The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in the nucleotide excision repair (NER). This protein was found to be a component of the protein complex that specifically complements the NER defect of xeroderma pigmentosum group C (XP-c) cell extracts in vitro. This protein was also 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, and thus this protein may be involved in the ubiquitin mediated proteolytic pathway in cells. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Sep 2011],domain:The ubiquitin-like domain mediates interaction with MJD.,function:Plays a central role both in proteosomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulun that are retrotranslocated in the cytosol. Involved in DNA excision repair by stabilizing XPC protein. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.,similarity:Belongs to the RAD23 family.,similarity:Contains 1 STI1 domain.,similarity:Contains 1 ubiquitin-like domain.,similarity:Contains 2 UBA domains.,subunit:Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B (By similarity). Interacts with the 26S proteasome. Interacts directly with NGLY1. Heterodimer of a 125 kDa subunit (p125) and of a 58 kDa subunit (p58). Interacts with MJD and XPC.,
