From: Novel APC gene mutations associated with protein alteration in diffuse type gastric cancer
Codon | Mutation | Amino acid change | Sift score | Polyphen2 score | SNPs & GO Effect/RI | Sample Frequency | Motifs | Domains | Amino acid property Change |
---|---|---|---|---|---|---|---|---|---|
1058 | GAT > GGTa | Asp(D) > Gly(G) | Pathological | 0.37 (Pathogenic) | Disease/3 | 5% | -- | Beta‐Catenin Binding | • The charge of the wild-type residue will be lost, this can cause loss of interactions with other molecules or residues • The mutation introduces a more hydrophobic residue at this position. This can result in loss of hydrogen bonds and/or disturb correct folding. |
1083 | GAT > GAG | Asp(D) > Glu(E) | Natural | 0.08 (Benign) | Natural/1 | 5% | -- | -- | • The mutant residue is bigger, this might lead to bumps. |
1108 | AAT > AGT | Asn(N) > Ser(S) | Natural | 0.08 (Benign) | Disease/0 | 15% | -- | Beta‐Catenin Binding | • The mutation introduces a more hydrophobic residue at this position. This can result in loss of hydrogen bonds and/or disturb correct folding. |
1247 | GCC > ACC | Ala(A) > Thr(T) | Natural | 0.10 (Benign) | Natural/3 | 15% | GSK3 phosphorylation site | Beta‐Catenin Binding | • The hydrophobicity of the wild-type and mutant residue differs. • Hydrophobic interactions, either in the core of the protein or on the surface, will be lost. |
1307 | ATA > AAAa | Ile(I) > Lys(K) | Pathological | 0.72 (Pathogenic) | Disease/7 | 5% | WDR5 WD40 repeat (blade 5,6)‐binding ligand | Beta‐Catenin Binding | • The mutation introduces a charge, this can cause repulsion of ligands or other residues with the same charge. |
1317 | GAA > CAA | Glu(E) > Gln(Q) | Pathological | 0.41 (Pathogenic) | Disease/4 | 10% | Glycosaminoglycan attachment site | Beta‐Catenin Binding | • The charge of the wild-type residue will be lost, this can cause loss of interactions with other molecules or residues. |