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. 2022 Jul 21;18(10):1104–1114. doi: 10.1038/s41589-022-01062-y

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 3 — (a) Schematic representation of data analysis and interpretation strategies of combining phosphoproteomics with solubility proteome profiling. (b) Scatter plot comparing the reproducibility of phosphopeptides solubility measurements (in log₂ scale) from three independent replicates from RNA-preserved and RNA-digested lysate. (c) Bar plot representation of number of phosphorylated serine (S), threonine (T) and tyrosine (Y) residues identified in this dataset. (d) Histogram showing the difference in solubility of phosphopeptides and their corresponding unmodified proteins (x-axis in log₂ scale) in RNA-preserved lysate. (e) Histogram showing the difference in RNA-bound fraction of phosphopeptides and their corresponding unmodified proteins (x-axis in log₂ scale). (f) Barplot representing the proportion of single, double and multiple phosphorylation sites containing peptides among differenentially soluble phosphopeptides. Fisher’s exact test was utilized to ascertain the significance. ** p-value < 0.01, * p-value < 0.05.

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