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Protein

Heat shock factor protein 1

Gene

Hsf1

Organism
Mus musculus (Mouse)
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. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi15 – 120By similarityAdd BLAST106

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-3371511. HSF1 activation.
R-MMU-3371568. Attenuation phase.
R-MMU-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock factor protein 1
Short name:
HSF 1
Alternative name(s):
Heat shock transcription factor 1
Short name:
HSTF 1
Gene namesi
Name:Hsf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:96238. Hsf1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Cytoplasmic during normal growth. On activation, translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • euchromatin Source: Ensembl
  • heterochromatin Source: Ensembl
  • nuclear stress granule Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • PML body Source: UniProtKB
  • pronucleus Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5313.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001245681 – 525Heat shock factor protein 1Add BLAST525

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei121Phosphoserine; by MAPKAPK2By similarity1
Modified residuei142Phosphothreonine; by CK2By similarity1
Modified residuei230PhosphoserineBy similarity1
Modified residuei292PhosphoserineBy similarity1
Cross-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei303PhosphoserineCombined sources1
Modified residuei307PhosphoserineCombined sources1
Modified residuei314PhosphoserineBy similarity1
Modified residuei323PhosphothreonineBy similarity1
Modified residuei326PhosphoserineBy similarity1
Modified residuei345PhosphoserineBy similarity1
Modified residuei415PhosphoserineBy similarity1
Modified residuei440PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated on multiple serine residues, a subset of which are involved in stress-related regulation of transcription activation. Constitutive phosphorylation represses transcriptional activity at normal temperatures. Levels increase on specific residues heat-shock and enhance HSF1 transactivation activity. Phosphorylation on Ser-307 derepresses activation on heat-stress and in combination with Ser-303 phosphorylation appears to be involved in recovery after heat-stress. Phosphorylated on Ser-230 by CAMK2, in vitro. Cadmium also enhances phosphorylation at this site. Phosphorylation on Ser-303 is a prerequisite for HSF1 sumoylation. Phosphorylation on Ser-121 inhibits transactivation and promotes HSP90 binding. Phosphorylation on Thr-142 also mediates transcriptional activity induced by heat (By similarity).By similarity
Sumoylated with SUMO1 and SUMO2 on heat-shock. Heat-inducible sumoylation occurs after 15 min of heat-shock, after which levels decrease and at 4 hours, levels return to control levels. Sumoylation has no effect on HSE binding nor on transcriptional activity. Phosphorylation on Ser-303 is a prerequisite for sumoylation (By similarity). Phosphorylation on Ser-326 plays an important role in heat activation of HSF1 transcriptional activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP38532.
PaxDbiP38532.
PeptideAtlasiP38532.
PRIDEiP38532.

PTM databases

iPTMnetiP38532.
PhosphoSitePlusiP38532.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022556.
CleanExiMM_HSF1.
ExpressionAtlasiP38532. baseline and differential.
GenevisibleiP38532. MM.

Interactioni

Subunit structurei

Monomer (By similarity). Under normal conditions, interacts with HSP90AA1 in the HSP90 multichaperone complex; the interaction prevents trimerization and activation of HSF1. On activation by heat-stress or by other factors such as metal ions, HSF1 is released from the complex, homotrimerizes, is hyperphosphorylated and translocated to the nucleus where, subsequently, it can activate transcription. Binds the complex through the regulatory domain. Interacts with SYMPK and CSTF2 in heat-stressed cells. Interacts with FKBP4 in the HSP90 multichaperone complex; the interaction is independent of the phosphorylation state of HSF1. Interacts with MAPKAPK2. Interacts with EEF1D at heat shock promoter elements (HSE) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200443. 14 interactors.
IntActiP38532. 13 interactors.
STRINGi10090.ENSMUSP00000072617.

Chemistry databases

BindingDBiP38532.

Structurei

3D structure databases

ProteinModelPortaliP38532.
SMRiP38532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni130 – 203Hydrophobic repeat HR-A/BAdd BLAST74
Regioni221 – 310Regulatory domainAdd BLAST90
Regioni367 – 525Transactivation domainAdd BLAST159
Regioni380 – 405Hydrophobic repeat HR-CAdd BLAST26

Sequence similaritiesi

Belongs to the HSF family.Curated

Phylogenomic databases

eggNOGiKOG0627. Eukaryota.
COG5169. LUCA.
GeneTreeiENSGT00390000001182.
HOGENOMiHOG000253917.
HOVERGENiHBG005999.
InParanoidiP38532.
KOiK09414.
OMAiQFSLEHV.
PhylomeDBiP38532.
TreeFamiTF330401.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR027072. HSF1.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR010542. Vert_HSTF_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 2 hits.
PTHR10015:SF182. PTHR10015:SF182. 2 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P38532-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLAVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG
60 70 80 90 100
QFAKEVLPKY FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ
110 120 130 140 150
HPCFLRGQEQ LLENIKRKVT SVSTLKSEDI KIRQDSVTRL LTDVQLMKGK
160 170 180 190 200
QECMDSKLLA MKHENEALWR EVASLRQKHA QQQKVVNKLI QFLISLVQSN
210 220 230 240 250
RILGVKRKIP LMLSDSNSAH SVPKYGRQYS LEHVHGPGPY SAPSPAYSSS
260 270 280 290 300
SLYSSDAVTS SGPIISDITE LAPTSPLASP GRSIDERPLS SSTLVRVKQE
310 320 330 340 350
PPSPPHSPRV LEASPGRPSS MDTPLSPTAF IDSILRESEP TPAASNTAPM
360 370 380 390 400
DTTGAQAPAL PTPSTPEKCL SVACLDKNEL SDHLDAMDSN LDNLQTMLTS
410 420 430 440 450
HGFSVDTSAL LDLFSPSVTM PDMSLPDLDS SLASIQELLS PQEPPRPIEA
460 470 480 490 500
ENSNPDSGKQ LVHYTAQPLF LLDPDAVDTG SSELPVLFEL GESSYFSEGD
510 520
DYTDDPTISL LTGTEPHKAK DPTVS
Length:525
Mass (Da):57,223
Last modified:August 30, 2002 - v2
Checksum:iDCB6418FC12F5F43
GO
Isoform 1 (identifier: P38532-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     413-434: Missing.

Show »
Length:503
Mass (Da):54,931
Checksum:i0795ABB6FA169F7B
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002416413 – 434Missing in isoform 1. 2 PublicationsAdd BLAST22

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61753 mRNA. Translation: CAA43892.1.
BC013716 mRNA. Translation: AAH13716.1.
AF059275 Genomic DNA. Translation: AAC80425.1.
CCDSiCCDS27572.1. [P38532-2]
PIRiA40583.
RefSeqiNP_032322.1. NM_008296.3. [P38532-2]
UniGeneiMm.347444.

Genome annotation databases

EnsembliENSMUST00000072838; ENSMUSP00000072617; ENSMUSG00000022556. [P38532-2]
GeneIDi15499.
KEGGimmu:15499.
UCSCiuc056yzg.1. mouse. [P38532-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61753 mRNA. Translation: CAA43892.1.
BC013716 mRNA. Translation: AAH13716.1.
AF059275 Genomic DNA. Translation: AAC80425.1.
CCDSiCCDS27572.1. [P38532-2]
PIRiA40583.
RefSeqiNP_032322.1. NM_008296.3. [P38532-2]
UniGeneiMm.347444.

3D structure databases

ProteinModelPortaliP38532.
SMRiP38532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200443. 14 interactors.
IntActiP38532. 13 interactors.
STRINGi10090.ENSMUSP00000072617.

Chemistry databases

BindingDBiP38532.
ChEMBLiCHEMBL5313.

PTM databases

iPTMnetiP38532.
PhosphoSitePlusiP38532.

Proteomic databases

MaxQBiP38532.
PaxDbiP38532.
PeptideAtlasiP38532.
PRIDEiP38532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072838; ENSMUSP00000072617; ENSMUSG00000022556. [P38532-2]
GeneIDi15499.
KEGGimmu:15499.
UCSCiuc056yzg.1. mouse. [P38532-1]

Organism-specific databases

CTDi3297.
MGIiMGI:96238. Hsf1.

Phylogenomic databases

eggNOGiKOG0627. Eukaryota.
COG5169. LUCA.
GeneTreeiENSGT00390000001182.
HOGENOMiHOG000253917.
HOVERGENiHBG005999.
InParanoidiP38532.
KOiK09414.
OMAiQFSLEHV.
PhylomeDBiP38532.
TreeFamiTF330401.

Enzyme and pathway databases

ReactomeiR-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-3371511. HSF1 activation.
R-MMU-3371568. Attenuation phase.
R-MMU-3371571. HSF1-dependent transactivation.

Miscellaneous databases

PROiP38532.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022556.
CleanExiMM_HSF1.
ExpressionAtlasiP38532. baseline and differential.
GenevisibleiP38532. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR027072. HSF1.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR010542. Vert_HSTF_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 2 hits.
PTHR10015:SF182. PTHR10015:SF182. 2 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHSF1_MOUSE
AccessioniPrimary (citable) accession number: P38532
Secondary accession number(s): O70462
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: August 30, 2002
Last modified: November 30, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.