G2/mitotic-specific cyclin-B1 - Homo sapiens (Human)

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P14635 (CCNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
G2/mitotic-specific cyclin-B1

Gene names

Name:	CCNB1
Synonyms:	CCNB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for the control of the cell cycle at the G2/M (mitosis) transition. Ref.15 Ref.16
Subunit structure	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. Ref.1 Ref.5 Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › centrosome Ref.5 Ref.6 Ref.9 Ref.11.
Developmental stage	Accumulates steadily during G2 and is abruptly destroyed at mitosis. Ref.1
Post-translational modification	Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases. Ref.10 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. Ref.6 Ref.9
Sequence similarities	Belongs to the cyclin family. Cyclin AB subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Molecular function	Cyclin
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome G2/M transition of mitotic cell cycle Non-traceable author statement. Source: UniProtKB M phase of mitotic cell cycle Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular response to fatty acid Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from electronic annotation. Source: Compara cellular response to iron(III) ion Inferred from electronic annotation. Source: Compara cellular response to organic cyclic compound Inferred from electronic annotation. Source: Compara digestive tract development Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara mitotic metaphase plate congression Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL mitotic nuclear envelope disassembly Traceable author statement. Source: Reactome mitotic prometaphase Inferred from direct assay PubMed 18195732. Source: BHF-UCL mitotic prophase Traceable author statement. Source: Reactome mitotic spindle checkpoint Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL mitotic spindle stabilization Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL negative regulation of gene expression Inferred from electronic annotation. Source: Compara negative regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara oocyte maturation Inferred from electronic annotation. Source: Compara positive regulation of attachment of spindle microtubules to kinetochore Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL positive regulation of cardiac muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of histone phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of mRNA 3'-end processing Inferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycle Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein complex assembly Inferred from electronic annotation. Source: Compara protein phosphorylation Inferred from electronic annotation. Source: Compara regulation of chromosome condensation Inferred from electronic annotation. Source: Compara regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro response to DDT Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara tissue regeneration Inferred from electronic annotation. Source: Compara ventricular cardiac muscle cell development Inferred from electronic annotation. Source: Compara
Cellular_component	centrosome Inferred from direct assay Ref.9. Source: UniProtKB condensed nuclear chromosome outer kinetochore Inferred from direct assay PubMed 18195732. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome spindle pole Inferred from direct assay PubMed 18195732. Source: BHF-UCL
Molecular_function	kinase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CCNB1IP1	Q9NPC3	2	EBI-495332,EBI-745269
CDK1	P06493	4	EBI-495332,EBI-444308
PKMYT1	Q99640	2	EBI-495332,EBI-495308
UHRF2	Q96PU4	2	EBI-495332,EBI-625304

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 433

433

G2/mitotic-specific cyclin-B1

PRO_0000080350

Regions

Region

169 – 177

Interaction with CDK2

Region

258 – 261

Interaction with CDK2

Compositional bias

51 – 85

Lys-rich

Amino acid modifications

Modified residue

N6-acetyllysine Ref.13

Modified residue

126

Phosphoserine; by CDK1 Ref.6 Ref.9

Modified residue

128

Phosphoserine Ref.6

Modified residue

133

Phosphoserine; by PLK1 Ref.6 Ref.9

Modified residue

147

Phosphoserine Ref.6 Ref.9

Modified residue

321

Phosphothreonine Ref.12

Experimental info

Mutagenesis

133

S → A: Strongly impairs phosphorylation by PLK1. Ref.6 Ref.9

Mutagenesis

147

S → A: Does not affect phosphorylation by PLK1. Ref.9

Secondary structure

433

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P14635 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: E2C4767AE8A11EC0
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FASTA

433

48,337

        10         20         30         40         50         60 
MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN KVSEQLQAKM 

        70         80         90        100        110        120 
PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE PEPEPEPEPV KEEKLSPEPI 

       130        140        150        160        170        180 
LVDTASPSPM ETSGCAPAEE DLCQAFSDVI LAVNDVDAED GADPNLCSEY VKDIYAYLRQ 

       190        200        210        220        230        240 
LEEEQAVRPK YLLGREVTGN MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP 

       250        260        270        280        290        300 
KKMLQLVGVT AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP 

       310        320        330        340        350        360 
LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC LALKILDNGE 

       370        380        390        400        410        420 
WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV KNKYATSKHA KISTLPQLNS 

       430 
ALVQDLAKAV AKV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2." Pines J., Hunter T. Cell 58:833-846(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, SUBUNIT.
[2]	NIEHS SNPs program Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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]. Tissue: Placenta.
[4]	"Structure and growth-dependent regulation of the human cyclin B1 promoter." Piaggio G., Farina A., Perrotti D., Manni I., Fuschi P., Sacchi A., Gaetano C. Exp. Cell Res. 216:396-402(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[5]	"Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-cyclin interaction." Kong M., Barnes E.A., Ollendorff V., Donoghue D.J. EMBO J. 19:1378-1388(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CCNF.
[6]	"Cooperative phosphorylation including the activity of polo-like kinase 1 regulates the subcellular localization of cyclin B1." Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E., Kaufmann M., Strebhardt K. Oncogene 21:8282-8292(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-128; SER-133 AND SER-147, MUTAGENESIS OF SER-133.
[7]	"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis." Rosse C., L'Hoste S., Offner N., Picard A., Camonis J. J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RALBP1.
[8]	"A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels." Toby G.G., Gherraby W., Coleman T.R., Golemis E.A. Mol. Cell. Biol. 23:2109-2122(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HEI10.
[9]	"Active cyclin B1-Cdk1 first appears on centrosomes in prophase." Jackman M., Lindon C., Nigg E.A., Pines J. Nat. Cell Biol. 5:143-148(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-133 AND SER-147, MUTAGENESIS OF SER-133 AND SER-147.
[10]	"NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry." Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H., Morris S.W., Peschel C., Duyster J. Cell 122:45-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[11]	"p21-mediated nuclear retention of cyclin B1-Cdk1 in response to genotoxic stress." Baus Charrier-Savournin F., Chateau M.-T., Gire V., Sedivy J., Piette J., Dulic V. Mol. Biol. Cell 15:3965-3976(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, MASS SPECTROMETRY.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Cyclin B and cyclin A confer different substrate recognition properties on CDK2." Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N. Cell Cycle 6:1350-1359(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 167-426 IN COMPLEX WITH PHOSPHORYLATED CDK2, FUNCTION.
[16]	"The crystal structure of human cyclin B." Petri E.T., Errico A., Escobedo L., Hunt T., Basavappa R. Cell Cycle 6:1342-1349(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 165-433, FUNCTION.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M25753 mRNA. No translation available.
AY338491 Genomic DNA. Translation: AAP88038.1.
BC006510 mRNA. Translation: AAH06510.1.

IPI

IPI00745793.

PIR

A32992.

RefSeq

NP_114172.1. NM_031966.3.

UniGene

Hs.23960.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B9R	X-ray	2.90	A/B	165-433	[»]
2JGZ	X-ray	2.90	B	167-426	[»]

DisProt

DP00223.

ProteinModelPortal

P14635.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59N.

IntAct

P14635. 15 interactions.

MINT

MINT-1202632.

STRING

9606.ENSP00000256442.

PTM databases

PhosphoSite

P14635.

Polymorphism databases

DMDM

116176.

Proteomic databases

PaxDb

P14635.

PRIDE

P14635.

Protocols and materials databases

DNASU

891.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256442; ENSP00000256442; ENSG00000134057.

GeneID

891.

KEGG

hsa:891.

UCSC

uc003jvm.3. human.

Organism-specific databases

CTD

891.

GeneCards

GC05P068462.

HGNC

HGNC:1579. CCNB1.

HPA

CAB000115.
CAB003804.

MIM

123836. gene.

neXtProt

NX_P14635.

PharmGKB

PA95.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5024.

HOGENOM

HOG000167672.

HOVERGEN

HBG061650.

InParanoid

P14635.

K05868.

OMA

RGLTKHM.

OrthoDB

EOG47WNP2.

PhylomeDB

P14635.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.
foxopathway. FoxO family signaling.

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

SignaLink

P14635.

Gene expression databases

ArrayExpress

P14635.

Bgee

P14635.

CleanEx

HS_CCNB1.

Genevestigator

P14635.

GermOnline

ENSG00000134057. Homo sapiens.

Family and domain databases

Gene3D

1.10.472.10. 2 hits.

InterPro

IPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]

Pfam

PF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001771. Cyclin_A_B_D_E. 1 hit.

SMART

SM00385. CYCLIN. 2 hits.
[Graphical view]

SUPFAM

SSF47954. Cyclin_like. 2 hits.

PROSITE

PS00292. CYCLINS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P14635.

ChEMBL

CHEMBL2412.

ChiTaRS

CCNB1. human.

EvolutionaryTrace

P14635.

GenomeRNAi

891.

NextBio

3686.

SOURCE

Search...

Entry information

Entry name

CCNB1_HUMAN

Accession

Primary (citable) accession number: P14635

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 29, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents