Aga
entrez
11593
canonical
uniprot
Q64191
canonical
ensembl
ENSMUSG00000031521
resolver
ensp
ENSMUSP00000033920
resolver
ensp
ENSMUSP00000148133
resolver
ensp
ENSMUSP00000255282
resolver
enst
ENSMUST00000033920
resolver
enst
ENSMUST00000211424
resolver
genesymbol
Aga
resolver
uniprot
A0A1B0GSZ5
resolver
uniprot
A2RSS6
resolver
uniprot
B7ZNK6
resolver
uniprot_entry
A0A1B0GSZ5_MOUSE
resolver
uniprot_entry
A2RSS6_MOUSE
resolver
uniprot_entry
ASPG_MOUSE
resolver
uniprot_entry
B7ZNK6_MOUSE
resolver
amino_acid_sequence
MERKSNLSLLLLLLVLGMPLVRGSSPLPLVVNTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCGPYKPSGFLKQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQAVEYMRGGDDPAIACQKVILRIQKYYPNFFGAVICASVNGSYGAACNKLPTFTQFSFMVSNSLHNEPTEKKVDCI
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:8586423}.
uniprot
proteins
mass_dalton
37022
uniprot
proteins
post_translational_modification
PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme (PubMed:8586423). The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. {ECO:0000250|UniProtKB:P20933, ECO:0000269|PubMed:8586423}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20933}.
uniprot
proteins
protein_family
Ntn-hydrolase family
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8586423
uniprot
proteins
sequence_length
346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome.
uniprot
proteins