Target type: biologicalprocess
The methylation of the N-terminal serine of proteins. [PMID:20668449]
N-terminal peptidyl-serine methylation is a post-translational modification that involves the addition of a methyl group to the nitrogen atom of the serine residue at the N-terminus of a protein. This modification is catalyzed by a family of enzymes known as N-terminal methyltransferases (NMTs). NMTs use S-adenosyl methionine (SAM) as a methyl donor. The methylation of the N-terminal serine residue can have a significant impact on the protein's structure, function, and stability. For example, N-terminal methylation can:
* Increase the protein's resistance to proteolysis.
* Alter the protein's interaction with other proteins or molecules.
* Affect the protein's localization within the cell.
The biological significance of N-terminal peptidyl-serine methylation is still being investigated, but it is thought to be involved in a variety of cellular processes, including:
* Protein folding and assembly
* Protein trafficking
* Signal transduction
* Gene expression
N-terminal peptidyl-serine methylation is a dynamic modification that can be regulated by various factors, such as cellular stress, developmental stage, and disease state. Its dysregulation has been implicated in various diseases, including cancer, neurodegenerative diseases, and metabolic disorders. Further research is needed to fully understand the roles of N-terminal peptidyl-serine methylation in health and disease.'
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Protein | Definition | Taxonomy |
---|---|---|
N-terminal Xaa-Pro-Lys N-methyltransferase 1 | A methyltransferase-like protein 11A that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9BV86] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
sch-202676 | SCH-202676: An allosteric modulator of both agonist and antagonist binding to G protein-coupled receptors; structure in first source |