Tag | Content |
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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 |
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33 | FILSKFKKAAPVENI | ubiquitination | [1] | 154 | GPNGEESKFNCGTVE | ubiquitination | [1] | 164 | CGTVEIYKCNRCGNI | ubiquitination | [1] | 285 | ELPRDQIKEEDLKFL | ubiquitination | [1] | 332 | RGKTQETKSESVSAA | ubiquitination | [1] | 341 | ESVSAASKSSNRGRE | ubiquitination | [1] | 355 | ESGSADWKAQRGEDG | ubiquitination | [1] |
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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, Villén 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. |
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