Closed Shellerstedt closed 4 years ago
Hi Sage,
We can add that. How does it connect to the protein? Through a lysine bond to a C-terminal glycine like Ubiq/SUMO/NEDD? The papers you provided seem to indicate that, but I'll admit that I didn't dig too deeply beyond the abstract
Can you help with the term definitions? Does this look correct?
Thanks! Paul
[Term] id: MOD:XXXXXX <-- I will fill this in name: urmylated lysine def: "A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a URM1 protein." [PubMed:10713047, PubMed:21209336] subset: PSI-MOD-slim xref: Origin: "K" xref: Source: "natural" xref: TermSpec: "none" is_a: MOD:00908 ! modified glycine residue is_a: MOD:01875 ! N6-acylated L-lysine relationship: contains MOD:00134 ! N6-glycyl-L-lysine
Hearing nothing, I'm just going to create this term. Let me know if there are any questions/concerns.
Looks good to me. Is there any appropriate mass delta?
It's an intact protein mod like SUMO/Ubiquitin, so I'm voting against having it specified mass delta... just specifying it "higher" in the ontology. (Sumo and Ubiq are modeled the same way)
okay, then fine for me, thanks!
Apologies for the delay - I was out part of last week and wanted to confirm it with a colleague. This looks good to us. Thank you for your help!
Best, Sage
Hi,
I can’t seem to find a term for urmylation (GO: “Covalent attachment of the ubiquitin-like protein URM1 to another protein”) and would like to request a new term if possible (or point me in the right direction if I’m missing something?)
Some relevant references:
Furukawa K, et al. (2000) A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. J Biol Chem 275(11):7462-5 PMID: 10713047
Van der Veen AG, et al. (2011) Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier. Proc Natl Acad Sci U S A 108(5):1763-70 PMID: 21209336
Looks like the appropriate term would be “urmylation” or perhaps “urmylated lysine.”
Thanks for your help!
Best, Sage (SGD curator)