Cancer Protein Description
This report provides a detailed description of a selected cancer protein with information collected from various sources, including UniProt, the Wellcome Trust Sanger Institute’s Catalogue of Somatic Mutations in Cancer (COSMIC), and the Atlas of Genetics and Cytogenetics in Oncology and Haematology.
| Protein Name: | DDB2 |
| Gene Name: | DDB2 |
| Protein Full Name: | DNA damage-binding protein 2 |
| Alias: | damage-specific DNA binding 2 (48kD); damage-specific DNA binding 2, 48kDa; damage-specific DNA binding protein 2; damage-specific DNA binding protein 2, 48kDa; damage-specific DNA-binding 2; DDB p48; DDB p48 subunit; DDBb; DNA damage-binding 2; FLJ34321; UV-damaged DNA-binding 2; UV-damaged DNA-binding protein 2; UV-DDB 2; UV-DDB2; xeroderma pigmentosum group E; xeroderma pigmentosum group E protein |
| Mass (Da): | 47864 |
| Number AA: | 427 |
| UniProt ID: | Q92466 |
| Locus ID: | 1643 |
| COSMIC ID: | DDB2 |
| Gene location on chromosome: | 11p12-11p11 |
| Cancer protein type: | TSP |
| Effect of cancer mutation on protein: | LOSS |
| Effect of active protein on cancer: | INHIBITS |
| Number of cancer specimens: | 20573 |
| Percent of cancer specimens with mutations: | 0.24 |
| Normal role description: | DDB2 plays a crucial role in DNA repair in response to UV-induced damage to DNA. Xeroderma Pigmentosum complementation group E, a recessive disease that is characterized by an increased sensitivity to UV light and a high predisposition for skin cancer development, is caused by mutation in DDB2. |
| Commentary on involvement of protein in cancer: | Required for DNA repair. Binds to DDB1 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 the substrate recognition module for the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB1-CUL4-ROC1 complex 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. The DDB1-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. Isoform D1 and isoform D2 inhibit UV-damaged DNA repair. |