Novel PTM site detection - (Apr/23/2012 )
Hi, Im currently looking at a transmembrane protein with implications in literature of being involved in cell adhesion and other processes. Similar proteins are trapped in the ER/golgi before shuttled to the membrane in a signal dependent manner, with thier cytoplasmic "tail" regions.
The "tail" for this protein is quite different to other family members, and very little data is avaliable as to its interactors and PTM. analysing primary sequences and computed seconday structure have shown its tail is highly disordered, and lacks many of the features more well characterised family members have (SH3 binding sequences, tyrosine residues).
Sequence analysis has shown this protein does have a few S/T that could be phosphorylatable, as well as a few lysine residues that could be Ubiquitylated.
my question is this. How would it be possible to detect/ prove any post translational modifications on this section of the protein, given only a small change in mass?