Supplementary Figure 6: SUMO and other PTMs compete for modification of lysines in a set of highly SUMOylated and functionally interconnected proteins. | Nature Structural & Molecular Biology

Supplementary Figure 6: SUMO and other PTMs compete for modification of lysines in a set of highly SUMOylated and functionally interconnected proteins.

From: Uncovering global SUMOylation signaling networks in a site-specific manner

Supplementary Figure 6

(a) STRING network analysis of all proteins where SUMOylation and acetylation occur on at least one of the same lysines. STRING interaction confidence was set at 0.7 or greater, and the size and color of individual proteins corresponds to the amount of SUMOylation sites per protein.

(b) As (a), but with SUMOylation and ubiquitylation occurring on at least one of the same lysines.

(c) As (a), but with SUMOylation, acetylation and ubiquitylation occurring on at least one of the same lysines.

(d) Schematic overview of the amount of SUMOylation sites identified per protein in total, or within the core STRING network (Fig. 6A), or within the three networks corresponding to (a), (b), and (c). Sites shared with the respective other PTMs are displayed in red. Additionally, the total amount of modification sites per protein for ubiquitylation and acetylation are shown.

(e) Overview of STRING analyses depicted in (a), (b), and (c). “Enrichment” is a ratio derived from the observed amount of interactions divided by the expected amount of interactions. “Connected” refers to the percentage of input proteins connected to the core cluster. P values for all individual analyses are < 1E-15.

(f) Overview of relative network score. This score was computed through multiplication of the interaction enrichment ratio, protein network connectivity, and the average STRING confidence of all interactions.

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