KAT6A is a histone acetyltransferase that acetylates lysine residues on histone H3 and H4, functioning as a component of the MOZ/MORF complex with histone acetyltransferase activity 1. Beyond histones, KAT6A acetylates the tumor suppressor p53 at specific lysine residues and regulates its transcriptional activity through PML association 2. KAT6A acts as a transcriptional coactivator for RUNX1 and RUNX2 and participates in a "writer-reader" epigenetic module with ENL, where KAT6A-catalyzed H3K9 acetylation recruits ENL to drive leukemogenic gene expression 3. In acute myeloid leukemia (AML), KAT6A drives critical differentiation-blocking gene expression programs; KAT6A inhibition shows strong anti-AML effects in vitro and in vivo 3. In breast cancer, KAT6A is frequently amplified/overexpressed and acetylates H3K23; selective KAT6A/B inhibition reduces estrogen signaling and cell cycle genes, showing efficacy in ER+ breast cancer models refractory to endocrine therapy 4. Combined KAT6A/B and Menin inhibition demonstrates synergistic anti-proliferative effects in ER+ breast cancer with clinical trial activity 5. Pathogenic KAT6A mutations cause Arboleda-Tham syndrome and neonatal leukemia with t(8;16) translocations 6. KAT6A functions broadly in hematopoietic differentiation, stem cell maintenance, and cell cycle regulation 7.