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HSP90AA1 — S100A2

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

Studies that report less than 10 interactions are marked with *

• IRef Intact Interaction: Complex of HSP90AA1-S100A2 (association, anti tag coimmunoprecipitation) Shimamoto et al., FEBS Lett 2010*
• IRef Intact Interaction: Complex of 156 proteins (association, anti tag coimmunoprecipitation) Lau et al., Cell 2012
• IRef Intact Interaction: Complex of S100A2-FKBP4-HSP90AA1 (association, anti tag coimmunoprecipitation) Shimamoto et al., FEBS Lett 2010*

Text-mined interactions from Literome

Shimamoto et al., FEBS Lett 2010 : Using glutathione-S transferase pull-down assays and immunoprecipitation, we have demonstrated that S100A1 and S100A2 specifically interact with the TPR domains of FKBP52 and CyP40 in a Ca ( 2+ ) -dependent manner, and lead to inhibition of the CyP40-Hsp90 and FKBP52-Hsp90 interactions
Shimamoto et al., J Biol Chem 2013 : GST pulldown assays indicated that Ca/S100A2 and S100P bind to the TPR domain and lead to interference with the interactions of CHIP with Hsp70, Hsp90 , HSF1, and Smad1