FNIP1
Gene Ontology Biological Process
- TOR signaling [IMP]
- cellular response to starvation [ISS]
- immature B cell differentiation [ISS]
- negative regulation of TOR signaling [ISS]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [ISS]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of B cell apoptotic process [ISS]
- positive regulation of GTPase activity [IDA]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- positive regulation of protein phosphorylation [IMP]
- regulation of pro-B cell differentiation [ISS]
- regulation of protein phosphorylation [IDA]
Gene Ontology Molecular Function
STIP1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-Western
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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and it is regulated by co-chaperones. Here we show that the tumour suppressor FLCN is an Hsp90 client protein and its binding partners FNIP1/FNIP2 function ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID