(data stored in ACNUC8465 zone)

SWISSPROT: M2K1_ORYSJ

ID   M2K1_ORYSJ              Reviewed;         355 AA.
AC   Q5QN75; Q0JMF0; Q9FQM4;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Mitogen-activated protein kinase kinase 1;
DE            Short=MAP kinase kinase 1;
DE            Short=MAPKK1;
DE            EC=2.7.12.2;
DE   AltName: Full=OsMEK1;
GN   Name=MKK1; Synonyms=MEK1; OrderedLocusNames=Os01g0510100, LOC_Os01g32660;
GN   ORFNames=P0455H03.45, P0520B06.8;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MPK5/MAPK5, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=12177502; DOI=10.1104/pp.006072;
RA   Wen J.-Q., Oono K., Imai R.;
RT   "Two novel mitogen-activated protein signaling components, OsMEK1 and
RT   OsMAP1, are involved in a moderate low-temperature signaling pathway in
RT   rice.";
RL   Plant Physiol. 129:1880-1891(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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 MPK5/MAPK5. {ECO:0000269|PubMed:12177502}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaf sheaths and panicles.
CC       {ECO:0000269|PubMed:12177502}.
CC   -!- INDUCTION: By low temperature (12 degrees Celsius) treatment.
CC       {ECO:0000269|PubMed:12177502}.
CC   -!- PTM: Phosphorylated on Ser-221 and Thr-227, which activates the enzyme.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
DR   EMBL; AF216314; AAG40578.1; -; mRNA.
DR   EMBL; AP003077; BAD73135.1; -; Genomic_DNA.
DR   EMBL; AP003435; BAD73553.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF05078.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS72372.1; -; Genomic_DNA.
DR   RefSeq; XP_015621394.1; XM_015765908.1.
DR   SMR; Q5QN75; -.
DR   STRING; 4530.OS01T0510100-01; -.
DR   PaxDb; Q5QN75; -.
DR   EnsemblPlants; Os01t0510100-01; Os01t0510100-01; Os01g0510100.
DR   GeneID; 4324023; -.
DR   Gramene; Os01t0510100-01; Os01t0510100-01; Os01g0510100.
DR   KEGG; osa:4324023; -.
DR   eggNOG; KOG0581; Eukaryota.
DR   eggNOG; ENOG410XQ5A; LUCA.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; Q5QN75; -.
DR   KO; K04368; -.
DR   OMA; WGTPFEQ; -.
DR   OrthoDB; 688282at2759; -.
DR   BRENDA; 2.7.12.2; 4460.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q5QN75; OS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009524; C:phragmoplast; IEA:EnsemblPlants.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004708; F:MAP kinase kinase activity; IEA:EnsemblPlants.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:EnsemblPlants.
DR   GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:EnsemblPlants.
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:0002229; P:defense response to oomycetes; IEA:EnsemblPlants.
DR   GO; GO:0010311; P:lateral root formation; IEA:EnsemblPlants.
DR   GO; GO:0007112; P:male meiosis cytokinesis; IEA:EnsemblPlants.
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; Q5QN75.
DR   SWISS-2DPAGE; Q5QN75.
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..355
FT                   /note="Mitogen-activated protein kinase kinase 1"
FT                   /id="PRO_0000239761"
FT   DOMAIN          71..330
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         77..85
FT                   /note="ATP"
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         100
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         227
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  40000 MW;  B579E8B7DCB861F4 CRC64;
     MRGKKPHKEL KLSVPAQETP VDKFLTASGT FKDGELRLNQ RGLQLISEET ADEPQSTNLK
     VEDVQLSMDD LEMIQVIGKG SGGIVQLVRH KWVGTLYALK GIQMNIQEAV RKQIVQELKI
     NQATQNAHIV LCHQSFYHNG VIYLVLEYMD RGSLADIIKQ VKTILEPYLA VLCKQVLEGL
     LYLHHERHVI HRDIKPSNLL VNRKGEVKIT DFGVSAVLAS SMGQRDTFVG TYNYMAPERI
     SGSSYDYKSD IWSLGLVILE CAIGRFPYIP SEGEGWLSFY ELLEAIVDQP PPSAPADQFS
     PEFCAFISSC IQKDPAERMS ASELLNHPFI KKFEDKDLDL RILVESLEPP MNISE
//

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