Fig. 6 | Nature Communications

Fig. 6

From: Site-specific characterization of endogenous SUMOylation across species and organs

Fig. 6

Evolutionary conservation of SUMO2/3 structural targeting preferences. a Schematic overview of structural properties of subsets of lysines in human SUMO2/3 target proteins, as compared to structural properties of all other lysines within the same proteins. A relative presence of 100% is indicative of no change as compared to the background. Ubiquitin (ubi) sites were derived from PhospoSitePlus (PSP), and only considered if detected in 3+ studies. “Both” corresponds to lysines detected as SUMOylated in this study, and ubiquitylated in PSP data. “C.” control, “H.” heat, “M.” MG132, “Dis.” disordered, “Gl.-ex.” globular-exposed, “Gl.-bu.” globular-buried. b As (a), but for lysines in mouse SUMO2/3 target proteins. Ubiquitin (ubi) sites were derived from PSP and only considered if detected in 2+ studies. c As (b), but comparing subsets of SUMOylated lysines to subsets of ubiquitylated lysines detected in the same organs in a ubiquitin proteomics study59. d Overview of the average Residue Conservation Scores (RCS) for lysine residues situated in all SUMO2/3 target proteins identified in this study. Error bars represent 10xSEM, n = 16,957 globular-buried, n = 124,495 globular-exposed, and n = 77,828 disordered lysine residues. “Dis.” disordered, “Gl.-ex.” globular-exposed, “Gl.-bu.” globular-buried. e Average delta RCS values derived from pairwise comparisons of all SUMOylated lysine residues to non-SUMOylated lysine residues within the same proteins and structural context. Error bars represent SD, n = 846, n = 754, n = 92, n = 8528, n = 7716, n = 812, n = 5679, n = 4875, and n = 804 pair-wise comparisons for listed values, respectively. **P < 0.001, determined by two-tailed paired Student’s t-testing. “H” human, “M” mouse, “Dis.” disordered, “Gl.-ex.” globular-exposed, “Gl.-bu.” globular-buried

Back to article page