NGLY1
entrez
55768
canonical
uniprot
Q96IV0
canonical
ensembl
ENSG00000151092
resolver
ensp
ENSP00000280700
resolver
ensp
ENSP00000379886
resolver
ensp
ENSP00000387430
resolver
ensp
ENSP00000389888
resolver
ensp
ENSP00000547261
resolver
ensp
ENSP00000599545
resolver
ensp
ENSP00000666687
resolver
ensp
ENSP00000666689
resolver
ensp
ENSP00000705179
resolver
ensp
ENSP00000705184
resolver
ensp
ENSP00000705187
resolver
ensp
ENSP00000783685
resolver
genesymbol
NGLY1
resolver
genesymbol_syn
PNG1
resolver
hgnc
HGNC:17646
resolver
uniprot
B4DJE9
resolver
uniprot
Q59FB1
resolver
uniprot
Q6PJD8
resolver
uniprot
Q9BVR8
resolver
uniprot
Q9NR70
resolver
uniprot_entry
NGLY1_HUMAN
resolver
uniprot_sec
B4DJE9
resolver
uniprot_sec
Q59FB1
resolver
uniprot_sec
Q6PJD8
resolver
uniprot_sec
Q9BVR8
resolver
uniprot_sec
Q9NR70
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by Z-VAD-fmk, a well-known caspase inhibitor, which inhibits enzyme activity through covalent binding of the carbohydrate to the single Cys-306 residue. {ECO:0000269|PubMed:15610852}.
uniprot
proteins
amino_acid_sequence
MAAAALGSSSGSASPAVAELCQNTPETFLEASKLLLTYADNILRNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIERSSRLDGSNKSHKVKSSQQPAASTQLPTTPSSNPSGLNQHTRNRQGQSSDPPSASTVAADSAILEVLQSNIQHVLVYENPALQEKALACIPVQELKRKSQEKLSRARKLDKGINISDEDFLLLELLHWFKEEFFHWVNNVLCSKCGGQTRSRDRSLLPSDDELKWGAKEVEDHYCDACQFSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRAVGFEARYVWDYTDHVWTEVYSPSQQRWLHCDACEDVCDKPLLYEIGWGKKLSYVIAFSKDEVVDVTWRYSCKHEEVIARRTKVKEALLRDTINGLNKQRQLFLSENRRKELLQRIIVELVEFISPKTPKPGELGGRISGSVAWRVARGEMGLQRKETLFIPCENEKISKQLHLCYNIVKDRYVRVSNNNQTISGWENGVWKMESIFRKVETDWHMVYLARKEGSSFAYISWKFECGSVGLKVDSISIRTSSQTFQTGTVEWKLRSDTAQVELTGDNSLHSYADFSGATEVILEAELSRGDGDVAWQHTQLFRQSLNDHEENCLEIIIKFSDL
uniprot
proteins
disease_involvement
DISEASE: Congenital disorder of deglycosylation 1 (CDDG1) [MIM:615273]: An autosomal recessive multisystem disorder characterized by developmental delay, hypotonia, abnormal involuntary movements and alacrima or poor tear production. Other features include microcephaly, intractable seizures, abnormal eye movements and evidence of liver dysfunction, probably due to cytoplasmic accumulation of storage material in vacuoles. {ECO:0000269|PubMed:22581936, ECO:0000269|PubMed:24651605}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.5.1.52
uniprot
proteins
function
FUNCTION: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. {ECO:0000269|PubMed:14749736, ECO:0000269|PubMed:15358861}.
uniprot
proteins
mass_dalton
74390
uniprot
proteins
protein_family
PNGase family
uniprot
proteins
protein_family
Transglutaminase-like superfamily
uniprot
proteins
pubmed
10831608
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14749736
uniprot
proteins
pubmed
15358861
uniprot
proteins
pubmed
15362974
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15610852
uniprot
proteins
pubmed
16055502
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16807242
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
22581936
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24651605
uniprot
proteins
sequence_length
654
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15358861}.
uniprot
proteins