Fig. 3

a Venn diagram of succinylated proteins identified in SCL patient fibroblasts and in mouse embryonic fibroblasts from Sirt5^−/− mice. Results from this study were compared to data deposited by Park et al.²⁶. b Venn diagram showing number of sites that are susceptible to hyper-succinylation in both conditions. Pairwise sequence alignments identified each lysine showing significant changes in succinylation levels in both data sets. c Boxplot of fold-changes of lysine succinylation found in SCL-deficient patient cells and mouse embryonic fibroblasts from Sirt5^−/− mice (n = 2 control fibroblast samples, n = 3 SCL patient-derived fibroblast samples; n = 2 control fibroblast samples, n = 1 patient-derived myotube samples; A technical replicate of patient-derived myotube samples was used). d Correlation of the number of suK marks on individual proteins found in data sets from SCL patient and Sirt5^−/− fibroblasts. Orange dots indicate the 11 most succinylated proteins in number of modified lysine sites identified in fibroblasts from SCL deficient patients (Total of 189 proteins, r² = 0.54). Gray band indicates 95% confidence interval. Red dots indicate the 11 proteins with the highest number of succinylation sites in SCL patient fibroblasts. e Boxplot showing fold-changes in succinylation of individual lysine residues among the 11 proteins with the highest numbers of suK marks. Note that only sites matched by sequence alignment of our human data to published mouse data are included in this analysis. The boxplots show the median, the first to third quartile, the 1.5x interquartile ranges, and outliers. SuK = succinyl-lysine.