BAIT
PRNP
ASCR, AltPrP, CD230, CJD, GSS, KURU, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, p27-30, RP5-1068H6.2
prion protein
GO Process (12)
GO Function (5)
GO Component (9)
Gene Ontology Biological Process
- axon guidance [TAS]
- cellular copper ion homeostasis [NAS]
- metabolic process [TAS]
- negative regulation of T cell receptor signaling pathway [ISS]
- negative regulation of activated T cell proliferation [ISS]
- negative regulation of calcineurin-NFAT signaling cascade [ISS]
- negative regulation of interferon-gamma production [ISS]
- negative regulation of interleukin-17 production [ISS]
- negative regulation of interleukin-2 production [ISS]
- negative regulation of protein phosphorylation [ISS]
- negative regulation of sequence-specific DNA binding transcription factor activity [ISS]
- response to oxidative stress [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
HSPA5
BIP, GRP78, HEL-S-89n, MIF2
heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
GO Process (14)
GO Function (10)
GO Component (12)
Gene Ontology Biological Process
- ATP catabolic process [ISS]
- ER-associated ubiquitin-dependent protein catabolic process [TAS]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- blood coagulation [TAS]
- cellular protein metabolic process [TAS]
- cellular response to glucose starvation [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- maintenance of protein localization in endoplasmic reticulum [IMP]
- negative regulation of apoptotic process [IMP, TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of cell migration [IMP]
- regulation of protein folding in endoplasmic reticulum [TAS]
- substantia nigra development [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- COP9 signalosome [IDA]
- endoplasmic reticulum [IDA, IMP, TAS]
- endoplasmic reticulum chaperone complex [IDA]
- endoplasmic reticulum lumen [TAS]
- endoplasmic reticulum membrane [TAS]
- endoplasmic reticulum-Golgi intermediate compartment [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- integral component of endoplasmic reticulum membrane [IDA]
- membrane [IDA]
- midbody [IDA]
- nucleus [IDA, IMP]
Homo sapiens
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome.
Familial prion diseases are thought to result from a change in structure of the mutant prion protein (PrP), which takes a pathogenic conformation. We have examined the role of molecular chaperones in the folding of normal and mutant PrP Q217R (PrP(217)) in transfected neuroblastoma cells. In a previous report we showed that, although most of the PrP(217) forms escape the ... [more]
J. Biol. Chem. Dec. 08, 2000; 275(49);38699-704 [Pubmed: 10970892]
Throughput
- Low Throughput
Curated By
- BioGRID