CDC37/YDR168W Summary Help

Standard Name CDC37 1, 2
Systematic Name YDR168W
Alias SMO1
Feature Type ORF, Verified
Description Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding (3, 4 and see Summary Paragraph)
Name Description Cell Division Cycle 5
Chromosomal Location
ChrIV:790328 to 791848 | ORF Map | GBrowse
Genetic position: 95 cM
Gene Ontology Annotations All CDC37 GO evidence and references
  View Computational GO annotations for CDC37
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Regulators 9 genes
Classical genetics
reduction of function
Large-scale survey
reduction of function
257 total interaction(s) for 195 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 14
  • Biochemical Activity: 1
  • Reconstituted Complex: 2
  • Two-hybrid: 15

Genetic Interactions
  • Dosage Growth Defect: 2
  • Dosage Rescue: 17
  • Negative Genetic: 121
  • Positive Genetic: 14
  • Synthetic Growth Defect: 33
  • Synthetic Lethality: 14
  • Synthetic Rescue: 3

Expression Summary
Length (a.a.) 506
Molecular Weight (Da) 58,385
Isoelectric Point (pI) 4.78
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:790328 to 791848 | ORF Map | GBrowse
Genetic position: 95 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1521 790328..791848 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002575

cdc37 was originally isolated in a mutant screen to identify genes required for the completion of start in the cell division cycle of yeast (6). Cdc37p plays a critical role in activating cyclin-dependent kinases (7). After the connection between Hsp82p and Cdc37p was made, several experiments were done to tie the functions of these proteins together. cdc37 hsp82 double mutants were shown to exhibit synthetic growth defects in yeast (8), and both mammalian Cdc37 and Hsp90 co-immunoprecipitate with the cell cycle regulator Cdk4 (9, 10). Cdc37p was then shown to be the 50 kDa protein found in complexes with several Hsp90 kinase targets (9). Because Cdc37p was only found in Hsp90 kinase complexes and not with other Hsp90 substrates, it was inititally proposed that Cdc37p may serve to target the Hsp90 chaperone complex specifically to its kinase substrates (9). Other work, however, has shown that Cdc37p affects some substrates independently of Hsp90, and Cdc37 itself acts as a chaperone in vitro; thus, its proposed function as just a targeting molecule may be an oversimplified model (8).

Last updated: 1999-03-23 Contact SGD

References cited on this page View Complete Literature Guide for CDC37
1) Reed SI  (1980) The selection of amber mutations in genes required for completion of start, the controlling event of the cell division cycle of S. cerevisiae. Genetics 95(3):579-88
2) Breter HJ, et al.  (1983) Isolation and transcriptional characterization of three genes which function at start, the controlling event of the Saccharomyces cerevisiae cell division cycle: CDC36, CDC37, and CDC39. Mol Cell Biol 3(5):881-91
3) Abbas-Terki T, et al.  (2002) The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically. Biol Chem 383(9):1335-42
4) Mandal AK, et al.  (2007) Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation. J Cell Biol 176(3):319-28
5) Hartwell LH, et al.  (1970) Genetic control of the cell-division cycle in yeast. I. Detection of mutants. Proc Natl Acad Sci U S A 66(2):352-9
6) Reed SI  (1980) The selection of S. cerevisiae mutants defective in the start event of cell division. Genetics 95(3):561-77
7) Deshaies RJ and Kirschner M  (1995) G1 cyclin-dependent activation of p34CDC28 (Cdc28p) in vitro. Proc Natl Acad Sci U S A 92(4):1182-6
8) Kimura Y, et al.  (1997) Cdc37 is a molecular chaperone with specific functions in signal transduction. Genes Dev 11(14):1775-85
9) Stepanova L, et al.  (1996) Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev 10(12):1491-502
10) Dai K, et al.  (1996) Physical interaction of mammalian CDC37 with CDK4. J Biol Chem 271(36):22030-4