Lysine acetyltransferases (KATs) catalyze the transfer of acetyl groups from acetyl-CoA to lysine residues. Our proteomic analysis revealed that KAT6A is acetylated at lysine 815 (K815), corresponding to mouse K816, in the hearts of mice fed a ketogenic diet under high blood pressure. To identify changes in KAT6A interaction partners by K815 acetylation in cardiomyocytes, we performed LC-MS/MS proteomics. We transfected adenovirus-carrying FLAG-KAT6A-wild type (WT, Control (Ctrl)), -K815R (an acetylation resistant mutant, KR), and -K815Q (an acetylation mimetic mutant, KQ) into cardiomyocytes for 2 days. Adenovirus-carrying FLAG was used as a control. KAT6A was immunoprecipitated with anti-FLAG affinity beads, followed by washing, competitive elution with 3x FLAG peptides, and separation by SDS-PAGE.