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Fig. 5 | BMC Genomics

Fig. 5

From: Self-regulation of functional pathways by motifs inside the disordered tails of beta-catenin

Fig. 5

a Interaction partners of beta-Catenin (CTNNB1). The interaction partners were extracted from the STRING database using threshold value 0.85. The colors of the symbols indicate the fraction of disordered residues in that protein, categorized into three groups: blue (0–30 % of residues are intrinsically disorder), pink (30–50 %), and red (>50 %). The shapes of the symbols specify the number of interaction partners of that protein: Circle - less than five partners; Hexagon - more than five interaction partners. Lines between proteins imply that these two proteins interact with each other. b Abundance of intrinsic disorder in the secondary interactome of beta-Catenin. The secondary interactome refers to all the proteins that interact with one of the interaction partners of beta-Catenin. X-axis presents proteins in the first interactome shown in (A). All the proteins were ranked based on the fractions of disordered residues, with (I), (II), and (III) corresponding to the red, pink, and blue groups in (A), respectively. The first Y-axis on left-hand side shows the number of residues in each protein (gray bar) and the number of disordered residues in each protein (pink bar). The second Y-axis on the right-hand side uses stacked bars to show the distribution of intrinsic disorder in all the interaction partners of that protein indicated on X-axis. From bottom to top, the bars indicate number of proteins with 0–30 % of disordered residues (dark gray), number of proteins with 30–50 % of disordered residues (green), and number of proteins with more than 50 % of disordered residues (dark green). Both the first and the second Y-axes use base-10 log scale

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