BAIT
HSP90AA1
EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP-2, LAP2
heat shock protein 90kDa alpha (cytosolic), class A member 1
GO Process (16)
GO Function (10)
GO Component (10)
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
Homo sapiens
PREY
NUDCD3
NudCL, hCG_18301
NudC domain containing 3
GO Process (0)
GO Function (1)
GO Component (0)
Gene Ontology Molecular Function
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
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]
Mol. Cell Proteomics Feb. 01, 2010; 9(2);255-70 [Pubmed: 19875381]
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
Curated By
- BioGRID