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Protein

Heat shock factor protein

Gene

HSF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. Also required for growth at normal temperatures.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi172 – 277106Add
BLAST

GO - Molecular functioni

GO - Biological processi

  • negative regulation of TOR signaling Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • regulation of establishment of protein localization to chromosome Source: SGD
  • regulation of transcription from RNA polymerase II promoter Source: SGD
  • response to heat Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30575-MONOMER.
ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-3371511. HSF1 activation.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock factor protein
Short name:
HSF
Alternative name(s):
Heat shock transcription factor
Short name:
HSTF
Gene namesi
Name:HSF1
Ordered Locus Names:YGL073W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL073W.
SGDiS000003041. HSF1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 833833Heat shock factor proteinPRO_0000124581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei97 – 971PhosphothreonineCombined sources
Modified residuei450 – 4501PhosphoserineCombined sources
Modified residuei458 – 4581PhosphoserineCombined sources
Modified residuei471 – 4711PhosphoserineCombined sources
Modified residuei478 – 4781PhosphoserineCombined sources
Modified residuei528 – 5281PhosphoserineCombined sources

Post-translational modificationi

Exhibits temperature-dependent phosphorylation that activates the transcriptional capacity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP10961.
PeptideAtlasiP10961.

PTM databases

iPTMnetiP10961.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

BioGridi33176. 71 interactions.
DIPiDIP-2374N.
IntActiP10961. 14 interactions.
MINTiMINT-2784846.

Structurei

3D structure databases

DisProtiDP00135.
ProteinModelPortaliP10961.
SMRiP10961. Positions 173-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni350 – 40253Involved in trimerizationAdd
BLAST

Sequence similaritiesi

Belongs to the HSF family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000001182.
InParanoidiP10961.
KOiK09419.
OrthoDBiEOG7FFN1G.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 2 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10961-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNAANTGTT NESNVSDAPR IEPLPSLNDD DIEKILQPND IFTTDRTDAS
60 70 80 90 100
TTSSTAIEDI INPSLDPQSA ASPVPSSSFF HDSRKPSTST HLVRRGTPLG
110 120 130 140 150
IYQTNLYGHN SRENTNPNST LLSSKLLAHP PVPYGQNPDL LQHAVYRAQP
160 170 180 190 200
SSGTTNAQPR QTTRRYQSHK SRPAFVNKLW SMLNDDSNTK LIQWAEDGKS
210 220 230 240 250
FIVTNREEFV HQILPKYFKH SNFASFVRQL NMYGWHKVQD VKSGSIQSSS
260 270 280 290 300
DDKWQFENEN FIRGREDLLE KIIRQKGSSN NHNSPSGNGN PANGSNIPLD
310 320 330 340 350
NAAGSNNSNN NISSSNSFFN NGHLLQGKTL RLMNEANLGD KNDVTAILGE
360 370 380 390 400
LEQIKYNQIA ISKDLLRINK DNELLWQENM MARERHRTQQ QALEKMFRFL
410 420 430 440 450
TSIVPHLDPK MIMDGLGDPK VNNEKLNSAN NIGLNRDNTG TIDELKSNDS
460 470 480 490 500
FINDDRNSFT NATTNARNNM SPNNDDNSID TASTNTTNRK KNIDENIKNN
510 520 530 540 550
NDIINDIIFN TNLANNLSNY NSNNNAGSPI RPYKQRYLLK NRANSSTSSE
560 570 580 590 600
NPSLTPFDIE SNNDRKISEI PFDDEEEEET DFRPFTSRDP NNQTSENTFD
610 620 630 640 650
PNRFTMLSDD DLKKDSHTND NKHNESDLFW DNVHRNIDEQ DARLQNLENM
660 670 680 690 700
VHILSPGYPN KSFNNKTSST NTNSNMESAV NVNSPGFNLQ DYLTGESNSP
710 720 730 740 750
NSVHSVPSNG SGSTPLPMPN DNDTEHASTS VNQGENGSGL TPFLTVDDHT
760 770 780 790 800
LNDNNTSEGS TRVSPDIKFS ATENTKVSDN LPSFNDHSYS TQADTAPENA
810 820 830
KKRFVEEIPE PAIVEIQDPT EYNDHRLPKR AKK
Length:833
Mass (Da):93,282
Last modified:July 1, 1989 - v1
Checksum:iDE66A4DFC9BEEA1A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti522 – 5221S → F in AAA34689 (PubMed:3044612).Curated
Sequence conflicti557 – 58024FDIES…EEEET → LISNLIMTAKFQKFLLMTKK KKKP in AAA34689 (PubMed:3044612).CuratedAdd
BLAST
Sequence conflicti831 – 8311A → V in AAA34689 (PubMed:3044612).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03139 Genomic DNA. Translation: AAA34688.1.
M22040 Genomic DNA. Translation: AAA34689.1.
Z72596 Genomic DNA. Translation: CAA96777.1.
BK006941 Genomic DNA. Translation: DAA08031.1.
PIRiA31593.
RefSeqiNP_011442.3. NM_001180938.3.

Genome annotation databases

EnsemblFungiiYGL073W; YGL073W; YGL073W.
GeneIDi852806.
KEGGisce:YGL073W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03139 Genomic DNA. Translation: AAA34688.1.
M22040 Genomic DNA. Translation: AAA34689.1.
Z72596 Genomic DNA. Translation: CAA96777.1.
BK006941 Genomic DNA. Translation: DAA08031.1.
PIRiA31593.
RefSeqiNP_011442.3. NM_001180938.3.

3D structure databases

DisProtiDP00135.
ProteinModelPortaliP10961.
SMRiP10961. Positions 173-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33176. 71 interactions.
DIPiDIP-2374N.
IntActiP10961. 14 interactions.
MINTiMINT-2784846.

PTM databases

iPTMnetiP10961.

Proteomic databases

MaxQBiP10961.
PeptideAtlasiP10961.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL073W; YGL073W; YGL073W.
GeneIDi852806.
KEGGisce:YGL073W.

Organism-specific databases

EuPathDBiFungiDB:YGL073W.
SGDiS000003041. HSF1.

Phylogenomic databases

GeneTreeiENSGT00390000001182.
InParanoidiP10961.
KOiK09419.
OrthoDBiEOG7FFN1G.

Enzyme and pathway databases

BioCyciYEAST:G3O-30575-MONOMER.
ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-3371511. HSF1 activation.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.

Miscellaneous databases

NextBioi972333.
PROiP10961.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 2 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation."
    Sorger P.K., Pelham H.R.B.
    Cell 54:855-864(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Isolation of the gene encoding the S. cerevisiae heat shock transcription factor."
    Wiederrecht G., Seto D., Parker C.S.
    Cell 54:841-853(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-97; SER-458; SER-471; SER-478 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSF_YEAST
AccessioniPrimary (citable) accession number: P10961
Secondary accession number(s): D6VU70, P11529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 11, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.