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YEAST:HSF

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) HSF1
Protein Name(s) Heat shock factor protein

HSF Heat shock transcription factor HSTF

External Links
UniProt P10961
EMBL J03139
M22040
Z72596
BK006941
PIR A31593
RefSeq NP_011442.3
DisProt DP00135
ProteinModelPortal P10961
SMR P10961
BioGrid 33176
DIP DIP-2374N
IntAct P10961
MINT MINT-2784846
STRING 4932.YGL073W
MaxQB P10961
PaxDb P10961
PeptideAtlas P10961
EnsemblFungi [example_ID YGL073W]
GeneID 852806
KEGG sce:YGL073W
CYGD YGL073w
SGD S000003041
eggNOG COG5169
GeneTree ENSGT00390000001182
InParanoid P10961
KO K09419
OrthoDB EOG7FFN1G
BioCyc YEAST:G3O-30575-MONOMER
Reactome REACT_205607
REACT_209789
REACT_219346
REACT_271186
NextBio 972333
Proteomes UP000002311
Genevestigator P10961
GO GO:0005634
GO:0043565
GO:0003700
GO:0032007
GO:0006357
GO:0009408
GO:0030474
GO:0006351
Gene3D 1.10.10.10
InterPro IPR000232
IPR027725
IPR011991
PANTHER PTHR10015
Pfam PF00447
PRINTS PR00056
SMART SM00415
PROSITE PS00434

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005739

mitochondrion

PMID:16823961[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:19111667[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:14576278[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

PMID:8745404[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:8745404[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0070202

regulation of establishment of protein localization to chromosome

PMID:23447536[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045944

positive regulation of transcription by RNA polymerase II

PMID:27320198[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_regulation_target:(UniProtKB:P31539)|has_regulation_target:(UniProtKB:P02829)|has_regulation_target:(UniProtKB:P25491)|has_regulation_target:(UniProtKB:P15108)|has_regulation_target:(UniProtKB:P10591)|has_regulation_target:(UniProtKB:P10592)|has_regulation_target:(UniProtKB:P53286)|has_regulation_target:(UniProtKB:P33416)|has_regulation_target:(UniProtKB:P25294)|has_regulation_target:(UniProtKB:P15705)|has_regulation_target:(UniProtKB:P35191)|has_regulation_target:(UniProtKB:O14467)|has_regulation_target:(UniProtKB:P53691)|has_regulation_target:(UniProtKB:Q12449)|has_regulation_target:(UniProtKB:P38260)|has_regulation_target:(UniProtKB:Q06469)|has_regulation_target:(UniProtKB:Q12329)|has_regulation_target:(UniProtKB:P53834)

Seeded From UniProt

complete

GO:1900036

positive regulation of cellular response to heat

PMID:22970306[7]

ECO:0000315

P

Deletion of Sir2 in a wild-type yeast positively regulates the HSF1 trimerizing and binding to HSE1. The positive regulation of HSF1 increases the amount of poly-glutamine CAG repeats seen in proteins. In Figure 1, a SDS-PAGE gel resolved with cell lysates from cultures that underwent heat-shock combined immunobloting with a mouse anti-flag antibody for the different poly-Q protein segments.

complete

involved_in

GO:0045944

positive regulation of transcription by RNA polymerase II

PMID:9296388[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

  • has_regulation_target:(SGD:S000004798)
  • happens_during:(GO:0034605)|has_regulation_target(SGD:S000006161)
  • happens_during:(GO:0034605)

Seeded From UniProt

complete

involved_in

GO:0032007

negative regulation of TOR signaling

PMID:18270585[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:3044612[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:8985158[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:2017170[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006357

regulation of transcription by RNA polymerase II

PMID:3044612[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:12821147[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003700

DNA-binding transcription factor activity

PMID:3044612[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0061408

positive regulation of transcription from RNA polymerase II promoter in response to heat stress

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000001154
UniProtKB:Q00613

P

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0001222
MGI:MGI:1347058
MGI:MGI:3045337
MGI:MGI:96238
MGI:MGI:96239
PANTHER:PTN000001154
RGD:1310808
SGD:S000005666
UniProtKB:P38529
UniProtKB:P38531
UniProtKB:Q00613
ZFIN:ZDB-GENE-000616-16
ZFIN:ZDB-GENE-011128-1
ZFIN:ZDB-GENE-050306-18

F

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:3045337
PANTHER:PTN000001154
RGD:620913
UniProtKB:O80982
UniProtKB:P38529
UniProtKB:P38531
UniProtKB:Q00613

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000195882
FB:FBgn0001222
MGI:MGI:3045337
MGI:MGI:96238
MGI:MGI:96239
PANTHER:PTN000001154
PomBase:SPAC2E12.02
PomBase:SPAC8C9.14
RGD:1310808
RGD:620913
SGD:S000001249
SGD:S000003041
SGD:S000005666
TAIR:locus:2005495
TAIR:locus:2075447
TAIR:locus:2117139
TAIR:locus:2144603
TAIR:locus:2149050
UniProtKB:I1LGH5
UniProtKB:I1MPZ9
UniProtKB:K7LH36
UniProtKB:O80982
UniProtKB:P38529
UniProtKB:P38530
UniProtKB:P38531
UniProtKB:Q00613
UniProtKB:Q43457
UniProtKB:Q5A287
UniProtKB:Q942D6
UniProtKB:Q9UBD0
WB:WBGene00002004

C

Seeded From UniProt

complete

enables

GO:0003700

DNA-binding transcription factor activity

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000195882
FB:FBgn0001222
PANTHER:PTN000001154
SGD:S000001249
SGD:S000003041
TAIR:locus:2149050

F

Seeded From UniProt

complete

enables

GO:0000978

RNA polymerase II proximal promoter sequence-specific DNA binding

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:96238
MGI:MGI:96239
PANTHER:PTN000001154
PomBase:SPAC2E12.02
PomBase:SPAC8C9.14
SGD:S000005666
UniProtKB:Q00613

F

Seeded From UniProt

complete

enables

GO:0003700

DNA-binding transcription factor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000232

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000232

C

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000232

P

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000232

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
  2. ↑ Badis, G et al. (2008) A library of yeast transcription factor motifs reveals a widespread function for Rsc3 in targeting nucleosome exclusion at promoters. Mol. Cell 32 878-87 PubMed GONUTS page
  3. ↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
  4. ↑ 4.0 4.1 Cho, HS et al. (1996) Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. Protein Sci. 5 262-9 PubMed GONUTS page
  5. ↑ Kim, S & Gross, DS (2013) Mediator recruitment to heat shock genes requires dual Hsf1 activation domains and mediator tail subunits Med15 and Med16. J. Biol. Chem. 288 12197-213 PubMed GONUTS page
  6. ↑ Solís, EJ et al. (2016) Defining the Essential Function of Yeast Hsf1 Reveals a Compact Transcriptional Program for Maintaining Eukaryotic Proteostasis. Mol. Cell 63 60-71 PubMed GONUTS page
  7. ↑ Cohen, A et al. (2012) Aggregation of polyQ proteins is increased upon yeast aging and affected by Sir2 and Hsf1: novel quantitative biochemical and microscopic assays. PLoS ONE 7 e44785 PubMed GONUTS page
  8. ↑ Zarzov, P et al. (1997) A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication. J. Cell. Sci. 110 ( Pt 16) 1879-91 PubMed GONUTS page
  9. ↑ Bandhakavi, S et al. (2008) Hsf1 activation inhibits rapamycin resistance and TOR signaling in yeast revealed by combined proteomic and genetic analysis. PLoS ONE 3 e1598 PubMed GONUTS page
  10. ↑ 10.0 10.1 10.2 Wiederrecht, G et al. (1988) Isolation of the gene encoding the S. cerevisiae heat shock transcription factor. Cell 54 841-53 PubMed GONUTS page
  11. ↑ Nwaka, S et al. (1996) The heat shock factor and mitochondrial Hsp70 are necessary for survival of heat shock in Saccharomyces cerevisiae. FEBS Lett. 399 259-63 PubMed GONUTS page
  12. ↑ Smith, BJ & Yaffe, MP (1991) A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle. Mol. Cell. Biol. 11 2647-55 PubMed GONUTS page
  13. ↑ Kaida, D et al. (2003) Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in budding yeast. Biochem. Biophys. Res. Commun. 306 1037-41 PubMed GONUTS page
  14. ↑ 14.0 14.1 14.2 14.3 14.4 14.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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