CDC37

Hsp90 co-chaperone Cdc37 is a is_associated_with::protein that in humans is encoded by the CDC37 is_associated_with::gene.

The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of is_associated_with::Saccharomyces cerevisiae. This protein is a molecular chaperone with specific function in cell is_associated_with::signal transduction. It has been shown to form complex with is_associated_with::Hsp90 and a variety of is_associated_with::protein kinases including is_associated_with::CDK4, is_associated_with::CDK6, SRC, is_associated_with::RAF1, MOK, as well as eIF-2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.

Interactions
CDC37 has been shown to interact with:


 * CDK4,
 * HSP90AA1
 * is_associated_with::IKBKG,
 * is_associated_with::IKK2, and
 * is_associated_with::STK11.

Domain architecture
CDC37 consists of three structural domains. The is_associated_with::N-terminal domain binds to is_associated_with::protein kinases. The central domain is the is_associated_with::Hsp90 chaperone (heat shock protein 90) binding domain. The function of the C-terminal domain is unclear.