DDB2

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DDB2
Protein DDB2 PDB 3EI4.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases DDB2, DDBB, UV-XPE, damage specific DNA binding protein 2
External IDs MGI: 1355314 HomoloGene: 83 GeneCards: DDB2
RNA expression pattern
PBB GE DDB2 203409 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000107
NM_001300734

NM_028119

RefSeq (protein)

NP_000098
NP_001287663

NP_082395

Location (UCSC) Chr 11: 47.21 – 47.24 Mb Chr 2: 91.21 – 91.24 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

DNA damage-binding protein 2 is a protein that in humans is encoded by the DDB2 gene.[3][4]

Function[edit]

DDB2 is the smaller subunit of a heterodimeric protein implicated in the etiology of xeroderma pigmentosum group E. This subunit appears to be required for DNA binding.[5]

Interactions[edit]

DDB2 has been shown to interact with CUL4A,[6] CUL4B[6] and DDB1.[6][7][8] Also, some researches about DDB2 show a relationship between DDB2 and PARP1.PARP1 as a novel DDB2-associated factor,which may help to recruitment a chromatin-remodeling enzyme,named ALC1.[9]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Keeney S, Chang GJ, Linn S (Oct 1993). "Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum E". The Journal of Biological Chemistry. 268 (28): 21293–300. PMID 8407967. 
  4. ^ Dualan R, Brody T, Keeney S, Nichols AF, Admon A, Linn S (Sep 1995). "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. PMID 8530102. doi:10.1006/geno.1995.1215. 
  5. ^ "Entrez Gene: DDB2 damage-specific DNA binding protein 2, 48kDa". 
  6. ^ a b c Guerrero-Santoro J, Kapetanaki MG, Hsieh CL, Gorbachinsky I, Levine AS, Rapić-Otrin V (Jul 2008). "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A". Cancer Research. 68 (13): 5014–22. PMID 18593899. doi:10.1158/0008-5472.CAN-07-6162. 
  7. ^ Bergametti F, Sitterlin D, Transy C (Jul 2002). "Turnover of hepatitis B virus X protein is regulated by damaged DNA-binding complex". Journal of Virology. 76 (13): 6495–501. PMC 136256Freely accessible. PMID 12050362. doi:10.1128/JVI.76.13.6495-6501.2002. 
  8. ^ Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (Oct 2001). "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo". Molecular and Cellular Biology. 21 (20): 6782–95. PMC 99856Freely accessible. PMID 11564863. doi:10.1128/MCB.21.20.6782-6795.2001. 
  9. ^ Pines A, Vrouwe MG, Marteijn JA, Typas D, Luijsterburg MS, Cansoy M, Hensbergen P, Deelder A, de Groot A, Matsumoto S, Sugasawa K, Thoma N, Vermeulen W, Vrieling H, Mullenders L (Oct 2012). "PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1". The Journal of Cell Biology. 199 (2): 235–49. PMC 3471223Freely accessible. PMID 23045548. doi:10.1083/jcb.201112132. 

Further reading[edit]

External links[edit]