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These tails are subject to a number of post-translational covalent modifications, including acetylation, phosphorylation, ubiquitination, sumoylation and methylation (reviewed in 1 ). Methylation been discovered on a range of lysine residues in numerous histones: K4 (utilizing the [only-letter amino-acid](http://gitlab.tangguo.ren/jimcheel951463/3881car-insuring/issues/1) code for lysine), K9, K27, K36 and K79 in histone H3, K20 in histone H4, K59 in the globular domain of histone H4 2 and K26 of histone H1B 3 A number of proteins chargeable for the methylation of particular residues have been characterized, and all however one among these contains a SET area |
