RAD23B

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RAD23 homolog B (S. cerevisiae)
PDB rendering based on 1dv0.
Available structures: 1dv0, 1p1a, 1pve, 1uel, 2f4m, 2f4o
Identifiers
Symbol(s) RAD23B; P58; HHR23B; HR23B
External IDs OMIM: 600062 MGI: 105128 HomoloGene: 37704
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5887 19359
Ensembl ENSG00000119318 ENSMUSG00000028426
Uniprot P54727 Q3TJ52
Refseq NM_002874 (mRNA)
NP_002865 (protein)		 NM_009011 (mRNA)
NP_033037 (protein)
Location Chr 9: 109.09 - 109.13 Mb Chr 4: 55.37 - 55.41 Mb
Pubmed search [1] [2]

RAD23 homolog B (S. cerevisiae), also known as RAD23B, is a human gene.

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.[1]

[edit] References

  1. ^ Entrez Gene: RAD23B RAD23 homolog B (S. cerevisiae).

[edit] Further reading

  • van der Spek PJ, Smit EM, Beverloo HB, et al. (1995). "Chromosomal localization of three repair genes: the xeroderma pigmentosum group C gene and two human homologs of yeast RAD23.". Genomics 23 (3): 651–8. doi:10.1006/geno.1994.1554. PMID 7851894. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298. 
  • Masutani C, Sugasawa K, Yanagisawa J, et al. (1994). "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. 13 (8): 1831–43. PMID 8168482. 
  • van der Spek PJ, Eker A, Rademakers S, et al. (1996). "XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes.". Nucleic Acids Res. 24 (13): 2551–9. PMID 8692695. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149. 
  • Sugasawa K, Ng JM, Masutani C, et al. (1998). "Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair.". Mol. Cell 2 (2): 223–32. PMID 9734359. 
  • Hiyama H, Yokoi M, Masutani C, et al. (1999). "Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome.". J. Biol. Chem. 274 (39): 28019–25. PMID 10488153. 
  • Miao F, Bouziane M, Dammann R, et al. (2000). "3-Methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteins.". J. Biol. Chem. 275 (37): 28433–8. doi:10.1074/jbc.M001064200. PMID 10854423. 
  • Wang G, Sawai N, Kotliarova S, et al. (2000). "Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B.". Hum. Mol. Genet. 9 (12): 1795–803. PMID 10915768. 
  • Araújo SJ, Nigg EA, Wood RD (2001). "Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome.". Mol. Cell. Biol. 21 (7): 2281–91. doi:10.1128/MCB.21.7.2281-2291.2001. PMID 11259578. 
  • Araki M, Masutani C, Takemura M, et al. (2001). "Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair.". J. Biol. Chem. 276 (22): 18665–72. doi:10.1074/jbc.M100855200. PMID 11279143. 
  • Park H, Suzuki T, Lennarz WJ (2001). "Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation.". Proc. Natl. Acad. Sci. U.S.A. 98 (20): 11163–8. doi:10.1073/pnas.201393498. PMID 11562482. 
  • Walters KJ, Kleijnen MF, Goh AM, et al. (2002). "Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a.". Biochemistry 41 (6): 1767–77. PMID 11827521. 
  • Lee SM, Li ML, Tse YC, et al. (2002). "Paeoniae Radix, a Chinese herbal extract, inhibit hepatoma cells growth by inducing apoptosis in a p53 independent pathway.". Life Sci. 71 (19): 2267–77. PMID 12215374. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Shimizu Y, Iwai S, Hanaoka F, Sugasawa K (2003). "Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase.". EMBO J. 22 (1): 164–73. doi:10.1093/emboj/cdg016. PMID 12505994. 
  • Ng JM, Vermeulen W, van der Horst GT, et al. (2003). "A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein.". Genes Dev. 17 (13): 1630–45. doi:10.1101/gad.260003. PMID 12815074. 
  • Ryu KS, Lee KJ, Bae SH, et al. (2003). "Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a.". J. Biol. Chem. 278 (38): 36621–7. doi:10.1074/jbc.M304628200. PMID 12832454. 
  • Fujiwara K, Tenno T, Sugasawa K, et al. (2004). "Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B.". J. Biol. Chem. 279 (6): 4760–7. doi:10.1074/jbc.M309448200. PMID 14585839. 
  • Glockzin S, Ogi FX, Hengstermann A, et al. (2004). "Involvement of the DNA repair protein hHR23 in p53 degradation.". Mol. Cell. Biol. 23 (24): 8960–9. PMID 14645509. 
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