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hsp90 Hsp90 chaperone [ Schizosaccharomyces pombe (fission yeast) ]

Gene ID: 2543539, updated on 4-Feb-2026
Official Symbol
hsp90
Official Full Name
Hsp90 chaperone
Primary source
PomBase:SPAC926.04c
Locus tag
SPOM_SPAC926.04C
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Schizosaccharomyces pombe (strain: 972h-)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces
Also known as
git10; swo1
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See hsp90 in Genome Data Viewer
Location:
chromosome: I
Exon count:
1
Sequence:
Chromosome: I; NC_003424.3 (3888558..3891139, complement)

Chromosome I - NC_003424.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene protein Ina22 Neighboring gene myosin II regulatory light chain Rlc1 Neighboring gene 5S ribosomal RNA Neighboring gene ncRNA Neighboring gene diphthamide biosynthesis protein Dph4

Genomic Sequence:
NC_003424.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. The molecular chaperone Hsp90 regulates heterochromatin assembly through stabilizing multiple complexes in fission yeast. Sun L, et al. J Cell Sci, 2020 Jul 7. PMID 32499408
  2. How does Hsp90 function in RNAi-dependent heterochromatin assembly? Kato H, et al. Curr Genet, 2019 Feb. PMID 29974204
  3. Protein phosphatase 2C, encoded by ptc1+, is important in the heat shock response of Schizosaccharomyces pombe. Shiozaki K, et al. Mol Cell Biol, 1994 Jun. PMID 8196617, Free PMC Article
  4. Genetic interactions between Hsp90 and the Cdc2 mitotic machinery in the fission yeast Schizosaccharomyces pombe. Muñoz MJ, et al. Mol Gen Genet, 1999 Mar. PMID 10102358
  5. Radicicol binding to Swo1/Hsp90 and inhibition of growth of specific temperature-sensitive cell cycle mutants of fission yeast. Ki SW, et al. Biosci Biotechnol Biochem, 2001 Nov. PMID 11791728

See all (39) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Studies suggest that it is possible that heat-shock protein 90 (Hsp90) and other molecular chaperones contribute to the modulation of still-unknown factors that regulate the intracellular heterochromatin assembly process [Review].
    Title: How does Hsp90 function in RNAi-dependent heterochromatin assembly?
  2. Study identified the S. pombe molecular chaperone proteins Hsp90 and Mas5 as novel regulators of RNAi-dependent heterochromatin assembly. Mutations in the genes encoding these proteins caused derepression of transcriptional silencing and decreases in H3K9me at the pericentromeric heterochromatin region, while having little effect on the subtelomeric heterochromatin, which can be maintained in the absence of RNAi.
    Title: RNAi-dependent heterochromatin assembly in fission yeast Schizosaccharomyces pombe requires heat-shock molecular chaperones Hsp90 and Mas5.
  3. Cochaperones can modify Hsp90 by strengthening of the coupling between ATP hydrolysis and a kinetic step involved in the Hsp90 system resulting in a stronger directionality.
    Title: Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery.
  4. The co-chaperones Sti1 and Aha1 bound Hsp90 and modulated its activity
    Title: Biochemical characterization and cooperation with co-chaperones of heat shock protein 90 from Schizosaccharomyces pombe.
  5. cochaperone Hsp90 may not be essential for Cdc37 function in S. pombe
    Title: Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90.
  6. Analyses of Myo2p, Swo1p, and the UCS domain protein Rng3p establish that Swo1p and Rng3p collaborate in vivo to modulate myosin II function.
    Title: Hsp90 protein in fission yeast Swo1p and UCS protein Rng3p facilitate myosin II assembly and function.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by PomBase

Function Evidence Code Pubs
enables ATP binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
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-dependent protein folding chaperone EXP
Inferred from Experiment
more info
 PubMed 
enables ATP-dependent protein folding chaperone IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP-dependent protein folding chaperone IEA
Inferred from Electronic Annotation
more info
  
enables ATP-dependent protein folding chaperone TAS
Traceable Author Statement
more info
 PubMed 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables protein folding chaperone EXP
Inferred from Experiment
more info
 PubMed 
enables unfolded protein binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in 'de novo' cotranslational protein folding TAS
Traceable Author Statement
more info
 PubMed 
involved_in cellular response to heat IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein folding IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein folding IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
  
involved_in protein folding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein stabilization IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol HDA PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in mitochondrion ISO
Inferred from Sequence Orthology
more info
  
is_active_in perinuclear region of cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in plasma membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in protein aggregate center IDA
Inferred from Direct Assay
more info
 PubMed 
part_of protein-containing complex IBA
Inferred from Biological aspect of Ancestor
more info
  
Preferred Names
Hsp90 chaperone

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Genome Annotation

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

Reference assembly

Genomic

  1. NC_003424.3 Reference assembly

    Range
    3888558..3891139 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001019786.3 → NP_594365.1  Hsp90 chaperone [Schizosaccharomyces pombe]

    See identical proteins and their annotated locations for NP_594365.1

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    P41887, Q9UUG4
    Conserved Domains (3) summary
    cd00075
    Location:29 → 161
    HATPase_c; Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins
    PTZ00272
    Location:4 → 704
    PTZ00272; heat shock protein 83 kDa (Hsp83); Provisional
    pfam00183
    Location:185 → 704
    HSP90; Hsp90 protein
Nucleotide Protein
Heading Accession and Version

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