CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019349
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase 
Protein Synonyms/Alias
 PNGase; hPNGase; N-glycanase 1; Peptide:N-glycanase 
Gene Name
 NGLY1 
Gene Synonyms/Alias
 PNG1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
92THLIFPKKASVEQLQubiquitination[1]
123SNKSHKVKSSQQPAAubiquitination[1, 2, 3]
204CIPVQELKRKSQEKLubiquitination[1, 2, 3, 4]
272LPSDDELKWGAKEVEubiquitination[1, 5]
276DELKWGAKEVEDHYCubiquitination[1, 5]
300PRYNNPEKLLETRCGubiquitination[1, 2, 3]
394VTWRYSCKHEEVIARubiquitination[1, 5]
406IARRTKVKEALLRDTubiquitination[1, 4, 5]
419DTINGLNKQRQLFLSubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
448LVEFISPKTPKPGELubiquitination[1]
451FISPKTPKPGELGGRubiquitination[1, 5]
477GEMGLQRKETLFIPCubiquitination[1]
501HLCYNIVKDRYVRVSubiquitination[1, 5]
584QTGTVEWKLRSDTAQubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 30 91 PUB.
 DOMAIN 454 654 PAW.
 ACT_SITE 309 309 Nucleophile (By similarity).
 ACT_SITE 336 336 By similarity.
 ACT_SITE 353 353 By similarity.
 METAL 250 250 Zinc (By similarity).
 METAL 253 253 Zinc (By similarity).
 METAL 283 283 Zinc (By similarity).
 METAL 286 286 Zinc (By similarity).
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 654 AA 
Protein Sequence
MAAAALGSSS GSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPNDEK YRSIRIGNTA 60
FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK IRDLIAIERS SRLDGSNKSH 120
KVKSSQQPAA STQLPTTPSS NPSGLNQHTR NRQGQSSDPP SASTVAADSA ILEVLQSNIQ 180
HVLVYENPAL QEKALACIPV QELKRKSQEK LSRARKLDKG INISDEDFLL LELLHWFKEE 240
FFHWVNNVLC SKCGGQTRSR DRSLLPSDDE LKWGAKEVED HYCDACQFSN RFPRYNNPEK 300
LLETRCGRCG EWANCFTLCC RAVGFEARYV WDYTDHVWTE VYSPSQQRWL HCDACEDVCD 360
KPLLYEIGWG KKLSYVIAFS KDEVVDVTWR YSCKHEEVIA RRTKVKEALL RDTINGLNKQ 420
RQLFLSENRR KELLQRIIVE LVEFISPKTP KPGELGGRIS GSVAWRVARG EMGLQRKETL 480
FIPCENEKIS KQLHLCYNIV KDRYVRVSNN NQTISGWENG VWKMESIFRK VETDWHMVYL 540
ARKEGSSFAY ISWKFECGSV GLKVDSISIR TSSQTFQTGT VEWKLRSDTA QVELTGDNSL 600
HSYADFSGAT EVILEAELSR GDGDVAWQHT QLFRQSLNDH EENCLEIIIK FSDL 654 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:EC.
 GO:0006516; P:glycoprotein catabolic process; IDA:UniProtKB. 
Interpro
 IPR008979; Galactose-bd-like.
 IPR006588; Peptide_N_glycanase_PAW_dom.
 IPR018997; PUB_domain.
 IPR006567; PUG-dom.
 IPR002931; Transglutaminase-like. 
Pfam
 PF04721; DUF750
 PF09409; PUB
 PF01841; Transglut_core 
SMART
 SM00613; PAW
 SM00580; PUG
 SM00460; TGc 
PROSITE
 PS51398; PAW 
PRINTS