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FKBP4 — HSP90AB1
Pathways - manually collected, often from reviews:
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
EcheverrÃa 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