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
DLG4
PSD95, SAP-90, SAP90
discs, large homolog 4 (Drosophila)
GO Process (18)
GO Function (11)
GO Component (21)
Gene Ontology Biological Process
- alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering [ISS, TAS]
- axon guidance [TAS]
- dendritic spine morphogenesis [ISS]
- establishment of protein localization [IDA]
- learning [TAS]
- negative regulation of receptor internalization [ISS]
- nervous system development [TAS]
- positive regulation of cytosolic calcium ion concentration [ISS]
- positive regulation of excitatory postsynaptic membrane potential [ISS]
- positive regulation of synaptic transmission [ISS]
- protein complex assembly [IDA]
- protein localization to synapse [IDA]
- receptor localization to synapse [ISS]
- regulation of N-methyl-D-aspartate selective glutamate receptor activity [ISS]
- regulation of long-term neuronal synaptic plasticity [ISS]
- signal transduction [TAS]
- synaptic transmission [TAS]
- synaptic vesicle maturation [ISS]
Gene Ontology Molecular Function- D1 dopamine receptor binding [ISS]
- P2Y1 nucleotide receptor binding [ISS]
- PDZ domain binding [ISS]
- acetylcholine receptor binding [ISS]
- beta-1 adrenergic receptor binding [ISS]
- ionotropic glutamate receptor binding [ISS]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein complex binding [ISS]
- protein phosphatase binding [ISS]
- scaffold protein binding [ISS]
- D1 dopamine receptor binding [ISS]
- P2Y1 nucleotide receptor binding [ISS]
- PDZ domain binding [ISS]
- acetylcholine receptor binding [ISS]
- beta-1 adrenergic receptor binding [ISS]
- ionotropic glutamate receptor binding [ISS]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein complex binding [ISS]
- protein phosphatase binding [ISS]
- scaffold protein binding [ISS]
Gene Ontology Cellular Component
- alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex [ISS]
- cell junction [ISS]
- cortical cytoskeleton [IDA]
- cytoplasm [ISS]
- dendrite cytoplasm [ISS]
- dendritic spine [ISS]
- endocytic vesicle membrane [TAS]
- endoplasmic reticulum [ISS]
- excitatory synapse [ISS]
- extrinsic component of cytoplasmic side of plasma membrane [ISS]
- ionotropic glutamate receptor complex [ISS]
- juxtaparanode region of axon [ISS]
- neuron projection terminus [ISS]
- neuron spine [ISS]
- neuronal postsynaptic density [ISS]
- plasma membrane [ISS, TAS]
- postsynaptic density [ISS]
- postsynaptic membrane [IDA]
- synapse [IDA]
- synaptic vesicle [ISS]
- voltage-gated potassium channel complex [ISS]
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 both Alzheimer's disease (AD) and non-AD brain tissue
Curated By
- BioGRID