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Methylation been found on a range of lysine residues in numerous histones: K4 (using the one-letter amino-acid code for lysine), K9, K27, K36 and K79 in histone H3, law firms K20 in histone H4, K59 in the globular area of histone H4 2 and K26 of histone H1B three A number of proteins chargeable for the methylation of specific residues have been characterized, and all however one in all these accommodates a SET domain; they make up the SET-area protein methyltransferase household (Desk 1 ).

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The exception to the rule is the DOT1 household, members of which methylate K79 in the globular area of histone H3 and that are structurally not associated to SET-area proteins 4 - 6 Current work suggests that SET-area-containing proteins methylate just a few proteins along with histones (see later); they need to due to this fact be named protein lysine methyltransferases slightly than histone lysine methyltransferases.

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These tails are subject to several submit-translational covalent modifications, including acetylation, phosphorylation, ubiquitination, sumoylation and methylation (reviewed in 1 ).