The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.
Belongs to the NC2 beta/DR1 family. Contains 1 histone-fold domain.
Phosphorylation regulates its interaction with TBP. Not phosphorylated when bound to DRAP1.
Western blot analysis on immunoprecipitation pellet from (1) 293T cell lysate or (2) 1X PBS (negative control) pulling down DR1 using ab180164 at 1/10 and HRP-conjugated anti-rabbit IgG preferentially detecting the non-reduced form of rabbit IgG.