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

The exception to the rule is the DOT1 family, members of which methylate K79 within the globular area of histone H3 and which are structurally not associated to SET-domain proteins 4 - 6 Latest work suggests that SET-domain-containing proteins methylate a number of proteins along with histones (see later)