CCB22_ARATH
ID CCB22_ARATH Reviewed; 429 AA.
AC Q39070; O81794;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cyclin-B2-2;
DE AltName: Full=Cyc2b-At;
DE AltName: Full=Cyclin-2b;
DE AltName: Full=G2/mitotic-specific cyclin-B2-2;
DE Short=CycB2;2;
GN Name=CYCB2-2; Synonyms=CYC2B; OrderedLocusNames=At4g35620;
GN ORFNames=F8D20.130;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Callus;
RX PubMed=7972055; DOI=10.1073/pnas.91.24.11313;
RA Ferreira P., Hemerly A., de Almeida Engler J., Bergounioux C., Burssens S.,
RA van Montagu M., Engler G., Inze D.;
RT "Three discrete classes of Arabidopsis cyclins are expressed during
RT different intervals of the cell cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11313-11317(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15208425; DOI=10.1104/pp.104.040436;
RA Wang G., Kong H., Sun Y., Zhang X., Zhang W., Altman N., dePamphilis C.W.,
RA Ma H.;
RT "Genome-wide analysis of the cyclin family in Arabidopsis and comparative
RT phylogenetic analysis of plant cyclin-like proteins.";
RL Plant Physiol. 135:1084-1099(2004).
RN [6]
RP INTERACTION WITH CDC20-1 AND CDC20-2.
RX PubMed=21687678; DOI=10.1371/journal.pone.0020618;
RA Kevei Z., Baloban M., Da Ines O., Tiricz H., Kroll A., Regulski K.,
RA Mergaert P., Kondorosi E.;
RT "Conserved CDC20 cell cycle functions are carried out by two of the five
RT isoforms in Arabidopsis thaliana.";
RL PLoS ONE 6:E20618-E20618(2011).
CC -!- SUBUNIT: Interacts with CDC20-1 and CDC20-2.
CC {ECO:0000269|PubMed:21687678}.
CC -!- INTERACTION:
CC Q39070; O48723: PLP2; NbExp=3; IntAct=EBI-2651372, EBI-4443426;
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:7972055}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; Z31401; CAA83276.1; -; mRNA.
DR EMBL; AL031135; CAA20032.1; -; Genomic_DNA.
DR EMBL; AL161587; CAB80278.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86541.1; -; Genomic_DNA.
DR EMBL; AK226721; BAE98826.1; -; mRNA.
DR PIR; T04667; T04667.
DR RefSeq; NP_195287.1; NM_119727.4.
DR AlphaFoldDB; Q39070; -.
DR SMR; Q39070; -.
DR BioGRID; 14996; 16.
DR IntAct; Q39070; 11.
DR STRING; 3702.AT4G35620.1; -.
DR PaxDb; Q39070; -.
DR PRIDE; Q39070; -.
DR ProteomicsDB; 224440; -.
DR EnsemblPlants; AT4G35620.1; AT4G35620.1; AT4G35620.
DR GeneID; 829714; -.
DR Gramene; AT4G35620.1; AT4G35620.1; AT4G35620.
DR KEGG; ath:AT4G35620; -.
DR Araport; AT4G35620; -.
DR TAIR; locus:2127948; AT4G35620.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_0_0_1; -.
DR InParanoid; Q39070; -.
DR OMA; QFDITDK; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; Q39070; -.
DR PRO; PR:Q39070; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39070; baseline and differential.
DR Genevisible; Q39070; AT.
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:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Reference proteome.
FT CHAIN 1..429
FT /note="Cyclin-B2-2"
FT /id="PRO_0000287013"
FT REGION 66..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 160
FT /note="E -> G (in Ref. 1; CAA83276)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="C -> R (in Ref. 1; CAA83276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 49787 MW; 5BDE8D7171A2FE09 CRC64;
MVNPEENNRN LVVKPITEIL QDDDKRSRKF GVEMKRQNRR ALGVINHNLV GAKAYPCVVN
KRRGLSQRKQ ESCDKKKLDS LHPSISRSQE ETKKLKPSGN EFGDCIFIDE EEEKNEEVTL
DQPMPMSLEE PYIEFDPMEE EVEMEDMEEE QEEPVLDIDE YDANNSLAAV EYVQDLYDFY
RKTERFSCVP LDYMAQQFDI SDKMRAILID WLIEVHDKFE LMNETLFLTV NLIDRFLSKQ
AVARKKLQLV GLVALLLACK YEEVSVPIVE DLVVISDKAY TRTDVLEMEK IMLSTLQFNM
SLPTQYPFLK RFLKAAQSDK KLEILASFLI ELALVDYEMV RYPPSLLAAT AVYTAQCTIH
GFSEWNSTCE FHCHYSENQL LECCRRMVRL HQKAGTDKLT GVHRKYSSSK FGYIATKYEA
AHFLVSDSH
