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Identification
HMDB Protein ID HMDBP10626
Secondary Accession Numbers
  • 16855
Name Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
Synonyms
  1. N-glycanase 1
  2. PNGase
  3. Peptide:N-glycanase
  4. hPNGase
Gene Name NGLY1
Protein Type Enzyme
Biological Properties
General Function Involved in protein binding
Specific 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 reticulun that are exported in the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
intracellular part
cytoplasm
Function
binding
protein binding
Process
metabolic process
catabolic process
macromolecule catabolic process
glycoprotein catabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location Chromosome:3
Locus 3p24.2
SNPs NGLY1
Gene Sequence
>1965 bp
ATGGCGGCGGCGGCATTGGGCAGCTCCTCAGGCTCGGCGTCCCCGGCCGTGGCTGAGCTC
TGCCAGAACACCCCGGAGACCTTTTTGGAGGCCTCCAAGCTGCTGCTCACCTATGCTGAC
AACATCCTCAGAAACCCTAATGATGAAAAATATAGATCCATCCGGATTGGAAACACAGCC
TTTTCTACTAGACTCTTGCCTGTCAGAGGAGCTGTTGAATGTTTATTTGAAATGGGCTTT
GAAGAGGGAGAAACACATCTCATCTTTCCTAAAAAAGCTTCAGTGGAGCAGCTGCAAAAA
ATTCGTGACCTGATTGCCATAGAGAGAAGTAGCAGACTGGATGGCTCAAATAAGAGCCAC
AAAGTAAAGTCATCTCAGCAACCTGCAGCCAGTACCCAGCTTCCTACAACACCATCTTCA
AATCCCAGTGGGTTAAACCAGCACACAAGGAACCGTCAAGGGCAGTCATCAGATCCACCA
TCTGCTTCAACGGTTGCTGCTGACTCAGCCATTCTAGAAGTTCTTCAGTCCAACATTCAG
CATGTGCTGGTCTATGAAAATCCTGCTCTTCAGGAGAAAGCGTTGGCTTGTATTCCGGTC
CAAGAACTAAAAAGGAAATCACAAGAAAAGTTATCGAGAGCTAGAAAATTGGATAAAGGT
ATCAATATAAGTGATGAGGATTTTCTTTTGCTGGAGCTTTTGCACTGGTTTAAGGAAGAA
TTTTTTCACTGGGTGAATAACGTTTTGTGCAGCAAATGTGGTGGACAGACTAGGTCTAGA
GATAGATCATTACTGCCCAGTGATGATGAGCTGAAGTGGGGTGCAAAGGAAGTGGAAGAT
CATTACTGTGATGCCTGCCAGTTCAGCAATCGATTCCCAAGATATAATAACCCTGAGAAA
CTTTTGGAAACAAGATGTGGACGGTGTGGCGAGTGGGCCAATTGTTTTACACTGTGCTGC
CGAGCTGTAGGGTTTGAAGCTCGCTATGTTTGGGATTACACAGACCATGTCTGGACAGAA
GTCTATTCTCCTTCTCAGCAGCGGTGGCTGCACTGTGATGCATGTGAAGATGTCTGTGAC
AAGCCACTCCTTTATGAAATAGGATGGGGCAAGAAGCTTTCCTATGTCATAGCATTTTCA
AAAGATGAGGTAGTTGATGTCACTTGGCGATATTCCTGCAAACATGAAGAGGTGATTGCC
AGAAGAACTAAGGTTAAAGAAGCATTACTTCGAGACACTATTAATGGGCTTAATAAGCAG
AGGCAACTGTTTTTGTCAGAAAACAGAAGGAAAGAACTTCTCCAGAGGATAATTGTGGAG
CTTGTTGAATTTATATCTCCCAAAACCCCTAAACCTGGAGAACTTGGGGGAAGAATATCT
GGGTCAGTGGCTTGGAGAGTAGCCCGAGGTGAAATGGGTCTACAGAGAAAAGAAACCTTG
TTTATTCCCTGTGAAAATGAGAAGATTTCTAAACAGCTCCACCTTTGTTACAATATTGTG
AAAGATCGTTATGTTCGAGTTTCAAATAACAATCAAACCATTTCTGGATGGGAGAATGGC
GTGTGGAAAATGGAATCTATATTCAGAAAAGTTGAAACAGACTGGCACATGGTATATTTG
GCCCGAAAGGAAGGATCATCTTTTGCTTATATTTCCTGGAAGTTTGAGTGTGGGTCAGTT
GGCCTAAAAGTAGATAGCATTTCTATTAGAACAAGTAGTCAAACTTTTCAGACTGGAACA
GTAGAATGGAAATTGCGATCTGATACAGCACAAGTAGAACTGACAGGCGATAACAGTCTT
CACTCCTATGCTGATTTTTCTGGTGCCACTGAAGTTATTTTGGAAGCAGAATTAAGCAGA
GGAGATGGTGATGTCGCTTGGCAACACACCCAGCTGTTTAGACAAAGCTTAAATGACCAT
GAAGAAAATTGTTTGGAGATAATTATAAAATTCAGTGACCTTTGA
Protein Properties
Number of Residues 654
Molecular Weight 74389.4
Theoretical pI 6.88
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
MAAAALGSSSGSASPAVAELCQNTPETFLEASKLLLTYADNILRNPNDEKYRSIRIGNTA
FSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIERSSRLDGSNKSH
KVKSSQQPAASTQLPTTPSSNPSGLNQHTRNRQGQSSDPPSASTVAADSAILEVLQSNIQ
HVLVYENPALQEKALACIPVQELKRKSQEKLSRARKLDKGINISDEDFLLLELLHWFKEE
FFHWVNNVLCSKCGGQTRSRDRSLLPSDDELKWGAKEVEDHYCDACQFSNRFPRYNNPEK
LLETRCGRCGEWANCFTLCCRAVGFEARYVWDYTDHVWTEVYSPSQQRWLHCDACEDVCD
KPLLYEIGWGKKLSYVIAFSKDEVVDVTWRYSCKHEEVIARRTKVKEALLRDTINGLNKQ
RQLFLSENRRKELLQRIIVELVEFISPKTPKPGELGGRISGSVAWRVARGEMGLQRKETL
FIPCENEKISKQLHLCYNIVKDRYVRVSNNNQTISGWENGVWKMESIFRKVETDWHMVYL
ARKEGSSFAYISWKFECGSVGLKVDSISIRTSSQTFQTGTVEWKLRSDTAQVELTGDNSL
HSYADFSGATEVILEAELSRGDGDVAWQHTQLFRQSLNDHEENCLEIIIKFSDL
GenBank ID Protein 21314690
UniProtKB/Swiss-Prot ID Q96IV0
UniProtKB/Swiss-Prot Entry Name NGLY1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_018297.3
GeneCard ID NGLY1
GenAtlas ID NGLY1
HGNC ID HGNC:17646
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  3. Suzuki T, Park H, Hollingsworth NM, Sternglanz R, Lennarz WJ: PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase. J Cell Biol. 2000 May 29;149(5):1039-52. [PubMed:10831608 ]
  4. McNeill H, Knebel A, Arthur JS, Cuenda A, Cohen P: A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs. Biochem J. 2004 Dec 1;384(Pt 2):391-400. [PubMed:15362974 ]
  5. Blom D, Hirsch C, Stern P, Tortorella D, Ploegh HL: A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. EMBO J. 2004 Feb 11;23(3):650-8. Epub 2004 Jan 29. [PubMed:14749736 ]
  6. Katiyar S, Li G, Lennarz WJ: 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. 2004 Sep 21;101(38):13774-9. Epub 2004 Sep 9. [PubMed:15358861 ]
  7. Misaghi S, Pacold ME, Blom D, Ploegh HL, Korbel GA: Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover. Chem Biol. 2004 Dec;11(12):1677-87. [PubMed:15610852 ]
  8. Katiyar S, Joshi S, Lennarz WJ: The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum. Mol Biol Cell. 2005 Oct;16(10):4584-94. Epub 2005 Jul 29. [PubMed:16055502 ]
  9. Allen MD, Buchberger A, Bycroft M: The PUB domain functions as a p97 binding module in human peptide N-glycanase. J Biol Chem. 2006 Sep 1;281(35):25502-8. Epub 2006 Jun 28. [PubMed:16807242 ]