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RAD23 homolog A

HHR23A, Rad23A
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair (NER). This protein was shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, as well as with ubiquitin protein ligase E6AP, and thus suggests that this protein may be involved in the ubiquitin mediated proteolytic pathway in cells. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, hHR23B, XPC, V1a, CAN
Papers on HHR23A
Ovarian steroids regulate gene expression related to DNA repair and neurodegenerative diseases in serotonin neurons of macaques.
Reddy et al., Beaverton, United States. In Mol Psychiatry, Dec 2015
NBN1, PCNA (proliferating nuclear antigen), GADD45A (DNA damage-inducible), RAD23A (DNA damage recognition) and GTF2H5 (gene transcription factor 2H5) significantly increased with E or E+P treatment (all analysis of variance (ANOVA), P<0.01).
hHR23A is required to control the basal turnover of Chk1.
Chuang et al., T'ai-chung-shih, Taiwan. In Cell Signal, Nov 2015
In this study, we show that the effect of hHR23A on Chk1 protein turnover could impact the cell cycle progression observed in hHR23A-knockdown cells.
The deubiquitinase ataxin-3 requires Rad23 and DnaJ-1 for its neuroprotective role in Drosophila melanogaster.
Todi et al., Detroit, United States. In Neurobiol Dis, Oct 2015
Here, we report that ataxin-3 requires its direct interaction with the ubiquitin-binding and proteasome-associated protein, Rad23 (known as hHR23A/B in mammals) in order to suppress toxicity from polyQ species in Drosophila.
Radioprotective effects of genistein on HL-7702 cells via the inhibition of apoptosis and DNA damage.
Yan et al., Shanghai, China. In Cancer Lett, Oct 2015
In the present study, we showed that low concentration of GEN (1.5 µM) protected L-02 cells against radiation damage via inhibition of apoptosis, alleviation of DNA damage and chromosome aberration, down-regulation of GRP78 and up-regulation of HERP, HUS1 and hHR23A.
Binding Pattern Elucidation of NNK and NNAL Cigarette Smoke Carcinogens with NER Pathway Enzymes: an Onco- Informatics Study.
Haque et al., Buraydah, Saudi Arabia. In Asian Pac J Cancer Prev, 2014
It was found that carcinogens are well capable to reduce the normal functioning of genes like RAD23A (HR23A), CCNH, CDK7 and CETN2.
Identification of genes whose expression is altered by obesity throughout the arterial tree.
Laughlin et al., United States. In Physiol Genomics, 2014
We found a total of 15 genes that were consistently upregulated with obesity (MIS18A, CTRB1, FAM151B, FOLR2, PXMP4, OAS1B, SREBF2, KLRA17, SLC25A44, SNX10, SLFN3, MEF2BNB, IRF7, RAD23A, LGALS3BP) and five genes that were consistently downregulated with obesity (C2, GOLGA7, RIN3, PCP4, CYP2E1).
Human RAD23 homolog A is required for the nuclear translocation of apoptosis-inducing factor during induction of cell death.
Chow et al., Zhongxing, China. In Biol Cell, 2014
RESULTS: By using yeast two-hybrid assay, we identified the human UV excision repair protein RAD23 homolog A (hHR23A) interacts with AIF and their interaction was confirmed by co-immunoprecipitation and fluorescence resonance energy transfer microscopy.
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.
Gronenborn et al., Pittsburgh, United States. In J Biol Chem, 2014
The human homolog of the yeast DNA repair protein RAD23, hHR23A, has been found previously to interact with the human immunodeficiency virus, type 1 accessory protein Vpr.
Ubiquitin-binding site 2 of ataxin-3 prevents its proteasomal degradation by interacting with Rad23.
Todi et al., Detroit, United States. In Nat Commun, 2013
Ataxin-3 interacts with the proteasome-associated proteins Rad23A/B through UbS2.
Erythropoietic defect associated with reduced cell proliferation in mice lacking the 26S proteasome shuttling factor Rad23b.
Gutiérrez et al., Rotterdam, Netherlands. In Mol Cell Biol, 2013
Rad23a and Rad23b proteins are linked to nucleotide excision DNA repair (NER) via association with the DNA damage recognition protein xeroderma pigmentosum group C (XPC) are and known to be implicated in protein turnover by the 26S proteasome.
Mixed-linkage ubiquitin chains send mixed messages.
Fushman et al., College Park, United States. In Structure, 2013
Linkage-selective receptors from hHR23A and Rap80 preferentially bound to the K48 or K63 linkages in the branched trimer.
RAD23A negatively regulates RIG-I/MDA5 signaling through promoting TRAF2 polyubiquitination and degradation.
Wang et al., Changchun, China. In Biochem Biophys Res Commun, 2013
In this study, UbL-UBA domain containing protein RAD23A was identified as a negative regulator of RIG-I/MDA5-mediated signaling activation through a small interfering RNA (siRNA)-based screening.
Oxidative stress and DNA damage signalling in skeletal muscle in pressure-induced deep tissue injury.
Siu et al., Hong Kong, Hong Kong. In Pflugers Arch, 2013
The transcript expression of the DNA-repairing enzyme, Rad23A, was significantly suppressed in compressed muscles.
RuvBL2 is involved in histone deacetylase inhibitor PCI-24781-induced cell death in SK-N-DZ neuroblastoma cells.
Ngai et al., Hong Kong, Hong Kong. In Plos One, 2012
Western blotting confirmed the expression level of five candidate proteins including prohibitin, hHR23a, RuvBL2, TRAP1 and PDCD6IP.
The crystal structure of the ubiquitin-like (UbL) domain of human homologue A of Rad23 (hHR23A) protein.
Agrawal et al., London, United Kingdom. In Protein Eng Des Sel, 2011
Determined is the three-dimensional structure of its ubiquitin-like (UbL) domain by X-ray crystallography.
HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome.
Zhao et al., Baltimore, United States. In Plos One, 2009
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
Crystallization and preliminary X-ray diffraction studies of the ubiquitin-like (UbL) domain of the human homologue A of Rad23 (hHR23A) protein.
Garcia-Maya et al., London, United Kingdom. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009
Pyramidal crystals of the UbL domain of hHR23A were diffracted to beyond 2 A resolution and the structure was solved by molecular replacement.
The ubiquitin receptor Rad23: at the crossroads of nucleotide excision repair and proteasomal degradation.
Hoogstraten et al., Stockholm, Sweden. In Dna Repair (amst), 2009
A protein that exemplifies the intimate link between the ubiquitin/proteasome system (UPS) and DNA repair is the yeast nucleotide excision repair (NER) protein Rad23 and its human orthologs hHR23A and hHR23B.
Defining how ubiquitin receptors hHR23a and S5a bind polyubiquitin.
Walters et al., Minneapolis, United States. In J Mol Biol, 2007
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.
Ubiquitin receptor proteins hHR23a and hPLIC2 interact.
Walters et al., Minneapolis, United States. In J Mol Biol, 2007
hHR23a and hPLIC2 interact via UBL/UBA domain interactions
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