Bromodomain and PHD finger containing (BRPF1) protein is a component of the MOZ/MORF complex which has histone H3 acetyltransferase activity. bromodomain of BRPF1 recognizes acetylated histone lysine residues and function as a 'reader' of these epigenetic histone marks to regulate chromatin structure and gene expression by linking associated proteins to the recognized acetylated nucleosomal targets. BRPF1 is known to positively regulate the transcription of RUNX1 and RUNX2. BRPF1 possesses a PWWP (Pro-Trp-Trp-Pro) domain that functions in the association of PWWP domain-containing proteins with chromatin. PWWP domains have been shown to bind DNA and also specifically recognized methylated lysine residues of histones. In doing so they are suspected to be involved in the mediation of the cross-talk between DNA and histone epigenetic marks. Mutations in PWWP domains have been shown to be associated with various human diseases, including cancer.
