M2K1_ARATH
ID M2K1_ARATH Reviewed; 354 AA.
AC Q94A06; O04440; O04661;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Mitogen-activated protein kinase kinase 1;
DE Short=AtMKK1;
DE Short=MAP kinase kinase 1;
DE EC=2.7.12.2;
DE AltName: Full=AtMEK1;
DE AltName: Full=NMAPKK;
GN Name=MKK1; Synonyms=MEK1; OrderedLocusNames=At4g26070; ORFNames=F20B18.180;
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), TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9426629; DOI=10.1023/a:1005963222768;
RA Morris P.C., Guerrier D., Leung J., Giraudat J.;
RT "Cloning and characterisation of MEK1, an Arabidopsis gene encoding a
RT homologue of MAP kinase kinase.";
RL Plant Mol. Biol. 35:1057-1064(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nanmori T., Matsuoka D., Deguchi M., Ariga H.;
RT "Nucleotide sequence of plant mapkk subfamily.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP SUBUNIT, AND INTERACTION WITH MEKK1 AND MPK4.
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 [8]
RP FUNCTION.
RX PubMed=10759527; DOI=10.1104/pp.122.4.1301;
RA Huang Y., Li H., Gupta R., Morris P.C., Luan S., Kieber J.J.;
RT "ATMPK4, an Arabidopsis homolog of mitogen-activated protein kinase, is
RT activated in vitro by AtMEK1 through threonine phosphorylation.";
RL Plant Physiol. 122:1301-1310(2000).
RN [9]
RP PHOSPHORYLATION AT THR-218 AND SER-224, AND MUTAGENESIS OF THR-218 AND
RP SER-224.
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 [10]
RP ACTIVITY REGULATION, PHOSPHORYLATION AT THR-218, AND MUTAGENESIS OF
RP THR-218; SER-220 AND SER-224.
RX PubMed=11874576; DOI=10.1046/j.0960-7412.2001.01246.x;
RA Matsuoka D., Nanmori T., Sato K., Fukami Y., Kikkawa U., Yasuda T.;
RT "Activation of AtMEK1, an Arabidopsis mitogen-activated protein kinase
RT kinase, in vitro and in vivo: analysis of active mutants expressed in E.
RT coli and generation of the active form in stress response in seedlings.";
RL Plant J. 29:637-647(2002).
RN [11]
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 [12]
RP ACTIVITY REGULATION.
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 [13]
RP ACTIVITY REGULATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17059410; DOI=10.1111/j.1365-313x.2006.02888.x;
RA Meszaros T., Helfer A., Hatzimasoura E., Magyar Z., Serazetdinova L.,
RA Rios G., Bardoczy V., Teige M., Koncz C., Peck S., Bogre L.;
RT "The Arabidopsis MAP kinase kinase MKK1 participates in defence responses
RT to the bacterial elicitor flagellin.";
RL Plant J. 48:485-498(2006).
RN [14]
RP INTERACTION WITH MEKK1, PHOSPHORYLATION AT THR-218 AND SER-224, AND
RP MUTAGENESIS OF LYS-97; THR-218 AND SER-224.
RX PubMed=16211390; DOI=10.1007/s00425-005-0126-7;
RA Hadiarto T., Nanmori T., Matsuoka D., Iwasaki T., Sato K., Fukami Y.,
RA Azuma T., Yasuda T.;
RT "Activation of Arabidopsis MAPK kinase kinase (AtMEKK1) and induction of
RT AtMEKK1-AtMEK1 pathway by wounding.";
RL Planta 223:708-713(2006).
RN [15]
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 [16]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=17728292; DOI=10.1093/jxb/erm144;
RA Xing Y., Jia W., Zhang J.;
RT "AtMEK1 mediates stress-induced gene expression of CAT1 catalase by
RT triggering H2O2 production in Arabidopsis.";
RL J. Exp. Bot. 58:2969-2981(2007).
RN [17]
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 [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18248592; DOI=10.1111/j.1365-313x.2008.03433.x;
RA Xing Y., Jia W., Zhang J.;
RT "AtMKK1 mediates ABA-induced CAT1 expression and H2O2 production via
RT AtMPK6-coupled signaling in Arabidopsis.";
RL Plant J. 54:440-451(2008).
RN [19]
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 [20]
RP INTERACTION WITH MPK4 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 [21]
RP FUNCTION.
RX PubMed=19484493; DOI=10.1007/s11103-009-9503-0;
RA Xing Y., Jia W., Zhang J.;
RT "AtMKK1 and AtMPK6 are involved in abscisic acid and sugar signaling in
RT Arabidopsis seed germination.";
RL Plant Mol. Biol. 70:725-736(2009).
RN [22]
RP INTERACTION WITH P.SYRINGAE HOPF2.
RX PubMed=20571112; DOI=10.1105/tpc.110.075697;
RA Wang Y., Li J., Hou S., Wang X., Li Y., Ren D., Chen S., Tang X.,
RA Zhou J.M.;
RT "A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis
RT mitogen-activated protein kinase kinases.";
RL Plant Cell 22:2033-2044(2010).
CC -!- FUNCTION: MEKK1, MKK1/MKK2 and MPK4/MPK6 function in a signaling
CC pathway that modulates the expression of genes responding to biotic and
CC abiotic stresses and also plays an important role in pathogen defense
CC by negatively regulating innate immunity. Activates by phosphorylation
CC the downstream MPK4. Acts redundantly with MKK2. MKK1-MPK6 module
CC mediates abscisic acid (ABA)-dependent CAT1 expression with H(2)O(2)
CC production and response to drought and salt stress. MKK1-MPK6 module is
CC also involved in sugar signaling during the process of seed
CC germination. {ECO:0000269|PubMed:10759527, ECO:0000269|PubMed:17059410,
CC ECO:0000269|PubMed:17728292, ECO:0000269|PubMed:18248592,
CC ECO:0000269|PubMed:18599650, ECO:0000269|PubMed:18982020,
CC ECO:0000269|PubMed:19484493}.
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 -!- 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;
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 -!- ACTIVITY REGULATION: Activated through serine and threonine
CC phosphorylation in response to wounding, cold, drought, salt stresses,
CC abscisic acid (ABA), hydrogen peroxide, bacterial flagellin and
CC laminarin beta-glucan. {ECO:0000269|PubMed:11874576,
CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:17059410,
CC ECO:0000269|PubMed:17728292}.
CC -!- SUBUNIT: Interacts with MEKK1 and MPK4. May form a ternary complex
CC composed of MEKK1 and MKK1/MKK2 and MPK4. Interacts with P.syringae
CC type III effector HopF2. Interacts with MPK11.
CC {ECO:0000269|PubMed:16211390, ECO:0000269|PubMed:18982020,
CC ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:20571112,
CC ECO:0000269|PubMed:9878570}.
CC -!- INTERACTION:
CC Q94A06; Q39008: MEKK1; NbExp=4; IntAct=EBI-994464, EBI-994439;
CC Q94A06; Q9LMM5: MPK11; NbExp=2; IntAct=EBI-994464, EBI-2358699;
CC Q94A06; Q8GYQ5: MPK12; NbExp=2; IntAct=EBI-994464, EBI-2128461;
CC Q94A06; Q39024: MPK4; NbExp=11; IntAct=EBI-994464, EBI-994375;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94A06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94A06-2; Sequence=VSP_019782, VSP_019783;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stem, flowers and siliques.
CC {ECO:0000269|PubMed:9426629}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:9426629}.
CC -!- PTM: Phosphorylation at Thr-218 and Ser-224 by MAP kinase kinase
CC kinases positively regulates kinase activity.
CC {ECO:0000269|PubMed:11874576, ECO:0000269|PubMed:11875555,
CC ECO:0000269|PubMed:16211390}.
CC -!- DISRUPTION PHENOTYPE: No obvious developmental defects under normal
CC growth conditions. Compromised in resistance to both virulent and
CC avirulent Pseudomonas syringae strains. Reduced sensitivity to abscisic
CC acid (ABA) during germination and reduced drought tolerance of
CC seedlings. Simultaneous knockdown of MKK1 and MKK2 results in dwarf and
CC small plants exhibiting a seedling-lethality phenotype.
CC {ECO:0000269|PubMed:17059410, ECO:0000269|PubMed:18248592,
CC ECO:0000269|PubMed:18599650, ECO:0000269|PubMed:18982020}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an 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; AF000977; AAB97145.1; -; mRNA.
DR EMBL; AB004796; BAA24079.1; -; mRNA.
DR EMBL; AL049483; CAB39672.1; -; Genomic_DNA.
DR EMBL; AL161564; CAB79462.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85152.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85153.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85154.1; -; Genomic_DNA.
DR EMBL; AY050774; AAK92709.1; -; mRNA.
DR EMBL; BT001935; AAN71934.1; -; mRNA.
DR EMBL; AY087065; AAM64626.1; -; mRNA.
DR PIR; T04262; T04262.
DR RefSeq; NP_194337.1; NM_118740.3. [Q94A06-1]
DR RefSeq; NP_849446.1; NM_179115.2. [Q94A06-2]
DR RefSeq; NP_974619.1; NM_202890.2. [Q94A06-1]
DR AlphaFoldDB; Q94A06; -.
DR SMR; Q94A06; -.
DR BioGRID; 14000; 8.
DR IntAct; Q94A06; 4.
DR STRING; 3702.AT4G26070.2; -.
DR iPTMnet; Q94A06; -.
DR PaxDb; Q94A06; -.
DR PRIDE; Q94A06; -.
DR ProteomicsDB; 238858; -. [Q94A06-1]
DR EnsemblPlants; AT4G26070.1; AT4G26070.1; AT4G26070. [Q94A06-2]
DR EnsemblPlants; AT4G26070.2; AT4G26070.2; AT4G26070. [Q94A06-1]
DR EnsemblPlants; AT4G26070.3; AT4G26070.3; AT4G26070. [Q94A06-1]
DR GeneID; 828713; -.
DR Gramene; AT4G26070.1; AT4G26070.1; AT4G26070. [Q94A06-2]
DR Gramene; AT4G26070.2; AT4G26070.2; AT4G26070. [Q94A06-1]
DR Gramene; AT4G26070.3; AT4G26070.3; AT4G26070. [Q94A06-1]
DR KEGG; ath:AT4G26070; -.
DR Araport; AT4G26070; -.
DR TAIR; locus:2120855; AT4G26070.
DR eggNOG; KOG0581; Eukaryota.
DR InParanoid; Q94A06; -.
DR PhylomeDB; Q94A06; -.
DR BRENDA; 2.7.12.2; 399.
DR PRO; PR:Q94A06; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94A06; baseline and differential.
DR Genevisible; Q94A06; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0042742; P:defense response to bacterium; IDA:TAIR.
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:0042542; P:response to hydrogen peroxide; IDA:TAIR.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP: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..354
FT /note="Mitogen-activated protein kinase kinase 1"
FT /id="PRO_0000245821"
FT DOMAIN 68..328
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11874576,
FT ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:16211390"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11875555,
FT ECO:0000269|PubMed:16211390"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O80397"
FT VAR_SEQ 308
FT /note="C -> W (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_019782"
FT VAR_SEQ 309..354
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_019783"
FT MUTAGEN 97
FT /note="K->R: Loss of kinase activity in vitro."
FT /evidence="ECO:0000269|PubMed:16211390"
FT MUTAGEN 218
FT /note="T->A: Loss of kinase activity in vitro; when
FT associated with E-224."
FT /evidence="ECO:0000269|PubMed:11874576,
FT ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:16211390"
FT MUTAGEN 218
FT /note="T->E: Constitutively active; when associated with D-
FT 224. Increases kinase activity in vitro; when associated
FT with E-224."
FT /evidence="ECO:0000269|PubMed:11874576,
FT ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:16211390"
FT MUTAGEN 220
FT /note="S->E: Increases kinase activity in vitro; when
FT associated with E-224."
FT /evidence="ECO:0000269|PubMed:11874576"
FT MUTAGEN 224
FT /note="S->D: Constitutively active; when associated with E-
FT 218."
FT /evidence="ECO:0000269|PubMed:11874576,
FT ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:16211390"
FT MUTAGEN 224
FT /note="S->E: Increases kinase activity in vitro; when
FT associated with E-218 or E-220."
FT /evidence="ECO:0000269|PubMed:11874576,
FT ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:16211390"
SQ SEQUENCE 354 AA; 39210 MW; D889CFBB97653B8E CRC64;
MNRGSLCPNP ICLPPLEQSI SKFLTQSGTF KDGDLRVNKD GIQTVSLSEP GAPPPIEPLD
NQLSLADLEV IKVIGKGSSG NVQLVKHKLT QQFFALKVIQ LNTEESTCRA ISQELRINLS
SQCPYLVSCY QSFYHNGLVS IILEFMDGGS LADLLKKVGK VPENMLSAIC KRVLRGLCYI
HHERRIIHRD LKPSNLLINH RGEVKITDFG VSKILTSTSS LANSFVGTYP YMSPERISGS
LYSNKSDIWS LGLVLLECAT GKFPYTPPEH KKGWSSVYEL VDAIVENPPP CAPSNLFSPE
FCSFISQCVQ KDPRDRKSAK ELLEHKFVKM FEDSDTNLSA YFTDAGSLIP PLAN
