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Database: UniProt
Entry: A0A1P8B7U0_ARATH
LinkDB: A0A1P8B7U0_ARATH
Original site: A0A1P8B7U0_ARATH 
ID   A0A1P8B7U0_ARATH        Unreviewed;       381 AA.
AC   A0A1P8B7U0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Cyclin B22 {ECO:0000313|EMBL:ANM67659.1};
GN   Name=CYCB2 {ECO:0000313|TAIR:AT4G35620};
GN   Synonyms=CYCB2:2 {ECO:0000313|EMBL:ANM67659.1}, Cyclin B2:2
GN   {ECO:0000313|EMBL:ANM67659.1};
GN   OrderedLocusNames=At4g35620 {ECO:0000313|Araport:AT4G35620,
GN   ECO:0000313|EMBL:ANM67659.1};
GN   ORFNames=F8D20.130 {ECO:0000313|EMBL:ANM67659.1}, F8D20_130
GN   {ECO:0000313|EMBL:ANM67659.1};
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 {ECO:0000313|EMBL:ANM67659.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:ANM67659.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=10617198; DOI=10.1038/47134;
RG   EU;
RG   CSHL and WU Arabidopsis Sequencing Project;
RA   Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA   Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA   Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA   Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA   Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA   Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA   Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA   Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Kotter 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., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA   Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA   Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA   Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA   Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA   Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA   Montfort 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., Sehkon 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., Nelson J.,
RA   Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA   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., Hoffmann J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
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   [2] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006955}.
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DR   EMBL; CP002687; ANM67659.1; -; Genomic_DNA.
DR   RefSeq; NP_001329476.1; NM_001342363.1.
DR   AlphaFoldDB; A0A1P8B7U0; -.
DR   SMR; A0A1P8B7U0; -.
DR   EnsemblPlants; AT4G35620.2; AT4G35620.2; AT4G35620.
DR   GeneID; 829714; -.
DR   Gramene; AT4G35620.2; AT4G35620.2; AT4G35620.
DR   Araport; AT4G35620; -.
DR   TAIR; AT4G35620; CYCB2.
DR   OMA; WSTTCEL; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; A0A1P8B7U0; baseline and differential.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR046965; Cyclin_A/B-like.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177:SF602; CYCLIN-B2-2; 1.
DR   PANTHER; PTHR10177; CYCLINS; 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; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT   DOMAIN          210..294
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          303..381
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          307..381
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          66..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  44291 MW;  55A6EDB9D826C249 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 L
//
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