CKB21_ARATH
ID CKB21_ARATH Reviewed; 313 AA.
AC Q8LF80; Q94EX2; Q9C527;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cyclin-dependent kinase B2-1;
DE Short=CDKB2;1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
GN Name=CDKB2-1; OrderedLocusNames=At1g76540; ORFNames=F14G6.14;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH CYCD4-1.
RX PubMed=12857813; DOI=10.1104/pp.103.020644;
RA Kono A., Umeda-Hara C., Lee J., Ito M., Uchimiya H., Umeda M.;
RT "Arabidopsis D-type cyclin CYCD4;1 is a novel cyclin partner of B2-type
RT cyclin-dependent kinase.";
RL Plant Physiol. 132:1315-1321(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=17099223; DOI=10.1093/pcp/pcl034;
RA Adachi S., Uchimiya H., Umeda M.;
RT "Expression of B2-type cyclin-dependent kinase is controlled by protein
RT degradation in Arabidopsis thaliana.";
RL Plant Cell Physiol. 47:1683-1686(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 CYCD4-1 and CKS1. {ECO:0000269|PubMed:11432958,
CC ECO:0000269|PubMed:12857813}.
CC -!- INTERACTION:
CC Q8LF80; O23249: CKS1; NbExp=5; IntAct=EBI-1253579, EBI-1253127;
CC Q8LF80; P42751: CYCD1-1; NbExp=2; IntAct=EBI-1253579, EBI-2025690;
CC Q8LF80; Q8LGA1: CYCD4-1; NbExp=4; IntAct=EBI-1253579, EBI-1253202;
CC -!- TISSUE SPECIFICITY: Expressed in root tips, shoot apical meristem, leaf
CC primordia vascular tissues and tapetum of anthers.
CC {ECO:0000269|PubMed:11432958, ECO:0000269|PubMed:12857813,
CC ECO:0000269|PubMed:17099223}.
CC -!- DEVELOPMENTAL STAGE: Expressed from early G2 phase and increases to
CC reach a peak at mitosis. {ECO:0000269|PubMed:12857813}.
CC -!- MISCELLANEOUS: Protein abundance may be regulated through proteasome-
CC mediated protein degradation.
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=AAM61558.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ297936; CAC34052.1; -; mRNA.
DR EMBL; AB047279; BAB62068.1; -; mRNA.
DR EMBL; AC015450; AAG51960.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35857.1; -; Genomic_DNA.
DR EMBL; AF389283; AAK63856.1; -; mRNA.
DR EMBL; AY143859; AAN28798.1; -; mRNA.
DR EMBL; AY085000; AAM61558.1; ALT_INIT; mRNA.
DR PIR; D96793; D96793.
DR RefSeq; NP_177780.1; NM_106304.3.
DR AlphaFoldDB; Q8LF80; -.
DR SMR; Q8LF80; -.
DR BioGRID; 29206; 40.
DR IntAct; Q8LF80; 14.
DR STRING; 3702.AT1G76540.1; -.
DR iPTMnet; Q8LF80; -.
DR PaxDb; Q8LF80; -.
DR PRIDE; Q8LF80; -.
DR ProteomicsDB; 246702; -.
DR EnsemblPlants; AT1G76540.1; AT1G76540.1; AT1G76540.
DR GeneID; 843987; -.
DR Gramene; AT1G76540.1; AT1G76540.1; AT1G76540.
DR KEGG; ath:AT1G76540; -.
DR Araport; AT1G76540; -.
DR TAIR; locus:2011761; AT1G76540.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; Q8LF80; -.
DR OMA; CHLRRIV; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; Q8LF80; -.
DR PRO; PR:Q8LF80; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LF80; baseline and differential.
DR Genevisible; Q8LF80; AT.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA: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; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:TAIR.
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:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:TAIR.
DR GO; GO:0016572; P:histone phosphorylation; IDA:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
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 Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..313
FT /note="Cyclin-dependent kinase B2-1"
FT /id="PRO_0000293115"
FT DOMAIN 14..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT CONFLICT 250
FT /note="S -> G (in Ref. 5; AAK63856/AAN28798)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="S -> F (in Ref. 5; AAK63856/AAN28798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 35593 MW; 7E0EBD7A553DB9C9 CRC64;
MDEGVIAVSA MDAFEKLEKV GEGTYGKVYR AREKATGKIV ALKKTRLHED EEGVPSTTLR
EISILRMLAR DPHVVRLMDV KQGLSKEGKT VLYLVFEYMD TDVKKFIRSF RSTGKNIPTQ
TIKSLMYQLC KGMAFCHGHG ILHRDLKPHN LLMDPKTMRL KIADLGLARA FTLPMKKYTH
EILTLWYRAP EVLLGATHYS TAVDMWSVGC IFAELVTNQA IFQGDSELQQ LLHIFKLFGT
PNEEMWPGVS TLKNWHEYPQ WKPSTLSSAV PNLDEAGVDL LSKMLQYEPA KRISAKMAME
HPYFDDLPEK SSL
