Histone acetyltransferases (HATs) involved in histone modifications are referred to as A-type or nuclear HATs. They can be grouped into at least four families based on sequence conservation within the HAT domain: Gcn5/PCAF, MYST, p300/CBP and Rtt109. The p300/CBP and Rtt109 families are specific to metazoans and fungi respectively (Marmorstein & Trievel 2009). Gcn5/PCAF and MYST family members have no significant sequence homology but share a globular alpha/beta fold with a common structure involved in acetyl-Coenzyme A (ACA) binding. Both use a conserved glutamate residue for the acetyl transfer reaction but may not share a common catalytic mechanism (Trievel et al. 1999, Tanner et al. 1999, Yan et al. 2002, Berndsen et al. 2007). The p300/CBP HAT domain has no homology with the other families but some structural conservation within theACA-binding core (Liu et al. 2008). In addition to histone acetylation, members of all 3 human HAT families have been shown to acetylate non-histones (Glozak et al. 2005).
HATs and histone deacetylase (HDAC) enzymes generally act not alone but as part of multiprotein complexes. There are numerous examples in which subunits of HAT or HDAC complexes influence their substrate specificity and lysine preference, which in turn, affect the broader functions of these enzymes (Shahbazian & Grunstein 2007).
N.B. The coordinates of post-translational modifications represented and described here follow UniProt standard practice whereby coordinates refer to the translated protein before any further processing. Histone literature typically refers to coordinates of the protein after the initiating methionine has been removed. Therefore the coordinates of post-translated residues in the Reactome database and described here are frequently +1 when compared with the literature.