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
DYNC1H1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.
Structural studies of the chaperone HSP90 have revealed that nucleotide and drug ligands induce several distinct conformational states; however, little is known how these conformations affect interactions with co-chaperones and client proteins. Here we use tandem affinity purification and LC-MS/MS to investigate the proteome-wide effects of ATP, ADP, and geldanamycin on the constituents of the human HSP90 interactome. We identified ... [more]
Throughput
- High Throughput
Ontology Terms
- cell line: hek-293 cell (BTO:0000007) [atp (CHEBI:15422)]
Additional Notes
- Mutants: HSP90AA1, Mutant: HSP90 E47A
- interaction increased in pull-downs using an E47A HSP90AA1 mutant that is unable to hydrolyze ATP
- interaction increased in the presence of ATP
- proteins pulled down using a TAP-tagged N- or C-terminal fragment of HSP90AA1
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| DYNC1H1 HSP90AA1 | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3679472 |
Curated By
- BioGRID