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: chaperone binding; heat shock protein binding; Hsp90 protein binding; kinase binding; protein binding; protein kinase binding; protein kinase regulator activity; protein-tyrosine kinase activity; unfolded protein binding
Biological Process: peptidyl-tyrosine phosphorylation; protein folding; protein stabilization; protein targeting; regulation of cyclin-dependent protein kinase activity
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.