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As non-sense mutations probably change protein function, we category them as functional variants, and assign them the highest quantitative weight among others.
There were no nucleotide and/or codon substitutions predicted to change protein function that correlated with resistant and susceptible phenotypes.
Still, many of those mutations were predicted to change protein function.
We compared disease-associated single point mutations (nsSNPs) predicted to change protein function with those of unknown disease-association.
This is because, even where they change the amino acid sequence of a protein, not all genetic variants change protein function or cause disease.
These findings are consistent with H2O2 effects being mediated through the production of RLS, which are well known to modify proteins and change protein function.
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Post-translational modifications (PTMs) play an important role in modulating diverse cellular processes, which can change protein functions by introducing new functional groups such as phospho, acetyl, ubiquityl and methyl groups (Huang et al. 2015; Santos et al. 2011).
Proteins function through interactions and mutations that disrupt interactions also change protein functions.
In mutation databases, like COSMIC [ 50, 55], there are thousands of experimentally verified cancer mutations but the precise mechanisms of mutations, how they change protein functions and contribute to cancer pathogenesis is unknown [ 56].
How acetylation is brought about and how it changes protein function is poorly understood.
Third, identification of the glutamine residues modified by 5-HT biotin/5-HT would be helpful in ultimately allowing for determination of how serotonylation changes protein function.
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