CWC23/YGL128C Summary 
CWC23 BASIC INFORMATION
| Standard Name | CWC23 1 |
|---|---|
| Systematic Name | YGL128C |
| Feature Type | ORF, Verified |
| Description | Component of a complex containing Cef1p, putatively involved in pre-mRNA splicing; has similarity to E. coli DnaJ and other DnaJ-like proteins and to S. pombe Cwf23p (1, 2, 3 and see Summary Paragraph) 
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| Name Description | Complexed With Cef1p 1 |
| GO Annotations | All CWC23 GO evidence and references |
|---|---|
| View Computational GO annotations for CWC23 | |
| Molecular Function | |
| Manually curated |
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| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Mutant Phenotype | All CWC23 Phenotype details and references |
|---|---|
| Classical genetics | |
| null |
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| Large-scale survey | |
| null |
| Interactions | CWC23 All interactions details and references |
|---|---|
| 63 total interaction(s) for 23 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000003096 |
|---|
CWC23 RESOURCES
| SGD ORF map | GBrowse |
|---|---|
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Click on histogram for expression summary
Expression Summary
ADDITIONAL INFORMATION for CWC23
SUMMARY PARAGRAPH for CWC23
Hsp40/DnaJ is a family of proteins, established by bacterial DnaJ, that regulates Hsp70 chaperone activity. Hsp40s stimulate the intrinsically weak ATPase activity of Hsp70 proteins and facilitate Hsp70 interaction with polypeptide substrates. Hsp70 family members often have multiple Hsp40 partners, and these specific pairings govern Hsp70 chaperone involvement in particular processes (reviewed in 4, 5, and 6). All Hsp40s contain a highly conserved 75-amino acid J domain, which interacts with the ATPase domain of Hsp70 to stimulate ATP hydrolysis. However, there are also other conserved structural domains, and based on the presence or absence of these regions, the Hsp40 family can be divided into three subtypes: type I, type II and type III (a comprehensive overview of the structural features of the different HSP40 subtypes can be found in 6). Sequence analysis of the S. cerevisiae genome has revealed 22 proteins in the Hsp40/DnaJ family: YDJ1, XDJ1, APJ1, SIS1, DJP1, ZUO1, SWA2, JJJ1, JJJ2, JJJ3, CAJ1, CWC23, MDJ1, MDJ2, PAM18, JAC1, JID1, SCJ1, HLJ1, JEM1, SEC63, and ERJ5 (6).
Last updated: 2006-12-19
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for CWC23]
| 1) | Ohi MD, et al. (2002) Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs. Mol Cell Biol 22(7):2011-24 |
| 2) | Haurie V, et al. (2001) The transcriptional activator Cat8p provides a major contribution to the reprogramming of carbon metabolism during the diauxic shift in Saccharomyces cerevisiae. J Biol Chem 276(1):76-85 |
| 3) | Tizon B, et al. (1999) Disruption of six novel Saccharomyces cerevisiae genes reveals that YGL129c is necessary for growth in non-fermentable carbon sources, YGL128c for growth at low or high temperatures and YGL125w is implicated in the biosynthesis of methionine. Yeast 15(2):145-54 |
| 4) | Qiu XB, et al. (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63(22):2560-2570 |
| 5) | Cyr DM, et al. (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81 |
| 6) | Walsh P, et al. (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71 |
