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 27-MAR-2024, entry version 129. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 41. DR IntAct; Q2V419; 9. DR STRING; 3702.Q2V419; -. DR iPTMnet; Q2V419; -. DR PaxDb; 3702-AT2G38620-2; -. 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; AT2G38620; CDKB1. DR eggNOG; KOG0594; Eukaryota. DR HOGENOM; CLU_000288_181_6_1; -. DR InParanoid; Q2V419; -. DR OMA; SLRDWHE; -. DR OrthoDB; 244018at2759; -. DR PhylomeDB; Q2V419; -. DR PRO; PR:Q2V419; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q2V419; baseline and differential. DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:TAIR. 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; IEA:UniProtKB-EC. 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:0010444; P:guard mother cell differentiation; IMP:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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:2000037; P:regulation of stomatal complex patterning; IMP:UniProtKB. DR CDD; cd07837; STKc_CdkB_plant; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF254; CYCLIN-DEPENDENT KINASE 2; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q2V419; AT. 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 //