BAIT

FES

FPS
FES proto-oncogene, tyrosine kinase
Homo sapiens
PREY

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
Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor.

Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF

A variety of regulatory proteins, including different classes of transcription factors and protein kinases, have been identified in complexes with Hsp90. On careful examination of unactivated progesterone receptor complexes, eight different protein participants have been identified, and each can be considered a component of the cytoplasmic molecular chaperone machinery. These proteins are Hsp90, Hsp70, Hip, p60, p23, FKBP51, FKBP52 and ... [more]

Cell Stress Chaperones Dec. 01, 1996; 1(4);237-50 [Pubmed: 9222609]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HSP90AA1 FES
Affinity Capture-Luminescence
Affinity Capture-Luminescence

An interaction is inferred when a bait protein, tagged with luciferase, is enzymatically detected in immunoprecipitates of the prey protein as light emission. The prey protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag.

High-BioGRID
-

Curated By

  • BioGRID