AGA across dismech

AGA (aspartylglucosaminidase) is named by 2 disorder entries: the disease it causes and the class entry for the glycoproteinoses.

How the entries record the gene

Both entries type AGA as causative (Aspartylglucosaminuria; Glycoprotein Storage Disease), with germline variants in Aspartylglucosaminuria (germline). No record is left untyped (0). ClinGen classifies AGA for 1 disease, and for Aspartylglucosaminuria its tier is definitive; the entry records that assertion in its gene_disease_validity.

Where the gene sits in the pathograph

In Aspartylglucosaminuria the gene is bound to two nodes (AGA lysosomal enzyme deficiency; AGA protein maturation and folding defects): loss of the GlcNAc-Asn-cleaving activity in the lysosome, and the failure of the mutant precursor to fold and mature. The processes carried by those nodes are glycoprotein catabolic process; protein deglycosylation; protein folding; protein maturation. The class entry Glycoprotein Storage Disease names AGA on its shared node Lysosomal Glycosidase Deficiency and Impaired Glycoprotein Catabolism, which marks glycoprotein catabolic process as decreased.

The gene reaches the lysosomal_substrate_accumulation module through its node, and no treatment record names it (0).

Normal function

The ai-gene-review ingest layer currently reports 0 core function terms for AGA, because the ingest tables are pinned to an ai-gene-review commit that predates the review of this gene. The upstream review, written in the same round of work as this page, gives N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity in the lysosome, acting in glycoprotein catabolism and protein deglycosylation, as the core function, and records the autoproteolytic activation of the precursor. Glycoprotein catabolic process and protein deglycosylation are the same terms the Aspartylglucosaminuria node marks as decreased, so the two layers should share them once the ingest pin is advanced; until then they share 0.