M2K2_ARATH
ID M2K2_ARATH Reviewed; 363 AA.
AC Q9S7U9; O80395;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Mitogen-activated protein kinase kinase 2;
DE Short=AtMAP2Kbeta;
DE Short=AtMKK2;
DE Short=MAP kinase kinase 2;
DE EC=2.7.12.2 {ECO:0000269|PubMed:15225555};
GN Name=MKK2; Synonyms=MAP2K, MK1; OrderedLocusNames=At4g29810;
GN ORFNames=F27B13.50;
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 [MRNA] (ISOFORM 1), SUBUNIT, TISSUE SPECIFICITY,
RP INTERACTION WITH MEKK1 AND MPK4, MUTAGENESIS OF LYS-99; THR-220 AND
RP THR-226, AND PHOSPHORYLATION AT THR-220 AND THR-226.
RC STRAIN=cv. Columbia;
RX PubMed=9878570; DOI=10.1006/bbrc.1998.9796;
RA Ichimura K., Mizoguchi T., Irie K., Morris P.C., Giraudat J., Matsumoto K.,
RA Shinozaki K.;
RT "Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting proteins and
RT analysis of a MAP kinase cascade in Arabidopsis.";
RL Biochem. Biophys. Res. Commun. 253:532-543(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Root;
RA Hamal A., Jouannic S., Leprince A.-S., Kreis M., Henry Y.;
RT "Molecular characterization and expression of an Arabidopsis thaliana L.
RT MAP kinase kinase cDNA AtMAP2Kalpha.";
RL Plant Sci. 140:41-52(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Sherman A., Fink G.R.;
RT "AMK1, a MAP kinase kinase from Arabidopsis thaliana is a functional
RT homolog of PBS2, the MAPKK of the osmolarity pathway in yeast Saccharomyces
RT cerevisiae.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP PHOSPHORYLATION AT THR-220 AND THR-226, AND MUTAGENESIS OF THR-220 AND
RP THR-226.
RX PubMed=11875555; DOI=10.1038/415977a;
RA Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L.,
RA Boller T., Ausubel F.M., Sheen J.;
RT "MAP kinase signalling cascade in Arabidopsis innate immunity.";
RL Nature 415:977-983(2002).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6;
RG MAPK group;
RT "Mitogen-activated protein kinase cascades in plants: a new nomenclature.";
RL Trends Plant Sci. 7:301-308(2002).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH MPK4
RP AND MPK6, PHOSPHORYLATION AT THR-220 AND THR-226, AND MUTAGENESIS OF
RP THR-220 AND THR-226.
RX PubMed=15225555; DOI=10.1016/j.molcel.2004.06.023;
RA Teige M., Scheikl E., Eulgem T., Doczi R., Ichimura K., Shinozaki K.,
RA Dangl J.L., Hirt H.;
RT "The MKK2 pathway mediates cold and salt stress signaling in Arabidopsis.";
RL Mol. Cell 15:141-152(2004).
RN [10]
RP GENE FAMILY.
RX PubMed=16537113; DOI=10.1016/j.tplants.2006.02.007;
RA Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M., Ehlting J.,
RA Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., Mundy J.,
RA Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., Seguin A., Ellis B.E.;
RT "Ancient signals: comparative genomics of plant MAPK and MAPKK gene
RT families.";
RL Trends Plant Sci. 11:192-198(2006).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17506336; DOI=10.1094/mpmi-20-5-0589;
RA Brader G., Djamei A., Teige M., Palva E.T., Hirt H.;
RT "The MAP kinase kinase MKK2 affects disease resistance in Arabidopsis.";
RL Mol. Plant Microbe Interact. 20:589-596(2007).
RN [12]
RP FUNCTION, INTERACTION WITH MEKK1 AND MPK4, AND DISRUPTION PHENOTYPE.
RX PubMed=18982020; DOI=10.1038/cr.2008.300;
RA Gao M., Liu J., Bi D., Zhang Z., Cheng F., Chen S., Zhang Y.;
RT "MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated protein
RT kinase cascade to regulate innate immunity in plants.";
RL Cell Res. 18:1190-1198(2008).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18599650; DOI=10.1104/pp.108.120006;
RA Qiu J.L., Zhou L., Yun B.W., Nielsen H.B., Fiil B.K., Petersen K.,
RA Mackinlay J., Loake G.J., Mundy J., Morris P.C.;
RT "Arabidopsis mitogen-activated protein kinase kinases MKK1 and MKK2 have
RT overlapping functions in defense signaling mediated by MEKK1, MPK4, and
RT MKS1.";
RL Plant Physiol. 148:212-222(2008).
RN [14]
RP INTERACTION WITH MPK4; MPK6; MPK10 AND MPK11.
RX PubMed=19513235; DOI=10.4161/psb.3.12.6848;
RA Lee J.S., Huh K.W., Bhargava A., Ellis B.E.;
RT "Comprehensive analysis of protein-protein interactions between Arabidopsis
RT MAPKs and MAPK kinases helps define potential MAPK signalling modules.";
RL Plant Signal. Behav. 3:1037-1041(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, 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 [16]
RP ACTIVITY REGULATION, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=23857079; DOI=10.1007/s10265-013-0576-0;
RA Furuya T., Matsuoka D., Nanmori T.;
RT "Phosphorylation of Arabidopsis thaliana MEKK1 via Ca(2+) signaling as a
RT part of the cold stress response.";
RL J. Plant Res. 126:833-840(2013).
RN [17]
RP INTERACTION WITH MAPKKK5, PHOSPHORYLATION BY MAPKKK5, AND MUTAGENESIS OF
RP LYS-99; THR-220 AND THR-226.
RC STRAIN=cv. Columbia;
RX PubMed=27679653; DOI=10.15252/embj.201694248;
RA Yamada K., Yamaguchi K., Shirakawa T., Nakagami H., Mine A., Ishikawa K.,
RA Fujiwara M., Narusaka M., Narusaka Y., Ichimura K., Kobayashi Y.,
RA Matsui H., Nomura Y., Nomoto M., Tada Y., Fukao Y., Fukamizo T., Tsuda K.,
RA Shirasu K., Shibuya N., Kawasaki T.;
RT "The Arabidopsis CERK1-associated kinase PBL27 connects chitin perception
RT to MAPK activation.";
RL EMBO J. 35:2468-2483(2016).
CC -!- FUNCTION: MEKK1, MKK1/MKK2 and MPK4 function in a signaling pathway
CC that modulates the expression of genes responding to biotic and abiotic
CC stresses and also plays an important role in pathogen defense by
CC negatively regulating innate immunity. Plays a role in abiotic stress
CC tolerance and plant disease resistance through activation of MPK4 and
CC MPK6 by phosphorylation. Acts redundantly with MKK1.
CC {ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:17506336,
CC ECO:0000269|PubMed:18599650, ECO:0000269|PubMed:18982020}.
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=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:15225555};
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=2.7.12.2; Evidence={ECO:0000269|PubMed:15225555};
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=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:15225555};
CC -!- ACTIVITY REGULATION: Activated in response to cold and salt stresses
CC through serine and threonine phosphorylation by MEKK1.
CC {ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:23857079}.
CC -!- SUBUNIT: Interacts with MEKK1, MPK4 and MPK6. May form a ternary
CC complex composed of MEKK1 and MKK1/MKK2 and MPK4. Interacts with MPK10
CC and MPK11. Interacts with MAPKKK5 mainly in the cytosol
CC (PubMed:27679653). {ECO:0000269|PubMed:15225555,
CC ECO:0000269|PubMed:18982020, ECO:0000269|PubMed:19513235,
CC ECO:0000269|PubMed:27679653, ECO:0000269|PubMed:9878570}.
CC -!- INTERACTION:
CC Q9S7U9; A0A178UNT9: At5g58950; NbExp=5; IntAct=EBI-994350, EBI-25512586;
CC Q9S7U9; Q9ZR37: DSPTP1; NbExp=5; IntAct=EBI-994350, EBI-25512239;
CC Q9S7U9; Q9M1Z5: MPK10; NbExp=2; IntAct=EBI-994350, EBI-2358527;
CC Q9S7U9; Q9LMM5: MPK11; NbExp=2; IntAct=EBI-994350, EBI-2358699;
CC Q9S7U9; Q9LQQ9: MPK13; NbExp=2; IntAct=EBI-994350, EBI-2358762;
CC Q9S7U9; Q39024: MPK4; NbExp=10; IntAct=EBI-994350, EBI-994375;
CC Q9S7U9; Q39026: MPK6; NbExp=8; IntAct=EBI-994350, EBI-349548;
CC Q9S7U9; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-994350, EBI-15192297;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9S7U9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9S7U9-2; Sequence=VSP_019784;
CC -!- PTM: Phosphorylation at Thr-220 and Thr-226 by MAP kinase kinase
CC kinases positively regulates kinase activity. Phosphorylated by MEKK1
CC in response to cold (PubMed:23857079). Phosphorylated by MAPKKK5
CC (PubMed:27679653). {ECO:0000269|PubMed:11875555,
CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:23857079,
CC ECO:0000269|PubMed:27679653, ECO:0000269|PubMed:9878570}.
CC -!- DISRUPTION PHENOTYPE: No obvious developmental defects under normal
CC growth conditions. Simultaneous knockdown of MKK1 and MKK2 results in
CC dwarf and small plants exhibiting a seedling-lethality phenotype.
CC {ECO:0000269|PubMed:17506336, ECO:0000269|PubMed:18599650,
CC ECO:0000269|PubMed:18982020}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; AB015313; BAA28828.1; -; mRNA.
DR EMBL; AJ006871; CAA07281.1; -; mRNA.
DR EMBL; AF067792; AAC72754.1; -; mRNA.
DR EMBL; AL050352; CAB43656.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79739.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85679.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85680.1; -; Genomic_DNA.
DR EMBL; AF385688; AAK60281.1; -; mRNA.
DR EMBL; AY078009; AAL77710.1; -; mRNA.
DR PIR; T08542; T08542.
DR PIR; T51735; T51735.
DR RefSeq; NP_001031751.1; NM_001036674.2. [Q9S7U9-2]
DR RefSeq; NP_194710.1; NM_119127.4. [Q9S7U9-1]
DR AlphaFoldDB; Q9S7U9; -.
DR SMR; Q9S7U9; -.
DR BioGRID; 14390; 11.
DR IntAct; Q9S7U9; 11.
DR STRING; 3702.AT4G29810.2; -.
DR iPTMnet; Q9S7U9; -.
DR MetOSite; Q9S7U9; -.
DR PaxDb; Q9S7U9; -.
DR PRIDE; Q9S7U9; -.
DR ProteomicsDB; 238788; -. [Q9S7U9-1]
DR EnsemblPlants; AT4G29810.1; AT4G29810.1; AT4G29810. [Q9S7U9-1]
DR EnsemblPlants; AT4G29810.2; AT4G29810.2; AT4G29810. [Q9S7U9-2]
DR GeneID; 829103; -.
DR Gramene; AT4G29810.1; AT4G29810.1; AT4G29810. [Q9S7U9-1]
DR Gramene; AT4G29810.2; AT4G29810.2; AT4G29810. [Q9S7U9-2]
DR KEGG; ath:AT4G29810; -.
DR Araport; AT4G29810; -.
DR TAIR; locus:2123909; AT4G29810.
DR eggNOG; KOG0581; Eukaryota.
DR InParanoid; Q9S7U9; -.
DR OMA; EAWASTF; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q9S7U9; -.
DR BRENDA; 2.7.12.2; 399.
DR PRO; PR:Q9S7U9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S7U9; baseline and differential.
DR Genevisible; Q9S7U9; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0060918; P:auxin transport; IMP:TAIR.
DR GO; GO:0009631; P:cold acclimation; IDA:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IGI:TAIR.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009875; P:pollen-pistil interaction; IGI:TAIR.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; 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 Alternative splicing; ATP-binding; Immunity; Innate immunity; Kinase;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..363
FT /note="Mitogen-activated protein kinase kinase 2"
FT /id="PRO_0000245822"
FT DOMAIN 70..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11875555,
FT ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:9878570"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11875555,
FT ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:9878570"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O80397"
FT VAR_SEQ 26
FT /note="L -> LRKGFGSLCR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_019784"
FT MUTAGEN 99
FT /note="K->R: Loss of interaction with MEKK1. Phosphorylated
FT by MAPKKK5."
FT /evidence="ECO:0000269|PubMed:27679653,
FT ECO:0000269|PubMed:9878570"
FT MUTAGEN 220
FT /note="T->A: Loss of interaction with MEKK1. Normal
FT phosphorylation by MAPKKK5; when associated with A-226."
FT /evidence="ECO:0000269|PubMed:11875555,
FT ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:27679653,
FT ECO:0000269|PubMed:9878570"
FT MUTAGEN 220
FT /note="T->E: Constitutively active; when associated with E-
FT 226."
FT /evidence="ECO:0000269|PubMed:11875555,
FT ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:9878570"
FT MUTAGEN 226
FT /note="T->A: Loss of interaction with MEKK1. Normal
FT phosphorylation by MAPKKK5; when associated with A-220."
FT /evidence="ECO:0000269|PubMed:11875555,
FT ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:27679653,
FT ECO:0000269|PubMed:9878570"
FT MUTAGEN 226
FT /note="T->E: Constitutively active; when associated with E-
FT 220."
FT /evidence="ECO:0000269|PubMed:11875555,
FT ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:9878570"
FT CONFLICT 314
FT /note="D -> E (in Ref. 2; CAA07281 and 3; AAC72754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39848 MW; 3E7EFC6D3A831D93 CRC64;
MKKGGFSNNL KLAIPVAGEQ SITKFLTQSG TFKDGDLRVN KDGVRIISQL EPEVLSPIKP
ADDQLSLSDL DMVKVIGKGS SGVVQLVQHK WTGQFFALKV IQLNIDEAIR KAIAQELKIN
QSSQCPNLVT SYQSFYDNGA ISLILEYMDG GSLADFLKSV KAIPDSYLSA IFRQVLQGLI
YLHHDRHIIH RDLKPSNLLI NHRGEVKITD FGVSTVMTNT AGLANTFVGT YNYMSPERIV
GNKYGNKSDI WSLGLVVLEC ATGKFPYAPP NQEETWTSVF ELMEAIVDQP PPALPSGNFS
PELSSFISTC LQKDPNSRSS AKELMEHPFL NKYDYSGINL ASYFTDAGSP LATLGNLSGT
FSV
