Cell Division Cycle Protein 37 (CDC37)
p50Cdc37; Hsp90 chaperone protein kinase-targeting subunit; Hsp90 co-chaperone Cdc37
Hsp90 co-chaperone Cdc37 is a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, as well as eIF-2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.
Human CDC37 contains 378 amino acids and shares 45% and 25% amino acid identity with Drosophila and S. cerevisiae CDC37, respectively. Mutations in yeast CDC37 cause cell cycle arrest in G1 phase, and yeast CDC37 is required for the association of CDC28 and cyclin and for the activation of CDC28.
Organism species: Homo sapiens (Human)
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Organism species: Mus musculus (Mouse)
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Organism species: Rattus norvegicus (Rat)
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