Fig. 4: Characteristics of site-specific N-glycoproteome identified in five species.

a Distribution of singly and multiply glycosylated proteins in each species. b Distribution of the number of glycans at each site in each species. c, Distribution of glycan size in each species. d Cellular localization of glycoproteins and the distribution of different glycan types on cellular localization in each species. e Recognition sequence motifs and the distribution of glycan types on different motifs in each species. (NXS/NXT, where N is asparagine, X is any amino acid except proline, S is serine, T is threonine; Others refer to N-X-Any motifs, where N is asparagine, X is any amino acid except proline, and Any represents any amino acid except serine and threonine.). f Secondary structure localization and the distribution of different glycan types on secondary structures in each species. In the Fig. 4d–f, the distribution of each glycan type was determined by normalizing through dividing the number of GPSMs for a glycan type within one category by the total number of GPSMs in that specific category (Supplementary Data). The secondary structure information in each species in Fig. 4f was obtained using a previously reported 3-state protein secondary structure prediction method⁵⁷ (Supplementary Note 7). g Correlation of overall site-specific glycosylation in five mouse tissues. h Correlation of overall site-specific glycosylation in three plant organs. In Fig. 4g, h, the correlation of tissue/organ-specific site-specific glycosylation in five mouse tissues and three plant organs is depicted using Pearson correlation analysis of the GPSMs in each species/organ. The numerical values in the heatmap represent the degree of correlation, with values closer to 1 indicating higher inter-tissue/organ correlation, while values closer to 0 indicating lower inter-tissue/organ correlation.