2.3.3.8	acetylation	human knee osteoarthritis chondrocytes exhibit increased ACLY activation (assessed by Ser-455 phosphorylation), associated with increased H3K9 and H3K27 acetylation	757200	
2.3.3.8	acetylation	the enzyme is activated by acetylation at lysine residues 540, 546, and 554	756333	
2.3.3.8	phosphoprotein	-	703014, 735902	
2.3.3.8	phosphoprotein	human knee osteoarthritis chondrocytes exhibit increased ACLY activation (assessed by Ser-455 phosphorylation), associated with increased H3K9 and H3K27 acetylation	757200	
2.3.3.8	phosphoprotein	phosphorylation of recombinant human ATP:citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Cyclic AMP-dependent protein kinase catalyzes the incorporation of 1 mol of phosphate per mol of enzyme homotetramer, and glycogen synthase kinase-3 incorporated an additional 2 mol of phosphate into the phosphorylated protein	488221	
2.3.3.8	phosphoprotein	phosphorylation of the enzyme at Thr446, Ser450 and Ser454 is enhanced by glucagon, insulin, vasopressin and transforming growth factor beta1	718760	
2.3.3.8	phosphoprotein	the enzyme is activated by phosphorylation	756333	
2.3.3.8	side-chain modification	citrate lyase phosphorylation by cAMP-dependent protein kinase or this kinase plus glycogen synthase kinase-3 decreases the maximal velocity whereas the apparent Km for citrate is unchanged	488205	
2.3.3.8	side-chain modification	contains 2 mol phosphate per mol of tetramer	488191, 488199	
2.3.3.8	side-chain modification	histidine phosphorylation of ATP-citrate lyase is inhibited by vanadate	488210