Phenotype-genotype correlation in Hirschsprung disease is illuminated by comparative analysis of the RET protein sequence -- Kashuk et al. 102 (25): 8949 Data Supplement - HTML Page - index.htslp -- Proceedings of the National Academy of Sciences

Kashuk et al. 10.1073/pnas.0503259102.

Supporting Information

Files in this Data Supplement:

Supporting Table 1
Supporting Table 2
Supporting Text
Supporting Figure 4
Supporting Figure 5
Supporting Figure 6
Supporting Figure 7

Supporting Figure 4 Fig. 4.
RET mutations do not localize exclusively within a single functional domain.

Supporting Figure 5 Fig. 5.
Multiple alignment of the human RET protein and 11 vertebrate orthologs.

Supporting Figure 6 Fig. 6.
Enlarged Fig. 2B. Heat plot of the RET protein. The RET protein is displayed in rows, each of 186 residues. The vertical axis of each row represents all 20 amino acids (A-Y, top-bottom). The wild-type residue at each position is represented in black. Tolerance for any change from the wild type to another residue is indicated by color: red, orange, yellow, green, and blue. Red represents changes that are most highly intolerant, progressing towards blue, representing changes that are most likely to be tolerated. Mutations are boxed in white and shown below the corresponding position.

Supporting Figure 7 Fig. 7.
Graph of overlapping relative rates of protein evolution and MAPP scores for RET. Graph of overlapping relative rates of protein evolution and MAPP scores for RET. At each residue, an average was taken of the impact scores for every possible amino acid change. These positional MAPP scores were smoothed with a 19-residue sliding window, similar to the window used for the relative rate calculation.