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Protein

G2/mitotic-specific cyclin-B1

Gene

CCNB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 activator activity Source: CAFA
  • cyclin-dependent protein serine/threonine kinase activity Source: Reactome
  • histone kinase activity Source: Ensembl
  • patched binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • ubiquitin-like protein ligase binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionCyclin
Biological processCell 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-4419969 Depolymerisation of the Nuclear Lamina
R-HSA-6804114 TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-68875 Mitotic Prophase
R-HSA-69273 Cyclin A/B1/B2 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
R-HSA-8878166 Transcriptional regulation by RUNX2
SignaLinkiP14635
SIGNORiP14635

Protein family/group databases

TCDBi1.I.1.1.3 the eukaryotic nuclear pore complex (e-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

EuPathDBiHostDB:ENSG00000134057.14
HGNCiHGNC:1579 CCNB1
MIMi123836 gene
neXtProtiNX_P14635

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
HPA061448

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

Show more details

GO - Molecular functioni

  • patched binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • ubiquitin-like protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107332, 148 interactors
CORUMiP14635
DIPiDIP-59N
ELMiP14635
IntActiP14635, 61 interactors
MINTiP14635
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 – 216Combined sources18
Helixi220 – 234Combined sources15
Helixi241 – 243Combined sources3
Helixi244 – 259Combined sources16
Helixi266 – 272Combined sources7
Beta strandi275 – 277Combined sources3
Helixi279 – 292Combined sources14
Turni293 – 295Combined sources3
Helixi302 – 312Combined sources11
Helixi317 – 330Combined sources14
Helixi334 – 336Combined sources3
Beta strandi337 – 339Combined sources3
Helixi341 – 356Combined sources16
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[»]
5LQFX-ray2.06B/E165-433[»]
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

CDDicd00043 CYCLIN, 2 hits
InterProiView protein in InterPro
IPR013763 Cyclin-like
IPR036915 Cyclin-like_sf
IPR004367 Cyclin_C-dom
IPR006671 Cyclin_N
PfamiView protein in Pfam
PF02984 Cyclin_C, 1 hit
PF00134 Cyclin_N, 1 hit
SMARTiView protein in SMART
SM00385 CYCLIN, 2 hits
SM01332 Cyclin_C, 1 hit
SUPFAMiSSF47954 SSF47954, 2 hits
PROSITEiView protein in PROSITE
PS00292 CYCLINS, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCCNB1_HUMAN
AccessioniPrimary (citable) accession number: P14635
Secondary accession number(s): A8K066, Q5TZP9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 23, 2018
This is version 191 of the entry and version 1 of the sequence. See 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

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