Bromodomain adjacent to zinc finger domain protein 2B (BAZ2B)

Bromodomain adjacent to zinc finger domain protein 2B (BAZ2B) is a multidomain histone-binding protein integral to chromatin remodeling and transcriptional regulation, characterized by both plant homeodomain (PHD) and bromodomain (BRD) motifs[1][2][4]. BAZ2B acts as a regulatory subunit of ATP-dependent chromatin remodeling complexes, controlling DNA accessibility during DNA-templated processes such as replication, transcription, and repair[4]. The protein recognizes acetylated lysine residues on histone tails, notably H3K14Ac, mediating recruitment of chromatin remodeling machinery and modulation of gene expression[1]. It represses mitochondrial gene expression, is implicated in neurodevelopment, aging, and cancer, and can be co-opted by viruses for their replication[1][2][3]. Disease associations include neurodevelopmental disorders, susceptibility to sudden cardiac death, and alterations in its levels have been observed in conditions like severe dry eye syndrome[1][4]. Selective small molecule inhibitors that target the BAZ2B bromodomain are under investigation for their potential therapeutic value[5].

Other names

KIAA1476WALp4hWALp4BAZ2Bbromodomain adjacent to zinc finger domain protein 2BWALP4

Inhibitors (such as D9T and UO1) bind to the bromodomain and block its recognition of acetylated lysine residues on histones, thereby altering chromatin remodeling and transcriptional regulation[5].