Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:
10882109, PubMed:
11278856, PubMed:
11705987, PubMed:
9892649, PubMed:
12732143, PubMed:
15882621, PubMed:
16473935, PubMed:
18593899). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV- induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:
10882109, PubMed:
11278856, PubMed:
11705987, PubMed:
16260596, PubMed:
12944386, PubMed:
14751237). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:
10882109, PubMed:
11278856, PubMed:
11705987, PubMed:
16260596, PubMed:
12944386). Also functions as the substrate recognition module for the DCX (DDB2- CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1) (PubMed:
12732143, PubMed:
15882621, PubMed:
16473935, PubMed:
18593899, PubMed:
26572825). The DDB2-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (PubMed:
16678110, PubMed:
16473935). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:
16678110, PubMed:
16473935). The DDB2-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:
15882621). The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to DNA damage, leading to its degradation: recognizes KAT7/HBO1 following phosphorylation by ATR (PubMed:
26572825).
