CCNB3_DROME
ID CCNB3_DROME Reviewed; 575 AA.
AC Q9I7I0; O96718; Q9TYG8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=G2/mitotic-specific cyclin-B3;
GN Name=CycB3; ORFNames=CG5814;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEGRADATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9851980; DOI=10.1101/gad.12.23.3741;
RA Jacobs H.W., Knoblich J.A., Lehner C.F.;
RT "Drosophila Cyclin B3 is required for female fertility and is dispensable
RT for mitosis like Cyclin B.";
RL Genes Dev. 12:3741-3751(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DEGRADATION.
RX PubMed=7588612; DOI=10.1002/j.1460-2075.1995.tb00164.x;
RA Sigrist S., Jacobs H., Stratmann R., Lehner C.F.;
RT "Exit from mitosis is regulated by Drosophila fizzy and the sequential
RT destruction of cyclins A, B and B3.";
RL EMBO J. 14:4827-4838(1995).
RN [6]
RP DEGRADATION.
RX PubMed=11369230; DOI=10.1016/s0960-9822(01)00204-4;
RA Parry D.H., O'Farrell P.H.;
RT "The schedule of destruction of three mitotic cyclins can dictate the
RT timing of events during exit from mitosis.";
RL Curr. Biol. 11:671-683(2001).
RN [7]
RP FUNCTION.
RX PubMed=12620185; DOI=10.1016/s0960-9822(03)00127-1;
RA Echard A., O'Farrell P.H.;
RT "The degradation of two mitotic cyclins contributes to the timing of
RT cytokinesis.";
RL Curr. Biol. 13:373-383(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Cyclins are positive regulatory subunits of the cyclin-
CC dependent kinases (CDKs), and thereby play an essential role in the
CC control of the cell cycle, notably via their destruction during cell
CC division. Probably functions redundantly with other cyclins in
CC regulation of cell cycle. Its presence may be required to delay a
CC deadline for completing cytokinesis that is ordinary imposed by nuclear
CC envelope reformation. Degradation of CycB and CycB3 promote cytokinesis
CC furrow initiation and ingression. Required with CycB for female
CC fertility. {ECO:0000269|PubMed:12620185, ECO:0000269|PubMed:9851980}.
CC -!- SUBUNIT: Interacts with Cdk1 kinase.
CC -!- INTERACTION:
CC Q9I7I0; P23572: Cdk1; NbExp=2; IntAct=EBI-150964, EBI-108689;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9851980}.
CC -!- TISSUE SPECIFICITY: In embryo, it is expressed in all mitotically
CC proliferating cells, with a high level in neuroblasts. Not expressed in
CC old embryos and thereafter. Not expressed in endoreplicating tissues.
CC {ECO:0000269|PubMed:9851980}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:9851980}.
CC -!- DOMAIN: The N-terminal destruction box (D-box) probably acts as a
CC recognition signal for degradation via the ubiquitin-proteasome
CC pathway. {ECO:0000250}.
CC -!- PTM: Ubiquitinated (Probable). Ubiquitination leads to its degradation
CC in early anaphase. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ006772; CAA07237.1; -; mRNA.
DR EMBL; AJ012568; CAA10059.1; -; Genomic_DNA.
DR EMBL; AE014297; AAG22169.1; -; Genomic_DNA.
DR EMBL; BT003185; AAO24940.1; -; mRNA.
DR RefSeq; NP_001262934.1; NM_001276005.1.
DR RefSeq; NP_651303.2; NM_143046.3.
DR AlphaFoldDB; Q9I7I0; -.
DR SMR; Q9I7I0; -.
DR BioGRID; 67895; 17.
DR DIP; DIP-22205N; -.
DR IntAct; Q9I7I0; 3.
DR MINT; Q9I7I0; -.
DR STRING; 7227.FBpp0084103; -.
DR iPTMnet; Q9I7I0; -.
DR PaxDb; Q9I7I0; -.
DR DNASU; 42971; -.
DR EnsemblMetazoa; FBtr0084728; FBpp0084103; FBgn0015625.
DR EnsemblMetazoa; FBtr0334578; FBpp0306645; FBgn0015625.
DR GeneID; 42971; -.
DR KEGG; dme:Dmel_CG5814; -.
DR CTD; 42971; -.
DR FlyBase; FBgn0015625; CycB3.
DR VEuPathDB; VectorBase:FBgn0015625; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000160459; -.
DR HOGENOM; CLU_020695_10_5_1; -.
DR InParanoid; Q9I7I0; -.
DR OMA; WMRTLLV; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; Q9I7I0; -.
DR BioGRID-ORCS; 42971; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CycB3; fly.
DR GenomeRNAi; 42971; -.
DR PRO; PR:Q9I7I0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0015625; Expressed in egg cell and 43 other tissues.
DR ExpressionAtlas; Q9I7I0; baseline and differential.
DR Genevisible; Q9I7I0; DM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:UniProtKB.
DR GO; GO:0035561; P:regulation of chromatin binding; IGI:FlyBase.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:InterPro.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IGI:FlyBase.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR015452; Cyclin_B3.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF214; PTHR10177:SF214; 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.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..575
FT /note="G2/mitotic-specific cyclin-B3"
FT /id="PRO_0000080376"
FT MOTIF 75..83
FT /note="D-box"
FT /evidence="ECO:0000305"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 242
FT /note="S -> P (in Ref. 1; CAA07237)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="G -> S (in Ref. 1; CAA10059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 64772 MW; 20426777DC9C9E22 CRC64;
MAPTKATTRA AITSGHHQLQ QAVNPILGAL GAATRKGLTR RAAATGNIDP NVENMQTRAK
RKADHSPIKN DKIKRSALGN LTNNVKIMTL HPAQDEEQSG VGKKPTAQQL QALMDAKKQE
NLSVNVFGAS KMTTRASSKV EDSVENCHKV LDKLEEALAR PKPRPKAVPA AKKTVLGEVQ
LPAMPNPMQI PVLLPPTHNL AAPQVAAVKP VRRISNDFNK TEDSLYMSAL EDVSSCDSMR
LSGNFEAARR RSAKLQQKTE QQPQPLLLTL PETAPSQVVP IPPVPEEVED FDRKNWDDPF
QVSHYAMDIF NYLKVREAEF PIADYMPRQI HLTTWMRTLL VDWMVEVQET FELNHETLYL
AVKIVDLYLC REVINKEKLQ LLGAAAFFIA CKYDERQPPL IEDFLYICDG AYNHDELVRM
ERETLRVIKY DLGIPLSYRF LRRYARCAKV PMPTLTLARY ILELSLMDYA NISFSDSQMA
SAALFMALRM HGGPGQLDKQ TWTSTLIYYT GYQLADFAEI VTALNAGLHR KPRATIKTIR
NKYSHKIFHE VAKVPLLTNQ ELFQGNLDLN ESNLS
