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. 2021 Jan 19;21:82. doi: 10.1186/s12885-021-07806-8

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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. 1 — Validation of K607E mutation on BCOR. a Schematic representation of mutation position and functional domains of the BCOR protein. b Representative sequencing traces of wild-type and K607E mutant BCOR. Lysine (AAG) was changed to Glutamic acid (GAG) at the 607th amino acid of BCOR. Left panel shows sequence obtained from the wild-type genomic DNA. Right panel shows sequence obtained from an NK/T-cell lymphoma sample. Arrows and red letters denote the location of the base change. The mutant sequence trace shows heterozygosity. c The genomic DNA of BCOR from lymphoma patients was analyzed by PCR amplification and Sanger sequencing. BBD, BCL6 Binding Domain; AF9BD, AF9 Binding Domain; ANK, Ankyrin Repeats