(data stored in ACNUC8465 zone)

SWISSPROT: B3H757_ARATH

ID   B3H757_ARATH            Unreviewed;       338 AA.
AC   B3H757;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   11-DEC-2019, entry version 86.
DE   SubName: Full=MAP kinase kinase 2 {ECO:0000313|EMBL:AEE85681.1};
GN   Name=MKK2 {ECO:0000313|EMBL:AEE85681.1};
GN   Synonyms=ATMKK2 {ECO:0000313|EMBL:AEE85681.1}, MAP KINASE KINASE 1
GN   {ECO:0000313|EMBL:AEE85681.1}, MAP kinase kinase 2
GN   {ECO:0000313|EMBL:AEE85681.1}, MK1 {ECO:0000313|EMBL:AEE85681.1};
GN   OrderedLocusNames=At4g29810 {ECO:0000313|Araport:AT4G29810,
GN   ECO:0000313|EMBL:AEE85681.1};
GN   ORFNames=F27B13.50 {ECO:0000313|EMBL:AEE85681.1}, F27B13_50
GN   {ECO:0000313|EMBL:AEE85681.1};
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 {ECO:0000313|EMBL:AEE85681.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:AEE85681.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=10617198; DOI=10.1038/47134;
RG   EU;
RG   CSHL and WU Arabidopsis Sequencing Project;
RA   Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA   Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA   Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA   Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA   Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA   Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA   Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA   Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Kotter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., Van Montagu M., Rogers J.,
RA   Cronin A., Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA   Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA   Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA   Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA   Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA   Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA   Montfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sehkon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
RA   Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA   Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2] {ECO:0000213|PubMed:19376835}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [3] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; CP002687; AEE85681.1; -; Genomic_DNA.
DR   RefSeq; NP_001119079.1; NM_001125607.1.
DR   SMR; B3H757; -.
DR   PRIDE; B3H757; -.
DR   ProMEX; B3H757; -.
DR   EnsemblPlants; AT4G29810.3; AT4G29810.3; AT4G29810.
DR   GeneID; 829103; -.
DR   Gramene; AT4G29810.3; AT4G29810.3; AT4G29810.
DR   Araport; AT4G29810; -.
DR   eggNOG; KOG0581; Eukaryota.
DR   eggNOG; ENOG410XQ5A; LUCA.
DR   HOGENOM; HOG000234206; -.
DR   OrthoDB; 688282at2759; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; B3H757; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; B3H757.
DR   SWISS-2DPAGE; B3H757.
KW   ATP-binding {ECO:0000256|RuleBase:RU000304};
KW   Kinase {ECO:0000313|EMBL:AEE85681.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000313|EMBL:AEE85681.1}.
FT   DOMAIN          79..338
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   338 AA;  37266 MW;  D64481CD152268B9 CRC64;
     MKKGGFSNNL KLAIPVAGEQ SITKFLRKGF GSLCRTQSGT FKDGDLRVNK DGVRIISQLE
     PEVLSPIKPA DDQLSLSDLD MVKVIGKGSS GVVQLVQHKW TGQFFALKVI QLNIDEAIRK
     AIAQELKINQ SSQCPNLVTS YQSFYDNGAI SLILEYMDGG SLADFLKSVK AIPDSYLSAI
     FRQVLQGLIY LHHDRHIIHR DLKPSNLLIN HRGEVKITDF GVSTVMTNTA GLANTFVGTY
     NYMSPERIVG NKYGNKSDIW SLGLVVLECA TGKFPYAPPN QEETWTSVFE LMEAIVDQPP
     PALPSGNFSP ELSSFISTCL QKDPNSRSSA KELMVCFI
//

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