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ATP5O — STIP1

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

Studies that report less than 10 interactions are marked with *

• IRef Intact Interaction: Complex of 185 proteins (association, cross-linking study) Humphries et al., Science signaling 2009
• IRef Intact Interaction: Complex of 244 proteins (association, pull down) Komarova et al., Mol Cell Proteomics 2011
• IRef Intact Interaction: Complex of 168 proteins (association, cross-linking study) Byron et al., Proteomics 2012
• IRef Intact Interaction: Complex of 306 proteins (association, pull down) Komarova et al., Mol Cell Proteomics 2011
• IRef Intact Interaction: Complex of 203 proteins (association, cross-linking study) Byron et al., Proteomics 2012
• IRef Intact Interaction: Complex of 156 proteins (association, anti tag coimmunoprecipitation) Lau et al., Cell 2012

Text-mined interactions from Literome

Wegele et al., J Biol Chem 2003 : Surprisingly, binding of Sti1 activates the ATPase of Ssa1 by a factor of about 200, which is in contrast to the behavior of Hop in the mammalian Hsp70 system
Jones et al., Mol Cell Biol 2004 : Sti1p , a TPR cochaperone homolog of mammalian Hop1 ( Hsp70/90 organizing protein ), activates Ssa1p ATPase , which promotes substrate binding by Ssa1p
Lee et al., EMBO J 2012 : Our data suggest that Sti1 inhibits Hsp90 's ATPase activity by preventing N-terminal dimerization and docking of the N-terminal domain with the middle domain
Prodromou et al., EMBO J 1999 : The inherent ATPase activity of Hsp90 is completely inhibited by binding of Sti1 , but is not affected by Cpr6, although Cpr6 can reactivate the ATPase activity by displacing Sti1 from Hsp90