wiki.Alumni.NET - Your Location Information Resource
Protein phosphorylation
From wiki.Alumni.NET
(New page: [Protein phosphorylation]http://www.creative-proteomics.com/services/phosphorylation.htm is the most commonly studied area of post-translational modification since it plays a vital role in...) |
|||
| Line 1: | Line 1: | ||
[Protein phosphorylation]http://www.creative-proteomics.com/services/phosphorylation.htm is the most commonly studied area of post-translational modification since it plays a vital role in intracellular signal transduction and is involved in regulating cell cycle progression, differentiation, transformation, development, peptide hormone response, and adaptation. It has been estimated that one third of mammalian proteins may be phosphorylated and this modification often plays a key role in modulating protein function. Reversible protein phosphorylation, principally on serine, threonine or tyrosine residues, is one of the most important and well-studied post-translational modifications. | [Protein phosphorylation]http://www.creative-proteomics.com/services/phosphorylation.htm is the most commonly studied area of post-translational modification since it plays a vital role in intracellular signal transduction and is involved in regulating cell cycle progression, differentiation, transformation, development, peptide hormone response, and adaptation. It has been estimated that one third of mammalian proteins may be phosphorylated and this modification often plays a key role in modulating protein function. Reversible protein phosphorylation, principally on serine, threonine or tyrosine residues, is one of the most important and well-studied post-translational modifications. | ||
| + | |||
| + | [protein n-acetylation]http://www.creative-proteomics.com/services/n-acetylation.htm, or the transfer of an acetyl group to nitrogen, occurs in almost all eukaryotic proteins through both irreversible and reversible mechanisms. N-terminal acetylation requires the cleavage of the N-terminal methionine by methionine aminopeptidase (MAP) before replacing the amino acid with an acetyl group from acetyl-CoA by N-acetyltransferase (NAT) enzymes. This type of acetylation is co-translational, in that N-terminus is acetylated on growing polypeptide chains that are still attached to the ribosome. While 80-90% of eukaryotic proteins are acetylated in this manner, the exact biological significance is still unclear. | ||
Revision as of 06:28, 12 October 2016
[Protein phosphorylation]http://www.creative-proteomics.com/services/phosphorylation.htm is the most commonly studied area of post-translational modification since it plays a vital role in intracellular signal transduction and is involved in regulating cell cycle progression, differentiation, transformation, development, peptide hormone response, and adaptation. It has been estimated that one third of mammalian proteins may be phosphorylated and this modification often plays a key role in modulating protein function. Reversible protein phosphorylation, principally on serine, threonine or tyrosine residues, is one of the most important and well-studied post-translational modifications.
[protein n-acetylation]http://www.creative-proteomics.com/services/n-acetylation.htm, or the transfer of an acetyl group to nitrogen, occurs in almost all eukaryotic proteins through both irreversible and reversible mechanisms. N-terminal acetylation requires the cleavage of the N-terminal methionine by methionine aminopeptidase (MAP) before replacing the amino acid with an acetyl group from acetyl-CoA by N-acetyltransferase (NAT) enzymes. This type of acetylation is co-translational, in that N-terminus is acetylated on growing polypeptide chains that are still attached to the ribosome. While 80-90% of eukaryotic proteins are acetylated in this manner, the exact biological significance is still unclear.
