M2K6_ARATH
ID M2K6_ARATH Reviewed; 356 AA.
AC Q9FJV0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Mitogen-activated protein kinase kinase 6;
DE Short=AtMKK6;
DE Short=MAP kinase kinase 6;
DE EC=2.7.12.2;
DE AltName: Full=Protein Arabidopsis NQK1 homolog;
GN Name=MKK6; Synonyms=ANQ1; OrderedLocusNames=At5g56580; ORFNames=MIK19.2;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=12704083; DOI=10.1101/gad.1071103;
RA Soyano T., Nishihama R., Morikiyo K., Ishikawa M., Machida Y.;
RT "NQK1/NtMEK1 is a MAPKK that acts in the NPK1 MAPKKK-mediated MAPK cascade
RT and is required for plant cytokinesis.";
RL Genes Dev. 17:1055-1067(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15474000; DOI=10.1016/j.febslet.2004.08.051;
RA Melikant B., Giuliani C., Halbmayer-Watzina S., Limmongkon A.,
RA Heberle-Bors E., Wilson C.;
RT "The Arabidopsis thaliana MEK AtMKK6 activates the MAP kinase AtMPK13.";
RL FEBS Lett. 576:5-8(2004).
RN [6]
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 [7]
RP INTERACTION WITH MPK4; MPK6 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 [8]
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).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21098735; DOI=10.1105/tpc.110.077164;
RA Kosetsu K., Matsunaga S., Nakagami H., Colcombet J., Sasabe M., Soyano T.,
RA Takahashi Y., Hirt H., Machida Y.;
RT "The MAP kinase MPK4 is required for cytokinesis in Arabidopsis thaliana.";
RL Plant Cell 22:3778-3790(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH MPK4.
RX PubMed=20802223; DOI=10.1093/pcp/pcq135;
RA Takahashi Y., Soyano T., Kosetsu K., Sasabe M., Machida Y.;
RT "HINKEL kinesin, ANP MAPKKKs and MKK6/ANQ MAPKK, which phosphorylates and
RT activates MPK4 MAPK, constitute a pathway that is required for cytokinesis
RT in Arabidopsis thaliana.";
RL Plant Cell Physiol. 51:1766-1776(2010).
RN [11]
RP INTERACTION WITH MPK4; MPK6; MPK11; MPK13 AND ANP3, DISRUPTION PHENOTYPE,
RP AND FUNCTION.
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 Arabidopsis.";
RL Plant J. 67:895-906(2011).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21904115; DOI=10.4161/psb.6.10.17089;
RA Zeng Q., Sritubtim S., Ellis B.E.;
RT "AtMKK6 and AtMPK13 are required for lateral root formation in
RT Arabidopsis.";
RL Plant Signal. Behav. 6:1436-1439(2011).
CC -!- FUNCTION: The ANPs-MKK6-MPK4 module is involved in the regulation of
CC plant cytokinesis during meiosis and mitosis. MKK6-MPK13 module
CC positively regulates lateral root formation. Phosphorylates and
CC activates MPK4. Activates MPK5 and MPK13 in vitro.
CC {ECO:0000269|PubMed:12704083, ECO:0000269|PubMed:15474000,
CC ECO:0000269|PubMed:20802223, ECO:0000269|PubMed:21098735,
CC ECO:0000269|PubMed:21575092, ECO:0000269|PubMed:21904115}.
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. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with P.syringae type III effector HopF2. Interacts
CC with MPK4, MPK6, MPK11 and MPK13. Interacts with ANP3.
CC {ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:20571112,
CC ECO:0000269|PubMed:20802223, ECO:0000269|PubMed:21575092}.
CC -!- INTERACTION:
CC Q9FJV0; Q8GYQ5: MPK12; NbExp=2; IntAct=EBI-1238868, EBI-2128461;
CC Q9FJV0; Q39024: MPK4; NbExp=4; IntAct=EBI-1238868, EBI-994375;
CC Q9FJV0; Q39026: MPK6; NbExp=5; IntAct=EBI-1238868, EBI-349548;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:20802223}. Note=Localized at the equatorial plane
CC of the phragmoplast.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and flower buds. Higher
CC levels in shoot apices and flowers. {ECO:0000269|PubMed:15474000,
CC ECO:0000269|PubMed:20802223}.
CC -!- PTM: Phosphorylation at Ser-221 and Thr-227 by MAP kinase kinase
CC kinases positively regulates kinase activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit a dwarf phenotype with fewer
CC flowers, large cells with multiple nuclei in various organs and large
CC malformed pollen grains. Defects in the formation of the cell plate.
CC RNAi MKK6 displays fewer lateral roots. {ECO:0000269|PubMed:12704083,
CC ECO:0000269|PubMed:20802223, ECO:0000269|PubMed:21098735,
CC ECO:0000269|PubMed:21575092, ECO:0000269|PubMed:21904115}.
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; AB104460; BAC76067.1; -; mRNA.
DR EMBL; AB013392; BAB09875.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96783.1; -; Genomic_DNA.
DR RefSeq; NP_200469.1; NM_125041.3.
DR AlphaFoldDB; Q9FJV0; -.
DR SMR; Q9FJV0; -.
DR BioGRID; 21003; 7.
DR IntAct; Q9FJV0; 6.
DR MINT; Q9FJV0; -.
DR STRING; 3702.AT5G56580.1; -.
DR iPTMnet; Q9FJV0; -.
DR PaxDb; Q9FJV0; -.
DR PRIDE; Q9FJV0; -.
DR ProteomicsDB; 238859; -.
DR EnsemblPlants; AT5G56580.1; AT5G56580.1; AT5G56580.
DR GeneID; 835759; -.
DR Gramene; AT5G56580.1; AT5G56580.1; AT5G56580.
DR KEGG; ath:AT5G56580; -.
DR Araport; AT5G56580; -.
DR TAIR; locus:2164981; AT5G56580.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q9FJV0; -.
DR OMA; YTVQFYG; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q9FJV0; -.
DR BRENDA; 2.7.12.2; 399.
DR PRO; PR:Q9FJV0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJV0; baseline and differential.
DR Genevisible; Q9FJV0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:TAIR.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:TAIR.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI: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:0002229; P:defense response to oomycetes; IGI:TAIR.
DR GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:UniProtKB.
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; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..356
FT /note="Mitogen-activated protein kinase kinase 6"
FT /id="PRO_0000245825"
FT DOMAIN 70..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 193
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 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O80396"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O80397"
SQ SEQUENCE 356 AA; 39837 MW; C95016C1DAE69CED CRC64;
MVKIKSNLKQ LKLSVPAQES PISSFLTASG TFHDGDFLLN QKGLRLTSDE KQSRQSDSKE
LDFEITAEDL ETVKVIGKGS GGVVQLVRHK WVGKFFAMKV IQMNIQEEIR KQIVQELKIN
QASSQCPHVV VCYHSFYHNG AFSLVLEYMD RGSLADVIRQ VKTILEPYLA VVCKQVLLGL
VYLHNERHVI HRDIKPSNLL VNHKGEVKIS DFGVSASLAS SMGQRDTFVG TYNYMSPERI
SGSTYDYSSD IWSLGMSVLE CAIGRFPYLE SEDQQNPPSF YELLAAIVEN PPPTAPSDQF
SPEFCSFVSA CIQKDPPARA SSLDLLSHPF IKKFEDKDID LGILVGTLEP PVNYLR
