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    RAD17 RAD17 checkpoint clamp loader component [ Homo sapiens (human) ]

    Gene ID: 5884, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Identification of RAD17 as a candidate cancer predisposition gene in families with histories of pancreatic and breast cancers.

    Identification of RAD17 as a candidate cancer predisposition gene in families with histories of pancreatic and breast cancers.
    Joris S, Giron P, Olsen C, Seneca S, Gheldof A, Staessens S, Shahi RB, De Brakeleer S, Teugels E, De Grève J, Hes FJ., Free PMC Article

    06/26/2024
    The C-terminal tail of Rad17, iVERGE, binds the 9-1-1 complex independently of AAA+ ATPase domains to provide another clamp-loader interface.

    The C-terminal tail of Rad17, iVERGE, binds the 9‒1‒1 complex independently of AAA+ ATPase domains to provide another clamp-loader interface.
    Fukumoto Y, Hoshino T, Nakayama Y, Ogra Y.

    09/28/2023
    The Cell Cycle Checkpoint Gene, RAD17 rs1045051, Is Associated with Prostate Cancer Risk.

    The Cell Cycle Checkpoint Gene, RAD17 rs1045051, Is Associated with Prostate Cancer Risk.
    Sun J, Lin W, Wang Q, Sakai A, Xue R, Watanabe M, Liu C, Sadahira T, Nasu Y, Xu A, Huang P.

    01/8/2022
    Nuclear translocation promotes proteasomal degradation of human Rad17 protein through the N-terminal destruction boxes.

    Nuclear translocation promotes proteasomal degradation of human Rad17 protein through the N-terminal destruction boxes.
    Fukumoto Y, Ikeuchi M, Qu L, Hoshino T, Yamaguchi N, Nakayama Y, Ogra Y., Free PMC Article

    12/4/2021
    IQGAP3 interacts with Rad17 to recruit the Mre11-Rad50-Nbs1 complex and contributes to radioresistance in lung cancer.

    IQGAP3 interacts with Rad17 to recruit the Mre11-Rad50-Nbs1 complex and contributes to radioresistance in lung cancer.
    Zeng Y, Jie X, Wu B, Wu G, Liu L, Xu S.

    03/28/2021
    The noncoding function of NELFA mRNA promotes the development of oesophageal squamous cell carcinoma by regulating the Rad17-RFC2-5 complex.

    The noncoding function of NELFA mRNA promotes the development of oesophageal squamous cell carcinoma by regulating the Rad17-RFC2-5 complex.
    Xu J, Wang G, Gong W, Guo S, Li D, Zhan Q., Free PMC Article

    02/6/2021
    Human Rad17 is constitutively phosphorylated in vivo on a C-terminal threonine, T670. Rad17-T670 is phosphorylated by casein kinase 1delta/epsilon.

    Human Rad17 C-terminal tail is phosphorylated by concerted action of CK1δ/ε and CK2 to promote interaction with the 9-1-1 complex.
    Fukumoto Y, Nakayama Y, Yamaguchi N.

    06/13/2020
    The potential G-quadruplex sequence (PQS) of the RAD17 gene promoter was analyzed in different sequence contexts. With two extra nucleotides of the native sequence on either side of the G4, the structure was found to fold into a hybrid-like G4, similar to the hybrid-1 fold that the human telomere sequence can adopt.

    The RAD17 Promoter Sequence Contains a Potential Tail-Dependent G-Quadruplex That Downregulates Gene Expression upon Oxidative Modification.
    Zhu J, Fleming AM, Burrows CJ., Free PMC Article

    04/6/2019
    Rad17-S667 in the C-terminal tail is constitutively phosphorylated in vivo in a casein kinase 2-dependent manner, and the phosphorylation is important for 9-1-1 interaction

    Casein kinase 2 promotes interaction between Rad17 and the 9-1-1 complex through constitutive phosphorylation of the C-terminal tail of human Rad17.
    Fukumoto Y, Takahashi K, Suzuki N, Ogra Y, Nakayama Y, Yamaguchi N.

    03/30/2019
    DDX11 orchestrates jointly with 9-1-1 and its loader, RAD17, DNA damage tolerance at sites of bulky lesions, and endogenous abasic sites. These functions may explain the essential roles of DDX11 and its similarity with 9-1-1 during development.

    Warsaw breakage syndrome DDX11 helicase acts jointly with RAD17 in the repair of bulky lesions and replication through abasic sites.
    Abe T, Ooka M, Kawasumi R, Miyata K, Takata M, Hirota K, Branzei D., Free PMC Article

    09/22/2018
    The Rad17 C-terminal tail is a molecular switch that regulates the 9-1-1 interaction and the ATR pathway.

    The polyanionic C-terminal tail of human Rad17 regulates interaction with the 9-1-1 complex.
    Fukumoto Y, Nakayama Y, Yamaguchi N.

    09/23/2017
    These data indicate that the interaction with the 9-1-1 complex is not required for Rad17 protein to be an efficient substrate for the UV-induced phosphorylation. Our data also raise the possibility that the 9-1-1 complex plays a negative regulatory role in the Rad17 phosphorylation. We also show that the nucleotide-binding activity of Rad17 is required for its nuclear localization.

    The KYxxL motif in Rad17 protein is essential for the interaction with the 9-1-1 complex.
    Fukumoto Y, Ikeuchi M, Nakayama Y, Yamaguchi N.

    05/20/2017
    In a Japanese population, the variant allele of hRAD17 is significantly associated with a decreased risk of Colorectal Cancer among light smokers and rectal cancer patients and with an increased risk of Colorectal Cancer among heavy smokers.

    Human RAD 17 Polymorphism at Codon 546 Is Associated with the Risk of Colorectal Cancer.
    Yasuda Y, Sakai A, Ito S, Sasai K, Yamamoto H, Matsubara N, Ouchida M, Katayama H, Shimizu K.

    03/25/2017
    Authors show that BRCA1 and RAD17 genes, whose derived proteins play a pivotal role in DNA damage repair, are transcriptional targets of gain-of-function mutant p53 proteins.

    Gain of function mutant p53 proteins cooperate with E2F4 to transcriptionally downregulate RAD17 and BRCA1 gene expression.
    Valenti F, Ganci F, Fontemaggi G, Sacconi A, Strano S, Blandino G, Di Agostino S., Free PMC Article

    03/5/2016
    USP20 and Rad17 interact, and that this interaction is enhanced by UV exposure. We show that USP20 regulation of Rad17 is at the protein level in a proteasome-dependent manner. USP20 depletion results in poor activation of Chk1 protein by phosphorylation

    Ubiquitin-specific peptidase 20 regulates Rad17 stability, checkpoint kinase 1 phosphorylation and DNA repair by homologous recombination.
    Shanmugam I, Abbas M, Ayoub F, Mirabal S, Bsaili M, Caulder EK, Weinstock DM, Tomkinson AE, Hromas R, Shaheen M., Free PMC Article

    12/20/2014
    These data suggest that v-Src attenuates ATR-Chk1 signaling through the inhibition of Rad17-Rad9 interaction.

    v-Src inhibits the interaction between Rad17 and Rad9 and induces replication fork collapse.
    Fukumoto Y, Miura T, Morii M, Kubota S, Honda T, Kubota S, Morinaga T, Yamaguchi N, Nakayama Y, Yamaguchi N.

    09/27/2014
    Rad17 is phosphorylated by ATM at Thr622 resulting in a direct interaction of Rad17 with NBS1, facilitating recruitment of MRE11, RAD50 and ATM to the DNA double-strand breaks.

    Rad17 recruits the MRE11-RAD50-NBS1 complex to regulate the cellular response to DNA double-strand breaks.
    Wang Q, Goldstein M, Alexander P, Wakeman TP, Sun T, Feng J, Lou Z, Kastan MB, Wang XF., Free PMC Article

    06/7/2014
    Our data suggest RAD17 as a novel target protein for gemcitabine combination therapy supplementing or complementing inhibition of CHK1.

    Depletion of RAD17 sensitizes pancreatic cancer cells to gemcitabine.
    Fredebohm J, Wolf J, Hoheisel JD, Boettcher M.

    05/24/2014
    Knockdown of Rad17 with two independent siRNAs significantly reduced Chk1 phosphorylation and substantial RPA32 Ser33 phosphorylation.

    Two distinct modes of ATR activation orchestrated by Rad17 and Nbs1.
    Shiotani B, Nguyen HD, Håkansson P, Maréchal A, Tse A, Tahara H, Zou L., Free PMC Article

    12/21/2013
    Data indicate that regulation of Rad17 turnover is through the Cdh1/anaphase-promoting complex pathway in breast cancer cells.

    Regulation of Rad17 protein turnover unveils an impact of Rad17-APC cascade in breast carcinogenesis and treatment.
    Zhou Z, Jing C, Zhang L, Takeo F, Kim H, Huang Y, Liu Z, Wan Y., Free PMC Article

    09/7/2013
    Rad9, Rad17, TopBP1 and claspin play essential roles in heat-induced activation of ATR kinase and heat tolerance.

    Rad9, Rad17, TopBP1 and claspin play essential roles in heat-induced activation of ATR kinase and heat tolerance.
    Tuul M, Kitao H, Iimori M, Matsuoka K, Kiyonari S, Saeki H, Oki E, Morita M, Maehara Y., Free PMC Article

    07/20/2013
    Proteolysis of Rad17 by Cdh1/APC regulates checkpoint termination and recovery from genotoxic stress

    Proteolysis of Rad17 by Cdh1/APC regulates checkpoint termination and recovery from genotoxic stress.
    Zhang L, Park CH, Wu J, Kim H, Liu W, Fujita T, Balasubramani M, Schreiber EM, Wang XF, Wan Y., Free PMC Article

    06/28/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Evaluating new candidate SNPs as low penetrance risk factors in sporadic breast cancer: a two-stage Spanish case-control study.
    Vega A, Salas A, Milne RL, Carracedo B, Ribas G, Ruibal A, de León AC, González-Hernández A, Benítez J, Carracedo A.

    11/5/2008
    hRAD17 delayed growth of NIH3T3 fibroblasts transformed by the H-ras oncogene in nude mice.

    The human homolog of fission yeast Rad17 is implicated in tumor growth.
    Beretta GL, Gatti L, Cesare MD, Corna E, Tinelli S, Carenini N, Zunino F, Perego P.

    01/21/2010
    Loss of hRAD17 expression occurs frequently in HNSCC, is often due to genomic deletion, and may facilitate genomic instability in HNSCC

    Downregulation of RAD17 in head and neck cancer.
    Zhao M, Begum S, Ha PK, Westra W, Califano J.

    01/21/2010
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