Table 1.
Summary of the data sets of post-translational modifications. All modifications were extracted from Swiss-Prot and HPRD. Glycosylation sites were also extracted from O-GlycBase and PDB. Phosphorylation sites were additionally extracted from PDB, phospho.ELM, PhosphoSite, and phosphoPOINT.
| Post-translational modification | Total sites | Total proteins | Human sites | Human proteins |
|---|---|---|---|---|
| Phosphorylation | 62,269 | 17,116 | 30,838 | 8,428 |
| N-linked glycosylation | 4,971 | 2,257 | 2,181 | 906 |
| O-linked glycosylation | 2,853 | 367 | 295 | 93 |
| Acetylation | 2,600 | 1,896 | 1,024 | 677 |
| Amidation | 2,163 | 1,339 | 44 | 30 |
| Hydroxylation | 1,301 | 251 | 211 | 29 |
| Proteolytic cleavage | 1,285 | 531 | 1,285 | 531 |
| Methylation | 911 | 407 | 430 | 143 |
| Pyrrolidone carboxylic acid | 728 | 590 | 78 | 74 |
| Ubiquitination | 516 | 353 | 266 | 196 |
| Carboxylation | 447 | 122 | 88 | 15 |
| SUMOylation | 381 | 201 | 319 | 160 |
| Palmitoylation | 328 | 200 | 163 | 88 |
| Sulfation | 229 | 145 | 80 | 38 |
| Myristoylation | 156 | 153 | 61 | 58 |