CWC23/YGL128C Summary Help

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)
Name Description Complexed With Cef1p 1
Chromosomal Location
ChrVII:270144 to 269293 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All CWC23 GO evidence and references
  View Computational GO annotations for CWC23
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Resources
Classical genetics
null
Large-scale survey
null
Resources
74 total interaction(s) for 33 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 54
  • Affinity Capture-RNA: 2
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Lethality: 2
  • Dosage Rescue: 2
  • Negative Genetic: 8
  • Synthetic Lethality: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 283
Molecular Weight (Da) 33,237
Isoelectric Point (pI) 6.11
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:270144 to 269293 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 2003-09-22
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..852 270144..269293 2011-02-03 2003-09-22
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003096
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 Contact SGD

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