=At5g35980 {ECO:0000312|Araport:AT5G35980};
GN   ORFNames=MEE13.9 {ECO:0000312|EMBL:BAB09254.1};
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, AND
RP   PHOSPHORYLATION AT SER-222.
RX   PubMed=26452715; DOI=10.1016/j.febslet.2015.09.025;
RA   Kim D., Ntui V.O., Zhang N., Xiong L.;
RT   "Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase.";
RL   FEBS Lett. 589:3321-3327(2015).
RN   [8]
RP   FUNCTION, INDUCTION BY DROUGHT STRESS, AND DISRUPTION PHENOTYPE.
RX   PubMed=27264339; DOI=10.1002/1873-3468.12234;
RA   Kim D., Ntui V.O., Xiong L.;
RT   "Arabidopsis YAK1 regulates abscisic acid response and drought
RT   resistance.";
RL   FEBS Lett. 590:2201-2209(2016).
CC   -!- FUNCTION: Dual specificity protein kinase that phosphorylates ANN1,
CC       ANN2 and CP29B at serine and threonine residues, and ANN1, ANN2 and
CC       ANN4 at tyrosine residues. May regulate the phosphorylation status of
CC       annexin proteins (PubMed:26452715). Acts as positive regulator in
CC       abscisic acid (ABA)-mediated regulation of postgermination growth and
CC       drought response. May regulate the expression of ABA-responsive genes
CC       such as RD22, RD29A, LTI65/RD29B and RAB18 (PubMed:27264339).
CC       {ECO:0000269|PubMed:26452715, ECO:0000269|PubMed:27264339}.
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=2.7.12.1;
CC         Evidence={ECO:0000269|PubMed:26452715};
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=2.7.12.1; Evidence={ECO:0000269|PubMed:26452715};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC         Evidence={ECO:0000269|PubMed:26452715};
CC   -!- INDUCTION: Induced by drought stress. {ECO:0000269|PubMed:27264339}.
CC   -!- PTM: Autophosphorylated at Ser-222. {ECO:0000269|PubMed:26452715}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant seedlings exhibit decreased sensitivity to
CC       abscisic acid (ABA) inhibition of seed germination, cotyledon greening,
CC       seedling growth, and stomatal movement. Decreased tolerance to drought
CC       stress. {ECO:0000269|PubMed:27264339}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AED94036.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB09254.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD93822.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAD93839.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB026643; BAB09254.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94035.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94036.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY093090; AAM13089.1; -; mRNA.
DR   EMBL; BT010549; AAQ65172.1; -; mRNA.
DR   EMBL; AK221229; BAD93822.1; ALT_FRAME; mRNA.
DR   EMBL; AK221235; BAD93839.1; ALT_FRAME; mRNA.
DR   EMBL; AK230350; BAF02149.1; -; mRNA.
DR   RefSeq; NP_001031970.1; NM_001036893.2.
DR   RefSeq; NP_198447.2; NM_122989.4.
DR   AlphaFoldDB; Q8RWH3; -.
DR   SMR; Q8RWH3; -.
DR   IntAct; Q8RWH3; 5.
DR   MINT; Q8RWH3; -.
DR   STRING; 3702.AT5G35980.1; -.
DR   iPTMnet; Q8RWH3; -.
DR   PaxDb; Q8RWH3; -.
DR   PRIDE; Q8RWH3; -.
DR   ProteomicsDB; 228629; -.
DR   EnsemblPlants; AT5G35980.1; AT5G35980.1; AT5G35980.
DR   GeneID; 833590; -.
DR   Gramene; AT5G35980.1; AT5G35980.1; AT5G35980.
DR   KEGG; ath:AT5G35980; -.
DR   Araport; AT5G35980; -.
DR   TAIR; locus:2162868; AT5G35980.
DR   eggNOG; KOG0667; Eukaryota.
DR   InParanoid; Q8RWH3; -.
DR   OrthoDB; 194243at2759; -.
DR   PhylomeDB; Q8RWH3; -.
DR   BRENDA; 2.7.12.1; 399.
DR   PRO; PR:Q8RWH3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8RWH3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; IDA:TAIR.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:TAIR.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR   GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IMP:TAIR.
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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Stress response;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..956
FT                   /note="Dual specificity protein kinase YAK1 homolog"
FT                   /id="PRO_0000442107"
FT   DOMAIN          122..464
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          620..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..762
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        249
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         128..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:26452715"
SQ   SEQUENCE   956 AA;  105523 MW;  45016D7F01E11481 CRC64;
     MDDIDSSDGA AAARAGEIGS IGVSTPWKPI QLVFKRYLPQ NGSASKVHVA VKKPVVVRLT
     RDLVETYKIC DPQFKYRGEL NPKRYLTTPS VGVNNDGFDN VNYDLILAVN DDFCSSDSRQ
     RYIVKDLLGH GTFGQVAKCW VPETNSFVAV KVIKNQLAYY QQALVEVSIL TTLNKKYDPE
     DKNHIVRIYD YFLHQSHLCI CFELLDMNLY ELIKINQFRG LSLSIVKLFS KQILLGLALL
     KDAGIIHCDL KPENILLCAS VKPTEIKIID FGSACMEDKT VYSYIQSRYY RSPEVLLGYQ
     YTTAIDMWSF GCIVAELFLG LPLFPGGSEF DILRRMIEIL GKQPPDYVLK EAKNTNKFFK
     CVGSVHNLGN GGTYGGLKSA YMALTGEEFE AREKKKPEIG KEYFNHKNLE EIVKSYPYKI
     NLPEDDVVKE TQIRLALIDF LKGLMEFDPA KRWSPFQAAK HPFITGEPFT CPYNPPPETP
     RVHVTQNIKV DHHPGEGHWF AAGLSPHVSG RTRIPMHNSP HFQMMPYSHA NSYGSIGSYG
     SYNDGTIQDN SYGSYGGTGN MFAYYSPVNH PGLYMQNQGG VSMLGTSPDA RRRVMQYPHG
     NGPNGLGTSP SAGNFAPLPL GTSPSQFTPN TNNQFLAGSP GHHGPTSPVR NSCHGSPLGK
     MAAFSQINRR MSAGYSGGSQ SQDSSLSQAQ GHGMDNFYQN EGYSGQFSGS PSRRQLDSGV
     KNRKQTQGGT TLSTGYSTHN NANSSLRSNM YNPSSTAHHL ENPDTALSVP DPGDWDPNYS
     DDLLLEEDSA DESSLANAFS RGMQLGSTDA SSYSRRFNSN ASTSSSNPTT QRRYAPNQAF
     SQVETGSPPS NDPHARFGQH IPGSQYIPHV SQNSPSRLGQ QPPQRYNHGR PNAGRTMDRN
     HMNAQLPPSN TNSGGQQRSP RSSSYTNGVP WGRRTNNHVP NVPSTSHGRV DYGSIA
 
 
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