ID   CCB12_ARATH             Reviewed;         445 AA.
AC   Q39067; Q9FG02;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Cyclin-B1-2;
DE   AltName: Full=Cyc1b-At;
DE   AltName: Full=Cyclin-1b;
DE   AltName: Full=G2/mitotic-specific cyclin-B1-2;
DE            Short=CycB1;2;
GN   Name=CYCB1-2; Synonyms=CYC1B; OrderedLocusNames=At5g06150;
GN   ORFNames=MBL20.2;
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].
RC   TISSUE=Flower meristem;
RX   PubMed=8193159; DOI=10.1016/0167-4781(94)90112-0;
RA   Day I.S., Reddy A.S.;
RT   "Cloning of a family of cyclins from Arabidopsis thaliana.";
RL   Biochim. Biophys. Acta 1218:115-118(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8605306; DOI=10.1007/bf00049332;
RA   Day I.S., Reddy A.S., Golovkin M.;
RT   "Isolation of a new mitotic-like cyclin from Arabidopsis: complementation
RT   of a yeast cyclin mutant with a plant cyclin.";
RL   Plant Mol. Biol. 30:565-575(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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   TISSUE SPECIFICITY.
RX   PubMed=9484485; DOI=10.1023/a:1005959311462;
RA   Day I.S., Reddy A.S.;
RT   "Isolation and characterization of two cyclin-like cDNAs from
RT   Arabidopsis.";
RL   Plant Mol. Biol. 36:451-461(1998).
RN   [6]
RP   INDUCTION.
RX   PubMed=15181207; DOI=10.1104/pp.104.040022;
RA   West G., Inze D., Beemster G.T.S.;
RT   "Cell cycle modulation in the response of the primary root of Arabidopsis
RT   to salt stress.";
RL   Plant Physiol. 135:1050-1058(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=11882294; DOI=10.1016/s0960-9822(02)00693-0;
RA   Schnittger A., Schoebinger U., Stierhof Y.-D., Huelskamp M.;
RT   "Ectopic B-type cyclin expression induces mitotic cycles in
RT   endoreduplicating Arabidopsis trichomes.";
RL   Curr. Biol. 12:415-420(2002).
RN   [8]
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   [9]
RP   DEVELOPMENTAL STAGE, AND INTERACTION WITH FZR1; FZR2 AND FZR3.
RX   PubMed=15970679;
RA   Fueloep K., Tarayre S., Kelemen Z., Horvath G., Kevei Z., Nikovics K.,
RA   Bako L., Brown S., Kondorosi A., Kondorosi E.;
RT   "Arabidopsis anaphase-promoting complexes: multiple activators and wide
RT   range of substrates might keep APC perpetually busy.";
RL   Cell Cycle 4:1084-1092(2005).
CC   -!- FUNCTION: May induce mitotic cell division.
CC       {ECO:0000269|PubMed:11882294}.
CC   -!- SUBUNIT: Interacts with FZR2/CCS52A1, FZR1/CCS52A2 and FZR3/CCS52B.
CC       {ECO:0000269|PubMed:15970679}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems and flowers.
CC       {ECO:0000269|PubMed:9484485}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during G2/M and M phases.
CC       {ECO:0000269|PubMed:15970679}.
CC   -!- INDUCTION: Transiently down-regulated by salt stress in roots.
CC       {ECO:0000269|PubMed:15181207}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {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; L27223; AAB02028.1; -; mRNA.
DR   EMBL; AP002544; BAB09680.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90976.1; -; Genomic_DNA.
DR   PIR; S65734; S65734.
DR   RefSeq; NP_196233.1; NM_120697.3.
DR   AlphaFoldDB; Q39067; -.
DR   SMR; Q39067; -.
DR   BioGRID; 15781; 19.
DR   IntAct; Q39067; 15.
DR   STRING; 3702.AT5G06150.1; -.
DR   iPTMnet; Q39067; -.
DR   PaxDb; Q39067; -.
DR   PRIDE; Q39067; -.
DR   ProteomicsDB; 223962; -.
DR   DNASU; 830502; -.
DR   EnsemblPlants; AT5G06150.1; AT5G06150.1; AT5G06150.
DR   GeneID; 830502; -.
DR   Gramene; AT5G06150.1; AT5G06150.1; AT5G06150.
DR   KEGG; ath:AT5G06150; -.
DR   Araport; AT5G06150; -.
DR   TAIR; locus:2160722; AT5G06150.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_020695_0_3_1; -.
DR   InParanoid; Q39067; -.
DR   OMA; YSKAENG; -.
DR   OrthoDB; 993640at2759; -.
DR   PhylomeDB; Q39067; -.
DR   PRO; PR:Q39067; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q39067; baseline and differential.
DR   Genevisible; Q39067; AT.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
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   GO; GO:0010332; P:response to gamma radiation; IEP:TAIR.
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; Mitosis; Reference proteome.
FT   CHAIN           1..445
FT                   /note="Cyclin-B1-2"
FT                   /id="PRO_0000287004"
FT   CONFLICT        200
FT                   /note="K -> R (in Ref. 1; AAB02028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="L -> Q (in Ref. 1; AAB02028)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   445 AA;  49847 MW;  6FA9A8A73296E095 CRC64;
     MATRANVPEQ VRGAPLVDGL KIQNKNGAVK SRRALGDIGN LVSVPGVQGG KAQPPINRPI
     TRSFRAQLLA NAQLERKPIN GDNKVPALGP KRQPLAARNP EAQRAVQKKN LVVKQQTKPV
     EVIETKKEVT KKEVAMSPKN KKVTYSSVLS ARSKAACGIV NKPKIIDIDE SDKDNHLAAV
     EYVDDMYSFY KEVEKESQPK MYMHIQTEMN EKMRAILIDW LLEVHIKFEL NLETLYLTVN
     IIDRFLSVKA VPKRELQLVG ISALLIASKY EEIWPPQVND LVYVTDNAYS SRQILVMEKA
     ILGNLEWYLT VPTQYVFLVR FIKASMSDPE MENMVHFLAE LGMMHYDTLT FCPSMLAASA
     VYTARCSLNK SPAWTDTLQF HTGYTESEIM DCSKLLAFLH SRCGESRLRA VYKKYSKAEN
     GGVAMVSPAK SLLSAAADWK KPVSS