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. 2021 Oct 22;11:20946. doi: 10.1038/s41598-021-00450-z

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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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Prediction of intrinsically disordered regions (IDRs) and phosphorylation sites in TBC1D10C. (a) Intrinsic disorder profiles of the amino acid composition of human TBC1D10C (green dotted line) and human Src (black dotted line) are plotted. Regions of amino acids are considered disordered above the confidence score (cutoff: 0.5; gray dashed line). A (N-terminal)-IDR in TBC1D10C similar to the (N-terminal)-IDR in Src as well as a (C-terminal)-IDR in TBC1D10C that includes the calcineurin interacting region (406–446 aa); (b) 13 and 6 putative phosphorylation sites are shown for the (N-terminal)-IDR in Src and TBC1D10C, respectively; (c) intrinsic disorder profile of the amino acid composition of human TBC1D10C (green dotted line) and human TBC1D10C GAP mutant (blue dotted line) are plotted; (d) prediction of protein-binding sites in the (N-terminal)-IDR of TBC1D10C (green dotted line) and TBC1D10C GAP mutant (blue dotted line) (residue 8, asp, aspartic acid is significantly different predicted as a protein-binding site as a consequence of R141K mutation in TBC1D10C).