Table 4.

Detection of somatic mutations in APC gene exon 15

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.

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