Bromodomain adjacent to zinc finger domain protein 1A (BAZ1A)

Bromodomain adjacent to zinc finger domain protein 1A (BAZ1A) is a regulatory subunit of the ATP-dependent chromatin assembly factor (ACF) and chromatin accessibility complex (CHRAC), both members of the imitation switch (ISWI) family of chromatin remodeling complexes[1][2][6]. BAZ1A contains a plant homeodomain (PHD) zinc finger, a bromodomain, a WAC motif, and a leucine-rich helical motif[1][2]. It functions as an epigenetic reader and is involved in the dynamic assembly and spacing of nucleosomes, thereby enabling chromatin to be remodeled in processes like DNA replication, gene transcription, and DNA repair[1][2][6]. BAZ1A directly cooperates with the ATPase SMARCA5, plays a critical role in various DNA repair pathways (nucleotide excision repair, non-homologous end joining, homologous recombination), and regulates gene expression, partly through transcriptional suppression of genes such as those under control of the vitamin D receptor[1][3][5]. Variants in BAZ1A are linked to neurodevelopmental disorders, including intellectual disability, and may affect pathways such as vitamin D metabolism and Wnt signaling[3][5][6]. BAZ1A is considered a potential drug target in epigenetics but, as of now, there are no small molecule drugs specifically targeting BAZ1A clinically reported[1].

Other names

ACF1WCRF180HSPC317hACF1WALp1Williams syndrome transcription factor-related chromatin-remodeling factor 180ATP-dependent chromatin remodeling proteinATP-utilizing chromatin assembly and remodeling factor 1CHRAC subunit ACF1hWALp1

Epigenetic regulation via chromatin remodeling; Reader of epigenetic marks (acetyl-lysine)