Affinage

RAD23A

Lysine-specific demethylase RAD23A · UniProt P54725

Length
363 aa
Mass
39.6 kDa
Annotated
2026-06-10
38 papers in source corpus 27 papers cited in narrative 27 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RAD23A (HHR23A) is a modular ubiquitin-shuttle factor that links the ubiquitin-proteasome system to nucleotide excision repair (NER) and to the regulated turnover of diverse substrates (PMID:15064742, PMID:9164480). Its architecture comprises an N-terminal UBL domain, two UBA domains, and an XPC-binding (XPCB) domain joined by flexible linkers; in the resting state intramolecular UBL–UBA contacts hold the protein in a closed conformation that is opened upon engagement of the proteasomal subunit S5a, which the UBL domain binds directly (PMID:14557549, PMID:21047872). The UBA domains recognize K48-linked polyubiquitin chains through hydrophobic surfaces, with affinity rising as a function of chain length and the UBL domain acting as an autoinhibitory regulator of chain binding (PMID:14621999, PMID:15321727). Through these modules RAD23A delivers ubiquitinated cargo to the 26S proteasome and protects or routes specific clients: it inhibits proteasomal degradation of ubiquitinated p53 in opposition to MDM2 (PMID:15064742), engages and promotes the turnover of Chk1 via its UBA domains (PMID:26296656), and shuttles TDP-43 to the proteasome such that its loss reduces TDP-43 aggregation (PMID:41371952). Substrate selection depends on cargo fold, RAD23A/B preferentially handling well-folded ubiquitinated substrates while unstructured-tailed substrates bypass it (PMID:40795920). In NER, RAD23A interacts with XPC at a conserved C-terminal region required for repair function and contributes to UV survival non-redundantly with RAD23B (PMID:9164480, PMID:21676658). Beyond proteostasis and repair, RAD23A negatively regulates RIG-I/MDA5 innate immune signaling by promoting TRAF2 polyubiquitination and degradation (PMID:23357418). RAD23A is itself a regulated target: it is ubiquitinated and degraded during S phase by E6AP/UBE3A, a degradation inhibited by UV damage (PMID:10373495), and it is co-opted by HIV-1 Vpr, which clamps the XPCB and UBA2 domains on opposite faces of its helical bundle to bridge Vpr to the 26S proteasome and support viral replication (PMID:24318982, PMID:34824204, PMID:20614012).

Mechanistic history

Synthesis pass · year-by-year structured walk · 9 steps
  1. 1997 Medium

    Establishing RAD23A's physical partners defined its two principal cellular contexts: it binds XPC at a conserved C-terminal region required for NER, and it is hijacked by HIV-1 Vpr through a discrete C-terminal region, linking the protein to both DNA repair and viral cell-cycle manipulation.

    Evidence Yeast two-hybrid, domain mapping, complementation assay, and recombinant binding with overexpression rescue

    PMID:9164480 PMID:9371639

    Open questions at the time
    • No structural model of the XPC or Vpr interface at this stage
    • Functional contribution of RAD23A versus RAD23B not separated
  2. 1999 High

    Identifying RAD23A as a substrate of E6AP that is degraded specifically in S phase, with UV damage blocking its turnover, showed the protein is itself a regulated node coupling its abundance to cell-cycle and DNA-damage state.

    Evidence In vitro ubiquitination, co-IP, dominant-negative E6AP, and cell-cycle synchronization

    PMID:10373495

    Open questions at the time
    • Functional consequence of S-phase RAD23A loss not defined
    • Substrates stabilized by RAD23A degradation not yet identified
  3. 2003 High

    NMR analysis resolved how the modular protein operates: a closed UBL–UBA conformation is opened by S5a, and the UBA domains read K48-linked ubiquitin via hydrophobic surfaces, explaining how RAD23A toggles between autoinhibited and proteasome-engaged states.

    Evidence NMR spectroscopy, residual dipolar coupling, chemical-shift perturbation, and ternary complex assays

    PMID:14557549 PMID:14621999

    Open questions at the time
    • Conformational dynamics in the context of intact cargo delivery not measured
    • Kinetics of the closed-to-open transition unresolved
  4. 2004 High

    Quantifying polyubiquitin recognition and dissecting the UBL autoinhibition, alongside the discovery that RAD23A protects ubiquitinated p53 against MDM2-driven degradation, established RAD23A as a chain-length-tuned receptor that can both deliver and protect ubiquitinated substrates.

    Evidence Surface plasmon resonance with chain-length panels and domain mutants; siRNA, in vitro degradation, and co-IP for p53/MDM2

    PMID:15064742 PMID:15321727 PMID:15322280

    Open questions at the time
    • Molecular switch between protective and delivery modes not defined
    • XPCB hydrophobic-patch function predicted but not experimentally validated
  5. 2006 Medium

    Distinguishing RAD23A from RAD23B at the proteasome (via Thr79) and mapping its interaction with the ubiquitin receptor hPLIC2 refined how paralog-specific contacts and a network of ubiquitin receptors organize shuttling.

    Evidence Site-directed mutagenesis, co-purification, NMR surface mapping, and co-IP with proteasome inhibition

    PMID:16712842 PMID:17098253

    Open questions at the time
    • Functional consequence of differential proteasome binding in vivo unclear
    • Stoichiometry of RAD23A/hPLIC2 complexes unknown
  6. 2011 Medium

    Long-term silencing showed RAD23A contributes to NER and UV survival independently of RAD23B, demonstrating non-redundant repair function despite shared partners.

    Evidence Stable EBV-plasmid siRNA silencing with UV survival and DNA repair assays

    PMID:21676658

    Open questions at the time
    • Molecular basis of the RAD23A-specific repair contribution not defined
    • Single cell-line context
  7. 2016 Medium

    Adding TRAF2, E2F1, Chk1, Beclin1/LC3, and refined p53 links expanded RAD23A's substrate/partner repertoire across innate immunity, cell-cycle control, NER recruitment, and autophagy, showing the shuttle factor regulates a broad set of clients beyond canonical repair.

    Evidence Co-IP, siRNA/overexpression, domain mapping, reporter and degradation assays, and localization imaging

    PMID:16105547 PMID:23357418 PMID:26296656 PMID:27028861 PMID:27613096

    Open questions at the time
    • Direct RAD23A-mediated ubiquitination of TRAF2 not shown in vitro
    • Autophagy link rests on a single co-IP with limited mechanistic resolution
  8. 2021 High

    Atomic-resolution structures of Vpr bound to the XPCB+UBA2 region, together with knockdown showing RAD23A bridges Vpr to the 26S proteasome, established the structural and functional basis for viral co-option distinct from the DCAF1 pathway.

    Evidence X-ray crystallography, NMR, biochemical binding, RNAi, and viral replication assays in primary macrophages

    PMID:20614012 PMID:24318982 PMID:34824204

    Open questions at the time
    • Fate of Vpr-recruited proteasomal cargo unresolved
    • How Vpr engagement reshapes endogenous RAD23A substrate handling unknown
  9. 2025 Medium

    Recent work defined substrate-fold selectivity, identified new shuttled clients (TDP-43, POLQ) and a UBL-specific deubiquitinase partner (MINDY3), and mapped TLS polymerase contacts, refining RAD23A as a fold-discriminating shuttle whose loss reshapes aggregation, repair-pathway choice, and DNA-damage responses.

    Evidence siRNA, sarkosyl fractionation, interactome/ubiquitin-chain analysis, degradation and MMEJ reporter assays, crystallography, and biochemical/structural binding (two preprints)

    PMID:37935254 PMID:40795920 PMID:41371952 PMID:bio_10.1101_2025.07.16.665128 PMID:bio_10.1101_2025.11.20.689626

    Open questions at the time
    • POLQ and MINDY3 findings are preprints awaiting peer review
    • How fold-selectivity is structurally encoded by the UBA domains not fully resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how RAD23A switches between protecting ubiquitinated substrates (p53) and delivering them for degradation, and what governs selection among its many candidate clients in vivo.
  • No unified model reconciling protective versus delivery functions
  • In vivo substrate hierarchy and competition not established
  • Physiological role of S-phase E6AP-driven RAD23A turnover unclear

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 4 GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005634 nucleus 2 GO:0005829 cytosol 2
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-73894 DNA Repair 3 R-HSA-1640170 Cell Cycle 2 R-HSA-168256 Immune System 1
Partners
CHK1HPLIC2MDM2MINDY3TRAF2UBE3AVPRXPC
Complex memberships
XPC-RAD23 NER complex

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 HHR23A (RAD23A) is ubiquitinated in vitro and in vivo by the E3 ubiquitin ligase E6AP (UBE3A) in an E6-independent manner. HHR23A binds E6AP directly, and overexpression of dominant-negative E6AP blocks HHR23A ubiquitination. HHR23A undergoes cell-cycle-dependent degradation specifically during S phase via E6AP, and UV-induced DNA damage inhibits this degradation. In vitro ubiquitination assay, co-immunoprecipitation, dominant-negative E6AP overexpression, cell-cycle synchronization experiments The Journal of biological chemistry High 10373495
2003 Full-length hHR23A adopts a closed conformation defined by intramolecular interactions between its N-terminal UBL domain and its two UBA domains. Binding of the proteasomal subunit S5a disrupts these interdomain interactions, causing hHR23A to adopt an open conformation. The protein contains four structured domains connected by flexible linkers. NMR spectroscopy, residual dipolar coupling, chemical shift perturbation analysis Proceedings of the National Academy of Sciences of the United States of America High 14557549
2003 hHR23A recognizes ubiquitin through a predominantly hydrophobic surface formed by residues within helix α1 and α3 of each of its two UBA domains; these surfaces bind a region on ubiquitin that includes K48. Binding ubiquitin requires a structural change in hHR23A, and hHR23A can form a ternary complex with ubiquitin and proteasomal subunit S5a. NMR chemical shift perturbation, 15N NMR relaxation experiments, binding assays Biochemistry High 14621999
2004 The UBL domain of HHR23A negatively regulates the interaction of its UBA domains with K48-linked polyubiquitin chains. Binding affinity for polyubiquitin increases with chain length and reaches maximum for chains of n=4–6 units, recognized by a single UBA domain. Leucine 8 of ubiquitin is an important determinant of chain recognition. Surface plasmon resonance, quantitative binding assays Journal of molecular biology High 15321727
2004 hHR23A and hHR23B inhibit proteasomal degradation of ubiquitinated p53. siRNA depletion of hHR23A accelerates p53 degradation, while overexpression or addition of purified hHR23 proteins blocks p53 degradation in vitro. An MDM2-hHR23A complex was identified, and an MDM2 mutant with increased hHR23A binding could ubiquitinate but not degrade p53; this defect was rescued by siRNA knockdown of hHR23A, indicating MDM2 acts post-ubiquitination to counteract hHR23A inhibition. siRNA knockdown, in vitro proteasome degradation assay, co-immunoprecipitation, overexpression rescue experiments Oncogene High 15064742
2000 Ataxin-3 interacts with both HHR23A and HHR23B via the UBL domain at the N-terminus of the HHR23 proteins. Mutant ataxin-3 recruits HHR23A to intranuclear inclusions through this interaction in 293 cells. Yeast two-hybrid screen, domain mapping, co-immunoprecipitation, immunofluorescence/colocalization Human molecular genetics Medium 10915768
1997 HIV-1 Vpr interacts physically with HHR23A. The Vpr-binding domain maps to a C-terminal 45-amino-acid region of HHR23A (the UBA2 domain). Overexpression of HHR23A or its truncated Vpr-binding domain partially alleviates Vpr-induced G2 arrest, indicating the Vpr-HHR23A interaction is functionally relevant for cell cycle arrest. Yeast two-hybrid, bacterially expressed recombinant protein direct binding, indirect immunofluorescence/confocal microscopy colocalization, overexpression rescue Journal of virology Medium 9371639
1997 XPC interacts in vivo with both HHR23B and HHR23A. Domain mapping shows both RAD23 homologs interact with XPC at the same highly conserved region in the C-terminal half of XPC. XPC mutants lacking this domain are deficient in both RAD23 binding and complementation of XPC cells, establishing this interaction as necessary for NER function. Yeast two-hybrid, domain deletion mapping, complementation assay Mutation research Medium 9164480
2000 The UBA2 domain of HHR23A interacts specifically with HIV-1 Vpr. A single point mutation P333E in the hydrophobic GFP-loop of UBA2 abolishes Vpr binding without major structural changes at distal sites. High-resolution NMR structures of wild-type and mutant UBA2 confirm the hydrophobic loop as the protein-protein interaction interface. In vitro binding assays, site-directed mutagenesis, NMR structure determination Biochemistry High 11087358
2004 The XPC-binding (XPCB) domain of hHR23A adopts a structure consisting of five amphipathic helices with hydrophobic patches on an otherwise hydrophilic surface, predicted to mediate interaction with XPC. This domain has limited sequence homology outside the Rad23 family except for sacsin. NMR solution structure determination Protein science Medium 15322280
2006 hHR23A and hHR23B have distinct (non-redundant) interactions with proteasomes and multiubiquitinated proteins despite redundant roles in DNA repair. Threonine-79 in hHR23A contributes to its weaker proteasome binding compared to hHR23B; converting T79P (the residue in hHR23B) increases hHR23A proteasome interaction. Both proteins bind Ataxin-3 similarly but co-purify with unique proteolytic and stress-responsive factors. Site-directed mutagenesis, co-purification/pulldown, binding assays FEBS letters Medium 16712842
2006 hHR23A interacts with hPLIC2 via UBL/UBA domain interactions, and these two ubiquitin receptor proteins associate in mammalian cells. Inhibition of the proteasome reduces the hHR23A/hPLIC2 interaction. NMR spectroscopy (binding surface mapping), co-immunoprecipitation in mammalian cells, proteasome inhibitor treatment Journal of molecular biology Medium 17098253
2005 hHR23A knockdown reduces DNA repair activity against UVC-induced damage and prevents normal UVC-induced induction of XPC expression. Co-immunoprecipitation shows hHR23A associates with a portion of hHR23B and the majority of p53, suggesting hHR23A regulates XPC function through its association with p53. RNA interference, Southwestern immunoblot, host-cell reactivation assay, co-immunoprecipitation Biochemical and biophysical research communications Medium 16105547
2010 The crystal structure of the UBL domain of hHR23A was determined. It shares the ubiquitin fold with overall Cα RMSD of 1.0–1.3 Å versus ubiquitin. Key residues Leu10, Ile49, and Met75 are disordered or have multiple conformations at the binding surface, suggesting conformational variability is important for interactions. Homology modelling suggests the UBL-UBA1 and UBL-UBA2 intramolecular interactions are structurally similar and mutually exclusive. X-ray crystallography, comparative homology modelling Protein engineering, design & selection Medium 21047872
2013 HIV-1 Vpr binds hHR23A using both the XPCB and UBA2 domains simultaneously, not just UBA2 alone. NMR mapping reveals Vpr contacts substantial surfaces on both UBA2 (interacting with α2 and α3 helices of Vpr) and XPCB. Vpr binding disrupts the intramolecular UBL-UBA2 interaction in hHR23A. K48-linked di-ubiquitin binding to UBA1 does not displace Vpr, forming a ternary hHR23A·Vpr·di-Ub(K48) complex. NMR chemical shift perturbation/structural mapping, in vitro binding studies, mutagenesis The Journal of biological chemistry High 24318982
2011 RAD23A and RAD23B participate in DNA repair and cell survival after UV irradiation with diverging functions. Long-term siRNA silencing of RAD23A in HeLa cells revealed it contributes to NER and UV survival independently from RAD23B. siRNA-mediated long-term gene silencing (EBV-derived plasmids), UV survival assay, DNA repair assay DNA repair Medium 21676658
2013 RAD23A negatively regulates RIG-I/MDA5 innate immune signaling by interacting with TRAF2 and promoting its polyubiquitination and proteasomal degradation. Knockdown of RAD23A augments RIG-I/MDA5-mediated IFN-β and proinflammatory cytokine expression; overexpression has the opposite effect. siRNA knockdown, ectopic overexpression, co-immunoprecipitation, Western blotting for TRAF2 levels, reporter assays Biochemical and biophysical research communications Medium 23357418
2016 E2F1 interacts directly with hHR23A proteins. This interaction stabilizes E2F1 by inhibiting its proteasomal degradation. Reciprocally, E2F1 regulates hHR23A subcellular localization, recruiting it to sites of UV-induced DNA photodamage, thereby enhancing NER in epidermal keratinocytes. Co-immunoprecipitation, proteasome inhibitor experiments, immunofluorescence/colocalization at DNA damage sites, UV survival/repair assays Oncotarget Medium 27028861
2015 hHR23A associates with Chk1 through its UBA domains and promotes Chk1 proteasomal degradation. Knockdown of hHR23A stabilizes Chk1 protein and increases its phosphorylation at S347, resulting in S-phase accumulation. DNA damage reduces the Chk1-hHR23A interaction, releasing Chk1 to activate cell cycle checkpoints. siRNA knockdown, co-immunoprecipitation, domain mapping (UBA domains), flow cytometry, Western blotting Cellular signalling Medium 26296656
2016 hHR23A interacts directly with Beclin 1 and LC3 (autophagy regulators). Knockdown of hHR23A increases autophagy flux as measured by EGFP-LC3 puncta, and overexpression reverses autophagy-related protein changes in knockdown cells. Co-immunoprecipitation, EGFP-LC3 puncta measurement, Western blotting, overexpression rescue Biochemical and biophysical research communications Low 27613096
2021 Atomic resolution structure of HIV-1 Vpr in complex with the C-terminal half of hHR23A (XPCB + UBA2 domains) was determined. XPCB and UBA2 domains bind to opposite sides of Vpr's 3-helix-bundle. DCAF1 and hHR23A use overlapping binding surfaces on Vpr, revealing that Vpr independently targets hHR23A- and DCAF1-dependent pathways. X-ray crystallography, NMR, biochemical binding assays Nature communications High 34824204
2010 hHR23A mediates the interaction of HIV-1 Vpr with the 26S proteasome (19S subunit). Depletion of hHR23A by RNAi disrupts Vpr-proteasome interaction in mammalian cells and significantly reduces HIV-1 replication in non-proliferating cells and primary macrophages. RNAi knockdown, co-immunoprecipitation, viral replication assay in primary macrophages PloS one Medium 20614012
2023 RAD23A UBA1 and UBA2 domains each interact with Y-family DNA polymerase Pol ι at distinct, separate sites within the Pol ι catalytic domain; the UBA2 ubiquitin-binding cleft is involved, while Pol ι contacts a distinct surface on UBA1. Both UBA domain interactions are necessary for stable binding. RAD23A and RAD23B interact similarly with all four Y-family TLS polymerases (Pol ι, Pol η, Pol κ, Rev1). Biochemical binding assays, cell-based assays, structural assays, domain mutagenesis/deletion Journal of molecular biology Medium 37935254
2025 RAD23A knockdown reduces insoluble TDP-43 levels in cells. RAD23A acts as a shuttle factor that promotes TDP-43 delivery to the proteasome; loss of RAD23A increases TDP-43 degradation and reduces aggregation. A proteomic screen identified USP13 (a deubiquitinase) as a modifier of TDP-43 aggregation, acting downstream of RAD23A. siRNA knockdown in inducible HEK293 cells and primary rat neurons, sarkosyl fractionation, discovery proteomics The Journal of neuroscience Medium 41371952
2025 Substrate structure (folded vs. unstructured tail) determines dependency on RAD23A/B for proteasomal degradation. Well-folded ubiquitinated substrates (Ub-GFP) depend on RAD23A/B for degradation, while substrates with an unstructured tail (Ub-GFP-tail) bypass RAD23A/B. RAD23A/B interact preferentially with well-folded substrates. RAD23A/B knockdown reduces apparent ubiquitin chain lengths on substrates but only impairs degradation of the folded substrate. siRNA knockdown, interactome analysis (co-IP/MS), ubiquitin chain analysis, degradation assays in human cells Journal of biochemistry Medium 40795920
2025 HPV16 E6 activates E6AP/UBE3A to promote ubiquitination and degradation of RAD23A. Loss of RAD23A leads to stabilization of POLQ (DNA Polymerase Theta), which RAD23A normally shuttles to the proteasome. This E6-UBE3A-RAD23A-POLQ axis promotes microhomology-mediated end joining (MMEJ) and viral genome integration. Overexpression, siRNA knockdown, ubiquitination assays, Western blotting, MMEJ reporter assay bioRxivpreprint Medium bio_10.1101_2025.11.20.689626
2025 The EF-hand domain of the deubiquitinase MINDY3 binds specifically to the UBL domain of RAD23A (and RAD23B) but not to other UBL domains tested. Crystal structure of the MINDY3 EF-hand:RAD23A UBL domain complex reveals the molecular basis for this specificity. MINDY3 can form a ternary complex with RAD23A/B and polyubiquitin, and the EF-hand domain mediates MINDY3 recruitment to DNA damage sites through RAD23 binding. Crystal structure determination, co-immunoprecipitation in cells, ternary complex assay, DNA damage recruitment assay bioRxivpreprint High bio_10.1101_2025.07.16.665128

Source papers

Stage 0 corpus · 38 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1999 Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination. The Journal of biological chemistry 174 10373495
2004 Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A. Journal of molecular biology 130 15321727
2003 DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. Proceedings of the National Academy of Sciences of the United States of America 129 14557549
2000 Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. Human molecular genetics 127 10915768
1997 Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular protein implicated in nucleotide excision DNA repair. Journal of virology 91 9371639
2003 Ubiquitin recognition by the DNA repair protein hHR23a. Biochemistry 80 14621999
2000 Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr. Biochemistry 69 11087358
2004 A post-ubiquitination role for MDM2 and hHR23A in the p53 degradation pathway. Oncogene 60 15064742
1998 HHR23A, the human homologue of the yeast repair protein RAD23, interacts specifically with Vpr protein and prevents cell cycle arrest but not the transcriptional effects of Vpr. Virology 53 9636371
1997 XPC interacts with both HHR23B and HHR23A in vivo. Mutation research 46 9164480
2025 Lactate accumulation induces H4K12la to activate super-enhancer-driven RAD23A expression and promote niraparib resistance in ovarian cancer. Molecular cancer 45 40102876
2006 Ubiquitin receptor proteins hHR23a and hPLIC2 interact. Journal of molecular biology 39 17098253
2001 Analysis of apoptosis induced by HIV-1 Vpr and examination of the possible role of the hHR23A protein. Experimental cell research 31 11426943
2006 Evidence for distinct functions for human DNA repair factors hHR23A and hHR23B. FEBS letters 30 16712842
2004 Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction. Protein science : a publication of the Protein Society 30 15322280
2002 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. Nucleic acids research 24 11788722
2001 Interaction of human immunodeficiency virus type 1 Vpr with the HHR23A DNA repair protein does not correlate with multiple biological functions of Vpr. Virology 24 11259200
2011 Differential contribution of XPC, RAD23A, RAD23B and CENTRIN 2 to the UV-response in human cells. DNA repair 21 21676658
2016 E2F1 interactions with hHR23A inhibit its degradation and promote DNA repair. Oncotarget 11 27028861
2010 HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome. PloS one 11 20614012
2005 HHR23A, a human homolog of Saccharomyces cerevisiae Rad23, regulates xeroderma pigmentosum C protein and is required for nucleotide excision repair. Biochemical and biophysical research communications 11 16105547
2013 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. The Journal of biological chemistry 10 24318982
2021 Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A. Nature communications 9 34824204
2023 A Novel Interaction Between RAD23A/B and Y-family DNA Polymerases. Journal of molecular biology 6 37935254
2013 RAD23A negatively regulates RIG-I/MDA5 signaling through promoting TRAF2 polyubiquitination and degradation. Biochemical and biophysical research communications 6 23357418
2016 Human Rad23A plays a regulatory role in autophagy. Biochemical and biophysical research communications 5 27613096
2015 hHR23A is required to control the basal turnover of Chk1. Cellular signalling 4 26296656
2010 The crystal structure of the ubiquitin-like (UbL) domain of human homologue A of Rad23 (hHR23A) protein. Protein engineering, design & selection : PEDS 4 21047872
2022 Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A. Biochemistry 3 35430812
2019 Complete 1H, 13C, 15N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223-363). Biomolecular NMR assignments 3 31463759
2026 Ubiquitin Proteasome System Components, RAD23A and USP13, Modulate TDP-43 Solubility and Neuronal Toxicity. The Journal of neuroscience : the official journal of the Society for Neuroscience 2 41371952
2025 Substrate structure determines p97- and RAD23A/B-mediated proteasomal degradation in human cells. Journal of biochemistry 1 40795920
2024 Reduction of RAD23A extends lifespan and mitigates pathology in TDP-43 mice. bioRxiv : the preprint server for biology 1 39314471
2026 Reduction of RAD23A extends lifespan and mitigates pathology in a mouse model of TDP-43 proteinopathy. Nature communications 0 41545357
2026 RAD23A promotes multiple myeloma cell survival through DNA damage response, proteostasis and enhanced metabolic activity. Toxicology and applied pharmacology 0 42092462
2023 1H, 15N, 13C resonance assignments for proteasome shuttle factor hHR23a. Research square 0 37645848
2023 1H, 15N, 13C resonance assignments for proteasome shuttle factor hHR23a. Biomolecular NMR assignments 0 37812322
2009 Crystallization and preliminary X-ray diffraction studies of the ubiquitin-like (UbL) domain of the human homologue A of Rad23 (hHR23A) protein. Acta crystallographica. Section F, Structural biology and crystallization communications 0 19724136

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