Closed ValWood closed 6 years ago
results in GPs like Tryptophan--tRNA ligase, cytoplasmic P23381 DNA repair protein XRCC1 P18887 Poly [ADP-ribose] polymerase 1 P09874 being annotated to protein glycosylation. Seems wrong? but maybe its OK? It might look odd to me because maybe fungi don't have this particular protein modification?
Indeed, "protein ADP ribosylation" is an asserted subclass of "protein glycosylation". This does seem wrong (dates from 2012); it should be directly under "protein modification process", right ?
Thanks, Pascale
From Wikipedia: Many different amino acid side chains have been described as ADP-ribose acceptors. From a chemical perspective, this modification represents protein glycosylation: the transfer of ADP-ribose occurs onto amino acid side chains with a nucleophilic oxygen, nitrogen, or sulfur, resulting in N-, O-, or S-glycosidic linkage to the ribose of the ADP-ribose[14]. Originally, acidic amino acids (glutamate and aspartate) were described as the main sites of ADP-ribosylation. However, many other ADP-ribose acceptor sites such as serine[15][16], arginine[17], cysteine[18], lysine[19], diphthamide[20], phosphoserine[21], and asparagine[22] have been identified in subsequent works. (https://en.wikipedia.org/wiki/ADP-ribosylation)
Maybe a workaround is to distinguish glycosylation processes that incorporate an adenine as part of the glyco moiety from ones that incorporate only monosaccharides and derivatives of them.
Right - another point where biologists and chemists diverge..... :(
I guess my issue is that the ADP-ribosylation and the protein glycosylation appear to occur in completely different contexts.
I don't mind the "nucleotide" part so much
GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity for example, sits comfortably in canonical "protein glycosylation"
but the "ribose" instead of the "hexose" addition appears to be a strong biological partitioning (in ER as part of glycosylation of cell surface proteins vs ribose as part of nuclear event, ( as far I can see...... but I would need to look into this further)
That's the beauty of the nucleotide part - without meaning to, it gives you exactly the differentium (?) that you need without further looking, because the ER events never incorporate one into a glyco-whatever-modified protein.
Of course, got you!
This is a child of "protein glycosylation" which seems wrong, so it seems that "protein glycosylation" should be resticted further in some way?