DDB1 Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2. The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1. DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver. Belongs to the DDB1 family. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage
Chromosomal Location of Human Ortholog: 19 A|19 6.66 cM
Cellular Component:  Cul4-RING E3 ubiquitin ligase complex; Cul4A-RING E3 ubiquitin ligase complex; Cul4B-RING E3 ubiquitin ligase complex; cytoplasm; nucleoplasm; nucleus; protein-containing complex
Molecular Function:  cullin family protein binding; damaged DNA binding; DNA binding; nucleic acid binding; protein binding; protein binding, bridging; protein-containing complex binding; WD40-repeat domain binding
Biological Process:  cellular response to DNA damage stimulus; DNA repair; histone H2A monoubiquitination; interaction with symbiont; negative regulation of apoptotic process; positive regulation by virus of viral protein levels in host cell; positive regulation of gluconeogenesis; positive regulation of protein catabolic process; positive regulation of viral genome replication; positive regulation of viral release from host cell; proteasomal protein catabolic process; proteasome-mediated ubiquitin-dependent protein catabolic process; protein ubiquitination; regulation of circadian rhythm; regulation of mitotic cell cycle phase transition; ubiquitin-dependent protein catabolic process; UV-damage excision repair; Wnt signaling pathway
Reference #:  Q3U1J4 (UniProtKB)
Alt. Names/Synonyms: 127kDa; AA408517; damage specific DNA binding protein 1; Damage-specific DNA-binding protein 1; damage-specific DNA-binding protein, DNA repair; damaged-DNA recognition protein 1; DDB p127 subunit; Ddb1; DNA damage-binding protein 1; DNA repair protein; p127-Ddb1; UV-damaged DNA-binding factor
Gene Symbols: Ddb1
Molecular weight: 126,853 Da
Basal Isoelectric point: 5.14  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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DDB1

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene