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| Term | HSP90-CDC37 chaperone complex | ID (Ontology) | GO:1990565 (Gene Ontology) | |||||||
| Definition | A protein kinase chaperone complex required for the proper folding, maturation and stabilization of target proteins (mostly signaling protein kinases, some steroid hormone receptors), usually during or immediately after completion of translation. The highly conserved, phosphorylated CDC37-Ser13 (vertebrates) or cdc37-Ser14 (yeast) is essential for complex assembly and target protein binding. CDC37-Ser13 (Ser14) is phosphorylated by Casein kinase II (CK2), which in turn is a target of CDC37 creating a positive feedback loop. Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.[ PubMed:21855797 PubMed:22939624 ] | |||||||||
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intracellular anatomical structure |__cytoplasm_____________________________ cellular anatomical structure | |__cytoplasm_____________________________| intracellular protein-containing complex | |__protein folding chaperone complex_____| HSP90-CDC37 chaperone complex 1 rec. |
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| Is a | protein folding chaperone complex | ||
| Part of | cytoplasm | ||
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