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. 2024 Jun 8;7:708. doi: 10.1038/s42003-024-06354-8

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Protein subcellular localization retrieved from Uniprot Subcellular Localization. The percentage of proteins in a given localization was determined using keyword analysis. The considered subcellular localizations in the analysis were cytoplasm (red), extracellular space (green), nucleus (dark blue), and plasma membrane (brown). b Protein subcellular localization from Gene Ontology (GO). The percentage of proteins in a particular localization was calculated using the same method as in a. c The percentage of total semi-tryptic peptides across 17 voxels. d The percentage of total miscleaved peptides across 17 voxels. e The ratio of trypsin cleavage at lysine and arginine residues. The trypsin preference of lysine over arginine at the C-term of identified tryptic peptides shown in blue or at the nearest upstream tryptic peptide (identified peptide N_term minus one aminoacid) shown in red was determined. The analysis shows an overall preference for tryptic cleavage at arginine in almost all voxels.