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. 2021 Aug 9;19:339. doi: 10.1186/s12967-021-03004-z

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© The Author(s) 2021

Open AccessThis 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. 2 — Phosphorylation of BCLAF1 Ser290 is significantly increased in gastric cancer. a Total counts of phosphorylated residues in BCLAF1. **p < 0.01 vs. Non-tumor based on Student's t-test. b MS/MS spectrum of pSer290-containing peptide, YSPSQN(pS290)PIHHIPSR in HGC gastric cancer cells. c Dot blotting of the phosphorylated (pSer290) and unmodified (Ser290) peptides with anti-pBCLAF1 (Ser290) antibody. d Western blotting of the total proteins from HGC cells overexpressing WT, S290A and S290D forms of BCLAF. 177 kD, GFP-tagged BCLAF; 150 kD, endogenous BCLAF