MKS1_ARATH
ID MKS1_ARATH Reviewed; 222 AA.
AC Q8LGD5; Q9LSA8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein MKS1;
DE AltName: Full=Protein MAP kinase 4 substrate 1;
DE AltName: Full=VQ motif-containing protein 21 {ECO:0000303|PubMed:22535423};
DE Short=AtVQ21 {ECO:0000303|PubMed:22535423};
GN Name=MKS1; Synonyms=VQ21 {ECO:0000303|PubMed:22535423};
GN OrderedLocusNames=At3g18690; ORFNames=MVE11.5;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-30, AND INTERACTION
RP WITH MPK4; WRKY25 AND WRKY33.
RX PubMed=15990873; DOI=10.1038/sj.emboj.7600737;
RA Andreasson E., Jenkins T., Brodersen P., Thorgrimsen S., Petersen N.H.T.,
RA Zhu S., Qiu J.-L., Micheelsen P., Rocher A., Petersen M., Newman M.-A.,
RA Bjoern Nielsen H., Hirt H., Somssich I.E., Mattsson O., Mundy J.;
RT "The MAP kinase substrate MKS1 is a regulator of plant defense responses.";
RL EMBO J. 24:2579-2589(2005).
RN [6]
RP PHOSPHORYLATION AT SER-72; SER-108 AND SER-120.
RX PubMed=17702678; DOI=10.1016/j.bbapap.2007.07.002;
RA Caspersen M.B., Qiu J.-L., Zhang X., Andreasson E., Naested H., Mundy J.,
RA Svensson B.;
RT "Phosphorylation sites of Arabidopsis MAP kinase substrate 1 (MKS1).";
RL Biochim. Biophys. Acta 1774:1156-1163(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP 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 [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22535423; DOI=10.1104/pp.112.196816;
RA Cheng Y., Zhou Y., Yang Y., Chi Y.J., Zhou J., Chen J.Y., Wang F., Fan B.,
RA Shi K., Zhou Y.H., Yu J.Q., Chen Z.;
RT "Structural and functional analysis of VQ motif-containing proteins in
RT Arabidopsis as interacting proteins of WRKY transcription factors.";
RL Plant Physiol. 159:810-825(2012).
CC -!- FUNCTION: Regulator of plant defense response. May contribute to MPK4-
CC regulated defense activation by coupling the kinase to specific WRKY
CC transcription factors. {ECO:0000269|PubMed:15990873}.
CC -!- SUBUNIT: Interacts with MPK4, WRKY25 and WRKY33.
CC {ECO:0000269|PubMed:15990873}.
CC -!- INTERACTION:
CC Q8LGD5; Q39024: MPK4; NbExp=9; IntAct=EBI-1392198, EBI-994375;
CC Q8LGD5; O22921: WRKY25; NbExp=3; IntAct=EBI-1392198, EBI-1392386;
CC Q8LGD5; Q8S8P5: WRKY33; NbExp=5; IntAct=EBI-1392198, EBI-1392374;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15990873}.
CC -!- PTM: Phosphorylated on serine residue by MPK4.
CC {ECO:0000269|PubMed:15990873, ECO:0000269|PubMed:17702678}.
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DR EMBL; AB026654; BAB01795.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76132.1; -; Genomic_DNA.
DR EMBL; BT024603; ABD43001.1; -; mRNA.
DR EMBL; AY084330; AAM60914.1; -; mRNA.
DR RefSeq; NP_566616.1; NM_112755.2.
DR AlphaFoldDB; Q8LGD5; -.
DR BioGRID; 6733; 6.
DR IntAct; Q8LGD5; 4.
DR MINT; Q8LGD5; -.
DR STRING; 3702.AT3G18690.1; -.
DR iPTMnet; Q8LGD5; -.
DR PaxDb; Q8LGD5; -.
DR PRIDE; Q8LGD5; -.
DR ProteomicsDB; 238709; -.
DR EnsemblPlants; AT3G18690.1; AT3G18690.1; AT3G18690.
DR GeneID; 821400; -.
DR Gramene; AT3G18690.1; AT3G18690.1; AT3G18690.
DR KEGG; ath:AT3G18690; -.
DR Araport; AT3G18690; -.
DR TAIR; locus:2093959; AT3G18690.
DR eggNOG; ENOG502S2J0; Eukaryota.
DR HOGENOM; CLU_074462_1_0_1; -.
DR InParanoid; Q8LGD5; -.
DR OMA; SPMFYGS; -.
DR OrthoDB; 1541298at2759; -.
DR PhylomeDB; Q8LGD5; -.
DR PRO; PR:Q8LGD5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LGD5; baseline and differential.
DR Genevisible; Q8LGD5; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; IMP:TAIR.
DR InterPro; IPR008889; VQ.
DR InterPro; IPR039607; VQ_8/17/18/20/21/25.
DR PANTHER; PTHR33143; PTHR33143; 1.
DR Pfam; PF05678; VQ; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Plant defense; Reference proteome.
FT CHAIN 1..222
FT /note="Protein MKS1"
FT /id="PRO_0000245828"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 83..92
FT /note="VQ"
FT /evidence="ECO:0000305"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15990873"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17702678"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17702678"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17702678,
FT ECO:0007744|PubMed:19376835"
FT CONFLICT 160
FT /note="L -> M (in Ref. 4; AAM60914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 23582 MW; 54CB8449CD5AC2B5 CRC64;
MDPSEYFAGG NPSDQQNQKR QLQICGPRPS PLSVHKDSHK IKKPPKHPAP PPNRDQPPPY
IPREPVVIYA VSPKVVHATA SEFMNVVQRL TGISSGVFLE SGGGGDVSPA ARLASTENAS
PRGGKEPAAR DETVEINTAM EEAAEFGGYA PGILSPSPAL LPTASTGIFS PMYHQGGMFS
PAIPLGLFSP AGFMSPFRSP GFTSLVASPT FADFFSHIWD QD
