TABLE 3.
Histone H3 and H4 residues that are known or potential targets of acetylation, methylation, and phosphorylation in S. cerevisiae
| Histone residue | Modificationa | Exists in S. cerevisiaeb |
| H3-R2 | Methylation | |
| H3-K4 | Methylation | Yes |
| H3-K9 | Acetylation | Yes |
| H3-K9 | Methylation | |
| H3-S10 | Phosphorylation | |
| H3-14 | Acetylation | Yes |
| H3-R17 | Methylation | |
| H3-K18 | Acetylation | Yes |
| H3-K23 | Acetylation | Yes |
| H3-R26 | Methylation | |
| H3-K27 | Acetylation | Yes |
| H3-K27 | Methylation | |
| H3-S28 | Phosphorylation | |
| H3-K36 | Methylation | Yes |
| H3-R53 | Methylation | |
| H3-K56 | Acetylation | Yes |
| H3-K79 | Methylation | Yes |
| H3-K115 | Acetylation | |
| H3-K122 | Acetylation | |
| H4-S1 | Phosphorylation | Yes |
| H4-K5 | Acetylation | Yes |
| H4-K8 | Acetylation | Yes |
| H4-K12 | Acetylation | Yes |
| H4-K16 | Acetylation | Yes |
| H4-K20 | Acetylation | |
| H4-K20 | Methylation | |
| H4-K31 | Acetylation | |
| H4-S47 | Phosphorylation | |
| H4-K59 | Methylation | |
| H4-K77 | Acetylation | |
| H4-K79 | Acetylation | |
| H4-K79 | Methylation | |
| H4-K91 | Acetylation | Yes |
| H4-R92 | Methylation |
a
Identified in bovine (Zhang et al. 2003; Mersfelder and Parthun 2006). Some histone modifications are known to exist in S. cerevisiae.
b
Reference describing histone modifications in S. cerevisiae include Suka et al. (2001); Ng et al. (2002); van Leeuwen et al. (2002); Ye et al. (2005); F. Xu et al. (2005); Masumoto et al. (2005); Hyland et al. (2005); Cheung et al. (2005); Mersfelder and Parthun (2006); Zhang (2008).