Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Global analysis of protein localization in budding yeast.
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.
A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p).
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Cdc37 supports HOG and PKC MAPK signaling by stabilizing/interacting with Hog1 and Slt2.
"levels of the MAPKs Hog1p and Slt2p (Mpk1p) in cells are reduced in a cdc37-S14A mutant, and consequently downstream responses mediated by Hog1p and Slt2p are compromised."
Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation.
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Cdc37 broadly stabilizes the yeast kinome.
"Of the 65 kinases assayed, 51 displayed reduced steady-state levels by at least twofold in the cdc37S14A mutant strain compared with the wild type."
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Cdc37 protects nascent kinase chains from rapid degradation.
"Results from our pulse-labeling studies showed that Cdc37 protects nascent kinase chains from rapid degradation shortly after synthesis."
An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.
Cdc37 is required for association of the protein kinase Cdc28 with G1 and mitotic cyclins.
The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication.
Cdc37 is a molecular chaperone with specific functions in signal transduction.
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Cdc37 has intrinsic chaperone activity and stabilizes kinase clients.
"In vitro, Cdc37 maintains denatured beta-galactosidase in an activation-competent state without reactivating it and stabilizes mature, but unstable, casein kinase II."
UniProt entry for CDC37/Hsp90 co-chaperone Cdc37
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UniProt summarizes Cdc37 as a kinase-binding Hsp90 co-chaperone.
"Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in their stabilization."
Falcon deep research report for CDC37
PANTHER family PTHR12800 CDC37-related metadata