MPK11_ARATH
ID MPK11_ARATH Reviewed; 369 AA.
AC Q9LMM5; B3H762;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Mitogen-activated protein kinase 11;
DE Short=AtMPK11;
DE Short=MAP kinase 11;
DE EC=2.7.11.24;
GN Name=MPK11; OrderedLocusNames=At1g01560; ORFNames=F22L4.10;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 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 [6]
RP INTERACTION WITH MKK1; MKK2 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 Arabidopsis
RT MAPKs and MAPK kinases helps define potential MAPK signalling modules.";
RL Plant Signal. Behav. 3:1037-1041(2008).
RN [7]
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 Arabidopsis.";
RL Plant J. 67:895-906(2011).
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=2.7.11.24;
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=2.7.11.24;
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MKK1, MKK2 and MKK6.
CC {ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:21575092}.
CC -!- INTERACTION:
CC Q9LMM5; Q9M4B5: AIP3; NbExp=3; IntAct=EBI-2358699, EBI-2130809;
CC Q9LMM5; Q94A06: MKK1; NbExp=2; IntAct=EBI-2358699, EBI-994464;
CC Q9LMM5; Q9S7U9: MKK2; NbExp=2; IntAct=EBI-2358699, EBI-994350;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LMM5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LMM5-2; Sequence=VSP_035539, VSP_035540;
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-198 and Tyr-200, which activates the
CC enzyme. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to introns retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; AC061957; AAF81314.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27305.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27306.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59779.1; -; Genomic_DNA.
DR EMBL; BX815051; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; C86146; C86146.
DR RefSeq; NP_001117210.1; NM_001123738.2. [Q9LMM5-1]
DR RefSeq; NP_001322113.1; NM_001331282.1. [Q9LMM5-2]
DR RefSeq; NP_563631.2; NM_100038.4. [Q9LMM5-2]
DR AlphaFoldDB; Q9LMM5; -.
DR SMR; Q9LMM5; -.
DR BioGRID; 24758; 3.
DR IntAct; Q9LMM5; 4.
DR STRING; 3702.AT1G01560.2; -.
DR iPTMnet; Q9LMM5; -.
DR PaxDb; Q9LMM5; -.
DR PRIDE; Q9LMM5; -.
DR ProteomicsDB; 250948; -. [Q9LMM5-1]
DR EnsemblPlants; AT1G01560.1; AT1G01560.1; AT1G01560. [Q9LMM5-2]
DR EnsemblPlants; AT1G01560.2; AT1G01560.2; AT1G01560. [Q9LMM5-1]
DR EnsemblPlants; AT1G01560.4; AT1G01560.4; AT1G01560. [Q9LMM5-2]
DR GeneID; 839523; -.
DR Gramene; AT1G01560.1; AT1G01560.1; AT1G01560. [Q9LMM5-2]
DR Gramene; AT1G01560.2; AT1G01560.2; AT1G01560. [Q9LMM5-1]
DR Gramene; AT1G01560.4; AT1G01560.4; AT1G01560. [Q9LMM5-2]
DR KEGG; ath:AT1G01560; -.
DR Araport; AT1G01560; -.
DR TAIR; locus:2025341; AT1G01560.
DR eggNOG; KOG0660; Eukaryota.
DR InParanoid; Q9LMM5; -.
DR OMA; KCWKELV; -.
DR PhylomeDB; Q9LMM5; -.
DR PRO; PR:Q9LMM5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMM5; baseline and differential.
DR Genevisible; Q9LMM5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; ISS: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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
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; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..369
FT /note="Mitogen-activated protein kinase 11"
FT /id="PRO_0000245811"
FT DOMAIN 40..326
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 198..200
FT /note="TXY"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 200
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT VAR_SEQ 256..275
FT /note="LIGSPDDSSLGFLRSDNARR -> VNFSLFHLTILFRFNLKKEH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_035539"
FT VAR_SEQ 276..369
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_035540"
FT CONFLICT 13
FT /note="N -> D (in Ref. 3; BX815051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 42475 MW; 446673DB42C3DAA6 CRC64;
MSIEKPFFGD DSNRGVSING GRYVQYNVYG NLFEVSKKYV PPLRPIGRGA SGIVCAAWNS
ETGEEVAIKK IGNAFGNIID AKRTLREIKL LKHMDHDNVI AIIDIIRPPQ PDNFNDVHIV
YELMDTDLHH IIRSNQPLTD DHSRFFLYQL LRGLKYVHSA NVLHRDLKPS NLLLNANCDL
KIGDFGLART KSETDFMTEY VVTRWYRAPE LLLNCSEYTA AIDIWSVGCI LGEIMTREPL
FPGRDYVQQL RLITELIGSP DDSSLGFLRS DNARRYVRQL PQYPRQNFAA RFPNMSVNAV
DLLQKMLVFD PNRRITVDEA LCHPYLAPLH EYNEEPVCVR PFHFDFEQPS LTEENIKELI
YRESVKFNP
