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hHR23A associates with Chk1 (show CHEK1 Proteins) through its ubiquitin-associated domains, and knockdown of hHR23A increases and stabilizes the protein level of Chk1 (show CHEK1 Proteins) and its phosphorylation at S347.
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.
this study identified RAD23A as a novel negative regulator of RIG-I (show DDX58 Proteins)/MDA5 (show IFIH1 Proteins) mediated anti-virus response.
Determined is the three-dimensional structure of its ubiquitin-like (UbL) domain by X-ray crystallography.
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
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
structures of the UBA domains of HHR23A reveal a conserved hydrophobic surface for protein-protein interactions
the solution structures of the HHR23A Ubl domain
Adopts a closed conformation and binds to the proteasomal subunit S5a (show Psmd4 Proteins) thereby changing its own conformation.
hHR23 binds to polyubiquitylated p53 (show TP53 Proteins) via its carboxyl-terminal ubiquitin-associated (Uba) domain shielding p53 (show TP53 Proteins) from deubiquitylation
the mammalian RAD23 proteins play a direct role in damage recognition by enhancing the binding of XPC (show XPC Proteins) to DNA damage in living cells in addition to stabilizing XPC (show XPC Proteins). RAD23 proteins rapidly dissociated from XPC (show XPC Proteins) upon binding to damaged DNA.
analysis of mHR23A/B double-mutant cells showed that HR23 proteins function in nucleotide excision repair by governing xeroderma pigmentosum group C protein (show HNRNPC Proteins) stability via partial protection against proteasomal degradation
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair. Proteins in this family have a modular domain structure consisting of an ubiquitin-like domain (UbL), ubiquitin-associated domain 1 (UbA1), XPC-binding domain and UbA2. The protein encoded by this gene plays an important role in nucleotide excision repair and also in delivery of polyubiquitinated proteins to the proteasome. Alternative splicing results in multiple transcript variants encoding multiple isoforms.
RAD23 homolog A
, UV excision repair protein RAD23 homolog A
, RAD23 homolog A (S. cerevisiae)
, RAD23, yeast homolog, A