Table 1. Summary of PTM abundance.
A) H1 canonical | |||||||||||||||||||||
Residue | - | S1 | T3 | S4 | K16 | S/T17 | K21 | K25 | S28 | K33 | T34 | S35 | K45 | S50 | K51 | K96 | K109 | S112 | K167 | S171 | S186 |
N-term Acetylation | 58% | ||||||||||||||||||||
Phosphorylation | 22% | 12% | 27% | 24% | 7% | 5% | 6% | 100% | 100% | ||||||||||||
Acetylation | 1% | <1% | 1% | <1% | <1% | 2% | 3% | ||||||||||||||
Monomethylation | 2% | 1% | 1% | ||||||||||||||||||
Dimethylation | 2% | 1% | 1% | 2% | |||||||||||||||||
Crotonylation | 1% |
The site, type and level of modification site occupancy of each PTM is indicated for each histone. For each PTM, the level of modification site occupancy is calculated by dividing the number of instances that a PTM was detected by the number of instances that a given amino acid was observed, providing an estimation of the relative abundance of each PTM. Sites of phosphorylation, which were detected only in IMAC/TiO2 enriched fractions, are not listed. Residues are numbered starting with the first residue after the cleaved methionine. Canonical H1 (1A), H2A (1B), H2B (1C), H3 (1D), and H4 (1E) histones are shown which represent sequences common across all subtypes.