HLJ1/YMR161W Summary Help

Standard Name HLJ1 1
Systematic Name YMR161W
Feature Type ORF, Verified
Description Co-chaperone for Hsp40p; anchored in the ER membrane; with its homolog Ydj1p promotes ER-associated protein degradation (ERAD) of integral membrane substrates; similar to E. coli DnaJ (2, 3, 4, 5 and see Summary Paragraph)
Name Description HomoLogous to E. coli dnaJ protein
Chromosomal Location
ChrXIII:577718 to 578392 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All HLJ1 GO evidence and references
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 83 genes
Resources
Classical genetics
null
Large-scale survey
null
repressible
Resources
179 total interaction(s) for 101 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Affinity Capture-RNA: 1
  • PCA: 2

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 64
  • Phenotypic Enhancement: 26
  • Phenotypic Suppression: 74
  • Positive Genetic: 8
  • Synthetic Growth Defect: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 224
Molecular Weight (Da) 25,008
Isoelectric Point (pI) 10.07
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIII:577718 to 578392 | 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..675 577718..578392 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 SGDIDS000004771
SUMMARY PARAGRAPH for HLJ1

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 6, 7, and 8). 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 8). 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 (8).

Last updated: 2006-12-19 Contact SGD

References cited on this page View Complete Literature Guide for HLJ1
1) Stepanek, P., et al.  (1995) HLJ1, a Saccharomyces cerevisiae homolog of Escherichia coli dnaJ with a high-copy lethal phenotype. Unpublished
2) Beilharz T, et al.  (2003) Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J Biol Chem 278(10):8219-23
3) Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
4) Huyer G, et al.  (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 279(37):38369-78
5) Youker RT, et al.  (2004) Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol Biol Cell 15(11):4787-97
6) 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
7) Cyr DM, et al.  (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81
8) Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71