CCNB_DROME
ID CCNB_DROME Reviewed; 530 AA.
AC P20439; Q0E8Y2; Q8MME2; Q9I7V2; Q9TYH6; Q9TYH7; Q9V3F4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=G2/mitotic-specific cyclin-B;
GN Name=CycB; ORFNames=CG3510;
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 [MRNA] (ISOFORM A).
RX PubMed=2139805; DOI=10.1016/0092-8674(90)90535-m;
RA Lehner C.F., O'Farrell P.H.;
RT "The roles of Drosophila cyclins A and B in mitotic control.";
RL Cell 61:535-547(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=2142452; DOI=10.1002/j.1460-2075.1990.tb07437.x;
RA Whitfield W.G.F., Gonzalez C., Maldonado-Codina G., Glover D.M.;
RT "The A- and B-type cyclins of Drosophila are accumulated and destroyed in
RT temporally distinct events that define separable phases of the G2-M
RT transition.";
RL EMBO J. 9:2563-2572(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS A; B
RP AND C).
RX PubMed=1451670; DOI=10.1242/dev.115.4.989;
RA Dalby B., Glover D.M.;
RT "3' non-translated sequences in Drosophila cyclin B transcripts direct
RT posterior pole accumulation late in oogenesis and peri-nuclear association
RT in syncytial embryos.";
RL Development 115:989-997(1992).
RN [4]
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 [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 289-301 AND 343-355.
RX PubMed=2564167; DOI=10.1038/338337a0;
RA Whitfield W.G.F., Gonzalez C., Sanchez-Herrero E., Glover D.M.;
RT "Transcripts of one of two Drosophila cyclin genes become localized in pole
RT cells during embryogenesis.";
RL Nature 338:337-340(1989).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, 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: Essential for the control of the cell cycle at the G2/M
CC (mitosis) transition.
CC -!- SUBUNIT: Interacts with the protein kinase Cdk1 to form a
CC serine/threonine kinase holoenzyme complex also known as maturation
CC promoting factor (MPF). The cyclin subunit imparts substrate
CC specificity to the complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=D;
CC IsoId=P20439-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P20439-2; Sequence=VSP_021569;
CC Name=C;
CC IsoId=P20439-3; Sequence=VSP_021570;
CC -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC destroyed at mitosis.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; M33192; AAA28436.1; -; mRNA.
DR EMBL; X55542; CAA39148.1; -; mRNA.
DR EMBL; AJ006773; CAA07238.1; -; Genomic_DNA.
DR EMBL; AJ006773; CAA07239.1; -; Genomic_DNA.
DR EMBL; AJ006773; CAA07240.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46904.1; -; Genomic_DNA.
DR EMBL; AE013599; AAG22197.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM71123.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM71124.1; -; Genomic_DNA.
DR EMBL; AY102682; AAM27511.1; -; mRNA.
DR PIR; A35144; A35144.
DR RefSeq; NP_726244.1; NM_166555.3. [P20439-1]
DR RefSeq; NP_726245.2; NM_166556.3.
DR RefSeq; NP_726246.1; NM_166557.3. [P20439-2]
DR RefSeq; NP_726247.1; NM_166558.2. [P20439-3]
DR AlphaFoldDB; P20439; -.
DR SMR; P20439; -.
DR BioGRID; 63230; 97.
DR IntAct; P20439; 7.
DR MINT; P20439; -.
DR STRING; 7227.FBpp0071822; -.
DR iPTMnet; P20439; -.
DR PaxDb; P20439; -.
DR PRIDE; P20439; -.
DR DNASU; 37618; -.
DR EnsemblMetazoa; FBtr0071911; FBpp0071822; FBgn0000405. [P20439-1]
DR EnsemblMetazoa; FBtr0071913; FBpp0071824; FBgn0000405. [P20439-2]
DR EnsemblMetazoa; FBtr0071914; FBpp0071825; FBgn0000405. [P20439-3]
DR GeneID; 37618; -.
DR KEGG; dme:Dmel_CG3510; -.
DR CTD; 37618; -.
DR FlyBase; FBgn0000405; CycB.
DR VEuPathDB; VectorBase:FBgn0000405; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000168350; -.
DR InParanoid; P20439; -.
DR OMA; VSYKMRA; -.
DR PhylomeDB; P20439; -.
DR Reactome; R-DME-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-DME-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DME-176412; Phosphorylation of the APC/C.
DR Reactome; R-DME-176417; Phosphorylation of Emi1.
DR Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DME-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DME-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-DME-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-DME-69478; G2/M DNA replication checkpoint.
DR Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-DME-8878166; Transcriptional regulation by RUNX2.
DR SignaLink; P20439; -.
DR BioGRID-ORCS; 37618; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CycB; fly.
DR GenomeRNAi; 37618; -.
DR PRO; PR:P20439; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000405; Expressed in cleaving embryo and 40 other tissues.
DR ExpressionAtlas; P20439; baseline and differential.
DR Genevisible; P20439; DM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; TAS:FlyBase.
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:FlyBase.
DR GO; GO:0051233; C:spindle midzone; IDA:FlyBase.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:FlyBase.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:FlyBase.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; TAS:FlyBase.
DR GO; GO:0048134; P:germ-line cyst formation; IMP:FlyBase.
DR GO; GO:0061952; P:midbody abscission; IMP:FlyBase.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
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: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; 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 Alternative splicing; Cell cycle; Cell division; Cyclin; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..530
FT /note="G2/mitotic-specific cyclin-B"
FT /id="PRO_0000080385"
FT REGION 76..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_021570"
FT VAR_SEQ 1..12
FT /note="MVGTTLKMRGDE -> MAALEK (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_021569"
FT CONFLICT 162
FT /note="R -> G (in Ref. 1; AAA28436)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="D -> N (in Ref. 2; CAA39148)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="L -> P (in Ref. 2; CAA39148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 59256 MW; D74ABEE0C8066D4A CRC64;
MVGTTLKMRG DENASENFKQ VQLKKLTVPS MEATTKRAAL GDLQNRGISR PIAAKDAAQK
DSKDLKLTDA LRNAKARVDS HWKKQPLGST NGNGNGAVPP KVNEGGVSAF LRSNSVRNRV
PTKTTVEPTK VTVKSSSSEN VNEPTLKRED SNLSKKSLTK LRAALAKPVM GVSGIRREPV
AVSRKEAETK KELPETKKDS LEVKKDATRM PLIRGNSAVT TTTSTMPTTM SLSSKRLAGI
EDIDANDKEN LVLVSEYVND IYDYLYQVEL EQPIHKDHLA GQKEVSHKMR AVLIDWINEV
HLQFHLAAET FQLAVAIIDR YLQVVKDTKR TYLQLVGVTA LFIATKYEEL FPPAIGDFVF
ITDDTYTARQ IRQMELQIFK AIDCNLSRPL PIHFLRRYSK AAGAEDEHHT MSKYFIELAS
VDYEMATYRP SEIAAASLFL SLHLLNGNHR AGTGFNDRHW TPTLTFYSRY SAAHLRPITR
LIAKLARDAP QAKLKAIYNK YQGSKFQKIA LRTELTGALM DSIVGQSQRK
