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Phosphorylation of Serine
There are a large variety of serine residues, and the phosphorylation of each residue can lead to different metabolic consequences.
 * Protein Kinase N1 is responsible for the phosphorylation of the TNF receptor-associated factor (TRAF1) on Serine 139 under specific conditions. Murine TRAF1 is also phosphorylated by the same kinase, which leads to the silencing of IKK/NF-kB activity. The elimination of phosphorylation on Serine 139 can be achieved by the replacement of TRAF1 with an Alanine residue, which consequently leads to the improved recruitment of TBK1.


 * At the Serine 789 residue, FGFR1 is phosphorylated by RSK2 when the kinase is in its active form. 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.


 * When serine 349 is phosphorylated, the binding affinity between protein complex p62 and the protein Keap1 is strengthened, which is associated with stress response.


 * When serine 337 is phosphorylated by protein kinase A in vitro, the DNA binding efficiency of the p50 subunit of NF-kB is greatly increased.