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O95067

- CCNB2_HUMAN

UniProt

O95067 - CCNB2_HUMAN

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Protein

G2/mitotic-specific cyclin-B2

Gene

CCNB2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. G2/M transition of mitotic cell cycle Source: Reactome
  2. growth Source: Ensembl
  3. in utero embryonic development Source: Ensembl
  4. mitotic cell cycle Source: Reactome
  5. mitotic nuclear division Source: UniProtKB-KW
  6. mitotic nuclear envelope disassembly Source: Reactome
  7. regulation of cell cycle Source: Reactome
  8. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  9. T cell homeostasis Source: Ensembl
  10. thymus development Source: Ensembl
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: Chromosome 15

Organism-specific databases

HGNCiHGNC:1580. CCNB2.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytosol Source: Reactome
  3. membrane Source: Ensembl
  4. microtubule cytoskeleton Source: LIFEdb
  5. nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26148.

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.
GenevestigatoriO95067.

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. 15 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.
OMAiVETIRIR.
OrthoDBiEOG7ZGX3C.
PhylomeDBiO95067.
TreeFamiTF101001.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10170.1.
PIRi T12530.
RefSeqi NP_004692.1. NM_004701.3.
UniGenei Hs.194698.

3D structure databases

ProteinModelPortali O95067.
SMRi O95067. Positions 131-390.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114581. 15 interactions.
DIPi DIP-31730N.
IntActi O95067. 19 interactions.
MINTi MINT-1201520.
STRINGi 9606.ENSP00000288207.

Chemistry

BindingDBi O95067.
ChEMBLi CHEMBL2094127.

PTM databases

PhosphoSitei O95067.

Proteomic databases

MaxQBi O95067.
PaxDbi O95067.
PRIDEi O95067.

Protocols and materials databases

DNASUi 9133.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000288207 ; ENSP00000288207 ; ENSG00000157456 .
GeneIDi 9133.
KEGGi hsa:9133.
UCSCi uc002afz.3. human.

Organism-specific databases

CTDi 9133.
GeneCardsi GC15P059397.
HGNCi HGNC:1580. CCNB2.
HPAi CAB009575.
HPA008873.
MIMi 602755. gene.
neXtProti NX_O95067.
PharmGKBi PA26148.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5024.
GeneTreei ENSGT00760000118939.
HOGENOMi HOG000167672.
HOVERGENi HBG061650.
InParanoidi O95067.
KOi K05868.
OMAi VETIRIR.
OrthoDBi EOG7ZGX3C.
PhylomeDBi O95067.
TreeFami TF101001.

Enzyme and pathway databases

Reactomei REACT_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.
SignaLinki O95067.

Miscellaneous databases

GeneWikii Cyclin_B2.
GenomeRNAii 9133.
NextBioi 34245.
PROi O95067.
SOURCEi Search...

Gene expression databases

Bgeei O95067.
CleanExi HS_CCNB2.
ExpressionAtlasi O95067. baseline and differential.
Genevestigatori O95067.

Family and domain databases

Gene3Di 1.10.472.10. 2 hits.
InterProi IPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view ]
Pfami PF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTi SM00385. CYCLIN. 2 hits.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 2 hits.
PROSITEi PS00292. CYCLINS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 127 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