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O95067

- CCNB2_HUMAN

UniProt

O95067 - CCNB2_HUMAN

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
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. protein binding Source: IntAct

    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

    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

    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

    ArrayExpressiO95067.
    BgeeiO95067.
    CleanExiHS_CCNB2.
    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. 12 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.
    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

    MALLRRPTVS SDLENIDTGV NSKVKSHVTI RRTVLEEIGN RVTTRAAQVA    50
    KKAQNTKVPV QPTKTTNVNK QLKPTASVKP VQMEKLAPKG PSPTPEDVSM 100
    KEENLCQAFS DALLCKIEDI DNEDWENPQL CSDYVKDIYQ YLRQLEVLQS 150
    INPHFLDGRD INGRMRAILV DWLVQVHSKF RLLQETLYMC VGIMDRFLQV 200
    QPVSRKKLQL VGITALLLAS KYEEMFSPNI EDFVYITDNA YTSSQIREME 250
    TLILKELKFE LGRPLPLHFL RRASKAGEVD VEQHTLAKYL MELTLIDYDM 300
    VHYHPSKVAA AASCLSQKVL GQGKWNLKQQ YYTGYTENEV LEVMQHMAKN 350
    VVKVNENLTK FIAIKNKYAS SKLLKISMIP QLNSKAVKDL ASPLIGRS 398
    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. 12 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.
    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

    ArrayExpressi O95067.
    Bgeei O95067.
    CleanExi HS_CCNB2.
    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

    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 1, 2014
    This is version 126 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