MPK20_ARATH
ID MPK20_ARATH Reviewed; 606 AA.
AC Q9SJG9; Q945L8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Mitogen-activated protein kinase 20;
DE Short=AtMPK20;
DE Short=MAP kinase 20;
DE EC=2.7.11.24;
GN Name=MPK20; OrderedLocusNames=At2g42880; ORFNames=F7D19.12;
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=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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 [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).
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 -!- INTERACTION:
CC Q9SJG9; O80931: AS1; NbExp=3; IntAct=EBI-2358896, EBI-763232;
CC Q9SJG9; Q17TI5: BRX; NbExp=5; IntAct=EBI-2358896, EBI-4426649;
CC Q9SJG9; Q9LQT8: GAI; NbExp=3; IntAct=EBI-2358896, EBI-963606;
CC Q9SJG9; Q9FX43: MKK9; NbExp=2; IntAct=EBI-2358896, EBI-2128545;
CC Q9SJG9; O23160: MYB73; NbExp=5; IntAct=EBI-2358896, EBI-25506855;
CC Q9SJG9; Q9SLH3: RGA; NbExp=5; IntAct=EBI-2358896, EBI-963624;
CC Q9SJG9; Q8GXW1: RGL2; NbExp=3; IntAct=EBI-2358896, EBI-963665;
CC Q9SJG9; Q93XX2: SEOA; NbExp=3; IntAct=EBI-2358896, EBI-4424691;
CC Q9SJG9; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-2358896, EBI-15192297;
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-187 and Tyr-189, which activates the
CC enzyme. {ECO:0000250}.
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; AC006931; AAD21721.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10180.1; -; Genomic_DNA.
DR EMBL; AF412082; AAL06535.1; -; mRNA.
DR EMBL; BT001021; AAN46775.1; -; mRNA.
DR PIR; D84859; D84859.
DR RefSeq; NP_565989.1; NM_129849.5.
DR AlphaFoldDB; Q9SJG9; -.
DR SMR; Q9SJG9; -.
DR BioGRID; 4225; 9.
DR IntAct; Q9SJG9; 10.
DR STRING; 3702.AT2G42880.1; -.
DR iPTMnet; Q9SJG9; -.
DR PaxDb; Q9SJG9; -.
DR PRIDE; Q9SJG9; -.
DR ProteomicsDB; 239068; -.
DR EnsemblPlants; AT2G42880.1; AT2G42880.1; AT2G42880.
DR GeneID; 818888; -.
DR Gramene; AT2G42880.1; AT2G42880.1; AT2G42880.
DR KEGG; ath:AT2G42880; -.
DR Araport; AT2G42880; -.
DR TAIR; locus:2052357; AT2G42880.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_13_1; -.
DR InParanoid; Q9SJG9; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q9SJG9; -.
DR PRO; PR:Q9SJG9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJG9; baseline and differential.
DR Genevisible; Q9SJG9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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 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.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..606
FT /note="Mitogen-activated protein kinase 20"
FT /id="PRO_0000245820"
FT DOMAIN 25..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 187..189
FT /note="TXY"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 189
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
SQ SEQUENCE 606 AA; 68775 MW; F36B44BDF6BD78A1 CRC64;
MQQDNRKKNN LEMEFFSDYG DANRFKVQEV IGKGSYGVVC SAIDTLTGEK VAIKKIHDIF
EHISDAARIL REIKLLRLLR HPDIVEIKHI MLPPSRREFK DIYVVFELME SDLHQVIKAN
DDLTREHYQF FLYQLLRALK YIHTANVYHR DLKPKNILAN ANCKLKICDF GLARVAFNDT
PTTIFWTDYV ATRWYRAPEL CGSFYSKYTP AIDIWSIGCI FAEVLMGKPL FPGKNVVHQL
DLMTDLLGTP SLDTISRVRN EKARRYLTSM RKKPPIPFAQ KFPNADPLSL KLLERLLAFD
PKDRPTAEEA LADPYFKGLA KVEREPSCQP ITKMEFEFER RKVTKEDIRE LISREILEYH
PQLLKDHMNG ADKASFLYPS AVDQFRRQFA HLEENSGKTG PVAPLERKHA SLPRSTVIHS
TAVARGGQPK LMNNTNTLNP ETTQNIPFNH ATIQAQQRNL SAAKPSTFMG PVAPFDNGRI
SRDAYDPRSF IRSTNLPFSQ QSAATVAMGK QQERRTTMEP EKQARQISQY NRYAPDVAIN
IDNNPFIMAR TGMNKAENIS DRIIIDTNLL QATAGIGVAA AAAAAAPGGS AHRKVGAVRY
GMSKMY
