Ngly1
entrez
59007
canonical
uniprot
Q9JI78
canonical
ensembl
ENSMUSG00000021785
resolver
ensp
ENSMUSP00000022310
resolver
ensp
ENSMUSP00000152998
resolver
ensp
ENSMUSP00000248153
resolver
enst
ENSMUST00000022310
resolver
enst
ENSMUST00000224656
resolver
genesymbol
Ngly1
resolver
uniprot
A0A286YCI0
resolver
uniprot
Q8K113
resolver
uniprot
Q9CTK3
resolver
uniprot_entry
A0A286YCI0_MOUSE
resolver
uniprot_entry
NGLY1_MOUSE
resolver
uniprot_sec
Q8K113
resolver
uniprot_sec
Q9CTK3
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
MASATLGSSSSSASPAVAELCQNTPETFLEASKLLLTYADNILRNPSDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIERSSRLDGSSKKVQFSQHPAAAKLPLEQSEDPAGLIRHSGNQTGQLPSLPSAPMVVGDSTILKVLQSNIQHVQLYENPVLQEKALTCIPVSELKRKAQEKLFRARKLDKGTNVSDEDFLLLELLHWFKEEFFRWVNNIVCSKCGGETRSRDEALLPNDDELKWGAKNVENHYCDACQLSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRALGFEARYVWDYTDHVWTEVYSPSQQRWLHCDACEDVCDKPLLYEIGWGKKLSYIIAFSKDEVVDVTWRYSCKHDEVMSRRTKVKEELLRETINGLNKQRQLSLSESRRKELLQRIIVELVEFISPKTPRPGELGGRVSGSLAWRVARGETGLERKEILFIPSENEKISKQFHLRYDIVRDRYIRVSDNNINISGWENGVWKMESIFRKVEKDWNMVYLARKEGSSFAYISWKFECGSAGLKVDTVSIRTSSQSFESGSVRWKLRSETAQVNLLGDKNLRSYNDFSGATEVTLEAELSRGDGDVAWQHTQLFRQSLNDSGENGLEIIITFNDL
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:11562482, ECO:0000269|PubMed:12606569, ECO:0000269|PubMed:15358861}.
uniprot
proteins
mass_dalton
74275
uniprot
proteins
mutagenesis
MUTAGEN 41; /note="N->P: Abolishes interaction with VCP."; /evidence="ECO:0000269|PubMed:16709668"; MUTAGEN 58; /note="N->A: Does not affect the interaction with VCP."; /evidence="ECO:0000269|PubMed:16709668"; MUTAGEN 79..80; /note="GF->AA: Abolishes interaction with VCP."; /evidence="ECO:0000269|PubMed:16709668"; MUTAGEN 306; /note="C->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:12606569
uniprot
proteins
protein_family
PNGase family
uniprot
proteins
protein_family
Transglutaminase-like superfamily
uniprot
proteins
pubmed
10831608
uniprot
proteins
pubmed
11562482
uniprot
proteins
pubmed
12606569
uniprot
proteins
pubmed
12711318
uniprot
proteins
pubmed
15358861
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15610852
uniprot
proteins
pubmed
16055502
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16249333
uniprot
proteins
pubmed
16500903
uniprot
proteins
pubmed
16709668
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8021270
uniprot
proteins
sequence_length
651
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:12606569, ECO:0000269|PubMed:16055502}.
uniprot
proteins