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
SCRIB
CRIB1, SCRB1, SCRIB1, Vartul
scribbled planar cell polarity protein
GO Process (13)
GO Function (1)
GO Component (9)
Gene Ontology Biological Process
- activation of Rac GTPase activity [IMP]
- apoptotic process involved in morphogenesis [IMP]
- cell migration [IMP]
- cell proliferation [IDA]
- establishment of apical/basal cell polarity [IMP]
- mammary gland duct morphogenesis [ISS]
- negative regulation of mitotic cell cycle [IDA]
- neural tube closure [IMP]
- positive chemotaxis [IMP]
- positive regulation of apoptotic process [IMP]
- positive regulation of receptor recycling [IMP]
- protein localization to adherens junction [IMP]
- single organismal cell-cell adhesion [IGI]
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
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
- 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