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P24385

- CCND1_HUMAN

UniProt

P24385 - CCND1_HUMAN

Protein

G1/S-specific cyclin-D1

Gene

CCND1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G1/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G1 phase. Hypophosphorylates RB1 in early G1 phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner.4 Publications

    GO - Molecular functioni

    1. cyclin-dependent protein serine/threonine kinase regulator activity Source: Ensembl
    2. enzyme binding Source: UniProtKB
    3. histone deacetylase binding Source: UniProtKB
    4. proline-rich region binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase activity Source: Ensembl
    7. protein kinase binding Source: UniProtKB
    8. transcription corepressor activity Source: UniProtKB
    9. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: Ensembl
    2. cell division Source: UniProtKB-KW
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. endoplasmic reticulum unfolded protein response Source: Ensembl
    5. fat cell differentiation Source: Ensembl
    6. G1/S transition of mitotic cell cycle Source: UniProtKB
    7. lactation Source: Ensembl
    8. Leydig cell differentiation Source: Ensembl
    9. liver development Source: Ensembl
    10. mammary gland alveolus development Source: Ensembl
    11. mammary gland epithelial cell proliferation Source: Ensembl
    12. mitotic cell cycle Source: Reactome
    13. mitotic G1 DNA damage checkpoint Source: UniProtKB
    14. negative regulation of cell cycle arrest Source: UniProtKB
    15. negative regulation of epithelial cell differentiation Source: Ensembl
    16. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    17. negative regulation of Wnt signaling pathway Source: Ensembl
    18. Notch signaling pathway Source: Reactome
    19. organ regeneration Source: Ensembl
    20. positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCL
    21. positive regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
    22. positive regulation of mammary gland epithelial cell proliferation Source: Ensembl
    23. positive regulation of protein phosphorylation Source: BHF-UCL
    24. re-entry into mitotic cell cycle Source: Ensembl
    25. response to calcium ion Source: Ensembl
    26. response to corticosterone Source: Ensembl
    27. response to drug Source: UniProtKB
    28. response to estrogen Source: Ensembl
    29. response to ethanol Source: Ensembl
    30. response to iron ion Source: Ensembl
    31. response to magnesium ion Source: Ensembl
    32. response to organonitrogen compound Source: Ensembl
    33. response to UV-A Source: BHF-UCL
    34. response to vitamin E Source: Ensembl
    35. response to X-ray Source: Ensembl
    36. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Cyclin, Repressor

    Keywords - Biological processi

    Cell cycle, Cell division, DNA damage, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_821. Cyclin D associated events in G1.
    SignaLinkiP24385.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G1/S-specific cyclin-D1
    Alternative name(s):
    B-cell lymphoma 1 protein
    Short name:
    BCL-1
    BCL-1 oncogene
    PRAD1 oncogene
    Gene namesi
    Name:CCND1
    Synonyms:BCL1, PRAD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1582. CCND1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Membrane 1 Publication
    Note: Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members.By similarity

    GO - Cellular componenti

    1. cyclin-dependent protein kinase holoenzyme complex Source: BHF-UCL
    2. cytosol Source: Reactome
    3. intracellular Source: LIFEdb
    4. membrane Source: UniProtKB-SubCell
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB
    7. tight junction Source: Ensembl
    8. transcriptional repressor complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving CCND1 may be a cause of B-lymphocytic malignancy, particularly mantle-cell lymphoma (MCL). Translocation t(11;14)(q13;q32) with immunoglobulin gene regions. Activation of CCND1 may be oncogenic by directly altering progression through the cell cycle.
    A chromosomal aberration involving CCND1 may be a cause of parathyroid adenomas. Translocation t(11;11)(q13;p15) with the parathyroid hormone (PTH) enhancer.
    Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving CCND1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi286 – 2861T → A: Reduces ubiquitination and subsequent degradation by the proteasome; when associated with A-288. Abolishes ubiquitination and subsequent degradation following DNA damage. 2 Publications
    Mutagenesisi288 – 2881T → A: Reduces ubiquitination and subsequent degradation by the proteasome; when associated with A-286. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    MIMi254500. phenotype.
    Orphaneti67038. B-cell chronic lymphocytic leukemia.
    52416. Mantle cell lymphoma.
    29073. Multiple myeloma.
    PharmGKBiPA75.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295G1/S-specific cyclin-D1PRO_0000080430Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki269 – 269Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei286 – 2861Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylation at Thr-286 by MAP kinases is required for ubiquitination and degradation following DNA damage. It probably plays an essential role for recognition by the FBXO31 component of SCF (SKP1-cullin-F-box) protein ligase complex.2 Publications
    Ubiquitinated, primarily as 'Lys-48'-linked polyubiquitination. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex containing FBXO4 and CRYAB. Following DNA damage it is ubiquitinated by some SCF (SKP1-cullin-F-box) protein ligase complex containing FBXO31. SCF-type ubiquitination is dependent on Thr-286 phosphorylation By similarity. Ubiquitinated also by UHRF2 apparently in a phosphorylation-independent manner. Ubiquitination leads to its degradation and G1 arrest. Deubiquitinated by USP2; leading to its stabilization.By similarity2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP24385.
    PaxDbiP24385.
    PRIDEiP24385.

    PTM databases

    PhosphoSiteiP24385.

    Expressioni

    Gene expression databases

    ArrayExpressiP24385.
    BgeeiP24385.
    CleanExiHS_CCND1.
    GenevestigatoriP24385.

    Organism-specific databases

    HPAiCAB000024.
    HPA027801.

    Interactioni

    Subunit structurei

    Interacts with FBXO4 By similarity. Interacts with either CDK4 or CDK6 protein kinase to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Component of the ternary complex CCND1/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase activity. Interacts directly with CDKN1B. Interacts with UHRF2; the interaction ubiquitinates CCND1 and appears to occur independently of phosphorylation. Can form similar complexes with either CDKN1A or CDKN2A. Interacts with USP2. Interacts (via cyclin N-terminal domain) with INSM1 (via N-terminal region); the interaction competes with the binding of CCND1 to CDK4 during cell cycle progression and inhibits CDK4 activity. Interacts with CDK4; the interaction is prevented with the binding of CCND1 to INSM1 during cell cycle progression.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA1P383983EBI-375001,EBI-349905
    CDK4P1180211EBI-375001,EBI-295644
    Cdk4P302852EBI-375001,EBI-847225From a different organism.
    CDK6Q005342EBI-375001,EBI-295663
    CDKN1AP389366EBI-375001,EBI-375077
    CDKN1BP465272EBI-375001,EBI-519280
    Ralbp1Q627962EBI-375001,EBI-3956409From a different organism.
    UHRF2Q96PU44EBI-375001,EBI-625304

    Protein-protein interaction databases

    BioGridi107067. 77 interactions.
    DIPiDIP-123N.
    IntActiP24385. 28 interactions.
    MINTiMINT-135422.
    STRINGi9606.ENSP00000227507.

    Structurei

    Secondary structure

    1
    295
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 113
    Helixi26 – 3712
    Helixi44 – 474
    Helixi54 – 7017
    Helixi77 – 8913
    Turni96 – 983
    Helixi99 – 11416
    Helixi121 – 1277
    Turni128 – 1303
    Helixi134 – 14714
    Turni148 – 1503
    Helixi157 – 16610
    Helixi172 – 19019
    Helixi194 – 1974
    Helixi200 – 21819
    Turni220 – 2223
    Helixi224 – 2263
    Helixi229 – 2379
    Helixi241 – 25515
    Turni256 – 2605
    Beta strandi261 – 2633

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W96X-ray2.30A1-271[»]
    2W99X-ray2.80A1-271[»]
    2W9FX-ray2.85A1-271[»]
    2W9ZX-ray2.45A16-271[»]
    ProteinModelPortaliP24385.
    SMRiP24385. Positions 22-267.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24385.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 152125Cyclin N-terminalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi272 – 2809Poly-Glu

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin D subfamily.Curated
    Contains 1 cyclin N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG5024.
    HOGENOMiHOG000008182.
    HOVERGENiHBG050837.
    InParanoidiP24385.
    KOiK04503.
    OMAiMKETVPL.
    OrthoDBiEOG7J447H.
    PhylomeDBiP24385.
    TreeFamiTF101004.

    Family and domain databases

    Gene3Di1.10.472.10. 2 hits.
    InterProiIPR013763. Cyclin-like.
    IPR014400. Cyclin_A/B/D/E/F.
    IPR004367. Cyclin_C-dom.
    IPR015451. Cyclin_D.
    IPR006671. Cyclin_N.
    [Graphical view]
    PANTHERiPTHR10177:SF67. PTHR10177:SF67. 1 hit.
    PfamiPF02984. Cyclin_C. 1 hit.
    PF00134. Cyclin_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
    SMARTiSM00385. CYCLIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.
    PROSITEiPS00292. CYCLINS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P24385-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEHQLLCCEV ETIRRAYPDA NLLNDRVLRA MLKAEETCAP SVSYFKCVQK    50
    EVLPSMRKIV ATWMLEVCEE QKCEEEVFPL AMNYLDRFLS LEPVKKSRLQ 100
    LLGATCMFVA SKMKETIPLT AEKLCIYTDN SIRPEELLQM ELLLVNKLKW 150
    NLAAMTPHDF IEHFLSKMPE AEENKQIIRK HAQTFVALCA TDVKFISNPP 200
    SMVAAGSVVA AVQGLNLRSP NNFLSYYRLT RFLSRVIKCD PDCLRACQEQ 250
    IEALLESSLR QAQQNMDPKA AEEEEEEEEE VDLACTPTDV RDVDI 295
    Length:295
    Mass (Da):33,729
    Last modified:March 1, 1992 - v1
    Checksum:i3CC00C9905F58D3A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301N → G in AAA52136. (PubMed:1827756)Curated
    Sequence conflicti168 – 1692MP → IA in M74092. (PubMed:1833066)Curated
    Sequence conflicti188 – 1881L → S in AAA52136. (PubMed:1827756)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59798 mRNA. Translation: CAA42470.1.
    M74092 mRNA. No translation available.
    M64349 mRNA. Translation: AAA52136.1.
    M73554 mRNA. Translation: AAA58392.1.
    Z23022 mRNA. Translation: CAA80558.1.
    BT019845 mRNA. Translation: AAV38648.1.
    AF511593 Genomic DNA. Translation: AAM34300.2.
    BC000076 mRNA. Translation: AAH00076.1.
    BC001501 mRNA. Translation: AAH01501.1.
    BC014078 mRNA. Translation: AAH14078.1.
    BC023620 mRNA. Translation: AAH23620.1.
    BC025302 mRNA. Translation: AAH25302.1.
    L09054 Genomic DNA. Translation: AAA36481.1.
    CCDSiCCDS8191.1.
    PIRiA38977.
    RefSeqiNP_444284.1. NM_053056.2.
    UniGeneiHs.523852.

    Genome annotation databases

    EnsembliENST00000227507; ENSP00000227507; ENSG00000110092.
    GeneIDi595.
    KEGGihsa:595.
    UCSCiuc001opa.3. human.

    Polymorphism databases

    DMDMi116152.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

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

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59798 mRNA. Translation: CAA42470.1 .
    M74092 mRNA. No translation available.
    M64349 mRNA. Translation: AAA52136.1 .
    M73554 mRNA. Translation: AAA58392.1 .
    Z23022 mRNA. Translation: CAA80558.1 .
    BT019845 mRNA. Translation: AAV38648.1 .
    AF511593 Genomic DNA. Translation: AAM34300.2 .
    BC000076 mRNA. Translation: AAH00076.1 .
    BC001501 mRNA. Translation: AAH01501.1 .
    BC014078 mRNA. Translation: AAH14078.1 .
    BC023620 mRNA. Translation: AAH23620.1 .
    BC025302 mRNA. Translation: AAH25302.1 .
    L09054 Genomic DNA. Translation: AAA36481.1 .
    CCDSi CCDS8191.1.
    PIRi A38977.
    RefSeqi NP_444284.1. NM_053056.2.
    UniGenei Hs.523852.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W96 X-ray 2.30 A 1-271 [» ]
    2W99 X-ray 2.80 A 1-271 [» ]
    2W9F X-ray 2.85 A 1-271 [» ]
    2W9Z X-ray 2.45 A 16-271 [» ]
    ProteinModelPortali P24385.
    SMRi P24385. Positions 22-267.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107067. 77 interactions.
    DIPi DIP-123N.
    IntActi P24385. 28 interactions.
    MINTi MINT-135422.
    STRINGi 9606.ENSP00000227507.

    Chemistry

    BindingDBi P24385.
    ChEMBLi CHEMBL3610.
    DrugBanki DB01169. Arsenic trioxide.

    PTM databases

    PhosphoSitei P24385.

    Polymorphism databases

    DMDMi 116152.

    Proteomic databases

    MaxQBi P24385.
    PaxDbi P24385.
    PRIDEi P24385.

    Protocols and materials databases

    DNASUi 595.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227507 ; ENSP00000227507 ; ENSG00000110092 .
    GeneIDi 595.
    KEGGi hsa:595.
    UCSCi uc001opa.3. human.

    Organism-specific databases

    CTDi 595.
    GeneCardsi GC11P069455.
    HGNCi HGNC:1582. CCND1.
    HPAi CAB000024.
    HPA027801.
    MIMi 168461. gene.
    254500. phenotype.
    neXtProti NX_P24385.
    Orphaneti 67038. B-cell chronic lymphocytic leukemia.
    52416. Mantle cell lymphoma.
    29073. Multiple myeloma.
    PharmGKBi PA75.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5024.
    HOGENOMi HOG000008182.
    HOVERGENi HBG050837.
    InParanoidi P24385.
    KOi K04503.
    OMAi MKETVPL.
    OrthoDBi EOG7J447H.
    PhylomeDBi P24385.
    TreeFami TF101004.

    Enzyme and pathway databases

    Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_821. Cyclin D associated events in G1.
    SignaLinki P24385.

    Miscellaneous databases

    ChiTaRSi CCND1. human.
    EvolutionaryTracei P24385.
    GeneWikii Cyclin_D1.
    GenomeRNAii 595.
    NextBioi 2419.
    PROi P24385.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24385.
    Bgeei P24385.
    CleanExi HS_CCND1.
    Genevestigatori P24385.

    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.
    IPR015451. Cyclin_D.
    IPR006671. Cyclin_N.
    [Graphical view ]
    PANTHERi PTHR10177:SF67. PTHR10177:SF67. 1 hit.
    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. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    PROSITEi PS00292. CYCLINS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel cyclin encoded by a bcl1-linked candidate oncogene."
      Motokura T., Bloom T., Kim H.G., Jueppner H., Ruderman J.V., Kronenberg H.M., Arnold A.
      Nature 350:512-515(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast."
      Lew D.J., Dulic V., Reed S.I.
      Cell 66:1197-1206(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Characterization of a candidate bcl-1 gene."
      Withers D.A., Harvey R.C., Faust J.B., Melnyk O., Carey K., Meeker T.C.
      Mol. Cell. Biol. 11:4846-4853(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Rearrangement of CCND1 (BCL1/PRAD1) 3' untranslated region in mantle-cell lymphomas and t(11q13)-associated leukemias."
      Rimokh R., Berger F., Bastard C., Klein B., French M., Archimbaud E., Rouault J.-P., Santa Lucia B., Duret L., Vuillaume M.
      Blood 83:3689-3696(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. NIEHS SNPs program
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [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 and Placenta.
    9. "The PRAD1/cyclin D1 proto-oncogene: genomic organization, 5' DNA sequence, and sequence of a tumor-specific rearrangement breakpoint."
      Motokura T., Arnold A.
      Genes Chromosomes Cancer 7:89-95(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
      Tissue: Placenta.
    10. "CDK6 (PLSTIRE) and CDK4 (PSK-J3) are a distinct subset of the cyclin-dependent kinases that associate with cyclin D1."
      Bates S., Bonetta L., McAllan D., Parry D., Holder A., Dickson C., Peters G.
      Oncogene 9:71-79(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDK4 AND CDK6.
    11. "Dysregulation of cyclin D1 by translocation into an IgH gamma switch region in two multiple myeloma cell lines."
      Chesi M., Bergsagel P.L., Brents L.A., Smith C.M., Gerhard D.S., Kuehl W.M.
      Blood 88:674-681(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MULTIPLE MYELOMA.
    12. Cited for: INTERACTION WITH CDK4 IN THE CCND1-CDK4-CDKN COMPLEX, SUBCELLULAR LOCATION, FUNCTION.
    13. "Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286."
      Germain D., Russell A., Thompson A., Hendley J.
      J. Biol. Chem. 275:12074-12079(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, MUTAGENESIS OF THR-286 AND THR-288.
    14. "Cyclin-dependent kinases regulate the antiproliferative function of Smads."
      Matsuura I., Denissova N.G., Wang G., He D., Long J., Liu F.
      Nature 430:226-231(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF CCND1-CDK4 COMPLEX IN SMAD PHOSPHORYLATION.
    15. "INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene through the recruitment of cyclin D1 and histone deacetylases."
      Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.
      Biochem. J. 397:169-177(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH INSM1.
    16. "Identification of an INSM1-binding site in the insulin promoter: negative regulation of the insulin gene transcription."
      Wang H.W., Muguira M., Liu W.D., Zhang T., Chen C., Aucoin R., Breslin M.B., Lan M.S.
      J. Endocrinol. 198:29-39(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH INSM1.
    17. "Zinc finger transcription factor INSM1 interrupts cyclin D1 and CDK4 binding and induces cell cycle arrest."
      Zhang T., Liu W.D., Saunee N.A., Breslin M.B., Lan M.S.
      J. Biol. Chem. 284:5574-5581(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INSM1 AND CDK4.
    18. "Suppression of cancer cell growth by promoting cyclin D1 degradation."
      Shan J., Zhao W., Gu W.
      Mol. Cell 36:469-476(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP2, UBIQUITINATION, DEUBIQUITINATION BY USP2.
    19. "F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage."
      Santra M.K., Wajapeyee N., Green M.R.
      Nature 459:722-725(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-286, UBIQUITINATION, MUTAGENESIS OF THR-286.
    20. "NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor."
      Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.
      Cell Cycle 10:3284-3299(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH UHRF2.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-271 IN COMPLEX WITH WILD TYPE AND MUTANTS ALA-172; PHE-172 AND ASP-172 CDK4.

    Entry informationi

    Entry nameiCCND1_HUMAN
    AccessioniPrimary (citable) accession number: P24385
    Secondary accession number(s): Q6LEF0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 163 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 11
      Human chromosome 11: 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