Skip to main content
. Author manuscript; available in PMC: 2015 Mar 1.
Published in final edited form as: ChemMedChem. 2014 Jan 21;9(3):511–522. doi: 10.1002/cmdc.201300444

Figure 1.

Figure 1

Schematic representations of human histone deacetylases (HDACs) with the locations of their conserved deacetylase domains; their respective superfamilies are indicated through the color of their deacetylase domains. Both classical HDACs and sirtuins are organized by homology class. Shown are Zn2+ (blue) and NAD+-dependent (red) deacetylase domains, their percentage identity and similarity to a class archetype (e.g., HDAC1, HDAC5, SIRT1), and total protein length in amino acids. HDAC11 has homology to both HDAC1 and HDAC5; the latter values are shown in parentheses. Also indicated are the locations of validated KDAC post-translation modifications including acetylation (orange A, top), SUMOylation (green S), ubiquitination (black U), and phosphorylation (red inverted P, bottom).