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Protein

G2/mitotic-specific cyclin-B1

Gene

Ccnb1

Organism
Mus musculus (Mouse)
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

  • histone kinase activity Source: Ensembl
  • kinase activity Source: MGI
  • patched binding Source: MGI
  • protein kinase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-113507. E2F-enabled inhibition of pre-replication complex formation.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-176417. Phosphorylation of Emi1.
R-MMU-2299718. Condensation of Prophase Chromosomes.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-MMU-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-MMU-380320. Recruitment of NuMA to mitotic centrosomes.
R-MMU-4419969. Depolymerisation of the Nuclear Lamina.
R-MMU-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-MMU-69273. Cyclin A/B1 associated events during G2/M transition.
R-MMU-69478. G2/M DNA replication checkpoint.
R-MMU-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
G2/mitotic-specific cyclin-B1
Gene namesi
Name:Ccnb1
Synonyms:Ccn-2, Ccnb1-rs13, Cycb, Cycb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:88302. Ccnb1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • condensed nuclear chromosome outer kinetochore Source: MGI
  • cytoplasm Source: MGI
  • membrane Source: MGI
  • nucleus Source: MGI
  • spindle pole Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430G2/mitotic-specific cyclin-B1PRO_0000080352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731N6-acetyllysineBy similarity
Modified residuei123 – 1231Phosphoserine; by CDK1By similarity
Modified residuei125 – 1251PhosphoserineBy similarity
Modified residuei130 – 1301Phosphoserine; by PLK1By similarity
Modified residuei144 – 1441PhosphoserineBy similarity
Modified residuei318 – 3181PhosphothreonineBy similarity

Post-translational modificationi

Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases (By similarity).By similarity
Phosphorylated by PLK1 at Ser-130 on centrosomes during prophase: phosphorylation by PLK1 does not cause nuclear import. Phosphorylation at Ser-144 was also reported to be mediated by PLK1 but Ser-130 seems to be the primary phosphorylation site (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP24860.
PaxDbiP24860.
PRIDEiP24860.

PTM databases

iPTMnetiP24860.
PhosphoSiteiP24860.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Gene expression databases

BgeeiP24860.
CleanExiMM_CCNB1.
ExpressionAtlasiP24860. baseline and differential.
GenevisibleiP24860. MM.

Interactioni

Subunit structurei

Interacts with the CDC2 protein kinase to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF). The cyclin subunit imparts substrate specificity to the complex. Binds HEI10. Interacts with catalytically active RALBP1 and CDC2 during mitosis to form an endocytotic complex during interphase. Interacts with CCNF; interaction is required for nuclear localization. Interacts with CDK5RAP3.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi234538. 10 interactions.
IntActiP24860. 2 interactions.
STRINGi10090.ENSMUSP00000071989.

Structurei

3D structure databases

ProteinModelPortaliP24860.
SMRiP24860. Positions 164-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 1749Interaction with CDK2By similarity
Regioni255 – 2584Interaction with CDK2By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi51 – 8535Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiKOG0653. Eukaryota.
COG5024. LUCA.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiP24860.
KOiK05868.
OMAiHMTVKNK.
OrthoDBiEOG7ZGX3C.
PhylomeDBiP24860.
TreeFamiTF101001.

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]

Sequencei

Sequence statusi: Complete.

P24860-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRVTRNTK INAENKAKVS MAGAKRVPVT VTAASKPGLR PRTALGDIGN
60 70 80 90 100
KVSEELQARV PLKREAKTLG TGKGTVKALP KPVEKVPVCE PEVELAEPEP
110 120 130 140 150
EPELEHVREE KLSPEPILVD NPSPSPMETS GCAPAEEYLC QAFSDVILAV
160 170 180 190 200
SDVDADDGAD PNLCSEYVKD IYAYLRQLEE EQSVRPKYLQ GREVTGNMRA
210 220 230 240 250
ILIDWLIQVQ MKFRLLQETM YMTVSIIDRF MQNSCVPKKM LQLVGVTAMF
260 270 280 290 300
IASKYEEMYP PEIGDFAFVT NNTYTKHQIR QMEMKILRVL NFSLGRPLPL
310 320 330 340 350
HFLRRASKVG EVDVEQHTLA KYLMELSMLD YDMVHFAPSQ IAAGAFCLAL
360 370 380 390 400
KILDNGEWTP TLQHYLSYSE DSLLPVMQHL AKNVVMVNCG LTKHMTVKNK
410 420 430
YAASKHAKIS TLAQLNCTLV QNLSKAVTKA
Length:430
Mass (Da):48,052
Last modified:October 1, 1996 - v3
Checksum:iF3BC9C856F66986E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251K → M in CAA45968 (PubMed:1280449).Curated
Sequence conflicti59 – 591R → T in CAA41545 (PubMed:1836195).Curated
Sequence conflicti130 – 1301S → C in CAA41545 (PubMed:1836195).Curated
Sequence conflicti139 – 1391L → P in CAA41545 (PubMed:1836195).Curated
Sequence conflicti157 – 1571D → S in CAA41545 (PubMed:1836195).Curated
Sequence conflicti241 – 2411L → I in CAA41545 (PubMed:1836195).Curated
Sequence conflicti257 – 2571E → D in CAA41545 (PubMed:1836195).Curated
Sequence conflicti315 – 3151E → R in CAA41545 (PubMed:1836195).Curated
Sequence conflicti331 – 3311Y → C in CAA45968 (PubMed:1280449).Curated
Sequence conflicti340 – 3434QIAA → RAFS in CAA41545 (PubMed:1836195).Curated
Sequence conflicti351 – 3511K → E in CAA41545 (PubMed:1836195).Curated
Sequence conflicti419 – 4191L → H in CAA41545 (PubMed:1836195).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64713 mRNA. Translation: CAA45968.1.
X58708 mRNA. Translation: CAA41545.1.
S43105 mRNA. Translation: AAB22970.1.
BC011478 mRNA. Translation: AAH11478.1.
BC085238 mRNA. Translation: AAH85238.1.
CCDSiCCDS36768.1.
PIRiA43285.
I48316.
JH0509.
RefSeqiNP_758505.2. NM_172301.3.
UniGeneiMm.260114.
Mm.380027.
Mm.482545.

Genome annotation databases

EnsembliENSMUST00000072119; ENSMUSP00000071989; ENSMUSG00000041431.
GeneIDi268697.
KEGGimmu:268697.
UCSCiuc007rro.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64713 mRNA. Translation: CAA45968.1.
X58708 mRNA. Translation: CAA41545.1.
S43105 mRNA. Translation: AAB22970.1.
BC011478 mRNA. Translation: AAH11478.1.
BC085238 mRNA. Translation: AAH85238.1.
CCDSiCCDS36768.1.
PIRiA43285.
I48316.
JH0509.
RefSeqiNP_758505.2. NM_172301.3.
UniGeneiMm.260114.
Mm.380027.
Mm.482545.

3D structure databases

ProteinModelPortaliP24860.
SMRiP24860. Positions 164-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234538. 10 interactions.
IntActiP24860. 2 interactions.
STRINGi10090.ENSMUSP00000071989.

PTM databases

iPTMnetiP24860.
PhosphoSiteiP24860.

Proteomic databases

EPDiP24860.
PaxDbiP24860.
PRIDEiP24860.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072119; ENSMUSP00000071989; ENSMUSG00000041431.
GeneIDi268697.
KEGGimmu:268697.
UCSCiuc007rro.1. mouse.

Organism-specific databases

CTDi891.
MGIiMGI:88302. Ccnb1.

Phylogenomic databases

eggNOGiKOG0653. Eukaryota.
COG5024. LUCA.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiP24860.
KOiK05868.
OMAiHMTVKNK.
OrthoDBiEOG7ZGX3C.
PhylomeDBiP24860.
TreeFamiTF101001.

Enzyme and pathway databases

ReactomeiR-MMU-113507. E2F-enabled inhibition of pre-replication complex formation.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-176417. Phosphorylation of Emi1.
R-MMU-2299718. Condensation of Prophase Chromosomes.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-MMU-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-MMU-380320. Recruitment of NuMA to mitotic centrosomes.
R-MMU-4419969. Depolymerisation of the Nuclear Lamina.
R-MMU-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-MMU-69273. Cyclin A/B1 associated events during G2/M transition.
R-MMU-69478. G2/M DNA replication checkpoint.
R-MMU-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.

Miscellaneous databases

PROiP24860.
SOURCEiSearch...

Gene expression databases

BgeeiP24860.
CleanExiMM_CCNB1.
ExpressionAtlasiP24860. baseline and differential.
GenevisibleiP24860. MM.

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. "Identification of a mouse B-type cyclin which exhibits developmentally regulated expression in the germ line."
    Chapman D.L., Wolgemuth D.J.
    Mol. Reprod. Dev. 33:259-269(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss Webster.
    Tissue: Testis.
  2. "Sequence of a cDNA encoding a mouse cyclin B protein."
    Paterno G.D., Downs K.M.
    Gene 108:315-316(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/He.
  3. "Expression of murine cyclin B1 mRNAs and genetic mapping of related genomic sequences."
    Hanley-Hyde J., Mushinski J.F., Sadofsky M., Huppi K., Krall M., Kozak C.A., Mock B.
    Genomics 13:1018-1030(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor and Olfactory epithelium.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiCCNB1_MOUSE
AccessioniPrimary (citable) accession number: P24860
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.