[1]	NUCLEOTIDE SEQUENCE [MRNA]. Kim D.G., Choi S.S., Kang Y.S., Lee K.H., Kim U.-J., Shin H.-S.; Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA]. Saito T., Miyajima N.; "G2/mitotic-specific cyclin B2."; Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan] Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.; "Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."; Genome Res. 11:422-435(2001).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-100 AND THR-395. NIEHS SNPs program; Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; THR-94; SER-99; SER-204; SER-392 AND SER-398, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan] Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.; "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."; Mol. Cell 31:438-448(2008).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-99 AND SER-398, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).

Comments

FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
SUBUNIT: 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.
INTERACTION:
P24941:CDK2; NbExp=1; IntAct=EBI-375024, EBI-375096;
P38936:CDKN1A; NbExp=1; IntAct=EBI-375024, EBI-375077;
P49736:MCM2; NbExp=1; IntAct=EBI-375024, EBI-374819;
DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly destroyed at mitosis.
SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ccnb2/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF002822; AAD09309.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020981; BAA78387.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL080146; CAB45739.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR533527; CAG38558.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY864066; AAW34361.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105086; AAI05087.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105112; AAI05113.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T12530; T12530.

NP_004692.1; -.

3D structure databases

HSSP

P20248; 1H1R. [HSSP ENTRY / PDB]

ModBase

O95067.

Protein-protein interaction databases

IntAct

O95067; 4.

PTM databases

PhosphoSite

O95067; -.

Enzyme and pathway databases

Reactome

REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.

Organism-specific databases

GC15P057184; -.

HGNC:1580; CCNB2.

CAB009575; -.
HPA008873; -.

MIM

602755; gene. [NCBI / EBI]

PharmGKB

PA26148; -.

GeneCards

O95067.

Gene expression databases

ArrayExpress

O95067; -.

CleanEx

HS_CCNB2; -.

GermOnline

ENSG00000157456; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0015630;	Cellular component: microtubule cytoskeleton (inferred from direct assay from LIFEdb).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0007067;	Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR015454; CycB.
IPR006670; Cyclin.
IPR014400; Cyclin_A_B_D_E.
IPR004367; Cyclin_C.
IPR006671; Cyclin_N.
IPR013763; Cyclin_related.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.472.10; Cyclin_related; 1.

PANTHER

PTHR10177:SF27; CycB; 1.

Pfam

PF02984; Cyclin_C; 1.
PF00134; Cyclin_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001771; Cyclin_A_B_D_E; 1.

SMART

SM00385; CYCLIN; 2.
SMART graphical view of domain structure.

PROSITE

PS00292; CYCLINS; 1.

Proteomics databases

PRIDE

O95067; -.

Genome annotation databases

Ensembl

ENSG00000157456; Homo sapiens. [Contig view]

GeneID

9133; -.

KEGG

hsa:9133; -.

Phylogenomic databases

HOGENOM

O95067; -.

HOVERGEN

O95067; -.

Other

O95067; -.

34245; -.

CCNB2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell cycle; Cell division; Cyclin; Mitosis; Phosphoprotein; Polymorphism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 398`	`398`	`G2/mitotic-specific cyclin-B2.`	`PRO_0000080361`
`MOD_RES`	`92 92`		`Phosphoserine.`
`MOD_RES`	`94 94`		`Phosphothreonine.`
`MOD_RES`	`99 99`		`Phosphoserine.`
`MOD_RES`	`204 204`		`Phosphoserine.`
`MOD_RES`	`392 392`		`Phosphoserine.`
`MOD_RES`	`398 398`		`Phosphoserine.`
`VARIANT`	`100 100`	`1`	`M -> T (in dbSNP:rs16941036 [NCBI]).`	`VAR_022221`
`VARIANT`	`135 135`	`1`	`V -> I (in dbSNP:rs2306785 [NCBI]).`	`VAR_053052`
`VARIANT`	`395 395`	`1`	`I -> T (in dbSNP:rs28383563 [NCBI]).`	`VAR_022222`

Sequence information

Length: 398 AA [This is the length of the unprocessed precursor]

Molecular weight: 45282 Da [This is the MW of the unprocessed precursor]

CRC64: 874466E1DD68A4C4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALLRRPTVS SDLENIDTGV NSKVKSHVTI RRTVLEEIGN RVTTRAAQVA KKAQNTKVPV 

        70         80         90        100        110        120 
QPTKTTNVNK QLKPTASVKP VQMEKLAPKG PSPTPEDVSM KEENLCQAFS DALLCKIEDI 

       130        140        150        160        170        180 
DNEDWENPQL CSDYVKDIYQ YLRQLEVLQS INPHFLDGRD INGRMRAILV DWLVQVHSKF 

       190        200        210        220        230        240 
RLLQETLYMC VGIMDRFLQV QPVSRKKLQL VGITALLLAS KYEEMFSPNI EDFVYITDNA 

       250        260        270        280        290        300 
YTSSQIREME TLILKELKFE LGRPLPLHFL RRASKAGEVD VEQHTLAKYL MELTLIDYDM 

       310        320        330        340        350        360 
VHYHPSKVAA AASCLSQKVL GQGKWNLKQQ YYTGYTENEV LEVMQHMAKN VVKVNENLTK 

       370        380        390 
FIAIKNKYAS SKLLKISMIP QLNSKAVKDL ASPLIGRS

O95067 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools