Figure 1
From: Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?
The human APC protein carries a large predicted disordered domain which is frequently hit by missense mutations in cancer. (A) Schematic representation of the APC scaffold protein and its protein interaction domains. Known interactors are APC (green), CRM1 (orange), PP2A (brown), β-catenin, CtBP (15aa repeats, blue), β-catenin (20 aa repeats, cyan), sequence B (yellow), Axin (SAMP-repeats, purple), Microtubules (dark green) and EB1 (light green). (B) Summary of disorder predictions performed for full-length human APC using different algorithms from publicly available servers [31–35]. Sequence segments with disorder probability above 50% are represented as black bars. (C) Distribution of missense mutations in the APC protein reported in various tumors, categorized as somatic (red), germline (black) or unknown origin (grey). Details on the location and nature of amino acid substitutions can be found in additional file 1, Table S1. (D) Summary of disorder predictions performed for β-catenin (black bars), done as in (B), and β-catenins's helical secondary structure elements as determined by crystallography (gray bars) [36].