JJJ1/YNL227C Summary

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.

Gene Ontology Annotations All JJJ1 GO evidence and references

	View Computational GO annotations for JJJ1
Molecular Function
Manually curated	ATPase activator activity (IDA)
Biological Process
Manually curated	endocytosis (IMP) ribosomal large subunit biogenesis (IMP) ribosomal subunit export from nucleus (IMP) rRNA processing (IMP)
High-throughput	regulation of cell size (IMP)
Cellular Component
Manually curated	cytoplasm (IDA) cytosol (IDA) colocalizes_with cytosolic large ribosomal subunit (IDA) nucleolus (IMP)
High-throughput	cytoplasm (IDA) mitochondrion (IDA)

Mutant phenotypes All JJJ1 Phenotype evidence and references

Classical genetics
null	27S rRNA precursor accumulation: increased cold sensitivity: increased Arx1p accumulation: increased Rpl25-GFP accumulation: increased GFP-Rap1 distribution: abnormal Slt2p modification: increased resistance to Calcofluor White: decreased resistance to sirolimus: decreased resistance to fluconazole: decreased resistance to cycloheximide: decreased
overexpression	TBSV replicon RNA (repRNA) accumulation: increased
Large-scale survey
null	cell cycle progression in G1 phase: delayed cell size: decreased cold sensitivity: increased competitive fitness: decreased fermentative growth: decreased rate haploinsufficient resistance to amitrole: decreased resistance to cycloheximide: decreased resistance to sodium arsenite: increased resistance to camptothecin: increased resistance to hydroxyurea: increased resistance to methyl methanesulfonate: increased resistance to mycophenolic acid: increased resistance to tunicamycin: increased resistance to benzo[a]pyrene: decreased sporulation: abnormal stress resistance: increased toxin resistance: increased vacuolar morphology: abnormal vegetative growth: decreased rate viable
overexpression	filamentous growth: increased
Resources	PROPHECY \| SCMD \| ScreenTroll \| Yeast Fitness Database

interactions All JJJ1 Interaction evidence and references

	135 total interaction(s) for 112 unique genes/features.
Physical Interactions	Affinity Capture-MS: 3 Affinity Capture-RNA: 1 Affinity Capture-Western: 9 Biochemical Activity: 13 Reconstituted Complex: 2 Two-hybrid: 4
Genetic Interactions	Dosage Lethality: 1 Dosage Rescue: 5 Negative Genetic: 24 Positive Genetic: 64 Synthetic Growth Defect: 4 Synthetic Lethality: 3 Synthetic Rescue: 2
Resources	BioGRID \| BOND \| BioPIXIE \| CYC2008 (complexes) \| Complexome \| DIP \| DRYGIN \| GeneMANIA \| InterologFinder

Expression Summary


Resources	Expression Summary \| Cell cycle and metabolic oscillation \| Cell cycle transcript profile \| Cyclebase \| Genevestigator \| GermOnline \| SPELL \| YMGV \| YeastFunc

Protein Information All JJJ1 Protein evidence and references

Localization	YeastRC \| Organelle DB (UMich) \| YPL+ \| YeastGFP
Phosphorylation	PhosphoGRID \| PhosphoPep Database
Structure	GPMDB \| SCOP \| YeastRC
Homologs	Ashbya (AGD) \| AspGD Homologs \| CGD Homologs \| CandidaDB Homologs \| Fungal Orthogroups Repository \| P-POD \| PDB Homologs \| PhylomeDB \| YGOB \| YOGY

sequence information

ChrXIV:222431 to 220659 | |

Note: this feature is encoded on the Crick strand.

Last Update

Coordinates: 2011-02-03 | Sequence: 1996-07-31

Subfeature details

	Relative Coordinates	Chromosomal Coordinates	Most Recent Updates
	Relative Coordinates	Chromosomal Coordinates	Coordinates	Sequence
CDS	1..1773	222431..220659	2011-02-03	1996-07-31

Retrieve sequences

Analyze Sequence

S288C only	BLASTP \| ATCC/WashU Clones \| BLASTN \| Design Primers \| Restriction Fragment Map \| Restriction Fragment Sizes \| Six-Frame Translation
S288C vs. other species	Fungal Alignment \| BLASTN vs. fungi \| BLASTP at NCBI \| BLASTP vs. fungi \| Synteny Viewer
S288C vs. other strains	Strain Alignment

Resources

External Links	All Associated Seq \| Entrez Gene \| Entrez RefSeq Protein \| MIPS \| Search all NCBI (Entrez) \| UniProtKB

Primary SGDID	S000005171

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

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