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The signaling capabilities of FGFR1 at the serine 777 site can be weakened by phosphorylation. Serine 1047 and serine 1048 have been linked to the decreased binding affinity of ubiquitin ligase c-Cbl to EFGR when they are phosphorylated. [61] When serine 349 is phosphorylated, the binding affinity between protein complex p62 and the protein ...
Phosphorylation can occur on serine, threonine and tyrosine side chains (in other words, on their residues) through phosphoester bond formation, on histidine, lysine and arginine through phosphoramidate bonds, and on aspartic acid and glutamic acid through mixed anhydride linkages.
However some non-phosphorylated amino acids appear chemically similar to phosphorylated amino acids. Therefore, by replacing an amino acid, the protein may maintain a higher level of activity. For example, aspartic acid can be considered chemically similar to phospho-serine, due to it also carrying a negative charge. Therefore, when an aspartic ...
Serine (symbol Ser or S) [3] [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated ...
Serine and threonine are amino acids which have similar side-chain compositions that contain a hydroxyl group and thus can be phosphorylated by enzymes called serine/threonine protein kinases. The addition of the phosphate group can be reversed by enzymes called serine/threonine phosphatases.
Serine/threonine protein kinases (EC 2.7.11.1) phosphorylate the OH group of serine or threonine (which have similar side chains). Activity of these protein kinases can be regulated by specific events (e.g., DNA damage), as well as numerous chemical signals, including cAMP/cGMP, diacylglycerol, and Ca 2+ /calmodulin.
A substantial number of phosphorylated histone residues are associated with gene expression. Interestingly, these are often related to regulation of proliferative genes. Phosphorylation of serines 10 and 28 of H3 and serine 32 of H2B has been associated with regulation of epidermal growth factor (EGF)-responsive gene transcription.
Kinases are either phosphorylated on serine and/or threonine residues, or solely on tyrosine residues. [5] This serves as a means to classify them as either Ser/Thr- or Tyr-kinases. Several residues within the primary structure may be autophosphorylated simultaneously.