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. 2021 Oct 4;11:19661. doi: 10.1038/s41598-021-98673-7

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© The Author(s) 2021

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 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/.

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Generation of NBS1 I171V knock-in HCT-116 cells. (a) Structure of human NBS1 protein. NBS1 contains FHA and BRCT1/2 domains at the N terminus and several DNA repair protein-binding regions at the C terminus. FHA and BRCT1/2 domains are involved in the IR-induced nuclear foci with phosphoproteins such as γ-H2AX. NBS1 I171V is located in the BRCT1 domain. (b) Sanger sequencing confirmed NBS1 I171V heterozygosity in ovarian cancer patient 18. (c) Targeting strategy for NBS1 I171V knock-in using the CRISPR/Cas9 system. Blue bases indicate silent mutations. (d–f) Sanger sequencing of NBS1^+/+ parental HCT116 cell (d), NBS1^+/+-edited HCT116 cell clone 1 (e), NBS1^I171V/I171V-edited HCT116 cell clone 1 (f). A single base substitution of the NBS1 I171V variant and a silent Sca I site are indicated by yellow boxes.