HSP90AA1
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- G2/M transition of mitotic cell cycle [TAS]
- axon guidance [TAS]
- chaperone-mediated protein complex assembly [IDA]
- innate immune response [TAS]
- mitochondrial transport [TAS]
- mitotic cell cycle [TAS]
- nitric oxide metabolic process [TAS]
- positive regulation of nitric oxide biosynthetic process [ISS]
- protein import into mitochondrial outer membrane [IDA]
- protein refolding [TAS]
- regulation of nitric-oxide synthase activity [TAS]
- response to unfolded protein [NAS]
- signal transduction [NAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ERN1
Gene Ontology Biological Process
- HAC1-type intron splice site recognition and cleavage [IDA]
- RNA phosphodiester bond hydrolysis, endonucleolytic [IDA, TAS]
- RNA splicing [IMP]
- activation of signaling protein activity involved in unfolded protein response [IDA, TAS]
- cell cycle arrest [ISS]
- cellular protein metabolic process [TAS]
- cellular response to vascular endothelial growth factor stimulus [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- endothelial cell proliferation [IDA]
- mRNA cleavage [IDA]
- mRNA splicing, via endonucleolytic cleavage and ligation [IDA]
- peptidyl-serine autophosphorylation [IDA]
- positive regulation of RNA splicing [IDA]
- positive regulation of endoplasmic reticulum unfolded protein response [IMP]
- protein phosphorylation [IDA]
- protein trans-autophosphorylation [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.
The molecular chaperone HSP90 regulates stability and function of multiple protein kinases. The HSP90-binding drug geldanamycin interferes with this activity and promotes proteasome-dependent degradation of most HSP90 client proteins. Geldanamycin also binds to GRP94, the HSP90 paralog located in the endoplasmic reticulum (ER). Because two of three ER stress sensors are transmembrane kinases, namely IRE1alpha and PERK, we investigated whether ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ERN1 HSP90AA1 | Affinity Capture-Western 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. | Low | - | BioGRID | - |
Curated By
- BioGRID