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. 2023 Sep 11;20:208. doi: 10.1186/s12974-023-02879-7

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© The Author(s) 2023

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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Identification of Kla proteome profile in BV2 cells. A Schematic representation of the experimental workflow of TMT labeling, affinity enrichment and mass spectrometry-based quantification of Kla in BV2_NC and BV2_Dox. B Pie chart displaying the distribution of the number of identified Kla sites per protein. C Motif analysis for the identified Kla proteins. D Icelogo representation showing flanking sequence preferences for all Kla sites between the upstream + 10 position and the downstream − 10 position. E Distribution of all lysines and lactylated lysines in the structured regions of proteins. F Bar graphs showing the representative ontology annotations enriched with Kla proteome