NGLY1

N-glycanase 1
PDB rendering based on 2ccq.
Available structures PDB 2CCQ, 2CM0
Identifiers
Symbols	NGLY1; FLJ11005; FLJ12409; PNG1; PNGase
External IDs	OMIM: 610661 MGI: 1913276 HomoloGene: 10117 GeneCards: NGLY1 Gene
EC number	3.5.1.52
Gene Ontology Molecular function • peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity • protein binding • hydrolase activity • metal ion binding Cellular component • cytoplasm Biological process • glycoprotein catabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	55768	59007
Ensembl	ENSG00000151092	ENSMUSG00000021785
UniProt	Q96IV0	n/a
RefSeq (mRNA)	NM_001145293.1	NM_021504.3
RefSeq (protein)	NP_001138765.1	NP_067479.2
Location (UCSC)	Chr 3: 25.76 – 25.83 Mb	Chr 14: 17.08 – 17.14 Mb
PubMed search	[1]	[2]

Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase is an enzyme that in humans is encoded by the NGLY1 gene.^[1]

References

1. ^ "Entrez Gene: NGLY1 N-glycanase 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55768. 

Further reading

• Suzuki T, Park H, Hollingsworth NM, et al. (2000). "PNG1, a Yeast Gene Encoding a Highly Conserved Peptide:N-Glycanase". J. Cell Biol. 149 (5): 1039–52. doi:10.1083/jcb.149.5.1039. PMC 2174826. PMID 10831608. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2174826. 
• Park H, Suzuki T, Lennarz WJ (2001). "Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation". Proc. Natl. Acad. Sci. U.S.A. 98 (20): 11163–8. doi:10.1073/pnas.201393498. PMC 58701. PMID 11562482. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=58701. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Blom D, Hirsch C, Stern P, et al. (2005). "A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised". EMBO J. 23 (3): 650–8. doi:10.1038/sj.emboj.7600090. PMC 1271816. PMID 14749736. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1271816. 
• Katiyar S, Li G, Lennarz WJ (2004). "A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (38): 13774–9. doi:10.1073/pnas.0405663101. PMC 518832. PMID 15358861. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=518832. 
• McNeill H, Knebel A, Arthur JS, et al. (2005). "A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs". Biochem. J. 384 (Pt 2): 391–400. doi:10.1042/BJ20041498. PMC 1134123. PMID 15362974. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1134123. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Misaghi S, Pacold ME, Blom D, et al. (2005). "Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover". Chem. Biol. 11 (12): 1677–87. doi:10.1016/j.chembiol.2004.11.010. PMID 15610852. 
• Katiyar S, Joshi S, Lennarz WJ (2006). "The Retrotranslocation Protein Derlin-1 Binds Peptide:N-Glycanase to the Endoplasmic Reticulum". Mol. Biol. Cell 16 (10): 4584–94. doi:10.1091/mbc.E05-04-0345. PMC 1237066. PMID 16055502. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1237066. 
• Allen MD, Buchberger A, Bycroft M (2006). "The PUB domain functions as a p97 binding module in human peptide N-glycanase". J. Biol. Chem. 281 (35): 25502–8. doi:10.1074/jbc.M601173200. PMID 16807242. 
• Altrich-VanLith ML, Ostankovitch M, Polefrone JM, et al. (2007). "Processing of a class I-restricted epitope from tyrosinase requires peptide N-glycanase and the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic proteases". J. Immunol. 177 (8): 5440–50. PMID 17015730.