HSP104 chaperone ATPase HSP104 [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Gene symbol: HSP104
Gene description: chaperone ATPase HSP104
Primary source: SGD:S000003949
Locus tag: YLL026W
See related: AllianceGenome:SGD:S000003949
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables several functions, including ATP hydrolysis activity; adenyl ribonucleotide binding activity; and chaperone binding activity. Involved in several processes, including cellular response to heat; chaperone cofactor-dependent protein refolding; and protein folding in endoplasmic reticulum. Located in cytoplasm and nuclear periphery. Part of TRC complex. Human ortholog(s) of this gene implicated in 3-methylglutaconic aciduria with cataracts, neurologic involvement and neutropenia. Orthologous to human CLPB (caseinolytic mitochondrial matrix peptidase chaperone subunit B). [provided by Alliance of Genome Resources, Apr 2022]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

Location:: chromosome: XII

Exon count:: 1

Sequence:: Chromosome: XII; NC_001144.5 (88623..91349)

Chromosome XII - NC_001144.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.
Title: Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.
Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [PSI[+]] Curing by Hsp104 Overexpression.
Title: Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [PSI(+)] Curing by Hsp104 Overexpression.
Substoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of Sup35 prion domain.
Title: Substoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of Sup35 prion domain.
Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation.
Title: Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation.
A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors.
Title: A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors.
Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.
Title: Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.
Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.
Title: Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.
Hsp104-dependent ability to assimilate mannitol and sorbitol conferred by a truncated Cyc8 with a C-terminal polyglutamine in Saccharomyces cerevisiae.
Title: Hsp104-dependent ability to assimilate mannitol and sorbitol conferred by a truncated Cyc8 with a C-terminal polyglutamine in Saccharomyces cerevisiae.
ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo.
Title: ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo.
Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.
Title: Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.

Submit: New GeneRIF Correction See all GeneRIFs (79)

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ADP binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP hydrolysis activity	IDA Inferred from Direct Assay more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular heat acclimation	IBA Inferred from Biological aspect of Ancestor more info
involved_in cellular heat acclimation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in chaperone cofactor-dependent protein refolding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding in endoplasmic reticulum	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein unfolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein unfolding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in stress granule disassembly	IDA Inferred from Direct Assay more info	PubMed
involved_in trehalose metabolism in response to heat stress	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of TRC complex	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	HDA more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in nuclear periphery	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: chaperone ATPase HSP104

NP_013074.1

Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate denatured, protein aggregates; responds to stresses (heat, ethanol, and sodium arsenite); required for the protein aggregate solid-to-liquid phase transition and dispersal of liquid condensates; involved in [PSI+] propagation; potentiated variants eliminate TDP-43 cytoplasmic aggregates to reduce proteotoxicity; becomes more abundant and forms cytoplasmic foci during replication stress

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001144.5 Reference assembly

Range

88623..91349

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181846.1 → NP_013074.1 TPA: chaperone ATPase HSP104 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013074.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VXX8, P31539

UniProtKB/TrEMBL

A0A6A5PQJ0, A7A0N1, B3LTE4, B5VMS0, C7GQD8, C8ZCU6, N1NZK6

Conserved Domains (1) summary

TIGR03346
Location:7 → 863

chaperone_ClpB; ATP-dependent chaperone ClpB

Nucleotide		Protein
Heading	Accession and Version	Protein

Protein Accession	Links
Protein Accession	GenPept Link	UniProtKB Link
5VJH_A.1
5VJH_B.1
5VJH_C.1
5VJH_D.1
5VJH_E.1
5VJH_F.1
5VY8_A.1
5VY8_B.1
5VY8_C.1
5VY8_D.1
5VY8_E.1
5VY8_F.1
5VY9_A.1
5VY9_B.1
5VY9_C.1
5VY9_D.1
5VY9_E.1
5VY9_F.1
5VYA_A.1
5VYA_B.1
5VYA_C.1
5VYA_D.1
5VYA_E.1
5VYA_F.1
P31539.2