ID MPK6_ARATH Reviewed; 395 AA. AC Q39026; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JUN-2015, entry version 147. DE RecName: Full=Mitogen-activated protein kinase 6; DE Short=AtMPK6; DE Short=MAP kinase 6; DE EC=2.7.11.24; GN Name=MPK6; OrderedLocusNames=At2g43790; ORFNames=F18O19.10; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX PubMed=8282107; DOI=10.1016/0014-5793(93)80852-L; RA Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H., RA Shinozaki K.; RT "ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana."; RL FEBS Lett. 336:440-444(1993). RN [2] 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., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [4] 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP ENZYME REGULATION, AND PHOSPHORYLATION AT THR-221 AND TYR-223. RX PubMed=10713056; DOI=10.1074/jbc.275.11.7521; RA Nuehse T.S., Peck S.C., Hirt H., Boller T.; RT "Microbial elicitors induce activation and dual phosphorylation of the RT Arabidopsis thaliana MAPK 6."; RL J. Biol. Chem. 275:7521-7526(2000). RN [6] RP ENZYME REGULATION, AND PHOSPHORYLATION. RX PubMed=11123804; DOI=10.1046/j.1365-313x.2000.00913.x; RA Ichimura K., Mizoguchi T., Yoshida R., Yuasa T., Shinozaki K.; RT "Various abiotic stresses rapidly activate Arabidopsis MAP kinases RT ATMPK4 and ATMPK6."; RL Plant J. 24:655-665(2000). RN [7] RP ENZYME REGULATION. RX PubMed=10717008; DOI=10.1073/pnas.97.6.2940; RA Kovtun Y., Chiu W.-L., Tena G., Sheen J.; RT "Functional analysis of oxidative stress-activated mitogen-activated RT protein kinase cascade in plants."; RL Proc. Natl. Acad. Sci. U.S.A. 97:2940-2945(2000). RN [8] RP ENZYME REGULATION. RX PubMed=11577197; DOI=10.1093/pcp/pce123; RA Yuasa T., Ichimura K., Mizoguchi T., Shinozaki K.; RT "Oxidative stress activates ATMPK6, an Arabidopsis homologue of MAP RT kinase."; RL Plant Cell Physiol. 42:1012-1016(2001). RN [9] RP ENZYME REGULATION. RX PubMed=11500556; DOI=10.1104/pp.126.4.1579; RA Desikan R., Hancock J.T., Ichimura K., Shinozaki K., Neill S.J.; RT "Harpin induces activation of the Arabidopsis mitogen-activated RT protein kinases AtMPK4 and AtMPK6."; RL Plant Physiol. 126:1579-1587(2001). RN [10] RP ENZYME REGULATION. RX PubMed=12220631; DOI=10.1016/S0014-5793(02)03162-9; RA Droillard M.-J., Boudsocq M., Barbier-Brygoo H., Lauriere C.; RT "Different protein kinase families are activated by osmotic stresses RT in Arabidopsis thaliana cell suspensions. Involvement of the MAP RT kinases AtMPK3 and AtMPK6."; RL FEBS Lett. 527:43-50(2002). RN [11] RP FUNCTION, AND MUTAGENESIS OF LYS-92 AND LYS-93. RX PubMed=11875555; DOI=10.1038/415977a; RA Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., RA Gomez-Gomez L., Boller T., Ausubel F.M., Sheen J.; RT "MAP kinase signalling cascade in Arabidopsis innate immunity."; RL Nature 415:977-983(2002). RN [12] 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 RT nomenclature."; RL Trends Plant Sci. 7:301-308(2002). RN [13] RP ENZYME REGULATION. RX PubMed=12628921; DOI=10.1093/emboj/cdg131; RA Ouaked F., Rozhon W., Lecourieux D., Hirt H.; RT "A MAPK pathway mediates ethylene signaling in plants."; RL EMBO J. 22:1282-1288(2003). RN [14] RP INTERACTION WITH NDPK2. RX PubMed=12506203; DOI=10.1073/pnas.252641899; RA Moon H., Lee B., Choi G., Shin D., Prasad D.T., Lee O., Kwak S.-S., RA Kim D.H., Nam J., Bahk J., Hong J.C., Lee S.Y., Cho M.J., Lim C.O., RA Yun D.-J.; RT "NDP kinase 2 interacts with two oxidative stress-activated MAPKs to RT regulate cellular redox state and enhances multiple stress tolerance RT in transgenic plants."; RL Proc. Natl. Acad. Sci. U.S.A. 100:358-363(2003). RN [15] RP FUNCTION, ENZYME REGULATION, AND INTERACTION WITH MKK2. 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 RT Arabidopsis."; RL Mol. Cell 15:141-152(2004). RN [16] RP FUNCTION. RX PubMed=15020743; DOI=10.1105/tpc.015552; RA Menke F.L.H., van Pelt J.A., Pieterse C.M.J., Klessig D.F.; RT "Silencing of the mitogen-activated protein kinase MPK6 compromises RT disease resistance in Arabidopsis."; RL Plant Cell 16:897-907(2004). RN [17] RP FUNCTION. RX PubMed=15539472; DOI=10.1105/tpc.104.026609; RA Liu Y., Zhang S.; RT "Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by RT MPK6, a stress-responsive mitogen-activated protein kinase, induces RT ethylene biosynthesis in Arabidopsis."; RL Plant Cell 16:3386-3399(2004). RN [18] RP ENZYME REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=15500467; DOI=10.1111/j.1365-313X.2004.02229.x; RA Ahlfors R., Macioszek V., Rudd J., Brosche M., Schlichting R., RA Scheel D., Kangasjarvi J.; RT "Stress hormone-independent activation and nuclear translocation of RT mitogen-activated protein kinases in Arabidopsis thaliana during ozone RT exposure."; RL Plant J. 40:512-522(2004). RN [19] RP ENZYME REGULATION. RX PubMed=15084727; DOI=10.1104/pp.103.037275; RA Miles G.P., Samuel M.A., Jones A.M., Ellis B.E.; RT "Mastoparan rapidly activates plant MAP kinase signaling independent RT of heterotrimeric G proteins."; RL Plant Physiol. 134:1332-1336(2004). RN [20] RP FUNCTION. RX PubMed=15964670; DOI=10.1016/j.envpol.2005.04.017; RA Miles G.P., Samuel M.A., Zhang Y., Ellis B.E.; RT "RNA interference-based (RNAi) suppression of AtMPK6, an Arabidopsis RT mitogen-activated protein kinase, results in hypersensitivity to ozone RT and misregulation of AtMPK3."; RL Environ. Pollut. 138:230-237(2005). RN [21] 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., RA Ehlting J., Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., RA Mundy J., Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., RA 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 [22] RP ENZYME REGULATION, AND DEPHOSPHORYLATION. RX PubMed=17586809; DOI=10.1074/jbc.M701888200; RA Lee J.S., Ellis B.E.; RT "Arabidopsis MAPK phosphatase 2 (MKP2) positively regulates oxidative RT stress tolerance and inactivates the MPK3 and MPK6 MAPKs."; RL J. Biol. Chem. 282:25020-25029(2007). RN [23] RP ENZYME REGULATION. 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 RT Arabidopsis."; RL Mol. Plant Microbe Interact. 20:589-596(2007). RN [24] RP FUNCTION. RX PubMed=17259259; DOI=10.1105/tpc.106.048298; RA Wang H., Ngwenyama N., Liu Y., Walker J.C., Zhang S.; RT "Stomatal development and patterning are regulated by environmentally RT responsive mitogen-activated protein kinases in Arabidopsis."; RL Plant Cell 19:63-73(2007). RN [25] RP ENZYME REGULATION, AND FUNCTION. RX PubMed=17369371; DOI=10.1105/tpc.106.046581; RA Takahashi F., Yoshida R., Ichimura K., Mizoguchi T., Seo S., RA Yonezawa M., Maruyama K., Yamaguchi-Shinozaki K., Shinozaki K.; RT "The mitogen-activated protein kinase cascade MKK3-MPK6 is an RT important part of the jasmonate signal transduction pathway in RT Arabidopsis."; RL Plant Cell 19:805-818(2007). RN [26] RP ENZYME REGULATION, AND INTERACTION WITH AP2C1. RX PubMed=17630279; DOI=10.1105/tpc.106.049585; RA Schweighofer A., Kazanaviciute V., Scheikl E., Teige M., Doczi R., RA Hirt H., Schwanninger M., Kant M., Schuurink R., Mauch F., Buchala A., RA Cardinale F., Meskiene I.; RT "The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and RT MPK6, modulates innate immunity, jasmonic acid, and ethylene levels in RT Arabidopsis."; RL Plant Cell 19:2213-2224(2007). RN [27] RP ENZYME REGULATION. RX PubMed=17933903; DOI=10.1105/tpc.106.050039; RA Doczi R., Brader G., Pettko-Szandtner A., Rajh I., Djamei A., RA Pitzschke A., Teige M., Hirt H.; RT "The Arabidopsis mitogen-activated protein kinase kinase MKK3 is RT upstream of group C mitogen-activated protein kinases and participates RT in pathogen signaling."; RL Plant Cell 19:3266-3279(2007). RN [28] RP FUNCTION, ENZYME REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=18273012; DOI=10.1038/nature06543; RA Yoo S.D., Cho Y.H., Tena G., Xiong Y., Sheen J.; RT "Dual control of nuclear EIN3 by bifurcate MAPK cascades in C2H4 RT signalling."; RL Nature 451:789-795(2008). RN [29] RP FUNCTION. 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 [30] RP INTERACTION WITH MKK2; MKK4; MKK5 AND MKK6. 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 RT Arabidopsis MAPKs and MAPK kinases helps define potential MAPK RT signalling modules."; RL Plant Signal. Behav. 3:1037-1041(2008). RN [31] RP FUNCTION. RX PubMed=18378893; DOI=10.1073/pnas.0711301105; RA Ren D., Liu Y., Yang K.Y., Han L., Mao G., Glazebrook J., Zhang S.; RT "A fungal-responsive MAPK cascade regulates phytoalexin biosynthesis RT in Arabidopsis."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5638-5643(2008). RN [32] RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP THR-226, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC STRAIN=cv. Columbia; RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004; RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., RA Andreasson E., Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from RT Arabidopsis thaliana."; RL J. Proteomics 72:439-451(2009). RN [33] RP ENZYME REGULATION, DEPHOSPHORYLATION, AND INTERACTION WITH MKP1 AND RP PTP1. RX PubMed=19789277; DOI=10.1105/tpc.109.067678; RA Bartels S., Anderson J.C., Gonzalez Besteiro M.A., Carreri A., RA Hirt H., Buchala A., Metraux J.P., Peck S.C., Ulm R.; RT "MAP kinase phosphatase1 and protein tyrosine phosphatase1 are RT repressors of salicylic acid synthesis and SNC1-mediated responses in RT Arabidopsis."; RL Plant Cell 21:2884-2897(2009). RN [34] RP FUNCTION, AND DISRUPTION PHENOTYPE. 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 RT in Arabidopsis seed germination."; RL Plant Mol. Biol. 70:725-736(2009). RN [35] RP FUNCTION, ENZYME REGULATION, AND DISRUPTION PHENOTYPE. RX PubMed=19251906; DOI=10.1104/pp.108.133439; RA Zhou C., Cai Z., Guo Y., Gan S.; RT "An arabidopsis mitogen-activated protein kinase cascade, MKK9-MPK6, RT plays a role in leaf senescence."; RL Plant Physiol. 150:167-177(2009). RN [36] RP INTERACTION WITH DSPTP1B/MKP2. RX PubMed=20626661; DOI=10.1111/j.1365-313X.2010.04297.x; RA Lumbreras V., Vilela B., Irar S., Sole M., Capellades M., Valls M., RA Coca M., Pages M.; RT "MAPK phosphatase MKP2 mediates disease responses in Arabidopsis and RT functionally interacts with MPK3 and MPK6."; RL Plant J. 63:1017-1030(2010). RN [37] RP INTERACTION WITH DSPTP1B/MKP2. RX PubMed=21057191; DOI=10.4161/psb.5.11.13645; RA Vilela B., Pages M., Lumbreras V.; RT "Regulation of MAPK signaling and cell death by MAPK phosphatase RT MKP2."; RL Plant Signal. Behav. 5:1497-1500(2010). RN [38] RP INTERACTION WITH MKK6. RX PubMed=21575092; DOI=10.1111/j.1365-313X.2011.04642.x; RA Zeng Q., Chen J.G., Ellis B.E.; RT "AtMPK4 is required for male-specific meiotic cytokinesis in RT Arabidopsis."; RL Plant J. 67:895-906(2011). RN [39] RP INDUCTION BY PATHOGEN. RX PubMed=21947882; DOI=10.1007/s11033-011-1232-1; RA Kannan P., Pandey D., Gupta A.K., Punetha H., Taj G., Kumar A.; RT "Expression analysis of MAP2K9 and MAPK6 during pathogenesis of RT Alternaria blight in Arabidopsis thaliana ecotype Columbia."; RL Mol. Biol. Rep. 39:4439-4444(2012). RN [40] RP FUNCTION. RX PubMed=23263767; DOI=10.1105/tpc.112.104695; RA Meng X., Wang H., He Y., Liu Y., Walker J.C., Torii K.U., Zhang S.; RT "A MAPK cascade downstream of ERECTA receptor-like protein kinase RT regulates Arabidopsis inflorescence architecture by promoting RT localized cell proliferation."; RL Plant Cell 24:4948-4960(2012). RN [41] RP INTERACTION WITH VQ4 AND IKU1/VQ14. RX PubMed=24750137; DOI=10.1111/nph.12817; RA Pecher P., Eschen-Lippold L., Herklotz S., Kuhle K., Naumann K., RA Bethke G., Uhrig J., Weyhe M., Scheel D., Lee J.; RT "The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and RT MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate RT immune responses."; RL New Phytol. 203:592-606(2014). RN [42] RP FUNCTION, AND INTERACTION WITH LIP5. RC STRAIN=cv. Columbia; RX PubMed=25010425; DOI=10.1371/journal.ppat.1004243; RA Wang F., Shang Y., Fan B., Yu J.-Q., Chen Z.; RT "Arabidopsis LIP5, a positive regulator of multivesicular body RT biogenesis, is a critical target of pathogen-responsive MAPK cascade RT in plant basal defense."; RL PLoS Pathog. 10:E1004243-E1004243(2014). RN [43] RP INTERACTION WITH RACK1A; RACK1B AND RACK1C. RX PubMed=25731164; DOI=10.1038/nature14243; RA Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y., RA Djonovic S., Millet Y., Bush J., McConkey B.J., Sheen J., RA Ausubel F.M.; RT "Pathogen-secreted proteases activate a novel plant immune pathway."; RL Nature 0:0-0(2015). CC -!- FUNCTION: Involved in oxidative stress-mediated signaling cascade CC (such as ozone). Involved in the innate immune MAP kinase CC signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of CC bacterial flagellin receptor FLS2. May be involved in CC hypersensitive response (HR)-mediated signaling cascade by CC modulating LIP5 phosphorylation and subsequent multivesicular CC bodies (MVBs) trafficking. May phosphorylate regulators of WRKY CC transcription factors. Phosphorylates 1-aminocyclopropane-1- CC carboxylic acid synthases (ACS2 and ACS6) and may be involved in CC the regulation of bacterial elicitor flagellin-induced ethylene CC production. Regulates locally gene-mediated and basal resistance CC response to certain pathogens. May be involved in the cold and CC salinity stress-mediated MAP kinase signaling cascade (MEKK1, CC MKK1/MKK2 and MPK4/MPK6). MKK1-MPK6 module mediates abscisic acid CC (ABA)-dependent CAT1 expression with H(2)O(2) production and CC response to drought and salt stress. MKK1-MPK6 module is also CC involved in sugar signaling during the process of seed CC germination. MKK3-MPK6 module plays an important role in the CC jasmonate signal transduction pathway through the negative CC regulation of MYC2/JIN1 expression. MKK9-MPK3/MPK6 module CC phosphorylates and activates EIN3, leading to the promotion of CC EIN3-mediated transcription in ethylene signaling. MPK3/MPK6 CC cascade regulates camalexin synthesis through transcriptional CC regulation of the biosynthetic genes after pathogen infection. CC MKK9-MPK6 module positively regulates leaf senescence. YDA- CC MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate before the CC guard mother cell (GMC) is specified. This MAPK cascade also CC functions downstream of the ER receptor in regulating coordinated CC local cell proliferation, which shapes the morphology of plant CC organs. {ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:15020743, CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:15539472, CC ECO:0000269|PubMed:15964670, ECO:0000269|PubMed:17259259, CC ECO:0000269|PubMed:17369371, ECO:0000269|PubMed:18248592, CC ECO:0000269|PubMed:18273012, ECO:0000269|PubMed:18378893, CC ECO:0000269|PubMed:19251906, ECO:0000269|PubMed:19484493, CC ECO:0000269|PubMed:23263767, ECO:0000269|PubMed:25010425}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Activated by threonine and tyrosine CC phosphorylation. Activated by the MAP kinase kinases MKK2, MKK3, CC MKK4, MKK5, MKK7 and MKK9. Activated in response to touch, CC wounding, low temperature, low humidity, salt stress, hydrogen CC peroxide, ozone, ACC (an ethylene precursor), jasmonic acid (JA), CC mastoparan and UVC. Activated in response to elicitors: CC oligogalacturonides, hexameric chitin fragments, fungal xylanase, CC and the bacterial flagellin and harpin. Activated upon Pseudomonas CC syringae pv. tomato DC3000 infection. Repressed by the protein CC phosphatase 2C AP2C1 and the protein-tyrosine-phosphatases MKP1 CC and PTP1. Repressed by DSPTP1B/MKP2-mediated dephosphorylation. CC {ECO:0000269|PubMed:10713056, ECO:0000269|PubMed:10717008, CC ECO:0000269|PubMed:11123804, ECO:0000269|PubMed:11500556, CC ECO:0000269|PubMed:11577197, ECO:0000269|PubMed:12220631, CC ECO:0000269|PubMed:12628921, ECO:0000269|PubMed:15084727, CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:15500467, CC ECO:0000269|PubMed:17369371, ECO:0000269|PubMed:17506336, CC ECO:0000269|PubMed:17586809, ECO:0000269|PubMed:17630279, CC ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:18273012, CC ECO:0000269|PubMed:19251906, ECO:0000269|PubMed:19789277}. CC -!- SUBUNIT: Interacts with MEKK1, MKK1 and MKK2. May form a ternary CC complex with MEKK1 and MKK1 or MKK2. Interacts with NDPK2, AP2C1, CC MKP1 and PTP1. Interacts with DSPTP1B/MKP2, especially during HR- CC like responses triggered by fungal elicitors. Interacts with MKK4, CC MKK5 and MKK6 (PubMed:12506203, PubMed:15225555, PubMed:17630279, CC PubMed:19513235, PubMed:19789277, PubMed:20626661, CC PubMed:21057191, PubMed:21575092). Binds to LIP5 CC (PubMed:25010425). Interacts with VQ4 and IKU1/VQ14 CC (PubMed:24750137). Interacts with RACK1A, RACK1B and RACK1C CC (PubMed:25731164). {ECO:0000269|PubMed:12506203, CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:17630279, CC ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:19789277, CC ECO:0000269|PubMed:20626661, ECO:0000269|PubMed:21057191, CC ECO:0000269|PubMed:21575092, ECO:0000269|PubMed:24750137, CC ECO:0000269|PubMed:25010425, ECO:0000269|PubMed:25731164}. CC -!- INTERACTION: CC O80719:At2g47060; NbExp=3; IntAct=EBI-349548, EBI-4436376; CC Q9FKG1:ERF104; NbExp=3; IntAct=EBI-349548, EBI-2360943; CC Q9S7U9:MKK2; NbExp=5; IntAct=EBI-349548, EBI-994350; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into CC the nucleus in response to phosphorylation. {ECO:0000305}. CC -!- INDUCTION: By Alternaria brassicae pathogen infection. CC {ECO:0000269|PubMed:21947882}. CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-221 and Tyr-223, which activates CC the enzyme. Dephosphorylated by DSPTP1B/MKP2. CC {ECO:0000269|PubMed:10713056, ECO:0000269|PubMed:11123804}. CC -!- DISRUPTION PHENOTYPE: Reduced sensitivity to abscisic acid (ABA) CC during germination. Delayed senescence phenotype. CC {ECO:0000269|PubMed:19251906, ECO:0000269|PubMed:19484493}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC CC Ser/Thr protein kinase family. MAP kinase subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D21842; BAA04869.1; -; mRNA. DR EMBL; AC002333; AAB64027.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10325.1; -; Genomic_DNA. DR EMBL; AY120737; AAM53295.1; -; mRNA. DR EMBL; BT008855; AAP68294.1; -; mRNA. DR PIR; S40472; S40472. DR RefSeq; NP_181907.1; NM_129941.3. DR UniGene; At.22266; -. DR UniGene; At.53112; -. DR ProteinModelPortal; Q39026; -. DR SMR; Q39026; 5-394. DR BioGrid; 4318; 21. DR DIP; DIP-31825N; -. DR IntAct; Q39026; 12. DR MINT; MINT-8086250; -. DR STRING; 3702.AT2G43790.1; -. DR PaxDb; Q39026; -. DR PRIDE; Q39026; -. DR EnsemblPlants; AT2G43790.1; AT2G43790.1; AT2G43790. DR GeneID; 818982; -. DR KEGG; ath:AT2G43790; -. DR GeneFarm; 821; 89. DR TAIR; AT2G43790; -. DR eggNOG; COG0515; -. DR HOGENOM; HOG000233024; -. DR InParanoid; Q39026; -. DR KO; K14512; -. DR OMA; QLPRHAR; -. DR PhylomeDB; Q39026; -. DR BioCyc; ARA:AT2G43790-MONOMER; -. DR BRENDA; 2.7.11.24; 399. DR Reactome; REACT_273308; ERK/MAPK targets. DR Reactome; REACT_274021; ERK2 activation. DR Reactome; REACT_310320; CREB phosphorylation through the activation of Ras. DR Reactome; REACT_310958; ERKs are inactivated. DR Reactome; REACT_322522; Signalling to ERK5. DR Reactome; REACT_330337; Signal transduction by L1. DR Reactome; REACT_340308; ERK1 activation. DR Reactome; REACT_340626; Regulation of HSF1-mediated heat shock response. DR Reactome; REACT_357967; Signaling by FGFR2. DR Reactome; REACT_358851; Signaling by FGFR1. DR Reactome; REACT_359363; Signaling by FGFR4. DR Reactome; REACT_360532; Signaling by FGFR3. DR PRO; PR:Q39026; -. DR Proteomes; UP000006548; Chromosome 2. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0009524; C:phragmoplast; IDA:TAIR. DR GO; GO:0009574; C:preprophase band; IDA:TAIR. DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IDA:TAIR. DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR. DR GO; GO:0010120; P:camalexin biosynthetic process; IMP:TAIR. DR GO; GO:0051301; P:cell division; IMP:TAIR. DR GO; GO:0042742; P:defense response to bacterium; IEP:TAIR. DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IMP:TAIR. DR GO; GO:0010229; P:inflorescence development; IMP:TAIR. DR GO; GO:0010150; P:leaf senescence; IMP:UniProtKB. DR GO; GO:0048481; P:ovule development; IGI:TAIR. DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW. DR GO; GO:0009555; P:pollen development; IGI:TAIR. DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR. DR GO; GO:0080136; P:priming of cellular response to stress; IMP:TAIR. DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR. DR GO; GO:0009409; P:response to cold; IDA:TAIR. DR GO; GO:0009723; P:response to ethylene; IDA:TAIR. DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB. DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:TAIR. DR GO; GO:0006970; P:response to osmotic stress; IDA:TAIR. DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR. DR GO; GO:0000302; P:response to reactive oxygen species; IEP:TAIR. DR GO; GO:0009651; P:response to salt stress; IGI:TAIR. DR GO; GO:0010224; P:response to UV-B; IMP:TAIR. DR GO; GO:0048364; P:root development; IMP:TAIR. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. 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; PS01351; MAPK; 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; Complete proteome; Cytoplasm; Hypersensitive response; KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense; KW Reference proteome; Serine/threonine-protein kinase; Stress response; KW Transferase. FT CHAIN 1 395 Mitogen-activated protein kinase 6. FT /FTId=PRO_0000186315. FT DOMAIN 63 348 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 69 77 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOTIF 221 223 TXY. FT ACT_SITE 189 189 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 92 92 ATP. FT MOD_RES 221 221 Phosphothreonine. FT {ECO:0000269|PubMed:10713056}. FT MOD_RES 223 223 Phosphotyrosine. FT {ECO:0000269|PubMed:10713056}. FT MOD_RES 226 226 Phosphothreonine. FT {ECO:0000269|PubMed:19245862}. FT MUTAGEN 92 92 K->M: Loss of kinase activity. FT {ECO:0000269|PubMed:11875555}. FT MUTAGEN 93 93 K->M: Loss of kinase activity. FT {ECO:0000269|PubMed:11875555}. SQ SEQUENCE 395 AA; 45058 MW; 296D2BD753C6DDA4 CRC64; MDGGSGQPAA DTEMTEAPGG FPAAAPSPQM PGIENIPATL SHGGRFIQYN IFGNIFEVTA KYKPPIMPIG KGAYGIVCSA MNSETNESVA IKKIANAFDN KIDAKRTLRE IKLLRHMDHE NIVAIRDIIP PPLRNAFNDV YIAYELMDTD LHQIIRSNQA LSEEHCQYFL YQILRGLKYI HSANVLHRDL KPSNLLLNAN CDLKICDFGL ARVTSESDFM TEYVVTRWYR APELLLNSSD YTAAIDVWSV GCIFMELMDR KPLFPGRDHV HQLRLLMELI GTPSEEELEF LNENAKRYIR QLPPYPRQSI TDKFPTVHPL AIDLIEKMLT FDPRRRITVL DALAHPYLNS LHDISDEPEC TIPFNFDFEN HALSEEQMKE LIYREALAFN PEYQQ //