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. 2018 Sep 24;6:99. doi: 10.1186/s40478-018-0600-7

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© The Author(s). 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 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.

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Fig. 1 — PKCγ mutations. a Domain structure of PKCγ. The localization of all reported SCA14 mutations is indicated. The two mutations investigated in this study (H36R, H101Q) are highlighted in bold. PKCγ is phosphorylated (P) at three conserved sites: at T514 in the catalytic domain and at T655 and T674 in the C-tail. PS: pseudosubstrate. b Sequence alignment of the two cysteine-rich subdomains C1A and C1B. The histidine residues at positions 36 and 101 (highlighted in bold) are located at equivalent positions within the two subdomains