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
TWF2
A6RP, A6r, PTK9L, MSTP011
twinfilin actin-binding protein 2
GO Process (10)
GO Function (5)
GO Component (8)
Gene Ontology Biological Process
- barbed-end actin filament capping [ISS]
- cellular response to growth factor stimulus [IMP]
- cellular response to retinoic acid [IMP]
- negative regulation of actin filament polymerization [ISS]
- positive regulation of axon extension [IMP]
- positive regulation of lamellipodium assembly [IMP]
- positive regulation of neuron projection development [IMP]
- regulation of actin cytoskeleton organization [IMP]
- regulation of microvillus length [IC]
- sequestering of actin monomers [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
Alterations in the brain interactome of the intrinsically disordered N-terminal domain of the cellular prion protein (PrPC) in Alzheimer's disease.
The cellular prion protein (PrPC) is implicated in neuroprotective signaling and neurotoxic pathways in both prion diseases and Alzheimer's disease (AD). Specifically, the intrinsically disordered N-terminal domain (N-PrP) has been shown to interact with neurotoxic ligands, such as A? and Scrapie prion protein (PrPSc), and to be crucial for the neuroprotective activity of PrPC. To gain further insight into cellular ... [more]
PLoS One May. 24, 2018; 13(5);e0197659 [Pubmed: 29791485]
Throughput
- High Throughput
Additional Notes
- interaction identified using tandem mass spectrometry in Alzheimer's disease (AD) brain tissue but not in non-AD brain tissue
Curated By
- BioGRID