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Reviewed, UniProtKB/Swiss-Prot O95067 (CCNB2_HUMAN)

Last modified November 3, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    G2/mitotic-specific cyclin-B2
Gene names
Name: CCNB2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Essential for the control of the cell cycle at the G2/M (mitosis) transition.

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.

Developmental stage

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Sequence similarities

Belongs to the cyclin family. Cyclin AB subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Coding sequence diversityPolymorphism
   Molecular functionCyclin
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

microtubule cytoskeleton

Inferred from direct assay. Source: LIFEdb

nucleus

Inferred from electronic annotation. Source: InterPro

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398G2/mitotic-specific cyclin-B2
PRO_0000080361

Amino acid modifications

Modified residue921Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue941Phosphothreonine Ref.8
Modified residue991Phosphoserine Ref.8 Ref.9
Modified residue2041Phosphoserine Ref.8
Modified residue3921Phosphoserine Ref.8
Modified residue3981Phosphoserine Ref.8 Ref.9

Natural variations

Natural variant1001M → T: dbSNP rs16941036. Ref.5
VAR_022221
Natural variant1351V → I: dbSNP rs2306785.
VAR_053052
Natural variant3951I → T: dbSNP rs28383563. Ref.5
VAR_022222

Sequences

Sequence LengthMass (Da)Tools
O95067-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 874466E1DD68A4C4

FASTA39845,282
        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 

« Hide

References

« Hide 'large scale' references
[1]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
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"G2/mitotic-specific cyclin B2."
Saito T., Miyajima N.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIEHS SNPs program
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-100 AND THR-395.
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY.
[8]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; THR-94; SER-99; SER-204; SER-392 AND SER-398, MASS SPECTROMETRY.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-99 AND SER-398, MASS SPECTROMETRY.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

AF002822 mRNA. Translation: AAD09309.1.
AB020981 mRNA. Translation: BAA78387.1.
AL080146 mRNA. Translation: CAB45739.1.
CR533527 mRNA. Translation: CAG38558.1.
AY864066 Genomic DNA. Translation: AAW34361.1.
BC105086 mRNA. Translation: AAI05087.1.
BC105112 mRNA. Translation: AAI05113.1.
IPIIPI00028266.
PIRT12530.
RefSeqNP_004692.1.
UniGeneHs.194698

3D structure databases

HSSPHSSP built from PDB template 1H1R based on UniProtKB P20248.
ModBaseSearch...

Protein-protein interaction databases

IntActO95067. 4 interactions.
STRINGO95067.

PTM databases

PhosphoSiteO95067.

Proteomic databases

PRIDEO95067.

Genome annotation databases

EnsemblENST00000288207; ENSP00000288207; ENSG00000157456; Homo sapiens. [Genome view]
GeneID9133.
KEGGhsa:9133.
UCSCuc002afz.1. human.

Organism-specific databases

CTD9133.
GeneCardsGC15P057184.
HGNCHGNC:1580. CCNB2.
HPACAB009575.
HPA008873.
MIM602755. gene.
PharmGKBPA26148.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO95067.
HOVERGENO95067.
OMARPTVSTD.

Enzyme and pathway databases

Pathway_Interaction_DBfoxm1pathway. FOXM1 transcription factor network.
ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.

Gene expression databases

ArrayExpressO95067.
BgeeO95067.
CleanExHS_CCNB2.
GenevestigatorO95067.
GermOnlineENSG00000157456. Homo sapiens.

Family and domain databases

InterProIPR015454. CycB.
IPR006670. Cyclin.
IPR014400. Cyclin_A_B_D_E.
IPR004367. Cyclin_C.
IPR006671. Cyclin_N.
IPR013763. Cyclin_related.
[Graphical view]
Gene3DG3DSA:1.10.472.10. Cyclin_related. 1 hit.
PANTHERPTHR10177:SF27. CycB. 1 hit.
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
PROSITEPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio34245.
SOURCESearch...

Entry information

Entry nameCCNB2_HUMAN
AccessionPrimary (citable) accession number: O95067
Secondary accession number(s): Q6FI99
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents