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Browse result for Down-regulation in Deamidation
※ introduction Deamidation is a chemical reaction in which an amide functional group in the side chain of the amino acids asparagine or glutamine is removed or converted to another functional group. Typically, asparagine is converted to aspartic acid or isoaspartic acid. Glutamine is converted to glutamic acid or pyroglutamic acid (5-oxoproline). In a protein or peptide, these reactions are important because they may alter its structure, stability or function and may lead to protein degradation. The net chemical change is the addition of a water group and removal of an ammonia group, which corresponds to a +1 (0.98402) Da mass increase. Although deamidation occurs on glutamine, glycosylated asparagine and other amides, these are negligible under typical proteolysis conditions.
Reference
Wiki: Deamidation
Reference
Wiki: Deamidation
| PTMD ID | UniProt Accession | Entrez ID | Gene Name | Protein Name | Organism |
|---|---|---|---|---|---|
| PTMD00623 | P60174 | 7167 | TPI1 | Triosephosphate isomerase | Homo sapiens |
