Skip to main content

Table 4 Detection of somatic mutations in APC gene exon 15

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.

  1. a- represents Novel mutations (unreported in the database); RI - Reliability Index