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Protein

G2/mitotic-specific cyclin-B2

Gene

CCNB2

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.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_150260. Condensation of Prometaphase Chromosomes.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_160122. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_1846. G2/M DNA replication checkpoint.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_2101. Cyclin B2 mediated events.
SignaLinkiO95067.

Names & Taxonomyi

Protein namesi
Recommended name:
G2/mitotic-specific cyclin-B2
Gene namesi
Name:CCNB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:1580. CCNB2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytosol Source: Reactome
  • membrane Source: Ensembl
  • microtubule cytoskeleton Source: LIFEdb
  • nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26148.

Polymorphism and mutation databases

BioMutaiCCNB2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398G2/mitotic-specific cyclin-B2PRO_0000080361Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei92 – 921Phosphoserine2 Publications
Modified residuei94 – 941Phosphothreonine1 Publication
Modified residuei99 – 991Phosphoserine2 Publications
Modified residuei392 – 3921Phosphoserine1 Publication
Modified residuei398 – 3981Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95067.
PaxDbiO95067.
PRIDEiO95067.

PTM databases

PhosphoSiteiO95067.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Gene expression databases

BgeeiO95067.
CleanExiHS_CCNB2.
ExpressionAtlasiO95067. baseline and differential.
GenevisibleiO95067. HS.

Organism-specific databases

HPAiCAB009575.
HPA008873.

Interactioni

Subunit structurei

Interacts with the CDK1 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.

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK2P249412EBI-375024,EBI-375096
FLNAP213338EBI-375024,EBI-350432

Protein-protein interaction databases

BioGridi114581. 16 interactions.
DIPiDIP-31730N.
IntActiO95067. 19 interactions.
MINTiMINT-1201520.
STRINGi9606.ENSP00000288207.

Structurei

3D structure databases

ProteinModelPortaliO95067.
SMRiO95067. Positions 131-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiO95067.
KOiK05868.
OMAiAPSAQNF.
OrthoDBiEOG7ZGX3C.
PhylomeDBiO95067.
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.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95067-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLRRPTVS SDLENIDTGV NSKVKSHVTI RRTVLEEIGN RVTTRAAQVA
60 70 80 90 100
KKAQNTKVPV QPTKTTNVNK QLKPTASVKP VQMEKLAPKG PSPTPEDVSM
110 120 130 140 150
KEENLCQAFS DALLCKIEDI DNEDWENPQL CSDYVKDIYQ YLRQLEVLQS
160 170 180 190 200
INPHFLDGRD INGRMRAILV DWLVQVHSKF RLLQETLYMC VGIMDRFLQV
210 220 230 240 250
QPVSRKKLQL VGITALLLAS KYEEMFSPNI EDFVYITDNA YTSSQIREME
260 270 280 290 300
TLILKELKFE LGRPLPLHFL RRASKAGEVD VEQHTLAKYL MELTLIDYDM
310 320 330 340 350
VHYHPSKVAA AASCLSQKVL GQGKWNLKQQ YYTGYTENEV LEVMQHMAKN
360 370 380 390
VVKVNENLTK FIAIKNKYAS SKLLKISMIP QLNSKAVKDL ASPLIGRS
Length:398
Mass (Da):45,282
Last modified:May 1, 1999 - v1
Checksum:i874466E1DD68A4C4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001M → T.1 Publication
Corresponds to variant rs16941036 [ dbSNP | Ensembl ].
VAR_022221
Natural varianti135 – 1351V → I.
Corresponds to variant rs2306785 [ dbSNP | Ensembl ].
VAR_053052
Natural varianti395 – 3951I → T.1 Publication
Corresponds to variant rs28383563 [ dbSNP | Ensembl ].
VAR_022222

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK001404 mRNA. Translation: BAG50905.1.
CH471082 Genomic DNA. Translation: EAW77563.1.
BC105086 mRNA. Translation: AAI05087.1.
BC105112 mRNA. Translation: AAI05113.1.
CCDSiCCDS10170.1.
PIRiT12530.
RefSeqiNP_004692.1. NM_004701.3.
UniGeneiHs.194698.

Genome annotation databases

EnsembliENST00000288207; ENSP00000288207; ENSG00000157456.
GeneIDi9133.
KEGGihsa:9133.
UCSCiuc002afz.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK001404 mRNA. Translation: BAG50905.1.
CH471082 Genomic DNA. Translation: EAW77563.1.
BC105086 mRNA. Translation: AAI05087.1.
BC105112 mRNA. Translation: AAI05113.1.
CCDSiCCDS10170.1.
PIRiT12530.
RefSeqiNP_004692.1. NM_004701.3.
UniGeneiHs.194698.

3D structure databases

ProteinModelPortaliO95067.
SMRiO95067. Positions 131-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114581. 16 interactions.
DIPiDIP-31730N.
IntActiO95067. 19 interactions.
MINTiMINT-1201520.
STRINGi9606.ENSP00000288207.

Chemistry

BindingDBiO95067.
ChEMBLiCHEMBL2094127.

PTM databases

PhosphoSiteiO95067.

Polymorphism and mutation databases

BioMutaiCCNB2.

Proteomic databases

MaxQBiO95067.
PaxDbiO95067.
PRIDEiO95067.

Protocols and materials databases

DNASUi9133.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288207; ENSP00000288207; ENSG00000157456.
GeneIDi9133.
KEGGihsa:9133.
UCSCiuc002afz.3. human.

Organism-specific databases

CTDi9133.
GeneCardsiGC15P059397.
HGNCiHGNC:1580. CCNB2.
HPAiCAB009575.
HPA008873.
MIMi602755. gene.
neXtProtiNX_O95067.
PharmGKBiPA26148.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiO95067.
KOiK05868.
OMAiAPSAQNF.
OrthoDBiEOG7ZGX3C.
PhylomeDBiO95067.
TreeFamiTF101001.

Enzyme and pathway databases

ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_150260. Condensation of Prometaphase Chromosomes.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_160122. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_1846. G2/M DNA replication checkpoint.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_2101. Cyclin B2 mediated events.
SignaLinkiO95067.

Miscellaneous databases

GeneWikiiCyclin_B2.
GenomeRNAii9133.
NextBioi34245.
PROiO95067.
SOURCEiSearch...

Gene expression databases

BgeeiO95067.
CleanExiHS_CCNB2.
ExpressionAtlasiO95067. baseline and differential.
GenevisibleiO95067. 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.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Brain.
  9. "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 SER-99; SER-392 AND SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; THR-94; SER-99 AND SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCCNB2_HUMAN
AccessioniPrimary (citable) accession number: O95067
Secondary accession number(s): B3KM93, Q6FI99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1999
Last modified: July 22, 2015
This is version 134 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.