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. Author manuscript; available in PMC: 2017 Feb 23.
Published in final edited form as: Methods Enzymol. 2016 Feb 16;574:31–52. doi: 10.1016/bs.mie.2016.01.008

Fig. 1.

Fig. 1

The dynamic regulation of lysine methylation on histone H3. Shown are major sites of methylation (me), acetylation (ac), and phosphorylation (p) on the N-terminal tail domain of histone H3. Known writers (methyltransferases; KMTs) and erasers (demethylases; KDMs) of lysine methylation are clustered by major histone substrate residue(s). Methylation products and substrates (mono-, me1; di-, me2; tri-, me3) of KMT and KDM reactions, respectively, are listed. Enzyme identification reflects both conventional and generic (Allis et al., 2007) nomenclature.