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    RAD23A RAD23 homolog A, nucleotide excision repair protein [ Homo sapiens (human) ]

    Gene ID: 5886, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A.

    Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A.
    Byeon IL, Calero G, Wu Y, Byeon CH, Jung J, DeLucia M, Zhou X, Weiss S, Ahn J, Hao C, Skowronski J, Gronenborn AM., Free PMC Article

    01/1/2022
    Kinetic Constraints in the Specific Interaction between Phosphorylated Ubiquitin and Proteasomal Shuttle Factors.

    Kinetic Constraints in the Specific Interaction between Phosphorylated Ubiquitin and Proteasomal Shuttle Factors.
    Qin LY, Gong Z, Liu K, Dong X, Tang C., Free PMC Article

    09/25/2021
    Histone H4K20 Demethylation by Two hHR23 Proteins.

    Histone H4K20 Demethylation by Two hHR23 Proteins.
    Cao X, Chen Y, Wu B, Wang X, Xue H, Yu L, Li J, Wang Y, Wang W, Xu Q, Mao H, Peng C, Han G, Chen CD.

    04/13/2021
    The HR23A-knockdown cells appear to undergo epithelial-mesenchymal transition and take on certain attributes of cancer stemness.

    HR23A-knockdown lung cancer cells exhibit epithelial-to-mesenchymal transition and gain stemness properties through increased Twist1 stability.
    Yu CY, Liu BH, Tang SY, Liang RY, Hsu KH, Chuang SM.

    03/21/2020
    Data indicate that HR23A protein-depleted cells exhibit enhanced autophagy when treated with DNA-damaging agents.

    Human Rad23A plays a regulatory role in autophagy.
    Tan X, Wang HC, Liang RY, Chuang SM.

    06/24/2017
    HR23A role in DNA reapair, in protein degradation and stability, tumorigenesis and neurodegenerative disorders [review]

    Two mammalian homologs of yeast Rad23, HR23A and HR23B, as multifunctional proteins.
    Yokoi M, Hanaoka F.

    02/4/2017
    hHR23A associates with Chk1 through its ubiquitin-associated domains, and knockdown of hHR23A increases and stabilizes the protein level of Chk1 and its phosphorylation at S347.

    hHR23A is required to control the basal turnover of Chk1.
    Tan X, Liang RY, Chuang SM.

    07/2/2016
    Data indicate that phosphorylation provides a mechanism to regulate Rad23/proteasome interaction.

    Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain.
    Liang RY, Chen L, Ko BT, Shen YH, Li YT, Chen BR, Lin KT, Madura K, Chuang SM., Free PMC Article

    04/25/2015
    Here, we show that hHR23A utilizes both the UBA2 and XPCB domains to form a stable complex with Vpr, linking Vpr directly to cellular DNA repair pathways and their probable exploitation by the virus.

    Binding of HIV-1 Vpr protein to the human homolog of the yeast DNA repair protein RAD23 (hHR23A) requires its xeroderma pigmentosum complementation group C binding (XPCB) domain as well as the ubiquitin-associated 2 (UBA2) domain.
    Jung J, Byeon IJ, DeLucia M, Koharudin LM, Ahn J, Gronenborn AM., Free PMC Article

    04/12/2014
    this study identified RAD23A as a novel negative regulator of RIG-I/MDA5 mediated anti-virus response.

    RAD23A negatively regulates RIG-I/MDA5 signaling through promoting TRAF2 polyubiquitination and degradation.
    Fang DF, He K, Wang J, Mu R, Tan B, Jian Z, Li HY, Song W, Chang Y, Gong WL, Li WH, Wang GJ.

    05/11/2013
    Determined is the three-dimensional structure of its ubiquitin-like (UbL) domain by X-ray crystallography.

    The crystal structure of the ubiquitin-like (UbL) domain of human homologue A of Rad23 (hHR23A) protein.
    Chen YW, Tajima T, Agrawal S.

    04/9/2011
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    Vpr promotes hHR23A-mediated protein-ubiquitination, and down-regulation of hHR23A using RNAi significantly reduced viral replication in non-proliferating MAGI-CCR5 cells and primary macrophages

    HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome.
    Li G, Elder RT, Dubrovsky L, Liang D, Pushkarsky T, Chiu K, Fan T, Sire J, Bukrinsky M, Zhao RY., Free PMC Article

    09/6/2010
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (2) articles

    Variation within DNA repair pathway genes and risk of multiple sclerosis.
    Briggs FB, Goldstein BA, McCauley JL, Zuvich RL, De Jager PL, Rioux JD, Ivinson AJ, Compston A, Hafler DA, Hauser SL, Oksenberg JR, Sawcer SJ, Pericak-Vance MA, Haines JL, Barcellos LF, International Multiple Sclerosis Genetics Consortium.

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium.

    06/30/2010
    Observational study of gene-disease association and gene-gene interaction. (HuGE Navigator)

    Comprehensive screen of genetic variation in DNA repair pathway genes and postmenopausal breast cancer risk.
    Monsees GM, Kraft P, Chanock SJ, Hunter DJ, Han J., Free PMC Article

    06/30/2010
    Pyramidal crystals of the UbL domain of hHR23A were diffracted to beyond 2 A resolution and the structure was solved by molecular replacement.

    Crystallization and preliminary X-ray diffraction studies of the ubiquitin-like (UbL) domain of the human homologue A of Rad23 (hHR23A) protein.
    Chen YW, Tajima T, Rees M, Garcia-Maya M., Free PMC Article

    01/21/2010
    Observational study of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Patterns of persistent DNA damage associated with sun exposure and the glutathione S-transferase M1 genotype in melanoma patients.
    Steinberg ML, Hubbard K, Utti C, Clas B, Hwang BJ, Hill HZ, Orlow I., Free PMC Article

    02/11/2009
    UIM2 domain of S5a binds preferentially to hHR23a over polyubiquitin, and a model is provided for the ternary complex that represents one of the mechanisms used by the proteasome to capture ubiquitylated substrates.

    Defining how ubiquitin receptors hHR23a and S5a bind polyubiquitin.
    Kang Y, Chen X, Lary JW, Cole JL, Walters KJ., Free PMC Article

    01/21/2010
    involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination

    Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination.
    Elder RT, Song XQ, Chen M, Hopkins KM, Lieberman HB, Zhao Y., Free PMC Article

    01/21/2010
    Adopts a closed conformation and binds to the proteasomal subunit S5a thereby changing its own conformation.

    DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a.
    Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM., Free PMC Article

    01/21/2010
    Ufd4, the E3 component of the UFD pathway, is involved in controlling the degradation of Rad4, and Ufd4 and Rad23 exhibit a synthetic inhibitory effect on Rad4 degradation

    A synthetic defect in protein degradation caused by loss of Ufd4 and Rad23.
    Ju D, Xie Y.

    01/21/2010
    the solution structures of the HHR23A Ubl domain

    Structural determinants for the binding of ubiquitin-like domains to the proteasome.
    Mueller TD, Feigon J., Free PMC Article

    01/21/2010
    Data suggest that the UBL domain of HHR23A negatively regulates polyubiquitin/UBA interactions and identify leucine 8 of ubiquitin as an important determinant of chain recognition.

    Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A.
    Raasi S, Orlov I, Fleming KG, Pickart CM.

    01/21/2010
    hHR23A regulates the function of xeroderma pigmentosum C by its association with the nucleotide excision repair activator p53

    HHR23A, a human homolog of Saccharomyces cerevisiae Rad23, regulates xeroderma pigmentosum C protein and is required for nucleotide excision repair.
    Hsieh HC, Hsieh YH, Huang YH, Shen FC, Tsai HN, Tsai JH, Lai YT, Wang YT, Chuang WJ, Huang W.

    01/21/2010
    hHR23B thus plays a critical role in the activation and function of p53 after specific genotoxic exposures.

    hHR23B is required for genotoxic-specific activation of p53 and apoptosis.
    Kaur M, Pop M, Shi D, Brignone C, Grossman SR., Free PMC Article

    01/21/2010
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