Summary

Name DDB1
Full Name DNA damage-binding protein 1
Synonyms DDB p127 subunit, DNA damage-binding protein a, DDBa, Damage-specific DNA-binding protein 1, HBV X-associated protein 1, XAP-1, UV-damaged DNA-binding factor, UV-damaged DNA-binding protein 1, UV-DDB 1, XPE-binding factor, XPE-BF, Xeroderma pigmentosum group E-complementing protein, XPCe | XAP1
Primary ID Q16531
Links - -
Type protein
Relations 9
Function 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:15448697, PubMed:14739464, PubMed:16260596, PubMed:16482215, PubMed:17079684, PubMed:16407242, PubMed:16407252, PubMed:16940174). 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:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). Also functions 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 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:28886238). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460). 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 (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621). 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 (PubMed:17041588). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity).

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Relations

Regulator Mechanism target score
+ form complex img/form-complex.png binding DDB2/DDB1 0.936
Publications: 1 Organism: Homo Sapiens
+ form complex img/form-complex.png binding EDVP 0.393
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/direct_inhibition.png deacetylation DDB1 0.364
Publications: 1
+ up-regulates img/indirect-activation.png DDB1 0.7
Publications: 1
+ up-regulates img/direct-activation.png binding E2F1 0.358
Publications: 1 Organism: Homo Sapiens
+ up-regulates img/indirect-activation.png RAD23A 0.587
Publications: 1
+ form complex img/form-complex.png binding DCX DET1-COP1 0.892
Publications: 1 Organism: Homo Sapiens
+ form complex img/form-complex.png binding Cullin4-RBX1-DDB1 0.917
Publications: 1 Organism: Homo Sapiens
+ up-regulates img/indirect-activation.png RAD23B 0.631
Publications: 1