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. 2017 Aug 31;7:10296. doi: 10.1038/s41598-017-09918-3

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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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Domain Analysis for Acetylated Peptides. (A) A list of annotated domains from UniProt was used to map the acetyl sites identified in this dataset to regions with specific functions, and a total of 300 acetyl sites mapped to specific domains. The full list is in the supplementary material (Supplementary Table S2). (B) Twelve acetyl sites detected in this study for p300 fall within the histone acetyltransferase (HAT) domain. Those highlighted in yellow map on the structure, and the starred sites have previously been reported to occur due to autocatalysis. (C) The previously solved structure of the HAT domain of p300⁵⁸ with four of the identified acetyl sites from this study highlighted in yellow.