Fig. 4
From: Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
Stoichiometry of histone acetylation. a The diagram shows all histone acetylation sites whose stoichiometry was determined in this study. The sites are ordered by descending stoichiometry. Note that high stoichiometry sites occur on the N-termini of core histones. b The stoichiometry of histone acetylation sites as determined in four independent studies17,18,19,20. c An anti-acetylated lysine immunoblot of HeLa whole cell lysate. Cells were boiled in 2% LDS to ensure histone extraction. Histones are annotated based on their expected molecular weight. d Histone acetylation sites constitute a majority of acetylated lysine residues in cells. Stoichiometry and protein copy numbers were used to calculate the number of acetylated lysine residues for the indicated classes of proteins. Source data are provided as a Source Data file
