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    TRIP12 thyroid hormone receptor interactor 12 [ Homo sapiens (human) ]

    Gene ID: 9320, updated on 7-Jul-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The neurodevelopmental and facial phenotype in individuals with a TRIP12 variant.

    The neurodevelopmental and facial phenotype in individuals with a TRIP12 variant.
    Aerden M, Denommé-Pichon AS, Bonneau D, Bruel AL, Delanne J, Gérard B, Mazel B, Philippe C, Pinson L, Prouteau C, Putoux A, Tran Mau-Them F, Viora-Dupont É, Vitobello A, Ziegler A, Piton A, Isidor B, Francannet C, Maillard PY, Julia S, Philippe A, Schaefer E, Koene S, Ruivenkamp C, Hoffer M, Legius E, Theunis M, Keren B, Buratti J, Charles P, Courtin T, Misra-Isrie M, van Haelst M, Waisfisz Q, Wieczorek D, Schmetz A, Herget T, Kortüm F, Lisfeld J, Debray FG, Bramswig NC, Atallah I, Fodstad H, Jouret G, Almoguera B, Tahsin-Swafiri S, Santos-Simarro F, Palomares-Bralo M, López-González V, Kibaek M, Tørring PM, Renieri A, Bruno LP, Õunap K, Wojcik M, Hsieh TC, Krawitz P, Van Esch H., Free PMC Article

    08/11/2023
    Analysis of Ku70 S155 Phospho-Specific BioID2 Interactome Identifies Ku Association with TRIP12 in Response to DNA Damage.

    Analysis of Ku70 S155 Phospho-Specific BioID2 Interactome Identifies Ku Association with TRIP12 in Response to DNA Damage.
    Abbasi S, Bayat L, Schild-Poulter C., Free PMC Article

    05/5/2023
    Small molecule Z363 co-regulates TAF10 and MYC via the E3 ligase TRIP12 to suppress tumour growth.

    Small molecule Z363 co-regulates TAF10 and MYC via the E3 ligase TRIP12 to suppress tumour growth.
    Xiong Y, Wang L, Xu S, Fu B, Che Y, Zaky MY, Tian R, Yao R, Guo D, Sha Z, Lin F, Lin X, Wu H., Free PMC Article

    01/21/2023
    Episignature Mapping of TRIP12 Provides Functional Insight into Clark-Baraitser Syndrome.

    Episignature Mapping of TRIP12 Provides Functional Insight into Clark-Baraitser Syndrome.
    van der Laan L, Rooney K, Alders M, Relator R, McConkey H, Kerkhof J, Levy MA, Lauffer P, Aerden M, Theunis M, Legius E, Tedder ML, Vissers LELM, Koene S, Ruivenkamp C, Hoffer MJV, Wieczorek D, Bramswig NC, Herget T, González VL, Santos-Simarro F, Tørring PM, Denomme-Pichon AS, Isidor B, Keren B, Julia S, Schaefer E, Francannet C, Maillard PY, Misra-Isrie M, Van Esch H, Mannens MMAM, Sadikovic B, van Haelst MM, Henneman P., Free PMC Article

    01/7/2023
    TRIP12 ubiquitination of glucocerebrosidase contributes to neurodegeneration in Parkinson's disease.

    TRIP12 ubiquitination of glucocerebrosidase contributes to neurodegeneration in Parkinson's disease.
    Seo BA, Kim D, Hwang H, Kim MS, Ma SX, Kwon SH, Kweon SH, Wang H, Yoo JM, Choi S, Kwon SH, Kang SU, Kam TI, Kim K, Karuppagounder SS, Kang BG, Lee S, Park H, Kim S, Yan W, Li YS, Kuo SH, Redding-Ochoa J, Pletnikova O, Troncoso JC, Lee G, Mao X, Dawson VL, Dawson TM, Ko HS., Free PMC Article

    04/16/2022
    TRIP12 has an inhibitory role in Epithelial-Mesenchymal Transition (EMT) and possibly, metastasis

    The oncogenic E3 ligase TRIP12 suppresses epithelial-mesenchymal transition (EMT) and mesenchymal traits through ZEB1/2.
    Lee KK, Rajagopalan D, Bhatia SS, Tirado-Magallanes R, Chng WJ, Jha S., Free PMC Article

    05/25/2021
    The Ubiquitin Ligase TRIP12 Limits PARP1 Trapping and Constrains PARP Inhibitor Efficiency.

    The Ubiquitin Ligase TRIP12 Limits PARP1 Trapping and Constrains PARP Inhibitor Efficiency.
    Gatti M, Imhof R, Huang Q, Baudis M, Altmeyer M., Free PMC Article

    05/8/2021
    Novel de novo TRIP12 mutation reveals variable phenotypic presentation while emphasizing core features of TRIP12 variations.

    Novel de novo TRIP12 mutation reveals variable phenotypic presentation while emphasizing core features of TRIP12 variations.
    Donoghue T, Garrity L, Ziolkowski A, McPhillips M, Buckman M, Goel H.

    05/1/2021
    Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12.

    Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12.
    Khan OM, Almagro J, Nelson JK, Horswell S, Encheva V, Keyan KS, Clurman BE, Snijders AP, Behrens A., Free PMC Article

    04/17/2021
    TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains.

    TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains.
    Kaiho-Soma A, Akizuki Y, Igarashi K, Endo A, Shoda T, Kawase Y, Demizu Y, Naito M, Saeki Y, Tanaka K, Ohtake F.

    04/17/2021
    Clark-Baraitser syndrome is associated with a nonsense alteration in the autosomal gene TRIP12.

    Clark-Baraitser syndrome is associated with a nonsense alteration in the autosomal gene TRIP12.
    Louie RJ, Friez MJ, Skinner C, Baraitser M, Clark RD, Schwartz CE, Stevenson RE.

    01/9/2021
    The E3 ubiquitin ligase TRIP12 participates in cell cycle progression and chromosome stability.

    The E3 ubiquitin ligase TRIP12 participates in cell cycle progression and chromosome stability.
    Larrieu D, Brunet M, Vargas C, Hanoun N, Ligat L, Dagnon L, Lulka H, Pommier RM, Selves J, Jády BE, Bartholin L, Cordelier P, Dufresne M, Torrisani J., Free PMC Article

    12/12/2020
    p16 overexpression led to downregulation of TRIP12, which in turn led to increased RNF168 levels, repressed DNA damage repair (DDR), increased 53BP1 foci and enhanced radioresponsiveness.

    TRIP12 as a mediator of human papillomavirus/p16-related radiation enhancement effects.
    Wang L, Zhang P, Molkentine DP, Chen C, Molkentine JM, Piao H, Raju U, Zhang J, Valdecanas DR, Tailor RC, Thames HD, Buchholz TA, Chen J, Ma L, Mason KA, Ang KK, Meyn RE, Skinner HD., Free PMC Article

    09/30/2017
    We describe the TRIP12-associated phenotype, showing that TRIP12 is a risk gene for non-syndromic intellectual disability with and without autism spectrum disorder, and that TRIP12 mutation carriers present with a broad phenotypic range within the neurodevelopmental phenotypes.

    Identification of new TRIP12 variants and detailed clinical evaluation of individuals with non-syndromic intellectual disability with or without autism.
    Bramswig NC, Lüdecke HJ, Pettersson M, Albrecht B, Bernier RA, Cremer K, Eichler EE, Falkenstein D, Gerdts J, Jansen S, Kuechler A, Kvarnung M, Lindstrand A, Nilsson D, Nordgren A, Pfundt R, Spruijt L, Surowy HM, de Vries BB, Wieland T, Engels H, Strom TM, Kleefstra T, Wieczorek D.

    07/29/2017
    nine presented pathogenic variants further document that TRIP12 haploinsufficiency causes a childhood-onset neurodevelopmental disorder

    Haploinsufficiency of the E3 ubiquitin-protein ligase gene TRIP12 causes intellectual disability with or without autism spectrum disorders, speech delay, and dysmorphic features.
    Zhang J, Gambin T, Yuan B, Szafranski P, Rosenfeld JA, Balwi MA, Alswaid A, Al-Gazali L, Shamsi AMA, Komara M, Ali BR, Roeder E, McAuley L, Roy DS, Manchester DK, Magoulas P, King LE, Hannig V, Bonneau D, Denommé-Pichon AS, Charif M, Besnard T, Bézieau S, Cogné B, Andrieux J, Zhu W, He W, Vetrini F, Ward PA, Cheung SW, Bi W, Eng CM, Lupski JR, Yang Y, Patel A, Lalani SR, Xia F, Stankiewicz P., Free PMC Article

    06/24/2017
    modulatory role for Trip12 in the USP7-dependent DNA damage response

    Trip12 is an E3 ubiquitin ligase for USP7/HAUSP involved in the DNA damage response.
    Liu X, Yang X, Li Y, Zhao S, Li C, Ma P, Mao B.

    05/13/2017
    Data indicate that E3 ubiquitin ligase thyroid hormone receptor-interacting protein 12 (TRIP12) promotes proteasomal degradation of pancreas transcription factor 1a (PTF1a)and regulates PTF1a activities.

    The E3 ubiquitin ligase thyroid hormone receptor-interacting protein 12 targets pancreas transcription factor 1a for proteasomal degradation.
    Hanoun N, Fritsch S, Gayet O, Gigoux V, Cordelier P, Dusetti N, Torrisani J, Dufresne M., Free PMC Article

    04/25/2015
    An exon3-skipping event in TRIP12 was detected in acute myeloid leukemia patients at remission

    RNA-Seq analysis identifies aberrant RNA splicing of TRIP12 in acute myeloid leukemia patients at remission.
    Gao P, Jin Z, Cheng Y, Cao X.

    01/10/2015
    HUWE1 and TRIP12 collaborate in degradation of ubiquitin-fusion proteins and misframed ubiquitin.

    HUWE1 and TRIP12 collaborate in degradation of ubiquitin-fusion proteins and misframed ubiquitin.
    Poulsen EG, Steinhauer C, Lees M, Lauridsen AM, Ellgaard L, Hartmann-Petersen R., Free PMC Article

    05/25/2013
    Study shows that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathway that ubiquitylates histones after DNA breakage.

    TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes.
    Gudjonsson T, Altmeyer M, Savic V, Toledo L, Dinant C, Grøfte M, Bartkova J, Poulsen M, Oka Y, Bekker-Jensen S, Mailand N, Neumann B, Heriche JK, Shearer R, Saunders D, Bartek J, Lukas J, Lukas C.

    11/3/2012
    data indicate that TRADD shuttles dynamically from the cytoplasm into the nucleus to modulate the interaction between p19(Arf) and its E3 ubiquitin ligase ULF, thereby promoting p19(Arf) protein stability and tumour suppression

    TRADD contributes to tumour suppression by regulating ULF-dependent p19Arf ubiquitylation.
    Chio II, Sasaki M, Ghazarian D, Moreno J, Done S, Ueda T, Inoue S, Chang YL, Chen NJ, Mak TW.

    08/18/2012
    we found somatic mutations of HERC2, HERC3, TRIP12, UBE2Q1 and UBE4B genes in gastric carcinoma and colorectal carcinomas with microsatellite instability

    Frameshift mutations of ubiquitination-related genes HERC2, HERC3, TRIP12, UBE2Q1 and UBE4B in gastric and colorectal carcinomas with microsatellite instability.
    Yoo NJ, Park SW, Lee SH.

    03/31/2012
    ULF is a bona fide E3 ligase for ARF and also suggest that ULF is an important target for activating the ARF-p53 axis in human acute myeloid leukaemia cells.

    Reactivating the ARF-p53 axis in AML cells by targeting ULF.
    Chen D, Yoon JB, Gu W., Free PMC Article

    12/16/2011
    Data show that the mechanism of BAF155-mediated stabilization of BAF57 involves blocking its ubiquitination by preventing interaction with TRIP12.

    Ubiquitin-dependent and ubiquitin-independent control of subunit stoichiometry in the SWI/SNF complex.
    Keppler BR, Archer TK., Free PMC Article

    02/26/2011
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
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