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. 2017 Jul 28;7:6829. doi: 10.1038/s41598-017-05748-5

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© The Author(s) 2017

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Multiple alignments of TANC N- and C- termini. Colour code based on Clustalx scheme. Linear motifs identified by ELM analysis are reported: DEG_Nend_Nbox_1: N-terminal motif that initiates protein degradation by binding to the N-box of N-recognins; DOC_PP1_RVXF_1: Protein phosphatase 1 catalytic subunit (PP1c) interacting motif; DOC_WW_Pin1_4: IV WW domain interaction motif; MOD_GSK3_1: GSK3 phosphorylation recognition site; MOD_NEK2_1: NEK2 phosphorylation motif; DEG_SCF_TRCP1_1: DSGxxS phospho-dependent degron recognized by F box protein of the SCF-betaTrCP1 complex; LIG_14-3-3_2: 14-3-3-binding motif; DOC_MAPK_1: MAPK docking motifs; LIG_PDZ_Class_1: PDZ-binding motif; LIG_14-3-3_3: 14-3-3-binding motif; LIG_EVH1_1: Proline-rich motif binding to signal transduction class I EVH1 domains. (A). N-terminus, (B). C-terminus.