a molecular chaperone that functions in cell signal transduction. Forms complexes with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. Also interacts with androgen receptor. It is thought to play a critical role in directing Hsp90 to its target kinases. Note: This description may include information from UniProtKB.
Molecular Function: protein C-terminus binding; protein kinase B binding; protein binding; heat shock protein binding; chaperone binding; unfolded protein binding; Hsp90 protein binding; protein kinase regulator activity; mitogen-activated protein kinase kinase kinase binding; kinase binding
Biological Process: protein folding; protein stabilization; regulation of cyclin-dependent protein kinase activity; protein targeting
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.