JJJ1/YNL227C Summary Help

Standard Name JJJ1 1
Systematic Name YNL227C
Feature Type ORF, Verified
Description Co-chaperone that stimulates the ATPase activity of Ssa1p; required for a late step of ribosome biogenesis; associated with the cytosolic large ribosomal subunit; contains a J-domain; mutation causes defects in fluid-phase endocytosis (1, 2, 3 and see Summary Paragraph)
Name Description J-protein (Type III) 1
Chromosomal Location
ChrXIV:222431 to 220659 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All JJJ1 GO evidence and references
  View Computational GO annotations for JJJ1
Molecular Function
Manually curated
Biological Process
Manually curated
High-throughput
Cellular Component
Manually curated
High-throughput
Regulators 5 genes
Resources
Classical genetics
null
overexpression
Large-scale survey
null
overexpression
Resources
139 total interaction(s) for 116 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 4
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 9
  • Biochemical Activity: 13
  • Co-crystal Structure: 2
  • Reconstituted Complex: 2
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 5
  • Negative Genetic: 24
  • Positive Genetic: 65
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 3
  • Synthetic Rescue: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 590
Molecular Weight (Da) 68,782
Isoelectric Point (pI) 6.14
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIV:222431 to 220659 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
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..1773 222431..220659 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 SGDIDS000005171
SUMMARY PARAGRAPH for JJJ1

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 1). 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 1). 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 (1).

Last updated: 2006-12-19 Contact SGD

References cited on this page View Complete Literature Guide for JJJ1
1) Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71
2) Wiederkehr A, et al.  (2001) Identification and characterization of Saccharomyces cerevisiae mutants defective in fluid-phase endocytosis. Yeast 18(8):759-73
3) Meyer AE, et al.  (2007) The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis. Proc Natl Acad Sci U S A 104(5):1558-63
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