CKB12_ARATH
ID CKB12_ARATH Reviewed; 311 AA.
AC Q2V419; Q56XK5; Q9ZVI4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cyclin-dependent kinase B1-2;
DE Short=CDKB1;2;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
GN Name=CDKB1-2; OrderedLocusNames=At2g38620; ORFNames=T6A23.18;
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 [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH CKS1.
RX PubMed=11432958; DOI=10.1093/jxb/52.359.1381;
RA Boudolf V., Rombauts S., Naudts M., Inze D., de Veylder L.;
RT "Identification of novel cyclin-dependent kinases interacting with the CKS1
RT protein of Arabidopsis.";
RL J. Exp. Bot. 52:1381-1382(2001).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11971144; DOI=10.1105/tpc.010445;
RA Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
RT "Genome-wide analysis of core cell cycle genes in Arabidopsis.";
RL Plant Cell 14:903-916(2002).
RN [6]
RP REVIEW.
RX PubMed=17094738; DOI=10.1146/annurev.genet.40.110405.090431;
RA Inze D., de Veylder L.;
RT "Cell cycle regulation in plant development.";
RL Annu. Rev. Genet. 40:77-105(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20675570; DOI=10.1105/tpc.110.074609;
RA Xie Z., Lee E., Lucas J.R., Morohashi K., Li D., Murray J.A., Sack F.D.,
RA Grotewold E.;
RT "Regulation of cell proliferation in the stomatal lineage by the
RT Arabidopsis MYB FOUR LIPS via direct targeting of core cell cycle genes.";
RL Plant Cell 22:2306-2321(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=24123248; DOI=10.1093/jxb/ert313;
RA Lee E., Liu X., Eglit Y., Sack F.;
RT "FOUR LIPS and MYB88 conditionally restrict the G1/S transition during
RT stomatal formation.";
RL J. Exp. Bot. 64:5207-5219(2013).
CC -!- FUNCTION: Together with CDKB1-1, promotes both the last division in the
CC stomatal cell lineage as well as the number of stomata
CC (PubMed:20675570). In collaboration with MYB124 and MYB88, restrict the
CC G1/S transition and chloroplast and nuclear number during stomatal
CC formation, and normally maintain fate and developmental progression
CC throughout the stomatal cell lineage (PubMed:24123248).
CC {ECO:0000269|PubMed:20675570, ECO:0000269|PubMed:24123248}.
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 CKS1. {ECO:0000269|PubMed:11432958}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2V419-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2V419-2; Sequence=VSP_026473, VSP_026474;
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:11432958}.
CC -!- DISRUPTION PHENOTYPE: No apparent stomatal abnormalities. The double
CC mutant cdkb1;1 cdkb1;2 has a reduced number of abnormal stomata
CC consisting in single guard cells (GC) (PubMed:20675570). The quadruple
CC mutant flp-1 myb88 cdkb1;1 cdkb1;2 has a reduced number of large single
CC guard cells blocked at mitosis, with strongly altered shape and size
CC and characterized by enlarged nucleus due to endomitosis and
CC endocycling, as well as extensive chloroplast replication
CC (PubMed:24123248). {ECO:0000269|PubMed:20675570,
CC ECO:0000269|PubMed:24123248}.
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=BAD95353.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ297937; CAC34053.1; -; mRNA.
DR EMBL; AC005499; AAC67356.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09557.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09558.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62340.1; -; Genomic_DNA.
DR EMBL; AK221669; BAD95353.1; ALT_SEQ; mRNA.
DR PIR; C84807; C84807.
DR RefSeq; NP_001031507.1; NM_001036430.3. [Q2V419-1]
DR RefSeq; NP_001324504.1; NM_001336710.1. [Q2V419-2]
DR RefSeq; NP_181396.2; NM_129419.3. [Q2V419-2]
DR AlphaFoldDB; Q2V419; -.
DR SMR; Q2V419; -.
DR BioGRID; 3786; 40.
DR IntAct; Q2V419; 9.
DR STRING; 3702.AT2G38620.2; -.
DR PaxDb; Q2V419; -.
DR PRIDE; Q2V419; -.
DR ProteomicsDB; 246701; -. [Q2V419-1]
DR EnsemblPlants; AT2G38620.1; AT2G38620.1; AT2G38620. [Q2V419-2]
DR EnsemblPlants; AT2G38620.2; AT2G38620.2; AT2G38620. [Q2V419-1]
DR EnsemblPlants; AT2G38620.3; AT2G38620.3; AT2G38620. [Q2V419-2]
DR GeneID; 818444; -.
DR Gramene; AT2G38620.1; AT2G38620.1; AT2G38620. [Q2V419-2]
DR Gramene; AT2G38620.2; AT2G38620.2; AT2G38620. [Q2V419-1]
DR Gramene; AT2G38620.3; AT2G38620.3; AT2G38620. [Q2V419-2]
DR KEGG; ath:AT2G38620; -.
DR Araport; AT2G38620; -.
DR TAIR; locus:2064087; AT2G38620.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; Q2V419; -.
DR OMA; FPKWEAT; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; Q2V419; -.
DR PRO; PR:Q2V419; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q2V419; baseline and differential.
DR Genevisible; Q2V419; AT.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:TAIR.
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:0030332; F:cyclin binding; IPI:TAIR.
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:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010444; P:guard mother cell differentiation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:TAIR.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR GO; GO:0032875; P:regulation of DNA endoreduplication; IMP:UniProtKB.
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:2000037; P:regulation of stomatal complex patterning; IMP:UniProtKB.
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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..311
FT /note="Cyclin-dependent kinase B1-2"
FT /id="PRO_0000293114"
FT DOMAIN 4..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT VAR_SEQ 236..257
FT /note="LLGTPTEQQWPGVMALRDWHVY -> YLLLVFDANVYVYRNQFRTLAH (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026473"
FT VAR_SEQ 258..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026474"
FT CONFLICT 231
FT /note="L -> I (in Ref. 4; BAD95353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 35582 MW; A04E60AEF83E5BB0 CRC64;
MEKYEKLEKV GEGTYGKVYK AMEKTTGKLV ALKKTRLEMD EEGIPPTALR EISLLQMLSQ
SIYIVRLLCV EHVIQSKDST VSHSPKSNLY LVFEYLDTDL KKFIDSHRKG SNPRPLEASL
VQRFMFQLFK GVAHCHSHGV LHRDLKPQNL LLDKDKGILK IADLGLSRAF TVPLKAYTHE
IVTLWYRAPE VLLGSTHYST AVDIWSVGCI FAEMIRRQAL FPGDSEFQQL LHIFRLLGTP
TEQQWPGVMA LRDWHVYPKW EPQDLSRAVP SLSPEGIDLL TQMLKYNPAE RISAKAALDH
PYFDSLDKSQ F
