Human DNA Damage-binding Protein 2, DDB2 ELI

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: 1$475.00|$350.001237).

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).

[Isoform D1]: Inhibits UV-damaged DNA repair.

[Isoform D2]: Inhibits UV-damaged DNA repair.