BAIT
FLCN
BHD, FLCL
folliculin
GO Process (28)
GO Function (2)
GO Component (5)
Gene Ontology Biological Process
- TOR signaling [IMP]
- cell-cell junction assembly [ISS]
- hemopoiesis [ISS]
- in utero embryonic development [ISS]
- negative regulation of ATP biosynthetic process [ISS]
- negative regulation of ERK1 and ERK2 cascade [ISS]
- negative regulation of Rho protein signal transduction [IMP]
- negative regulation of TOR signaling [ISS]
- negative regulation of cell growth [IDA]
- negative regulation of cell migration [IMP]
- negative regulation of cell proliferation involved in kidney development [ISS]
- negative regulation of energy homeostasis [ISS]
- negative regulation of gene expression [ISS]
- negative regulation of mitochondrion organization [ISS]
- negative regulation of protein kinase B signaling [ISS]
- negative regulation of protein localization to nucleus [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of TOR signaling [ISS]
- positive regulation of apoptotic process [ISS]
- positive regulation of cell adhesion [IMP]
- positive regulation of protein phosphorylation [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transforming growth factor beta receptor signaling pathway [IDA, ISS]
- regulation of TOR signaling [ISS]
- regulation of cytokinesis [IMP]
- regulation of histone acetylation [ISS]
- regulation of pro-B cell differentiation [ISS]
- regulation of protein phosphorylation [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
CCT8
C21orf112, Cctq, D21S246, PRED71
chaperonin containing TCP1, subunit 8 (theta)
GO Process (4)
GO Function (2)
GO Component (7)
Gene Ontology Biological Process
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
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]
Nat Commun Jun. 29, 2016; 7();12037 [Pubmed: 27353360]
Throughput
- Low Throughput
Curated By
- BioGRID