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Damage-specific DNA binding protein 1, 127kDa
Protein DDB1 PDB 2b5l.png
PDB rendering based on 2b5l.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs OMIM600045 MGI1202384 HomoloGene1448 GeneCards: DDB1 Gene
Species Human Mouse
Entrez 1642 13194
Ensembl ENSG00000167986 ENSMUSG00000024740
UniProt Q16531 Q3U1J4
RefSeq (mRNA) NM_001923 NM_015735
RefSeq (protein) NP_001914 NP_056550
Location (UCSC) Chr 11:
61.07 – 61.11 Mb
Chr 19:
10.61 – 10.63 Mb
PubMed search [1] [2]

DNA damage-binding protein 1 is a protein that in humans is encoded by the DDB1 gene.[1][2][3]


This gene encodes the large subunit of DNA damage-binding protein that is a heterodimer composed of a large and a small (DDB2) subunit. This protein functions in nucleotide excision repair. Its defective activity causes the repair defect in the patients with xeroderma pigmentosum complementation group E (XPE). However, it remains for mutation analysis to demonstrate whether the defect in XPE patients is in this gene or the gene encoding the small subunit. In addition, Best vitelliform macular dystrophy is mapped to the same region as this gene on 11q, but no sequence alternations of this gene are demonstrated in Best disease patients.[3]


DDB1 has been shown to interact with Transcription initiation protein SPT3 homolog,[4] GCN5L2,[5] DDB2,[6][7] CUL4A,[7] CUL4B[7] and P21.[8]


  1. ^ Dualan R, Brody T, Keeney S, Nichols AF, Admon A, Linn S (Feb 1996). "Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for the p127 and p48 subunits of a human damage-specific DNA binding protein". Genomics 29 (1): 62–9. doi:10.1006/geno.1995.1215. PMID 8530102. 
  2. ^ Seki N, Hayashi A, Hattori A, Kozuma S, Sasaki M, Suzuki Y, Sugano S, Muramatsu M, Saito T (Jan 2000). "cDNA cloning, tissue expression, and chromosomal assignment of a mouse gene, encoding a 127 kDa UV-damaged DNA binding protein which is defective in XPE cells". DNA Res 6 (5): 319–22. doi:10.1093/dnares/6.5.319. PMID 10574459. 
  3. ^ a b "Entrez Gene: DDB1 damage-specific DNA binding protein 1, 127kDa". 
  4. ^ Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (October 2001). "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo". Mol. Cell. Biol. 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863. 
  5. ^ Huang J, Chen J (July 2008). "VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation". Oncogene 27 (29): 4056–64. doi:10.1038/onc.2008.44. PMID 18332868. 
  6. ^ Bergametti F, Sitterlin D, Transy C (July 2002). "Turnover of hepatitis B virus X protein is regulated by damaged DNA-binding complex". J. Virol. 76 (13): 6495–501. doi:10.1128/JVI.76.13.6495-6501.2002. PMC 136256. PMID 12050362. 
  7. ^ a b c Guerrero-Santoro J, Kapetanaki MG, Hsieh CL, Gorbachinsky I, Levine AS, Rapić-Otrin V (July 2008). "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A". Cancer Res. 68 (13): 5014–22. doi:10.1158/0008-5472.CAN-07-6162. PMID 18593899. 
  8. ^ Abbas T, Sivaprasad U, Terai K, Amador V, Pagano M, Dutta A (September 2008). "PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex". Genes Dev. 22 (18): 2496–506. doi:10.1101/gad.1676108. PMC 2546691. PMID 18794347. 

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