APJ1/YNL077W Summary Help

APJ1 BASIC INFORMATION

Standard Name APJ1
Systematic Name YNL077W
Feature Type ORF, Verified
Description Putative chaperone of the HSP40 (DNAJ) family; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies (1, 2 and see Summary Paragraph)
Name Description Anti-Prion DnaJ 1
GO Annotations All APJ1 GO evidence and references
    View Computational GO annotations for APJ1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Mutant Phenotype All APJ1 Phenotype details and references
Large-scale survey
null
Interactions APJ1 All interactions details and references
10 total interaction(s) for 10 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 6
Genetic Interactions
  • Dosage Rescue: 1
  • Synthetic Growth Defect: 2
Sequence Information
ChrXIV:481393 to 482979 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2010-01-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1587 481393..482979 2010-01-05 1996-07-31
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000005021

APJ1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
 GBrowse
  • Literature
  • Retrieve Sequences
  • Sequence Analysis Tools
  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
  • Maps & Displays
  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for APJ1

SUMMARY PARAGRAPH for APJ1

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 3, 4, and 5). 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 5). 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 (5).

Last updated: 2006-12-19

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for APJ1]

1) Kryndushkin DS, et al.  (2002) Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277(26):23702-8
2) Reinders J, et al.  (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54
3) 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
4) Cyr DM, et al.  (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81
5) Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71