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. 2017 Dec 13;7:17486. doi: 10.1038/s41598-017-17756-6

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© The Author(s) 2017

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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Characteristics of the 2-hydroxyisobutyrylated sites. (a) Conserved motifs of 2-hydroxyisobutyryl-21-mers flanking the modification sites (‘K’ in position 0). The size of each letter correlates to the frequency of that amino acid residue occurring in that position. (b) Frequency of each motif occurred in the identified 2-hydroxyisobutyrylated peptides. (c) Heat map of the amino acid compositions around the 2-hydroxyisobutyrylation sites. The –log10 (Fisher’s exact test p value) for every amino acid in each position (from −10 to 10) is shown. (d) Secondary structure and surface accessibility analyses of 2-hydroxyisobutyrylated lysine residues.