This entry represents Det1 family proteins []. Det1 (de-etiolated-1) is an essential negative regulator of plant light responses, and it is a component of the Arabidopsis CDD complex containing DDB1 and COP10 ubiquitin E2 variant. Mammalian Det1 forms stable DDD-E2 complexes, consisting of DDB1, DDA1 (DET1, DDB1 Associated 1), is a member of the UBE2E group of canonical ubiquitin conjugating enzymes and modulates Cul4A function [].
DNA damage-binding protein 2 (DDB2) is required for DNA repair. It 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 []. It is also involved in the initiation of nucleotide excision repair via an ubiquitin ligase complex together with DDB1 and CUL4A (cullin 4A) [].
DDA1 is a core subunit of multiple Cul4-based E3 ligases (CRL4s), involved in ubiquitination and subsequent proteasomal degradation of target proteins, which regulate key developmental and stress responses in eukaryotes [, ]. In mammals, DDA1 binds to DET1 and DDB1 to form DDD complexes, which recruit specific ubiquitin-conjugating UBE2E enzymes to form DDD-E2 complexes []. The DDD-E2 complex provides a platform for interaction with Cul4A and beta-transducing (also called WD40) repeat proteins. DDA1 is conserved in higher eukaryotes, including Arabidopsis [].
This entry represents the N-terminal domain of DDA1 (DET1- and DDB1-associated protein 1) ubiquitin ligase, which binds strongly with Det1 (De-etiolated 1) and DDB1 (Damaged DNA binding protein 1 associated 1). Together DDA1, DDB1 and Det1 form the DDD core complex, which recruits a specific UBE2E enzyme to form specific DDD-E2 complexes []. Component of the DDD-E2 complexes which may provide a platform for interaction with cul4a and WD repeat proteins. These proteins may be involved in ubiquitination and subsequent proteasomal degradation of target proteins.
