APJ1/YNL077W Summary Help

Standard Name APJ1 1
Systematic Name YNL077W
Feature Type ORF, Verified
Description Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress (1, 2, 3, 4 and see Summary Paragraph)
Name Description Anti-Prion DnaJ 1
Chromosomal Location
ChrXIV:481391 to 482977 | ORF Map | GBrowse
Gbrowse
Gene Ontology 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
Regulators 18 genes
Resources
Classical genetics
null
overexpression
Large-scale survey
null
overexpression
Resources
36 total interaction(s) for 33 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 6

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 19
  • Phenotypic Enhancement: 1
  • Positive Genetic: 4
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 528
Molecular Weight (Da) 58,888
Isoelectric Point (pI) 6.87
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIV:481391 to 482977 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1587 481391..482977 2011-02-03 1996-07-31
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 SGDIDS000005021
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 5, 6, and 7). 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 7). 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 (7).

Last updated: 2006-12-19 Contact SGD

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) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
4) Sahi C, et al.  (2013) Sequential duplications of an ancient member of the DnaJ-family expanded the functional chaperone network in the eukaryotic cytosol. Mol Biol Evol 30(5):985-98
5) 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
6) Cyr DM, et al.  (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81
7) Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71