Linked Life Data

CPATH-20613

Source:http://cbio.mskcc.org/cpath#CPATH-20613

Statements in which the resource exists.
SubjectPredicateObjectContext
cpath:CPATH-20613rdf:typehttp://www.biopax.org/relea...lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...cpath:CPATH-LOCAL-85903lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...cpath:CPATH-LOCAL-85904lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...cpath:CPATH-LOCAL-85905lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...cpath:CPATH-LOCAL-85906lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...cpath:CPATH-LOCAL-85907lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...cpath:CPATH-LOCAL-85908lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...cpath:CPATH-LOCAL-90782lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidaselld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...NGLY1_MOUSElld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...cpath:CPATH-LOCAL-85901lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...Peptide:N-glycanaselld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...PNGaselld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...mPNGaselld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...3.5.1.52lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...N-glycanase 1lld:biogrid
cpath:CPATH-20613http://www.biopax.org/relea...FUNCTION: 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 reticulun that are exported in the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. CATALYTIC ACTIVITY: Hydrolysis of an N(4)-(acetyl-beta-D- glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl- beta-D-glucosaminylamine and a peptide containing an aspartate residue. COFACTOR: Binds 1 zinc ion per subunit. ENZYME REGULATION: Inhibited by Z-VAD-fmk, a well-known caspase inhibitor, which inhibits enzyme activity through covalent binding of the carbohydrate to the single Cys-306 residue. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=114 uM for fetuin glycopeptide I; Vmax=0.0964 nmol/min/mg enzyme with fetuin glycopeptide I as substrate; SUBUNIT: Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with the proteasome components RAD23B and PSMC1. Interacts with directly with VCP. Interacts with DERL1, bringing it close to the endoplasmic reticulum membrane. Interacts with SAKS1. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Ubiquitously expressed with highest level in testis. DOMAIN: The PUB domain mediates the interaction with VCP. SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase family. SIMILARITY: Contains 1 PAW domain. SIMILARITY: Contains 1 PUB (PUG) domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.lld:biogrid
cpath:CPATH-20613skos:exactMatchuniprot-protein:Q9JI78lld:mappings
cpath:CPATH-20613skos:closeMatchentrez-gene:59007lld:mappings
cpath:CPATH-LOCAL-10510930http://www.biopax.org/relea...cpath:CPATH-20613lld:biogrid
cpath:CPATH-LOCAL-10523786http://www.biopax.org/relea...cpath:CPATH-20613lld:biogrid
cpath:CPATH-LOCAL-10533055http://www.biopax.org/relea...cpath:CPATH-20613lld:biogrid