NAGA
entrez
4668
canonical
uniprot
P17050
canonical
ensembl
ENSG00000198951
resolver
ensp
ENSP00000379680
resolver
ensp
ENSP00000384603
resolver
ensp
ENSP00000385283
resolver
ensp
ENSP00000568733
resolver
ensp
ENSP00000628300
resolver
enst
ENST00000396398
resolver
enst
ENST00000402937
resolver
enst
ENST00000403363
resolver
enst
ENST00000898674
resolver
enst
ENST00000958241
resolver
genesymbol
NAGA
resolver
hgnc
HGNC:7631
resolver
uniprot_entry
NAGAB_HUMAN
resolver
amino_acid_sequence
MLLKTVLLLGHVAQVLMLDNGLLQTPPMGWLAWERFRCNINCDEDPKNCISEQLFMEMADRMAQDGWRDMGYTYLNIDDCWIGGRDASGRLMPDPKRFPHGIPFLADYVHSLGLKLGIYADMGNFTCMGYPGTTLDKVVQDAQTFAEWKVDMLKLDGCFSTPEERAQGYPKMAAALNATGRPIAFSCSWPAYEGGLPPRVNYSLLADICNLWRNYDDIQDSWWSVLSILNWFVEHQDILQPVAGPGHWNDPDMLLIGNFGLSLEQSRAQMALWTVLAAPLLMSTDLRTISAQNMDILQNPLMIKINQDPLGIQGRRIHKEKSLIEVYMRPLSNKASALVFFSCRTDMPYRYHSSLGQLNFTGSVIYEAQDVYSGDIISGLRDETNFTVIINPSGVVMWYLYPIKNLEMSQQ
uniprot
proteins
disease_involvement
DISEASE: Schindler disease (SCHIND) [MIM:609241]: Form of NAGA deficiency characterized by early-onset neuroaxonal dystrophy and neurological signs (convulsion during fever, epilepsy, psychomotor retardation and hypotonia). NAGA deficiency is typically classified in three main phenotypes: NAGA deficiency type I (Schindler disease or Schindler disease type I) with severe manifestations; NAGA deficiency type II (Kanzazi disease or Schindler disease type II) which is mild; NAGA deficiency type III (Schindler disease type III) characterized by mild-to-moderate neurologic manifestations. NAGA deficiency results in the increased urinary excretion of glycopeptides and oligosaccharides containing alpha-N-acetylgalactosaminyl moieties. Inheritance is autosomal recessive. {ECO:0000269|PubMed:2243144, ECO:0000269|PubMed:8782044}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Kanzaki disease (KANZD) [MIM:609242]: Autosomal recessive disorder characterized by late-onset, angiokeratoma corporis diffusum and mild intellectual impairment. {ECO:0000269|PubMed:11251574, ECO:0000269|PubMed:8040340}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.2.1.49
uniprot
proteins
function
FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids. {ECO:0000269|PubMed:9741689}.
uniprot
proteins
mass_dalton
46565
uniprot
proteins
mutagenesis
MUTAGEN 201; /note="N->Q: Loss of glycosylation site; no effect on enzyme activity and stability."; /evidence="ECO:0000269|PubMed:19683538
uniprot
proteins
protein_family
Glycosyl hydrolase 27 family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
11251574
uniprot
proteins
pubmed
1418679
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1646157
uniprot
proteins
pubmed
17693683
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19683538
uniprot
proteins
pubmed
2174888
uniprot
proteins
pubmed
2243144
uniprot
proteins
pubmed
2256909
uniprot
proteins
pubmed
2372288
uniprot
proteins
pubmed
2551294
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
8040340
uniprot
proteins
pubmed
8782044
uniprot
proteins
pubmed
9741689
uniprot
proteins
sequence_length
411
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9741689}.
uniprot
proteins