Brd2 is a highly conserved member of the BET subfamily of bromodomain proteins that contain two tandem N-terminal bromodomains and a single C-terminal extra-terminal (ET) domain. In addition to its involvement in guiding the expression of cell cycle genes through its binding to multiple E2Fs, Brd2 has been shown to be associated with several regulators of transcription, including TFIID and Swi/Snf complexes. First identified as a nuclear serine/threonine kinase, Brd2, like other bromodomain proteins, is thought to function in mammalian development by regulating chromatin structure and transcription. Brd2 has been shown to bind to histone H4 via acetylated Lys12, a substrate of several histone acetyltransferase transcriptional coactivators.
