CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011002
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase 
Protein Synonyms/Alias
 PNGase; Peptide:N-glycanase 1; yPNG1 
Gene Name
 PNG1 
Gene Synonyms/Alias
 YPL096W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
33FILSKFKKAAPVENIubiquitination[1]
154GPNGEESKFNCGTVEubiquitination[1]
164CGTVEIYKCNRCGNIubiquitination[1]
285ELPRDQIKEEDLKFLubiquitination[1]
332RGKTQETKSESVSAAubiquitination[1]
341ESVSAASKSSNRGREubiquitination[1]
355ESGSADWKAQRGEDGubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
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. Involved in the formation of free oligosaccharide in cytosol. 
Sequence Annotation
 ACT_SITE 191 191 Nucleophile.
 ACT_SITE 218 218
 ACT_SITE 235 235
 METAL 129 129 Zinc.
 METAL 132 132 Zinc.
 METAL 165 165 Zinc.
 METAL 168 168 Zinc.
 BINDING 238 238 Substrate.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 363 AA 
Protein Sequence
MGEVYEKNNI DFDSIAKMLL IKYKDFILSK FKKAAPVENI RFQNLVHTNQ FAQGVLGQSQ 60
HLCTVYDNPS WHSIVLETLD LDLIYKNVDK EFAKDGHAEG ENIYTDYLVK ELLRYFKQDF 120
FKWCNKPDCN HCGQNTSENM TPLGSQGPNG EESKFNCGTV EIYKCNRCGN ITRFPRYNDP 180
IKLLETRKGR CGEWCNLFTL ILKSFGLDVR YVWNREDHVW CEYFSNFLNR WVHVDSCEQS 240
FDQPYIYSIN WNKKMSYCIA FGKDGVVDVS KRYILQNELP RDQIKEEDLK FLCQFITKRL 300
RYSLNDDEIY QLACRDEQEQ IELIRGKTQE TKSESVSAAS KSSNRGRESG SADWKAQRGE 360
DGK 363 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0003684; F:damaged DNA binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IDA:SGD.
 GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IMP:SGD.
 GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
 GO:0006517; P:protein deglycosylation; IDA:SGD. 
Interpro
 IPR018325; Rad4/PNGase_transGLS-fold.
 IPR002931; Transglutaminase-like. 
Pfam
 PF03835; Rad4 
SMART
 SM00460; TGc 
PROSITE
  
PRINTS