| 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 | |
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| Molecular Function | |
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| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| 176 total interaction(s) for 98 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000004771 |
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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).
| 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 |







