DDB1

DDB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2B5L, 2B5M, 2B5N, 2HYE, 3E0C, 3EI1, 3EI2, 3EI3, 3EI4, 3I7H, 3I7K, 3I7L, 3I7N, 3I7O, 3I7P, 3I89, 3I8C, 3I8E, 4A08, 4A09, 4A0A, 4A0B, 4A0K, 4A0L, 4A11, 4CI1, 4CI2, 4CI3, 4E54, 4E5Z, 4TZ4, 5FQD, 5HXB
Identifiers
Aliases	DDB1, DDBA, UV-XAP1, XPCE, XPE, XPE-BF, damage specific DNA binding protein 1, WHIKERS
External IDs	OMIM: 600045; MGI: 1202384; HomoloGene: 1448; GeneCards: DDB1; OMA:DDB1 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q12.2 Start 61,299,451 bp End 61,342,596 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19 A|19 6.66 cM Start 10,582,691 bp End 10,607,183 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal gland right adrenal cortex left adrenal gland left adrenal cortex ventricular zone stromal cell of endometrium right testis ganglionic eminence left testis right uterine tube Top expressed in Ileal epithelium neural layer of retina spermatocyte choroid plexus of fourth ventricle gastrula ventricular zone epiblast tail of embryo lactiferous gland hand More reference expression data BioGPS n/a
Gene ontology Molecular function DNA binding protein binding nucleic acid binding damaged DNA binding protein-macromolecule adaptor activity cullin family protein binding WD40-repeat domain binding protein-containing complex binding Cellular component cytoplasm nucleoplasm Cul4A-RING E3 ubiquitin ligase complex Cul4B-RING E3 ubiquitin ligase complex extracellular exosome nucleus extracellular space Cul4-RING E3 ubiquitin ligase complex protein-containing complex Biological process regulation of mitotic cell cycle phase transition nucleotide-excision repair nucleotide-excision repair, DNA damage recognition positive regulation by virus of viral protein levels in host cell histone H2A monoubiquitination negative regulation of apoptotic process Wnt signaling pathway global genome nucleotide-excision repair biological process involved in interaction with symbiont positive regulation of viral genome replication transcription-coupled nucleotide-excision repair viral process nucleotide-excision repair, DNA incision UV-damage excision repair DNA repair proteasome-mediated ubiquitin-dependent protein catabolic process nucleotide-excision repair, DNA incision, 3'-to lesion nucleotide-excision repair, preincision complex stabilization nucleotide-excision repair, DNA duplex unwinding nucleotide-excision repair, preincision complex assembly nucleotide-excision repair, DNA incision, 5'-to lesion post-translational protein modification proteasomal protein catabolic process cellular response to DNA damage stimulus protein ubiquitination positive regulation of protein catabolic process ubiquitin-dependent protein catabolic process regulation of circadian rhythm positive regulation of gluconeogenesis rhythmic process Sources:Amigo / QuickGO
Orthologs 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: 61.3 – 61.34 Mb Chr 19: 10.58 – 10.61 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Gene

The gene's position is on chromosome 11q12-q13.

Protein

The DDB1 gene encodes the large subunit of DNA damage-binding protein, a heterodimer composed of a large and a small (DDB2) subunit. DDB1 contains 1140 amino acids, amounting to a mass of 127 kDa.

Function

As its name suggests, DDB1 was initially implicated in the process of a specific type of DNA repair known as nucleotide excision repair. Since then, researchers have found that DDB1 primarily functions as a core component of the CUL4A- and CUL4B-based E3 ubiquitin ligase complexes. DDB1 serves as a bridge or adaptor protein which interacts with dozens of proteins known as DDB1 and CUL4-associated factors (DCAFs). These DCAFs are often ubiquitin ligase substrates and regulate numerous essential processes in the cell including DNA repair (DDB2), DNA replication, chromatin remodeling (Cdt2) and more.

Interactions

DDB1 has been shown to interact with Transcription initiation protein SPT3 homolog, GCN5L2, DDB2, CUL4A, CUL4B and P21.

Further reading

• Chu G, Chang E (1988). "Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA". Science. 242 (4878): 564–7. Bibcode:1988Sci...242..564C. doi:10.1126/science.3175673. PMID 3175673.
• Lee TH, Elledge SJ, Butel JS (1995). "Hepatitis B virus X protein interacts with a probable cellular DNA repair protein". J. Virol. 69 (2): 1107–14. doi:10.1128/JVI.69.2.1107-1114.1995. PMC 188683. PMID 7815490.
• Keeney S, Eker AP, Brody T, et al. (1994). "Correction of the DNA repair defect in xeroderma pigmentosum group E by injection of a DNA damage-binding protein" (PDF). Proc. Natl. Acad. Sci. U.S.A. 91 (9): 4053–6. Bibcode:1994PNAS...91.4053K. doi:10.1073/pnas.91.9.4053. PMC 43721. PMID 8171034.
• Keeney S, Chang GJ, Linn S (1993). "Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum E." J. Biol. Chem. 268 (28): 21293–300. doi:10.1016/S0021-9258(19)36923-6. PMID 8407967.
• Hwang BJ, Liao JC, Chu G (1996). "Isolation of a cDNA encoding a UV-damaged DNA binding factor defective in xeroderma pigmentosum group E cells". Mutat. Res. 362 (1): 105–17. doi:10.1016/0921-8777(95)00040-2. PMID 8538642.
• Nichols AF, Ong P, Linn S (1996). "Mutations specific to the xeroderma pigmentosum group E Ddb- phenotype". J. Biol. Chem. 271 (40): 24317–20. doi:10.1074/jbc.271.40.24317. PMID 8798680.
• Liu W, Nichols AF, Graham JA, et al. (2000). "Nuclear transport of human DDB protein induced by ultraviolet light". J. Biol. Chem. 275 (28): 21429–34. doi:10.1074/jbc.M000961200. PMID 10777491.
• Martinez E, Palhan VB, Tjernberg A, et al. (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.
• Chen X, Zhang Y, Douglas L, Zhou P (2002). "UV-damaged DNA-binding proteins are targets of CUL-4A-mediated ubiquitination and degradation". J. Biol. Chem. 276 (51): 48175–82. doi:10.1074/jbc.M106808200. PMID 11673459.
• Rapić-Otrin V, McLenigan MP, Bisi DC, et al. (2002). "Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation". Nucleic Acids Res. 30 (11): 2588–98. doi:10.1093/nar/30.11.2588. PMC 117178. PMID 12034848.
• Bergametti F, Sitterlin D, Transy C (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.
• Bontron S, Lin-Marq N, Strubin M (2002). "Hepatitis B virus X protein associated with UV-DDB1 induces cell death in the nucleus and is functionally antagonized by UV-DDB2". J. Biol. Chem. 277 (41): 38847–54. doi:10.1074/jbc.M205722200. PMID 12151405.
• Andrejeva J, Poole E, Young DF, et al. (2002). "The p127 subunit (DDB1) of the UV-DNA damage repair binding protein is essential for the targeted degradation of STAT1 by the V protein of the paramyxovirus simian virus 5". J. Virol. 76 (22): 11379–86. doi:10.1128/JVI.76.22.11379-11386.2002. PMC 136798. PMID 12388698.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Groisman R, Polanowska J, Kuraoka I, et al. (2003). "The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage". Cell. 113 (3): 357–67. doi:10.1016/S0092-8674(03)00316-7. PMID 12732143. S2CID 11639677.
• Leupin O, Bontron S, Strubin M (2003). "Hepatitis B virus X protein and simian virus 5 V protein exhibit similar UV-DDB1 binding properties to mediate distinct activities". J. Virol. 77 (11): 6274–83. doi:10.1128/JVI.77.11.6274-6283.2003. PMC 154990. PMID 12743284.
• Wertz IE, O'Rourke KM, Zhang Z, et al. (2004). "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase" (PDF). Science. 303 (5662): 1371–4. Bibcode:2004Sci...303.1371W. doi:10.1126/science.1093549. PMID 14739464. S2CID 40501515.
• Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.