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Protein

G2/mitotic-specific cyclin-B1

Gene

CCNB1

Organism
Homo sapiens (Human)
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.2 Publications

GO - Molecular functioni

  • cyclin-dependent protein serine/threonine kinase activity Source: Reactome
  • histone kinase activity Source: Ensembl
  • patched binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-113507. E2F-enabled inhibition of pre-replication complex formation.
R-HSA-156711. Polo-like kinase mediated events.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69478. G2/M DNA replication checkpoint.
R-HSA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
SignaLinkiP14635.
SIGNORiP14635.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
G2/mitotic-specific cyclin-B1
Gene namesi
Name:CCNB1
Synonyms:CCNB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:1579. CCNB1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • condensed nuclear chromosome outer kinetochore Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • membrane Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • spindle pole Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi133S → A: Strongly impairs phosphorylation by PLK1. 2 Publications1
Mutagenesisi147S → A: Does not affect phosphorylation by PLK1. 1 Publication1

Organism-specific databases

DisGeNETi891.
OpenTargetsiENSG00000134057.
PharmGKBiPA95.

Chemistry databases

ChEMBLiCHEMBL2412.

Polymorphism and mutation databases

BioMutaiCCNB1.
DMDMi116176.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000803501 – 433G2/mitotic-specific cyclin-B1Add BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei73N6-acetyllysineCombined sources1
Modified residuei126Phosphoserine; by CDK12 Publications1
Modified residuei128Phosphoserine1 Publication1
Modified residuei133Phosphoserine; by PLK12 Publications1
Modified residuei147Phosphoserine2 Publications1
Modified residuei321PhosphothreonineCombined sources1

Post-translational modificationi

Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases.1 Publication
Phosphorylated by PLK1 at Ser-133 on centrosomes during prophase: phosphorylation by PLK1 does not cause nuclear import. Phosphorylation at Ser-147 was also reported to be mediated by PLK1 but Ser-133 seems to be the primary phosphorylation site.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP14635.
MaxQBiP14635.
PaxDbiP14635.
PeptideAtlasiP14635.
PRIDEiP14635.

PTM databases

iPTMnetiP14635.
PhosphoSitePlusiP14635.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.1 Publication

Gene expression databases

BgeeiENSG00000134057.
CleanExiHS_CCNB1.
ExpressionAtlasiP14635. baseline and differential.
GenevisibleiP14635. HS.

Organism-specific databases

HPAiCAB000115.
CAB003804.
HPA030741.

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 (PubMed:15790566).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNB1IP1Q9NPC32EBI-495332,EBI-745269
CDK1P0649310EBI-495332,EBI-444308
CDKN1BP465272EBI-495332,EBI-519280
FOXO1Q127782EBI-495332,EBI-1108782
PKMYT1Q996405EBI-495332,EBI-495308
UBE2KP610862EBI-495332,EBI-473850
UHRF2Q96PU42EBI-495332,EBI-625304

GO - Molecular functioni

  • patched binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107332. 130 interactors.
DIPiDIP-59N.
IntActiP14635. 58 interactors.
MINTiMINT-1202632.
STRINGi9606.ENSP00000256442.

Chemistry databases

BindingDBiP14635.

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi171 – 184Combined sources14
Turni189 – 194Combined sources6
Beta strandi195 – 197Combined sources3
Helixi199 – 215Combined sources17
Helixi220 – 235Combined sources16
Helixi241 – 243Combined sources3
Helixi244 – 259Combined sources16
Helixi266 – 272Combined sources7
Turni273 – 275Combined sources3
Helixi279 – 292Combined sources14
Turni293 – 295Combined sources3
Helixi302 – 312Combined sources11
Helixi317 – 330Combined sources14
Helixi334 – 336Combined sources3
Beta strandi337 – 339Combined sources3
Helixi341 – 355Combined sources15
Helixi363 – 369Combined sources7
Helixi373 – 391Combined sources19
Helixi399 – 403Combined sources5
Helixi407 – 409Combined sources3
Helixi412 – 414Combined sources3
Helixi416 – 419Combined sources4
Helixi421 – 428Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B9RX-ray2.90A/B165-433[»]
2JGZX-ray2.90B167-426[»]
4Y72X-ray2.30B165-433[»]
4YC3X-ray2.70B165-433[»]
5HQ0X-ray2.30B165-433[»]
DisProtiDP00223.
ProteinModelPortaliP14635.
SMRiP14635.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14635.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni169 – 177Interaction with CDK29
Regioni258 – 261Interaction with CDK24

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi51 – 85Lys-richAdd BLAST35

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiKOG0653. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiP14635.
KOiK05868.
OMAiHMTVKNK.
OrthoDBiEOG091G0E9B.
PhylomeDBiP14635.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P14635-1) [UniParc]FASTAAdd to basket

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
MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN
60 70 80 90 100
KVSEQLQAKM PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE
110 120 130 140 150
PEPEPEPEPV KEEKLSPEPI LVDTASPSPM ETSGCAPAEE DLCQAFSDVI
160 170 180 190 200
LAVNDVDAED GADPNLCSEY VKDIYAYLRQ LEEEQAVRPK YLLGREVTGN
210 220 230 240 250
MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP KKMLQLVGVT
260 270 280 290 300
AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP
310 320 330 340 350
LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC
360 370 380 390 400
LALKILDNGE WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV
410 420 430
KNKYATSKHA KISTLPQLNS ALVQDLAKAV AKV
Length:433
Mass (Da):48,337
Last modified:April 1, 1990 - v1
Checksum:iE2C4767AE8A11EC0
GO
Isoform 2 (identifier: P14635-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     362-398: Missing.

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):44,102
Checksum:i1B7AFCE21614F6D5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti108E → G in BAF82120 (PubMed:14702039).Curated1
Sequence conflicti153V → A in BAF82120 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_053892362 – 398Missing in isoform 2. 1 PublicationAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25753 mRNA. No translation available.
AY338491 Genomic DNA. Translation: AAP88038.1.
AK289431 mRNA. Translation: BAF82120.1.
BT020128 mRNA. Translation: AAV38930.1.
AC010273 Genomic DNA. No translation available.
AC022107 Genomic DNA. No translation available.
BC006510 mRNA. Translation: AAH06510.1.
CCDSiCCDS3997.1. [P14635-1]
PIRiA32992.
RefSeqiNP_114172.1. NM_031966.3. [P14635-1]
UniGeneiHs.23960.

Genome annotation databases

EnsembliENST00000256442; ENSP00000256442; ENSG00000134057. [P14635-1]
ENST00000505500; ENSP00000424588; ENSG00000134057. [P14635-2]
GeneIDi891.
KEGGihsa:891.
UCSCiuc003jvm.4. human. [P14635-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25753 mRNA. No translation available.
AY338491 Genomic DNA. Translation: AAP88038.1.
AK289431 mRNA. Translation: BAF82120.1.
BT020128 mRNA. Translation: AAV38930.1.
AC010273 Genomic DNA. No translation available.
AC022107 Genomic DNA. No translation available.
BC006510 mRNA. Translation: AAH06510.1.
CCDSiCCDS3997.1. [P14635-1]
PIRiA32992.
RefSeqiNP_114172.1. NM_031966.3. [P14635-1]
UniGeneiHs.23960.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B9RX-ray2.90A/B165-433[»]
2JGZX-ray2.90B167-426[»]
4Y72X-ray2.30B165-433[»]
4YC3X-ray2.70B165-433[»]
5HQ0X-ray2.30B165-433[»]
DisProtiDP00223.
ProteinModelPortaliP14635.
SMRiP14635.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107332. 130 interactors.
DIPiDIP-59N.
IntActiP14635. 58 interactors.
MINTiMINT-1202632.
STRINGi9606.ENSP00000256442.

Chemistry databases

BindingDBiP14635.
ChEMBLiCHEMBL2412.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP14635.
PhosphoSitePlusiP14635.

Polymorphism and mutation databases

BioMutaiCCNB1.
DMDMi116176.

Proteomic databases

EPDiP14635.
MaxQBiP14635.
PaxDbiP14635.
PeptideAtlasiP14635.
PRIDEiP14635.

Protocols and materials databases

DNASUi891.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256442; ENSP00000256442; ENSG00000134057. [P14635-1]
ENST00000505500; ENSP00000424588; ENSG00000134057. [P14635-2]
GeneIDi891.
KEGGihsa:891.
UCSCiuc003jvm.4. human. [P14635-1]

Organism-specific databases

CTDi891.
DisGeNETi891.
GeneCardsiCCNB1.
HGNCiHGNC:1579. CCNB1.
HPAiCAB000115.
CAB003804.
HPA030741.
MIMi123836. gene.
neXtProtiNX_P14635.
OpenTargetsiENSG00000134057.
PharmGKBiPA95.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0653. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiP14635.
KOiK05868.
OMAiHMTVKNK.
OrthoDBiEOG091G0E9B.
PhylomeDBiP14635.
TreeFamiTF101001.

Enzyme and pathway databases

ReactomeiR-HSA-113507. E2F-enabled inhibition of pre-replication complex formation.
R-HSA-156711. Polo-like kinase mediated events.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69478. G2/M DNA replication checkpoint.
R-HSA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
SignaLinkiP14635.
SIGNORiP14635.

Miscellaneous databases

ChiTaRSiCCNB1. human.
EvolutionaryTraceiP14635.
GeneWikiiCyclin_B1.
GenomeRNAii891.
PROiP14635.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000134057.
CleanExiHS_CCNB1.
ExpressionAtlasiP14635. baseline and differential.
GenevisibleiP14635. HS.

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...

Entry informationi

Entry nameiCCNB1_HUMAN
AccessioniPrimary (citable) accession number: P14635
Secondary accession number(s): A8K066, Q5TZP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 177 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.