BAIT
PRDX1
MSP23, NKEF-A, NKEFA, PAG, PAGA, PAGB, PRX1, PRXI, TDPX2, RP11-291L19.4
peroxiredoxin 1
GO Process (3)
GO Function (4)
GO Component (5)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
PRDX2
Tdpx1
peroxiredoxin 2
GO Process (21)
GO Function (2)
GO Component (4)
Gene Ontology Biological Process
- T cell proliferation [ISO]
- activation of MAPK activity [ISO]
- cellular response to oxidative stress [ISO]
- homeostasis of number of cells [ISO]
- hydrogen peroxide catabolic process [ISO]
- hydrogen peroxide metabolic process [ISO]
- negative regulation of NF-kappaB transcription factor activity [ISO]
- negative regulation of T cell differentiation [ISO]
- negative regulation of extrinsic apoptotic signaling pathway [ISO]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [ISO]
- negative regulation of lipopolysaccharide-mediated signaling pathway [ISO]
- negative regulation of neuron apoptotic process [IMP]
- negative regulation of reactive oxygen species metabolic process [ISO]
- positive regulation of blood coagulation [ISO]
- regulation of apoptotic process [ISO]
- regulation of hydrogen peroxide metabolic process [ISO]
- removal of superoxide radicals [ISO]
- respiratory burst involved in inflammatory response [ISO]
- response to lipopolysaccharide [ISO]
- response to oxidative stress [IMP, ISO]
- thymus development [ISO]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Rattus norvegicus
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
Structural and biochemical analyses reveal ubiquitin C-terminal hydrolase-L1 as a specific client of the peroxiredoxin II chaperone.
Peroxiredoxins (Prxs) play dual roles as both thiol-peroxidases and molecular chaperones. Peroxidase activity enables various intracellular functions, however, the physiological roles of Prxs as chaperones are not well established. To study the chaperoning function of Prx, we previously sought to identify heat-induced Prx-binding proteins as the clients of a Prx chaperone. By using His-tagged Prx I as a bait, we ... [more]
Arch. Biochem. Biophys. Dec. 15, 2017; 640();61-74 [Pubmed: 29339092]
Throughput
- High Throughput
Curated By
- BioGRID