NGLY1

From Wikipedia, the free encyclopedia

N-glycanase 1

PDB rendering based on 2ccq.

Available structures: 2ccq, 2cm0, 2d5u, 2hpj, 2hpl

Identifiers

Symbol(s)

NGLY1; FLJ11005; FLJ12409; PNG1

External IDs

OMIM: 610661 MGI: 1913276 HomoloGene: 10117

Gene ontology
Molecular Function:	• peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity • protein binding • zinc ion binding • hydrolase activity • metal ion binding
Cellular Component:	• cytoplasm
Biological Process:	• glycoprotein catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_018297 (mRNA)
NP_060767 (protein)

NM_021504 (mRNA)
NP_067479 (protein)

Location

Chr 3: 25.74 - 25.8 Mb

n/a

Pubmed search

[1]

[2]

N-glycanase 1, also known as NGLY1, is a human gene.^[1]

[edit] References

^ Entrez Gene: NGLY1 N-glycanase 1.

[edit] 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. PMID 10831608.
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. PMID 11562482.
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. PMID 12477932.
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. PMID 14749736.
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. PMID 15358861.
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. PMID 15362974.
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. PMID 15489334.
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. PMID 16055502.
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.