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. 2019 Nov 7;9:16257. doi: 10.1038/s41598-019-52723-3

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© The Author(s) 2019

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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Putative lysine residues acetylated on endogenous DVL-1 under different oxygen tension and their approximate location on DVL structural domain. (A) The table indicates putative lysine residues on DVL-1 that were found to be acetylated under different oxygen tension (2.5% O₂ and 20% O₂) in MDA-MB-231 and MDA-MB-468 cells along with their representative peptide as detected by liquid chromatography mass spectrometry (LC-MS/MS) analyses. (B) Approximate representation of position of acetylated lysine (K) residues on DVL-1 conserved domain is shown. NH₂ represents N-terminal; followed by amino-terminal DIX domain, a central PDZ, and a carboxyl-terminal DEP domain, and C representing C-terminal.