ATPase family AAA domain-containing protein 2B (ATAD2B)

ATPase family AAA domain-containing protein 2B (ATAD2B) is a nuclear enzyme belonging to the AAA+ ATPase superfamily and contains an N-terminal bromodomain that recognizes acetylated lysine residues, primarily on histone H4 and H2A tails[1][2][3][5]. This dual functionality—ATPase activity and chromatin reading—positions ATAD2B as a modulator of chromatin structure and gene expression, likely influencing both developmental processes such as neuronal differentiation and the progression of certain cancers[2][3]. While its paralog ATAD2 is thoroughly implicated in oncogenesis, the precise biological functions of ATAD2B are less defined but are thought to overlap in chromatin regulation. ATAD2B’s bromodomain is able to recognize multiple combinations of histone acetyl modifications and remains unaffected by nearby post-translational modifications that restrict its paralog. ATAD2B is of growing interest in epigenetic drug discovery, but selective inhibitors and biomarker utility have not yet been demonstrated in clinical trials[2][5].

Other names

ATAD2BKIAA1240ATPase family AAA domain containing 2BATPase family AAA domain-containing protein 2B

Potential small-molecule inhibition of the bromodomain to block recognition of acetylated histone lysines, thereby altering chromatin structure and affecting gene expression[2][5]; ATPase domain inhibition (theoretical, no specific inhibitors known)