AGA
entrez
175
canonical
uniprot
P20933
canonical
ensembl
ENSG00000038002
resolver
ensp
ENSP00000264595
resolver
ensp
ENSP00000667201
resolver
enst
ENST00000264595
resolver
genesymbol
AGA
resolver
hgnc
HGNC:318
resolver
uniprot
B2R7H2
resolver
uniprot
D3DP47
resolver
uniprot
Q4W5Q2
resolver
uniprot
Q6FHN6
resolver
uniprot
Q9UCK6
resolver
uniprot
Q9UCK7
resolver
uniprot
Q9UCK8
resolver
uniprot_entry
ASPG_HUMAN
resolver
uniprot_sec
B2R7H2
resolver
uniprot_sec
D3DP47
resolver
uniprot_sec
Q4W5Q2
resolver
uniprot_sec
Q6FHN6
resolver
uniprot_sec
Q9UCK6
resolver
uniprot_sec
Q9UCK7
resolver
uniprot_sec
Q9UCK8
resolver
amino_acid_sequence
MARKSNLPVLLVPFLLCQALVRCSSPLPLVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGILKQDIPIHKETEDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEFFGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCI
uniprot
proteins
disease_involvement
DISEASE: Aspartylglucosaminuria (AGU) [MIM:208400]: 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. {ECO:0000269|PubMed:11309371, ECO:0000269|PubMed:1301945, ECO:0000269|PubMed:1703489, ECO:0000269|PubMed:1904874, ECO:0000269|PubMed:2011603, ECO:0000269|PubMed:8776587, ECO:0000269|PubMed:9137882}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.5.1.26
uniprot
proteins
function
FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. {ECO:0000269|PubMed:1703489, ECO:0000269|PubMed:1904874, ECO:0000269|PubMed:2401370}.
uniprot
proteins
mass_dalton
37208
uniprot
proteins
post_translational_modification
PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. {ECO:0000269|PubMed:1281977, ECO:0000269|PubMed:1703489, ECO:0000269|PubMed:1904874}.; PTM: N-glycosylated. {ECO:0000269|PubMed:2401370}.
uniprot
proteins
protein_family
Ntn-hydrolase family
uniprot
proteins
pubmed
11309371
uniprot
proteins
pubmed
1281977
uniprot
proteins
pubmed
1301945
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
1703489
uniprot
proteins
pubmed
1840528
uniprot
proteins
pubmed
1904874
uniprot
proteins
pubmed
2011603
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2265705
uniprot
proteins
pubmed
2401370
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
8776587
uniprot
proteins
pubmed
8846222
uniprot
proteins
pubmed
9137882
uniprot
proteins
sequence_length
346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome.
uniprot
proteins