Proteomics data for PML peptides modified by phosphorylation, SUMO1 or SUMO2/3. Relating to Fig. S1 and Fig. 6. (A) Schematic representation of the PML-V sequence with sites of phosphorylation identified in this study indicated. Relative phosphopeptide intensity at each site is approximated by circle size. Positions of proline residues are shown by red bars. (B) Average (column) and SEM (bars) for the sum all phosphopeptide intensities identified in each sample prepared in the proteomics experiment described in Fig. S1. Ordinary one-way ANOVA P value is indicated. Number of purifications, n = 4. (C) As in B but showing the contribution of individual sites to overall peptide intensities. (D) Schematic representation of the PML-V sequence indicating sites of SUMO1 (left) and SUMO2/3 (right) modification identified in this study. Relative peptide intensity at each site is approximated by circle size. (E) Column charts of average intensity values for the SUMO1 (left) and SUMO2/3 (right) branched peptides diagnostic of PML modification at the indicated sites. Error bars show SEM (n = 4). (F)t test summary for the pairwise comparisons indicated for each SUMO-PML modification. Welch’s correction was applied for heteroskedastic data. Red entries are P < 0.05, and boxed values show sites where SUMO-PML peptide intensities were significantly higher for the mutant than the WT (last four columns). The number of different peptides used for each site is indicated (evidence count).