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FKBP4 — HSP90AB1

Pathways - manually collected, often from reviews:

• Reactome Reaction: FKBP4 → HSP90AB1 (indirect_complex) Guo et al., J Biol Chem 2001*, Nair et al., Cell Stress Chaperones 1996

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Dip Interaction: Complex of HSP90AB1-FKBP4-STIP1 (physical association, cosedimentation in solution) Li et al., Nature structural & molecular biology 2011
• IRef Dip Interaction: Complex of FKBP4-HSP90AB1-AR (anti bait coimmunoprecipitation) De Leon et al., Proc Natl Acad Sci U S A 2011*
• IRef Dip Interaction: FKBP4 — HSP90AB1 (direct interaction, anti bait coimmunoprecipitation) De Leon et al., Proc Natl Acad Sci U S A 2011*
• IRef Dip Interaction: FKBP4 — HSP90AB1 (direct interaction, cosedimentation in solution) Li et al., Nature structural & molecular biology 2011
• IRef Intact Interaction: Complex of 33 proteins (association, tandem affinity purification) Gano et al., Mol Cell Proteomics 2010
• IRef Intact Interaction: Complex of 29 proteins (association, anti tag coimmunoprecipitation) Skarra et al., Proteomics 2011
• IRef Intact Interaction: Complex of 29 proteins (association, tandem affinity purification) Gano et al., Mol Cell Proteomics 2010
• IRef Intact Interaction: Complex of 46 proteins (association, tandem affinity purification) Gano et al., Mol Cell Proteomics 2010

Text-mined interactions from Literome

Renoir et al., C R Acad Sci III 1992 : It is suggested that a functional interaction between HBI and receptor activity may be mediated by hsp90
Echeverría et al., Mol Cell Biol 2009 : Interestingly, the binding of hsp70 and p23 to Nup62 does not require the presence of hsp90, whereas the association of FKBP52 and PP5 is hsp90 dependent , as indicated by the results of experiments where the hsp90 function was disrupted with radicicol