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RAD23BRAD23 homolog B (S. cerevisiae) |
Known also as: P58; HR23B; HHR23B;
| NCBI Gene ID: | 5887 |
| NCBI Ensembl Id: | ENSG00000119318 |
| MIM Id: (from NCBI OMIM database) | 600062 |
| Species: | Homo sapiens |
| 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. [provided by RefSeq] |
Gene sequence:
| [Download sequence] |
Proteins coded by this gene:
References:
| Authors | Title | Journal |
| Masutani C, Sugasawa K, Yanagisawa J, Sonoyama T, Ui M, Enomoto T, Takio K, Tanaka K, van der Spek PJ, Bootsma D, et al. | Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. | EMBO J April 15, 1994 |
| Lindahl T, Wood RD | Quality control by DNA repair. | Science Dec. 3, 1999 |
| Boutet SC, Disatnik MH, Chan LS, Iori K, Rando TA | Regulation of Pax3 by proteasomal degradation of monoubiquitinated protein in skeletal muscle progenitors. | Cell July 27, 2007 |
| Sugasawa K, Akagi J, Nishi R, Iwai S, Hanaoka F | Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning. | Mol Cell Nov. 25, 2009 |
Last modification of this entry: Oct. 6, 2010.
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