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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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi15 – 120106By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular response to heat Source: UniProtKB
  • defense response Source: Ensembl
  • embryonic placenta development Source: MGI
  • embryonic process involved in female pregnancy Source: MGI
  • female meiotic division Source: MGI
  • in utero embryonic development Source: MGI
  • mRNA transcription Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of tumor necrosis factor production Source: MGI
  • positive regulation of multicellular organism growth Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein phosphorylation Source: MGI
  • response to heat Source: MGI
  • response to lipopolysaccharide Source: MGI
  • spermatogenesis Source: MGI
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
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • pronucleus Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5313.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 525525Heat shock factor protein 1PRO_0000124568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei121 – 1211Phosphoserine; by MAPKAPK2By similarity
Modified residuei142 – 1421Phosphothreonine; by CK2By similarity
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei292 – 2921PhosphoserineBy similarity
Cross-linki298 – 298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei303 – 3031PhosphoserineCombined sources
Modified residuei307 – 3071PhosphoserineCombined sources
Modified residuei314 – 3141PhosphoserineBy similarity
Modified residuei323 – 3231PhosphothreonineBy similarity
Modified residuei326 – 3261PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei415 – 4151PhosphoserineBy similarity
Modified residuei440 – 4401PhosphoserineBy similarity

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.
PhosphoSiteiP38532.

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

Protein-protein interaction databases

BioGridi200443. 14 interactions.
IntActiP38532. 13 interactions.
STRINGi10090.ENSMUSP00000072617.

Chemistry

BindingDBiP38532.

Structurei

3D structure databases

ProteinModelPortaliP38532.
SMRiP38532. Positions 10-123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 20374Hydrophobic repeat HR-A/BAdd
BLAST
Regioni221 – 31090Regulatory domainAdd
BLAST
Regioni367 – 525159Transactivation domainAdd
BLAST
Regioni380 – 40526Hydrophobic repeat HR-CAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei413 – 43422Missing in isoform 1. 2 PublicationsVSP_002416Add
BLAST

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_008296.2. [P38532-2]
XP_006520536.1. XM_006520473.2. [P38532-1]
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_008296.2. [P38532-2]
XP_006520536.1. XM_006520473.2. [P38532-1]
UniGeneiMm.347444.

3D structure databases

ProteinModelPortaliP38532.
SMRiP38532. Positions 10-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200443. 14 interactions.
IntActiP38532. 13 interactions.
STRINGi10090.ENSMUSP00000072617.

Chemistry

BindingDBiP38532.
ChEMBLiCHEMBL5313.

PTM databases

iPTMnetiP38532.
PhosphoSiteiP38532.

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: September 7, 2016
This is version 150 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.