protein
N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
Gene
AGA
Organism
Homo sapiens(9606)
Length
346 aa
Mass
37,208 Da
N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase (AGA) is a lysosomal enzyme that catalyzes the hydrolysis of the GlcNAc-Asn bond in asparagine-linked glycoproteins (UniProt: P20933). This 346-amino acid protein plays a critical role in the catabolism of glycoproteins within the lysosomal compartment.
Mutations in AGA cause aspartylglucosaminuria (AGU; MIM 208400), a rare inborn lysosomal storage disorder characterized by accumulation of glycoasparagine and progressive intellectual disability beginning in early childhood, along with coarse facial features and connective tissue abnormalities (UniProt: P20933). The protein is central to normal lysosomal glycoprotein degradation pathways.
In Alzheimer's disease, AGA is upregulated in post-mortem human brain tissue relative to age-matched controls, with a mean log2 fold-change of +0.7974 detected across one subcellular fraction in TMT-labeled proteomics (Chaparral AD proteomics). This upregulation may reflect altered lysosomal protein metabolism or increased protein turnover in the AD brain environment, though the functional significance requires further investigation.
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
↑ Up in ADP3
not detected
P2
not detected
S2
+0.797
S3
not detected
Mean log₂FC across detected fractions: +0.7974 (1 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
Browse all →Tau molecular diversity contributes to clinical heterogeneity in Alzheimer's disease.
Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Function
Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins
Disease associations
AspartylglucosaminuriaAGU
An inborn lysosomal storage disease causing excess accumulation of glycoasparagine in the body tissues and its increased excretion in urine. Clinical features include mild to severe intellectual disability manifesting from the age of two, coarse facial features and mild connective tissue abnormalities.
Sources
Last updated 5/8/2026, 6:36:19 AM