Additionally, mutations in residues neighboring the binding site also show the same trend in an altered EC50 and cooperativity but with no apparent effect on cell surface expression or trafficking, such as the FHH/NSHPT mutations S171N, R227Q, R227L, S296N, F351V, W352X, C395R, G397R, the ADH mutations E191K, E241K, Q245R, and cancer-associated mutations, S169F and S171G. This evidence concerns the gene CASR and cancer.