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    RBM14 RNA binding motif protein 14 [ Homo sapiens (human) ]

    Gene ID: 10432, updated on 19-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    O-GlcNAcylation of RBM14 contributes to elevated cellular O-GlcNAc through regulation of OGA protein stability.

    O-GlcNAcylation of RBM14 contributes to elevated cellular O-GlcNAc through regulation of OGA protein stability.
    Kweon TH, Jung H, Ko JY, Kang J, Kim W, Kim Y, Kim HB, Yi EC, Ku NO, Cho JW, Yang WH.

    06/14/2024
    NONO promotes gallbladder cancer cell proliferation by enhancing oncogenic RNA splicing of DLG1 through interaction with IGF2BP3/RBM14.

    NONO promotes gallbladder cancer cell proliferation by enhancing oncogenic RNA splicing of DLG1 through interaction with IGF2BP3/RBM14.
    Yang ZY, Zhao C, Liu SL, Pan LJ, Zhu YD, Zhao JW, Wang HK, Ye YY, Qiang J, Shi LQ, Mei JW, Xie Y, Gong W, Shu YJ, Dong P, Xiang SS.

    03/26/2024
    The RNA-binding motif protein 14 regulates telomere integrity at the interface of TERRA and telomeric R-loops.

    The RNA-binding motif protein 14 regulates telomere integrity at the interface of TERRA and telomeric R-loops.
    Wang Y, Zhu W, Jang Y, Sommers JA, Yi G, Puligilla C, Croteau DL, Yang Y, Kai M, Liu Y., Free PMC Article

    12/20/2023
    RNA-binding protein 14 promotes phase separation to sustain prostate specific antigen expression under androgen deprivation in human prostate cancer.

    RNA-binding protein 14 promotes phase separation to sustain prostate specific antigen expression under androgen deprivation in human prostate cancer.
    Tsuji K, Kawata H, Kamiakito T, Nakaya T, Tanaka A.

    12/6/2023
    RBM14 as a novel epigenetic-activated tumor oncogene is implicated in the reprogramming of glycolysis in lung cancer.

    RBM14 as a novel epigenetic-activated tumor oncogene is implicated in the reprogramming of glycolysis in lung cancer.
    Hu Y, Mu H, Deng Z., Free PMC Article

    04/19/2023
    METTL3 promotes m6A hypermethylation of RBM14 via YTHDF1 leading to the progression of hepatocellular carcinoma.

    METTL3 promotes m6A hypermethylation of RBM14 via YTHDF1 leading to the progression of hepatocellular carcinoma.
    Hu J, Yang L, Peng X, Mao M, Liu X, Song J, Li H, Chen F.

    10/8/2022
    canonical nonhomologous end joining pathway utilizes damage-induced transcription and intrinsically disordered protein RBM14 for efficient repair of double-strand breaks.

    Intrinsically disordered protein RBM14 plays a role in generation of RNA:DNA hybrids at double-strand break sites.
    Jang Y, Elsayed Z, Eki R, He S, Du KP, Abbas T, Kai M., Free PMC Article

    07/18/2020
    The influenza A virus NS1 protein is both necessary and sufficient for RBM14 relocalization, and relocalization also requires the double-stranded RNA (dsRNA) binding capacity of NS1.

    Nucleolar Relocalization of RBM14 by Influenza A Virus NS1 Protein.
    Beyleveld G, Chin DJ, Moreno Del Olmo E, Carter J, Najera I, Cillóniz C, Shaw ML., Free PMC Article

    02/2/2019
    RBM14 plays crucial role in regulation of non-homologous end joining upon DNA damage.

    RNA-binding protein RBM14 regulates dissociation and association of non-homologous end joining proteins.
    Simon NE, Yuan M, Kai M., Free PMC Article

    04/14/2018
    RBM14 connects key paraspeckle subcomplexes via interactions mediated by its prion-like domain.

    Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles.
    Hennig S, Kong G, Mannen T, Sadowska A, Kobelke S, Blythe A, Knott GJ, Iyer KS, Ho D, Newcombe EA, Hosoki K, Goshima N, Kawaguchi T, Hatters D, Trinkle-Mulcahy L, Hirose T, Bond CS, Fox AH., Free PMC Article

    11/7/2015
    This study identifies a cellular protein named RBM14 that is associated with XPO1 (CRM1), a nuclear protein that binds to the HIV-1 Rev protein and mediates nuclear export of incompletely spliced HIV-1 viral RNAs

    Mining the human complexome database identifies RBM14 as an XPO1-associated protein involved in HIV-1 Rev function.
    Budhiraja S, Liu H, Couturier J, Malovannaya A, Qin J, Lewis DE, Rice AP., Free PMC Article

    05/23/2015
    upon RBM14 depletion, a part of the ectopic centriolar protein complexes in turn assemble into structures more akin to centrioles, presumably by incorporating HsSAS-6, a cartwheel component, and cause multipolar spindle formation.

    RBM14 prevents assembly of centriolar protein complexes and maintains mitotic spindle integrity.
    Shiratsuchi G, Takaoka K, Ashikawa T, Hamada H, Kitagawa D., Free PMC Article

    03/21/2015
    RBM14 promotes radio-resistance in glioblastoma by regulating DNA repair and cell differentiation.

    RNA binding protein RBM14 promotes radio-resistance in glioblastoma by regulating DNA repair and cell differentiation.
    Yuan M, Eberhart CG, Kai M., Free PMC Article

    02/21/2015
    CoAA is involved in the migration-enhancing action of PEA3 on MCF7 metastatic human cancer cells.

    The coactivator activator CoAA regulates PEA3 group member transcriptional activity.
    Verreman K, Baert JL, Verger A, Drobecq H, Ferreira E, de Launoit Y, Monte D.

    11/26/2011
    CoAA binds Runx2 and prevents Runx2 binding to DNA; CoAA is expressed at high levels in human fetal osteoblasts and osteosarcoma cell lines

    Co-activator activator (CoAA) prevents the transcriptional activity of Runt domain transcription factors.
    Li X, Hoeppner LH, Jensen ED, Gopalakrishnan R, Westendorf JJ., Free PMC Article

    01/21/2010
    The alternative splicing imbalance of CoAA and RBM4, because of loss of their common enhancer in cancer, may deregulate stem/progenitor cell differentiation

    Functional pre- mRNA trans-splicing of coactivator CoAA and corepressor RBM4 during stem/progenitor cell differentiation.
    Brooks YS, Wang G, Yang Z, Smith KK, Bieberich E, Ko L., Free PMC Article

    01/21/2010
    The CoAA gene is amplified in human cancers

    Gene amplification and associated loss of 5' regulatory sequences of CoAA in human cancers.
    Sui Y, Yang Z, Xiong S, Zhang L, Blanchard KL, Peiper SC, Dynan WS, Tuan D, Ko L., Free PMC Article

    01/21/2010
    CoAA regulates transcription-coupled alternative splicing.

    CoAA, a nuclear receptor coactivator protein at the interface of transcriptional coactivation and RNA splicing.
    Auboeuf D, Dowhan DH, Li X, Larkin K, Ko L, Berget SM, O'Malley BW., Free PMC Article

    04/14/2009
    Cloning of the coactivator CoAA gene.

    Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM).
    Iwasaki T, Chin WW, Ko L.

    04/14/2009
    The switched alternative splicing of CoAA regulates stem cell differentiation.

    Switched alternative splicing of oncogene CoAA during embryonal carcinoma stem cell differentiation.
    Yang Z, Sui Y, Xiong S, Liour SS, Phillips AC, Ko L., Free PMC Article

    04/14/2009
    CoAA is a potential tumor suppressor in renal carcinoma and CoAM is a counterbalancing splice isoform.

    Dual roles for coactivator activator and its counterbalancing isoform coactivator modulator in human kidney cell tumorigenesis.
    Kang YK, Schiff R, Ko L, Wang T, Tsai SY, Tsai MJ, O'Malley BW., Free PMC Article

    01/21/2010
    SYT interacts with SYT-interacting protein/co-activator activator

    The proto-oncoprotein SYT interacts with SYT-interacting protein/co-activator activator (SIP/CoAA), a human nuclear receptor co-activator with similarity to EWS and TLS/FUS family of proteins.
    Perani M, Antonson P, Hamoudi R, Ingram CJ, Cooper CS, Garrett MD, Goodwin GH.

    01/21/2010
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