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possible new child term (if appropriate): glutaminylated glutamate
reference: PMID:28801462 Jank T, et al. (2017) Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A. J. Biol. Chem. 292(39):16014-16023
from the intro: "Here we describe, for the first time, a novel type of posttranslational modification, the glutaminylation of a glutamate residue, that occurs within the helix A*–loop–helix A region of yeast eEF1A. We show that the glutamine residue is attached via its amino group to the side chain carboxyl group of Glu45 within eEF1A."
The text was updated successfully, but these errors were encountered:
MOD:02025 is (I believe) the glutaminylated glutamate that you note (references the same PMID)... although the description doesn't seem correct... thoughts @pabinz or @ricardblum (should we remove the word "free" because it's in the context of a polypeptide)? We could certainly add in the generic glutaminylated residue following that same rubric, just on the generic amino acid "X".
[Term]
id: MOD:02025
name: 5-glutaminyl glutamic acid
def: "A protein modification that effectively converts the alpha amino group of a glutamine residue to glutaminyl glutamic acid by forming an isopeptide bond with the side chain carboxyl group of a free glutamic acid." [PubMed:28801462]
xref: DiffAvg: "128.13"
xref: DiffFormula: "C 5 H 8 N 2 O 2"
xref: DiffMono: "128.058576"
xref: Formula: "C 10 H 15 N 3 O 5"
xref: MassAvg: "257.24"
xref: MassMono: "257.101167"
xref: Origin: "E"
xref: Source: "natural"
xref: TermSpec: "none"
is_a: MOD:00906 ! modified L-glutamic acid residue
I agree the definition needs fixing. This is the term I requested for
translation elongation factor EF-1 alpha glutamination so it should refer to a protein chain
New Term Request: glutaminylated residue
possible new child term (if appropriate): glutaminylated glutamate
reference: PMID:28801462 Jank T, et al. (2017) Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A. J. Biol. Chem. 292(39):16014-16023
from the intro: "Here we describe, for the first time, a novel type of posttranslational modification, the glutaminylation of a glutamate residue, that occurs within the helix A*–loop–helix A region of yeast eEF1A. We show that the glutamine residue is attached via its amino group to the side chain carboxyl group of Glu45 within eEF1A."
The text was updated successfully, but these errors were encountered: