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    CCNDBP1 cyclin D1 binding protein 1 [ Homo sapiens (human) ]

    Gene ID: 23582, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    rs66651343 and rs12909095 confer lung cancer risk by regulating CCNDBP1 expression.

    rs66651343 and rs12909095 confer lung cancer risk by regulating CCNDBP1 expression.
    Shi Q, Ruan J, Yang YC, Shi XQ, Liu SD, Wang HY, Zhang SJ, Wang SQ, Zhong L, Sun C., Free PMC Article

    04/19/2023
    Grap2 cyclin D interacting protein negatively regulates CREBbinding protein, inhibiting fibroblastlike synoviocyte growth.

    Grap2 cyclin D interacting protein negatively regulates CREB‑binding protein, inhibiting fibroblast‑like synoviocyte growth.
    Fujita H, Aratani S, Nakajima T.

    05/15/2021
    MEK2 is a critical modulating mechanism to down-regulate GCIP stability and function in cancer cells.

    MEK2 is a critical modulating mechanism to down-regulate GCIP stability and function in cancer cells.
    Liang RY, Liu BH, Huang CJ, Lin KT, Ko CC, Huang LL, Hsu B, Wu CY, Chuang SM.

    10/3/2020
    Data suggest MAID/CCNDBP1 inhibits cell migration induced by TGFB1 (transforming growth factor-beta1) but not by BMP4 (bone morphogenetic protein-4); MAID does not alter cell proliferation, epithelial-mesenchymal transition, or TGFB3-induced apoptosis.

    Maid is a negative regulator of transforming growth factor-β-induced cell migration.
    Motizuki M, Saitoh M, Miyazawa K.

    07/30/2016
    GCIP underexpression is associated with Osteosarcoma.

    miR-9 Modulates Osteosarcoma Cell Growth by Targeting the GCIP Tumor Suppressor.
    Zhu SW, Li JP, Ma XL, Ma JX, Yang Y, Chen Y, Liu W.

    03/26/2016
    Data indicate that grap2 and cyclin D1 interacting protein (GCIP) and inhibitor of of DNA binding/differentiation 1 (Id1) are inversely expressed in non-small cell lung cancer (NSCLC) cell lines and specimens.

    GCIP functions as a tumor suppressor in non-small cell lung cancer by suppressing Id1-mediated tumor promotion.
    Chen KY, Chen CC, Tseng YL, Chang YC, Chang MC., Free PMC Article

    05/16/2015
    The first structure of a free-standing human dominant-negative helix-loop-helix protein (DIP1) was reported. DIP1 adopts a V-shaped conformation, with N-terminal and C-terminal five-helix bundles connected by the HLH region.

    Structure of a dominant-negative helix-loop-helix transcriptional regulator suggests mechanisms of autoinhibition.
    Ishii R, Isogaya K, Seto A, Koinuma D, Watanabe Y, Arisaka F, Yaguchi S, Ikushima H, Dohmae N, Miyazono K, Miyazawa K, Ishitani R, Nureki O., Free PMC Article

    08/18/2012
    It is proposed for the first time that Rad may promote carcinogenesis at least in part by inhibiting GCIP-mediated tumor suppression.

    A novel senescence-evasion mechanism involving Grap2 and Cyclin D interacting protein inactivation by Ras associated with diabetes in cancer cells under doxorubicin treatment.
    Lee I, Yeom SY, Lee SJ, Kang WK, Park C.

    06/28/2010
    Crystallization and preliminary X-ray diffraction analysis of GCIP/HHM transcriptional regulator

    Crystallization and preliminary X-ray diffraction analysis of GCIP/HHM transcriptional regulator.
    Seto A, Ikushima H, Suzuki T, Sato Y, Fukai S, Yuki K, Miyazawa K, Miyazono K, Ishitani R, Nureki O., Free PMC Article

    01/21/2010
    decreased expression of GCIP in vivo is present in human breast carcinoma.

    Immunohistochemical expression of GCIP in breast carcinoma: relationship with tumour grade, disease-free survival, mucinous differentiation and response to chemotherapy.
    Chen WC, Su PF, Jin YT, Chang MC, Chang TW.

    01/21/2010
    Data suggest that HHM/Maid regulates a subset of TGF-beta target genes including the Olig1-Smad synexpression group.

    An Id-like molecule, HHM, is a synexpression group-restricted regulator of TGF-beta signalling.
    Ikushima H, Komuro A, Isogaya K, Shinozaki M, Hellman U, Miyazawa K, Miyazono K., Free PMC Article

    01/21/2010
    CT847 interacts with mammalian Grap2 cyclin D-interacting protein

    Human GCIP interacts with CT847, a novel Chlamydia trachomatis type III secretion substrate, and is degraded in a tissue-culture infection model.
    Chellas-Géry B, Linton CN, Fields KA.

    01/21/2010
    P0 overexpression may cause tumorigenesis in breast and liver tissues at least in part by inhibiting GCIP-mediated tumor suppression.

    Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of P0 is associated with cellular proliferation in breast and liver carcinoma cells.
    Chang TW, Chen CC, Chen KY, Su JH, Chang JH, Chang MC.

    01/21/2010
    In transgenic mice, GCIP functions as a transcriptional suppressor, regulates cyclin D1 expression, inhibits cell growth and colony formation in human HepG2 cells, suggesting GCIP plays a significant role in tumor initiation and development.

    Expression of GCIP in transgenic mice decreases susceptibility to chemical hepatocarcinogenesis.
    Ma W, Xia X, Stafford LJ, Yu C, Wang F, LeSage G, Liu M.

    01/21/2010
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