CKB21_ORYSJ
ID CKB21_ORYSJ Reviewed; 326 AA.
AC Q0J4I1; B9G1R8; Q40734; Q6Z8N6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cyclin-dependent kinase B2-1;
DE Short=CDKB2;1;
DE Short=CDKB;2;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=CDC2Os-3;
GN Name=CDKB2-1; Synonyms=SS224;
GN OrderedLocusNames=Os08g0512600, LOC_Os08g40170;
GN ORFNames=OsJ_27911 {ECO:0000312|EMBL:EEE68985.1}, P0711H09.13;
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 [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 [2]
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 [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-326.
RC TISSUE=Callus;
RX PubMed=7703506; DOI=10.3109/10425179409039714;
RA Kidou S., Umeda M., Uchimiya H.;
RT "Nucleotide sequence of rice (oryza sativa L.) cDNA homologous to cdc2
RT gene.";
RL DNA Seq. 5:125-129(1994).
RN [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=9880343; DOI=10.1104/pp.119.1.31;
RA Umeda M., Umeda-Hara C., Yamaguchi M., Hashimoto J., Uchimiya H.;
RT "Differential expression of genes for cyclin-dependent protein kinases in
RT rice plants.";
RL Plant Physiol. 119:31-40(1999).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=10987556; DOI=10.1007/s004250000295;
RA Fabian T., Lorbiecke R., Umeda M., Sauter M.;
RT "The cell cycle genes cycA1;1 and cdc2Os-3 are coordinately regulated by
RT gibberellin in planta.";
RL Planta 211:376-383(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CYCB2-1 AND CYCB2-2.
RX PubMed=12753582; DOI=10.1046/j.1365-313x.2003.01736.x;
RA Lee J., Das A., Yamaguchi M., Hashimoto J., Tsutsumi N., Uchimiya H.,
RA Umeda M.;
RT "Cell cycle function of a rice B2-type cyclin interacting with a B-type
RT cyclin-dependent kinase.";
RL Plant J. 34:417-425(2003).
RN [10]
RP INDUCTION, AND GENE FAMILY.
RX PubMed=17443292; DOI=10.1007/s11103-007-9154-y;
RA Guo J., Song J., Wang F., Zhang X.S.;
RT "Genome-wide identification and expression analysis of rice cell cycle
RT genes.";
RL Plant Mol. Biol. 64:349-360(2007).
CC -!- FUNCTION: Forms a complex with CYCB2-1 or CYCB2-2 that activates CDK
CC kinase in tobacco BY2 cells during G2/M (mitosis) phases. May be
CC involved in the regulation of the cell cycle at the G2/M transition.
CC {ECO:0000269|PubMed:10987556, ECO:0000269|PubMed:12753582}.
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=2.7.11.22;
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=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC -!- SUBUNIT: Interacts with CYCB2-1 and CYCB2-2. Binding to CYCB2-1 or
CC CYCB2-2 activates CDK kinase. {ECO:0000269|PubMed:12753582}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12753582}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:12753582}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:12753582}.
CC Note=Associated to mitotic spindle during metaphase, and progressively
CC localized the phragmoplast during telophase.
CC -!- TISSUE SPECIFICITY: Expressed in the dividing region of the root apex
CC and the intercalary meristem of internodes.
CC {ECO:0000269|PubMed:10987556, ECO:0000269|PubMed:9880343}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the G2/M phases.
CC {ECO:0000269|PubMed:10987556, ECO:0000269|PubMed:9880343}.
CC -!- INDUCTION: By cytokinin, gibberellin (GA3) and submergence. Down-
CC regulated by the replication blocking agent hydroxyurea.
CC {ECO:0000269|PubMed:10987556, ECO:0000269|PubMed:17443292,
CC ECO:0000269|PubMed:9880343}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19553.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD10065.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP004765; BAD10065.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008214; BAF24134.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06213.1; -; Genomic_DNA.
DR EMBL; CM000145; EEE68985.1; -; Genomic_DNA.
DR EMBL; AK059682; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; D64036; BAA19553.1; ALT_INIT; mRNA.
DR PIR; T04109; T04109.
DR RefSeq; XP_015648777.1; XM_015793291.1.
DR AlphaFoldDB; Q0J4I1; -.
DR SMR; Q0J4I1; -.
DR STRING; 4530.OS08T0512600-01; -.
DR PaxDb; Q0J4I1; -.
DR PRIDE; Q0J4I1; -.
DR EnsemblPlants; Os08t0512600-01; Os08t0512600-01; Os08g0512600.
DR GeneID; 4346016; -.
DR Gramene; Os08t0512600-01; Os08t0512600-01; Os08g0512600.
DR KEGG; osa:4346016; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; Q0J4I1; -.
DR OMA; CHLRRIV; -.
DR OrthoDB; 1010560at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q0J4I1; OS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; 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;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..326
FT /note="Cyclin-dependent kinase B2-1"
FT /id="PRO_0000296099"
FT DOMAIN 28..318
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CONFLICT 29
FT /note="E -> G (in Ref. 5; AK059682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 36977 MW; DC539454B81481EE CRC64;
MAALHHQAAA APVTTTTDGG ELRAMDLYEK LEKVGEGTYG KVYKAREKAT GRIVALKKTR
LPEDDEGVPP TALREVSLLR MLSQDSHVVR LLDLKQGQNK EGQTILYLVF EYMDTDLKKF
IRAHRQNLQK IPVPTVKILM YQLCKGVAFC HGRGVLHRDL KPHNLLMDRK TMALKIADLG
LSRSFTVPLK KYTHEILTLW YRAPEVLLGA AHYSTPVDIW SVGCIFAELA TNQPLFAGDS
EVQQLLHIFK LLGTPNEQVW PGVSKLPNWH EYPQWNPSKV SDLVHGLDAD ALDLLEKMLQ
YEPSKRISAK KAMEHPYFND VNKELY
