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P14635

- CCNB1_HUMAN

UniProt

P14635 - CCNB1_HUMAN

Protein

G2/mitotic-specific cyclin-B1

Gene

CCNB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Essential for the control of the cell cycle at the G2/M (mitosis) transition.2 Publications

    GO - Molecular functioni

    1. kinase activity Source: Ensembl
    2. patched binding Source: BHF-UCL
    3. protein binding Source: IntAct
    4. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cellular response to fatty acid Source: Ensembl
    3. cellular response to hypoxia Source: Ensembl
    4. cellular response to iron(III) ion Source: Ensembl
    5. cellular response to organic cyclic compound Source: Ensembl
    6. digestive tract development Source: Ensembl
    7. G1/S transition of mitotic cell cycle Source: Reactome
    8. G2/M transition of mitotic cell cycle Source: Reactome
    9. in utero embryonic development Source: Ensembl
    10. mitotic cell cycle Source: Reactome
    11. mitotic metaphase plate congression Source: BHF-UCL
    12. mitotic nuclear envelope disassembly Source: Reactome
    13. mitotic spindle checkpoint Source: BHF-UCL
    14. mitotic spindle stabilization Source: BHF-UCL
    15. negative regulation of gene expression Source: Ensembl
    16. negative regulation of protein phosphorylation Source: Ensembl
    17. oocyte maturation Source: Ensembl
    18. positive regulation of attachment of spindle microtubules to kinetochore Source: BHF-UCL
    19. positive regulation of cardiac muscle cell proliferation Source: Ensembl
    20. positive regulation of histone phosphorylation Source: Ensembl
    21. positive regulation of mitotic cell cycle Source: BHF-UCL
    22. positive regulation of mRNA 3'-end processing Source: Ensembl
    23. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    24. protein complex assembly Source: Ensembl
    25. protein phosphorylation Source: Ensembl
    26. regulation of cell cycle Source: Reactome
    27. regulation of chromosome condensation Source: Ensembl
    28. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
    29. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    30. response to DDT Source: Ensembl
    31. response to drug Source: Ensembl
    32. response to mechanical stimulus Source: Ensembl
    33. spermatogenesis Source: Ensembl
    34. tissue regeneration Source: Ensembl
    35. ventricular cardiac muscle cell 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_1321. E2F-enabled inhibition of pre-replication complex formation.
    REACT_150182. MASTL Facilitates Mitotic Progression.
    REACT_150260. Condensation of Prometaphase Chromosomes.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    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_172744. Condensation of Prophase Chromosomes.
    REACT_1846. G2/M DNA replication checkpoint.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_200828. Depolymerisation of the Nuclear Lamina.
    REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6875. Phosphorylation of Emi1.
    REACT_6904. Phosphorylation of the APC/C.
    SignaLinkiP14635.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G2/mitotic-specific cyclin-B1
    Gene namesi
    Name:CCNB1
    Synonyms:CCNB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1579. CCNB1.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. condensed nuclear chromosome outer kinetochore Source: BHF-UCL
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Reactome
    5. membrane Source: Ensembl
    6. nucleoplasm Source: Reactome
    7. nucleus Source: BHF-UCL
    8. spindle pole Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi133 – 1331S → A: Strongly impairs phosphorylation by PLK1. 2 Publications
    Mutagenesisi147 – 1471S → A: Does not affect phosphorylation by PLK1. 1 Publication

    Organism-specific databases

    PharmGKBiPA95.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 433433G2/mitotic-specific cyclin-B1PRO_0000080350Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei73 – 731N6-acetyllysine1 Publication
    Modified residuei126 – 1261Phosphoserine; by CDK12 Publications
    Modified residuei128 – 1281Phosphoserine1 Publication
    Modified residuei133 – 1331Phosphoserine; by PLK12 Publications
    Modified residuei147 – 1471Phosphoserine2 Publications
    Modified residuei321 – 3211Phosphothreonine1 Publication

    Post-translational modificationi

    Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases.1 Publication
    Phosphorylated by PLK1 at Ser-133 on centrosomes during prophase: phosphorylation by PLK1 does not cause nuclear import. Phosphorylation at Ser-147 was also reported to be mediated by PLK1 but Ser-133 seems to be the primary phosphorylation site.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP14635.
    PaxDbiP14635.
    PRIDEiP14635.

    PTM databases

    PhosphoSiteiP14635.

    Expressioni

    Developmental stagei

    Accumulates steadily during G2 and is abruptly destroyed at mitosis.1 Publication

    Gene expression databases

    ArrayExpressiP14635.
    BgeeiP14635.
    CleanExiHS_CCNB1.
    GenevestigatoriP14635.

    Organism-specific databases

    HPAiCAB000115.
    CAB003804.
    HPA030741.

    Interactioni

    Subunit structurei

    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. Binds HEI10. Interacts with catalytically active RALBP1 and CDC2 during mitosis to form an endocytotic complex during interphase. Interacts with CCNF; interaction is required for nuclear localization.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCNB1IP1Q9NPC32EBI-495332,EBI-745269
    CDK1P064936EBI-495332,EBI-444308
    FOXO1Q127782EBI-495332,EBI-1108782
    PKMYT1Q996404EBI-495332,EBI-495308
    UBE2KP610862EBI-495332,EBI-473850
    UHRF2Q96PU42EBI-495332,EBI-625304

    Protein-protein interaction databases

    BioGridi107332. 86 interactions.
    DIPiDIP-59N.
    IntActiP14635. 24 interactions.
    MINTiMINT-1202632.
    STRINGi9606.ENSP00000256442.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni173 – 1775
    Helixi178 – 1836
    Turni189 – 1924
    Beta strandi193 – 1975
    Helixi199 – 21517
    Helixi220 – 23415
    Helixi241 – 2433
    Helixi244 – 25916
    Helixi266 – 2727
    Beta strandi275 – 2773
    Helixi279 – 29214
    Helixi302 – 31110
    Helixi317 – 32913
    Helixi330 – 3323
    Helixi334 – 3363
    Beta strandi337 – 3393
    Helixi343 – 35614
    Helixi365 – 3684
    Turni375 – 3784
    Helixi379 – 38911
    Helixi399 – 4035
    Helixi407 – 4093
    Helixi412 – 4143
    Helixi420 – 4223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B9RX-ray2.90A/B165-433[»]
    2JGZX-ray2.90B167-426[»]
    DisProtiDP00223.
    ProteinModelPortaliP14635.
    SMRiP14635. Positions 167-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14635.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni169 – 1779Interaction with CDK2
    Regioni258 – 2614Interaction with CDK2

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi51 – 8535Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin AB subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5024.
    HOGENOMiHOG000167672.
    HOVERGENiHBG061650.
    InParanoidiP14635.
    KOiK05868.
    OMAiHMTVKNK.
    OrthoDBiEOG7ZGX3C.
    PhylomeDBiP14635.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P14635-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN    50
    KVSEQLQAKM PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE 100
    PEPEPEPEPV KEEKLSPEPI LVDTASPSPM ETSGCAPAEE DLCQAFSDVI 150
    LAVNDVDAED GADPNLCSEY VKDIYAYLRQ LEEEQAVRPK YLLGREVTGN 200
    MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP KKMLQLVGVT 250
    AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP 300
    LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC 350
    LALKILDNGE WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV 400
    KNKYATSKHA KISTLPQLNS ALVQDLAKAV AKV 433
    Length:433
    Mass (Da):48,337
    Last modified:April 1, 1990 - v1
    Checksum:iE2C4767AE8A11EC0
    GO
    Isoform 2 (identifier: P14635-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         362-398: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:396
    Mass (Da):44,102
    Checksum:i1B7AFCE21614F6D5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081E → G in BAF82120. (PubMed:14702039)Curated
    Sequence conflicti153 – 1531V → A in BAF82120. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei362 – 39837Missing in isoform 2. 1 PublicationVSP_053892Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25753 mRNA. No translation available.
    AY338491 Genomic DNA. Translation: AAP88038.1.
    AK289431 mRNA. Translation: BAF82120.1.
    BT020128 mRNA. Translation: AAV38930.1.
    AC010273 Genomic DNA. No translation available.
    AC022107 Genomic DNA. No translation available.
    BC006510 mRNA. Translation: AAH06510.1.
    CCDSiCCDS3997.1. [P14635-1]
    PIRiA32992.
    RefSeqiNP_114172.1. NM_031966.3. [P14635-1]
    UniGeneiHs.23960.

    Genome annotation databases

    EnsembliENST00000256442; ENSP00000256442; ENSG00000134057. [P14635-1]
    ENST00000505500; ENSP00000424588; ENSG00000134057. [P14635-2]
    GeneIDi891.
    KEGGihsa:891.
    UCSCiuc003jvm.3. human. [P14635-1]

    Polymorphism databases

    DMDMi116176.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25753 mRNA. No translation available.
    AY338491 Genomic DNA. Translation: AAP88038.1 .
    AK289431 mRNA. Translation: BAF82120.1 .
    BT020128 mRNA. Translation: AAV38930.1 .
    AC010273 Genomic DNA. No translation available.
    AC022107 Genomic DNA. No translation available.
    BC006510 mRNA. Translation: AAH06510.1 .
    CCDSi CCDS3997.1. [P14635-1 ]
    PIRi A32992.
    RefSeqi NP_114172.1. NM_031966.3. [P14635-1 ]
    UniGenei Hs.23960.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B9R X-ray 2.90 A/B 165-433 [» ]
    2JGZ X-ray 2.90 B 167-426 [» ]
    DisProti DP00223.
    ProteinModelPortali P14635.
    SMRi P14635. Positions 167-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107332. 86 interactions.
    DIPi DIP-59N.
    IntActi P14635. 24 interactions.
    MINTi MINT-1202632.
    STRINGi 9606.ENSP00000256442.

    Chemistry

    BindingDBi P14635.
    ChEMBLi CHEMBL1907602.

    PTM databases

    PhosphoSitei P14635.

    Polymorphism databases

    DMDMi 116176.

    Proteomic databases

    MaxQBi P14635.
    PaxDbi P14635.
    PRIDEi P14635.

    Protocols and materials databases

    DNASUi 891.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256442 ; ENSP00000256442 ; ENSG00000134057 . [P14635-1 ]
    ENST00000505500 ; ENSP00000424588 ; ENSG00000134057 . [P14635-2 ]
    GeneIDi 891.
    KEGGi hsa:891.
    UCSCi uc003jvm.3. human. [P14635-1 ]

    Organism-specific databases

    CTDi 891.
    GeneCardsi GC05P068462.
    HGNCi HGNC:1579. CCNB1.
    HPAi CAB000115.
    CAB003804.
    HPA030741.
    MIMi 123836. gene.
    neXtProti NX_P14635.
    PharmGKBi PA95.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5024.
    HOGENOMi HOG000167672.
    HOVERGENi HBG061650.
    InParanoidi P14635.
    KOi K05868.
    OMAi HMTVKNK.
    OrthoDBi EOG7ZGX3C.
    PhylomeDBi P14635.
    TreeFami TF101001.

    Enzyme and pathway databases

    Reactomei REACT_1006. Polo-like kinase mediated events.
    REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
    REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
    REACT_150182. MASTL Facilitates Mitotic Progression.
    REACT_150260. Condensation of Prometaphase Chromosomes.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    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_172744. Condensation of Prophase Chromosomes.
    REACT_1846. G2/M DNA replication checkpoint.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_200828. Depolymerisation of the Nuclear Lamina.
    REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6875. Phosphorylation of Emi1.
    REACT_6904. Phosphorylation of the APC/C.
    SignaLinki P14635.

    Miscellaneous databases

    ChiTaRSi CCNB1. human.
    EvolutionaryTracei P14635.
    GeneWikii Cyclin_B1.
    GenomeRNAii 891.
    NextBioi 35463711.
    PROi P14635.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14635.
    Bgeei P14635.
    CleanExi HS_CCNB1.
    Genevestigatori P14635.

    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. "Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2."
      Pines J., Hunter T.
      Cell 58:833-846(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, SUBUNIT.
    2. NIEHS SNPs program
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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] (ISOFORM 1).
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    7. "Structure and growth-dependent regulation of the human cyclin B1 promoter."
      Piaggio G., Farina A., Perrotti D., Manni I., Fuschi P., Sacchi A., Gaetano C.
      Exp. Cell Res. 216:396-402(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
    8. "Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-cyclin interaction."
      Kong M., Barnes E.A., Ollendorff V., Donoghue D.J.
      EMBO J. 19:1378-1388(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CCNF.
    9. "Cooperative phosphorylation including the activity of polo-like kinase 1 regulates the subcellular localization of cyclin B1."
      Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E., Kaufmann M., Strebhardt K.
      Oncogene 21:8282-8292(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-128; SER-133 AND SER-147, MUTAGENESIS OF SER-133.
    10. "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
      Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
      J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RALBP1.
    11. "A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels."
      Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.
      Mol. Cell. Biol. 23:2109-2122(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEI10.
    12. "Active cyclin B1-Cdk1 first appears on centrosomes in prophase."
      Jackman M., Lindon C., Nigg E.A., Pines J.
      Nat. Cell Biol. 5:143-148(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-133 AND SER-147, MUTAGENESIS OF SER-133 AND SER-147.
    13. "NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry."
      Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H., Morris S.W., Peschel C., Duyster J.
      Cell 122:45-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    14. "p21-mediated nuclear retention of cyclin B1-Cdk1 in response to genotoxic stress."
      Baus Charrier-Savournin F., Chateau M.-T., Gire V., Sedivy J., Piette J., Dulic V.
      Mol. Biol. Cell 15:3965-3976(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "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 THR-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Cyclin B and cyclin A confer different substrate recognition properties on CDK2."
      Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.
      Cell Cycle 6:1350-1359(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 167-426 IN COMPLEX WITH PHOSPHORYLATED CDK2, FUNCTION.
    19. "The crystal structure of human cyclin B."
      Petri E.T., Errico A., Escobedo L., Hunt T., Basavappa R.
      Cell Cycle 6:1342-1349(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 165-433, FUNCTION.

    Entry informationi

    Entry nameiCCNB1_HUMAN
    AccessioniPrimary (citable) accession number: P14635
    Secondary accession number(s): A8K066, Q5TZP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 153 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3