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Protein

G2/mitotic-specific cyclin-B

Gene

CycB

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for the control of the cell cycle at the G2/M (mitosis) transition.

GO - Molecular functioni

  • cyclin-dependent protein serine/threonine kinase regulator activity Source: FlyBase

GO - Biological processi

  • attachment of spindle microtubules to kinetochore Source: FlyBase
  • cell separation after cytokinesis Source: FlyBase
  • cellular response to DNA damage stimulus Source: FlyBase
  • embryonic development via the syncytial blastoderm Source: FlyBase
  • G2/M transition of mitotic cell cycle Source: FlyBase
  • mitotic chromosome movement towards spindle pole Source: FlyBase
  • mitotic cytokinesis Source: FlyBase
  • regulation of chromatin binding Source: FlyBase
  • regulation of protein kinase activity Source: GOC
  • syncytial blastoderm mitotic cell cycle Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-DME-113507. E2F-enabled inhibition of pre-replication complex formation.
R-DME-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-DME-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-DME-176412. Phosphorylation of the APC/C.
R-DME-2500257. Resolution of Sister Chromatid Cohesion.
R-DME-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-DME-4419969. Depolymerisation of the Nuclear Lamina.
R-DME-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-DME-69273. Cyclin A/B1 associated events during G2/M transition.
R-DME-69478. G2/M DNA replication checkpoint.
R-DME-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiP20439.

Names & Taxonomyi

Protein namesi
Recommended name:
G2/mitotic-specific cyclin-B
Gene namesi
Name:CycB
ORF Names:CG3510
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0000405. CycB.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: FlyBase
  • cytoplasm Source: FlyBase
  • nuclear cyclin-dependent protein kinase holoenzyme complex Source: FlyBase
  • nucleus Source: FlyBase
  • pole plasm Source: FlyBase
  • spindle Source: FlyBase
  • spindle midzone Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530G2/mitotic-specific cyclin-BPRO_0000080385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei137 – 1371Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20439.

PTM databases

iPTMnetiP20439.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Gene expression databases

BgeeiP20439.
ExpressionAtlasiP20439. differential.
GenevisibleiP20439. DM.

Interactioni

Subunit structurei

Interacts with the protein kinase Cdk1 to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF). The cyclin subunit imparts substrate specificity to the complex.

Protein-protein interaction databases

BioGridi63230. 70 interactions.
IntActiP20439. 7 interactions.
MINTiMINT-1544963.
STRINGi7227.FBpp0071822.

Structurei

3D structure databases

ProteinModelPortaliP20439.
SMRiP20439. Positions 255-523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiKOG0653. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
InParanoidiP20439.
KOiK05868.
OMAiNEPTLKR.
OrthoDBiEOG7ZGX3C.
PhylomeDBiP20439.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P20439-1) [UniParc]FASTAAdd to basket

Also known as: D

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVGTTLKMRG DENASENFKQ VQLKKLTVPS MEATTKRAAL GDLQNRGISR
60 70 80 90 100
PIAAKDAAQK DSKDLKLTDA LRNAKARVDS HWKKQPLGST NGNGNGAVPP
110 120 130 140 150
KVNEGGVSAF LRSNSVRNRV PTKTTVEPTK VTVKSSSSEN VNEPTLKRED
160 170 180 190 200
SNLSKKSLTK LRAALAKPVM GVSGIRREPV AVSRKEAETK KELPETKKDS
210 220 230 240 250
LEVKKDATRM PLIRGNSAVT TTTSTMPTTM SLSSKRLAGI EDIDANDKEN
260 270 280 290 300
LVLVSEYVND IYDYLYQVEL EQPIHKDHLA GQKEVSHKMR AVLIDWINEV
310 320 330 340 350
HLQFHLAAET FQLAVAIIDR YLQVVKDTKR TYLQLVGVTA LFIATKYEEL
360 370 380 390 400
FPPAIGDFVF ITDDTYTARQ IRQMELQIFK AIDCNLSRPL PIHFLRRYSK
410 420 430 440 450
AAGAEDEHHT MSKYFIELAS VDYEMATYRP SEIAAASLFL SLHLLNGNHR
460 470 480 490 500
AGTGFNDRHW TPTLTFYSRY SAAHLRPITR LIAKLARDAP QAKLKAIYNK
510 520 530
YQGSKFQKIA LRTELTGALM DSIVGQSQRK
Length:530
Mass (Da):59,256
Last modified:June 21, 2005 - v2
Checksum:iD74ABEE0C8066D4A
GO
Isoform B (identifier: P20439-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MVGTTLKMRGDE → MAALEK

Show »
Length:524
Mass (Da):58,580
Checksum:iECFAD5B6DCCF5D0E
GO
Isoform C (identifier: P20439-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Show »
Length:500
Mass (Da):55,923
Checksum:i9DAA664A643C9936
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621R → G in AAA28436 (PubMed:2139805).Curated
Sequence conflicti383 – 3831D → N in CAA39148 (PubMed:2142452).Curated
Sequence conflicti515 – 5151L → P in CAA39148 (PubMed:2142452).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3030Missing in isoform C. CuratedVSP_021570Add
BLAST
Alternative sequencei1 – 1212MVGTT…MRGDE → MAALEK in isoform B. CuratedVSP_021569Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33192 mRNA. Translation: AAA28436.1.
X55542 mRNA. Translation: CAA39148.1.
AJ006773 Genomic DNA. Translation: CAA07238.1.
AJ006773 Genomic DNA. Translation: CAA07239.1.
AJ006773 Genomic DNA. Translation: CAA07240.1.
AE013599 Genomic DNA. Translation: AAF46904.1.
AE013599 Genomic DNA. Translation: AAG22197.1.
AE013599 Genomic DNA. Translation: AAM71123.1.
AE013599 Genomic DNA. Translation: AAM71124.1.
AY102682 mRNA. Translation: AAM27511.1.
PIRiA35144.
RefSeqiNP_726244.1. NM_166555.3. [P20439-1]
NP_726245.2. NM_166556.3.
NP_726246.1. NM_166557.3. [P20439-2]
NP_726247.1. NM_166558.2. [P20439-3]
UniGeneiDm.7295.

Genome annotation databases

EnsemblMetazoaiFBtr0071911; FBpp0071822; FBgn0000405. [P20439-1]
GeneIDi37618.
KEGGidme:Dmel_CG3510.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33192 mRNA. Translation: AAA28436.1.
X55542 mRNA. Translation: CAA39148.1.
AJ006773 Genomic DNA. Translation: CAA07238.1.
AJ006773 Genomic DNA. Translation: CAA07239.1.
AJ006773 Genomic DNA. Translation: CAA07240.1.
AE013599 Genomic DNA. Translation: AAF46904.1.
AE013599 Genomic DNA. Translation: AAG22197.1.
AE013599 Genomic DNA. Translation: AAM71123.1.
AE013599 Genomic DNA. Translation: AAM71124.1.
AY102682 mRNA. Translation: AAM27511.1.
PIRiA35144.
RefSeqiNP_726244.1. NM_166555.3. [P20439-1]
NP_726245.2. NM_166556.3.
NP_726246.1. NM_166557.3. [P20439-2]
NP_726247.1. NM_166558.2. [P20439-3]
UniGeneiDm.7295.

3D structure databases

ProteinModelPortaliP20439.
SMRiP20439. Positions 255-523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63230. 70 interactions.
IntActiP20439. 7 interactions.
MINTiMINT-1544963.
STRINGi7227.FBpp0071822.

PTM databases

iPTMnetiP20439.

Proteomic databases

PaxDbiP20439.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071911; FBpp0071822; FBgn0000405. [P20439-1]
GeneIDi37618.
KEGGidme:Dmel_CG3510.

Organism-specific databases

CTDi37618.
FlyBaseiFBgn0000405. CycB.

Phylogenomic databases

eggNOGiKOG0653. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
InParanoidiP20439.
KOiK05868.
OMAiNEPTLKR.
OrthoDBiEOG7ZGX3C.
PhylomeDBiP20439.

Enzyme and pathway databases

ReactomeiR-DME-113507. E2F-enabled inhibition of pre-replication complex formation.
R-DME-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-DME-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-DME-176412. Phosphorylation of the APC/C.
R-DME-2500257. Resolution of Sister Chromatid Cohesion.
R-DME-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-DME-4419969. Depolymerisation of the Nuclear Lamina.
R-DME-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-DME-69273. Cyclin A/B1 associated events during G2/M transition.
R-DME-69478. G2/M DNA replication checkpoint.
R-DME-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiP20439.

Miscellaneous databases

ChiTaRSiCycB. fly.
GenomeRNAii37618.
PROiP20439.

Gene expression databases

BgeeiP20439.
ExpressionAtlasiP20439. differential.
GenevisibleiP20439. DM.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The roles of Drosophila cyclins A and B in mitotic control."
    Lehner C.F., O'Farrell P.H.
    Cell 61:535-547(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  2. "The A- and B-type cyclins of Drosophila are accumulated and destroyed in temporally distinct events that define separable phases of the G2-M transition."
    Whitfield W.G.F., Gonzalez C., Maldonado-Codina G., Glover D.M.
    EMBO J. 9:2563-2572(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  3. "3' non-translated sequences in Drosophila cyclin B transcripts direct posterior pole accumulation late in oogenesis and peri-nuclear association in syncytial embryos."
    Dalby B., Glover D.M.
    Development 115:989-997(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A; B AND C).
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  6. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  7. "Transcripts of one of two Drosophila cyclin genes become localized in pole cells during embryogenesis."
    Whitfield W.G.F., Gonzalez C., Sanchez-Herrero E., Glover D.M.
    Nature 338:337-340(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 289-301 AND 343-355.
  8. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiCCNB_DROME
AccessioniPrimary (citable) accession number: P20439
Secondary accession number(s): Q0E8Y2
, Q8MME2, Q9I7V2, Q9TYH6, Q9TYH7, Q9V3F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 21, 2005
Last modified: June 8, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.