(data stored in ACNUC8465 zone)

SWISSPROT: M2K10_ARATH

ID   M2K10_ARATH             Reviewed;         305 AA.
AC   Q9LQM8; A0MEA5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   11-DEC-2019, entry version 147.
DE   RecName: Full=Mitogen-activated protein kinase kinase 10;
DE            Short=AtMKK10;
DE            Short=MAP kinase kinase 10;
DE            EC=2.7.12.2;
GN   Name=MKK10; OrderedLocusNames=At1g32320; ORFNames=F27G20_9, F5D14.7;
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
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 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   -!- 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   -!- SUBUNIT: Interacts with P.syringae type III effector HopF2.
CC       {ECO:0000269|PubMed:20571112}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28427.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
DR   EMBL; AC007767; AAF81327.1; -; Genomic_DNA.
DR   EMBL; AC084110; AAG60170.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31463.1; -; Genomic_DNA.
DR   EMBL; DQ446313; ABE65677.1; -; mRNA.
DR   EMBL; DQ652874; ABK28427.1; ALT_SEQ; mRNA.
DR   PIR; G86447; G86447.
DR   RefSeq; NP_174510.1; NM_102965.1.
DR   SMR; Q9LQM8; -.
DR   BioGrid; 25358; 10.
DR   IntAct; Q9LQM8; 9.
DR   STRING; 3702.AT1G32320.1; -.
DR   PaxDb; Q9LQM8; -.
DR   EnsemblPlants; AT1G32320.1; AT1G32320.1; AT1G32320.
DR   GeneID; 840124; -.
DR   Gramene; AT1G32320.1; AT1G32320.1; AT1G32320.
DR   KEGG; ath:AT1G32320; -.
DR   Araport; AT1G32320; -.
DR   TAIR; locus:2028301; AT1G32320.
DR   eggNOG; KOG0581; Eukaryota.
DR   eggNOG; ENOG410XQ5A; LUCA.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; Q9LQM8; -.
DR   OMA; VVLLECH; -.
DR   OrthoDB; 688282at2759; -.
DR   PhylomeDB; Q9LQM8; -.
DR   PRO; PR:Q9LQM8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LQM8; baseline and differential.
DR   Genevisible; Q9LQM8; 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; TAS:TAIR.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
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;
DR   PRODOM; Q9LQM8.
DR   SWISS-2DPAGE; Q9LQM8.
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..305
FT                   /note="Mitogen-activated protein kinase kinase 10"
FT                   /id="PRO_0000428626"
FT   DOMAIN          48..302
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         54..62
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   COMPBIAS        31..36
FT                   /note="Poly-Ser"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         77
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7U9"
FT   MOD_RES         200
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O80397"
SQ   SEQUENCE   305 AA;  34022 MW;  3081A5DC889D8F2A CRC64;
     MTLVRERRHQ EPLTLSIPPL IYHGTAFSVA SSSSSSPETS PIQTLNDLEK LSVLGQGSGG
     TVYKTRHRRT KTLYALKVLR PNLNTTVTVE ADILKRIESS FIIKCYAVFV SLYDLCFVME
     LMEKGSLHDA LLAQQVFSEP MVSSLANRIL QGLRYLQKMG IVHGDIKPSN LLINKKGEVK
     IADFGASRIV AGGDYGSNGT CAYMSPERVD LEKWGFGGEV GFAGDVWSLG VVVLECYIGR
     YPLTKVGDKP DWATLFCAIC CNEKVDIPVS CSLEFRDFVG RCLEKDWRKR DTVEELLRHS
     FVKNR
//

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