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ATPase p97 + H2O
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a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase. Phosphorylation of p97s highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors
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class I MHC HC + H2O
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the enzyme is involved proteasomal degradation of glycosylated type I membrane protein class I MHC heavy chain, dislocated from ER to cytosol by cytomegalovirus-encoded glycoprotein US2 protein, overview
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concanavalin A-precursor + H2O
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deglycosylation leads to conversion into an active lectin
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melanopsin + H2O
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N-glycoprotein + H2O
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PNGase is involved in the release of N-glycans from N-glycoproteins
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Oryzias latipes glycophosphoprotein MU-1 + H2O
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acid PNGase M from blastoderm stage 11, yolk-absorptive stage
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Oryzias latipes glycophosphoprotein MU-2 + H2O
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acid PNGase M from blastoderm stage 11, yolk-absorptive stage
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proton-coupled folate transporter + H2O
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tyrosinase + H2O
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the enzyme is required for processing of a class I-restricted epitope from tyrosinase together with the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic protease, overview
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additional information
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additional information
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the AtPNG1 gene encodes a bona fide peptide:N-glycanase that contributes to ERAD related protein quality control in plants
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additional information
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the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
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additional information
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the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
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additional information
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the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
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additional information
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the enzyme deglycosylates misfolded glycoproteins, the enzyme is a mediator for p97 functions, the PUB domain functions as a p97 binding module in human enzyme, p97 is an AAA ATPase with an ubiquitin-selective molecular machine involved in multiple cellular processes including protein degradation through the ubiquitin-proteasome system
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additional information
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the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
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additional information
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the cytoplasmic PNGase in mammals is able to bind to p97/VCP/Cdc48, a key ATPases accosiated with diverse cellular activities (AAA) adenosine triphosphate (ATPase) for the ERAD pathway, as well as other ERAD or ubiquitinx02proteasome pathway-related proteins, some of which are intrinsic membrane proteins
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additional information
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the cytoplasmic PNGase in mammals is able to bind to p97/VCP/Cdc48, a key ATPases accosiated with diverse cellular activities (AAA) adenosine triphosphate (ATPase) for the ERAD pathway, as well as other ERAD or ubiquitinx02proteasome pathway-related proteins, some of which are intrinsic membrane proteins
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additional information
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the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
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additional information
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the enzyme mediates the binding of the cytoplasmic proteins p97 and HR23B to the proteasome through formation of a ternary complex, p97 binds the autocrine motility factor receptor AMFR, modeling of interaction of the endoplasmic reticulum with the proteasome, overview
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additional information
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the enzyme removes N-linked oligosaccharides from misfolded glycoproteins as part of endoplasmic reticulum-associated degradation pathway involving a complex formation with proteins HR23B, cytosolic protein Y33K, p97, and autocrine motility factor receptor AMFR, the AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase AMFR, the N-terminus of PNGase interacts with the C-terminal tail of AMFR, complex formation model, overview
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additional information
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the enzyme removes N-linked oligosaccharides from misfolded glycoproteins as part of endoplasmic reticulum-associated degradation pathway involving a tight complex-formation with protein HR23, HR23 is also involved in DNA repair, co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways, overview
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additional information
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the cytoplasmic PNGase in mammals is able to bind to p97/VCP/Cdc48, a key ATPases accosiated with diverse cellular activities (AAA) adenosine triphosphate (ATPase) for the ERAD pathway, as well as other ERAD or ubiquitinx02proteasome pathway-related proteins, some of which are intrinsic membrane proteins
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additional information
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involved in proteasomal degradation of misfolded glycoproteins
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additional information
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the cytosolic enzyme deglycosylates misfolded glycoproteins prior to the endoplasmic reticulum-associated protein degradation
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additional information
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the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
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additional information
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catalyses the de-glycosylation of unfolded glycoproteins
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additional information
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catalyses the de-glycosylation of unfolded glycoproteins
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additional information
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protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
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additional information
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protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
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additional information
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protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
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additional information
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SpPNGase deglycosylates the misfolded glycoproteins
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additional information
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the enzyme hydrolyses the beta-aspartyl-glycosylamine bond of N-linked glycoproteins/glycopeptides and releases free N-glycans
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additional information
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the enzyme hydrolyses the beta-aspartyl-glycosylamine bond of N-linked glycoproteins/glycopeptides and releases free N-glycans
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