EC Number   |
Natural Substrates |
|---|
   3.5.1.52 | ATPase p97 + H2O |
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 |
| 3.5.1.52 | class I MHC HC + H2O |
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 |
| 3.5.1.52 | concanavalin A-precursor + H2O |
deglycosylation leads to conversion into an active lectin |
| 3.5.1.52 | melanopsin + H2O |
- |
| 3.5.1.52 | more |
involved in proteasomal degradation of misfolded glycoproteins |
| 3.5.1.52 | more |
the cytosolic enzyme deglycosylates misfolded glycoproteins prior to the endoplasmic reticulum-associated protein degradation |
| 3.5.1.52 | more |
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 |
| 3.5.1.52 | more |
the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol |
| 3.5.1.52 | more |
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 |
| 3.5.1.52 | more |
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 |
