ID   HSF1_MOUSE              Reviewed;         525 AA.
AC   P38532; O70462;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   02-SEP-2026, entry version 206.
DE   RecName: Full=Heat shock factor protein 1 {ECO:0000250|UniProtKB:Q00613};
DE            Short=HSF 1;
DE   AltName: Full=Heat shock transcription factor 1 {ECO:0000250|UniProtKB:Q00613};
DE            Short=HSTF 1;
GN   Name=Hsf1 {ECO:0000312|MGI:MGI:96238};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DNA-BINDING.
RC   STRAIN=WEHI-3;
RX   PubMed=1717345; DOI=10.1101/gad.5.10.1902;
RA   Sarge K.D., Zimarino V., Holm K., Wu C., Morimoto R.I.;
RT   "Cloning and characterization of two mouse heat shock factors with distinct
RT   inducible and constitutive DNA-binding ability.";
RL   Genes Dev. 5:1902-1911(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-525 (ISOFORM 2).
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   PubMed=9829985; DOI=10.1074/jbc.273.49.32514;
RA   Zhang Y., Koushik S., Dai R., Mivechi N.F.;
RT   "Structural organization and promoter analysis of murine heat shock
RT   transcription factor-1 gene.";
RL   J. Biol. Chem. 273:32514-32521(1998).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-307, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [5]
RP   FUNCTION.
RX   PubMed=20231359; DOI=10.1128/mcb.01025-09;
RA   Iida R., Ueki M., Yasuda T.;
RT   "A novel transcriptional repressor, Rhit, is involved in heat-inducible and
RT   age-dependent expression of Mpv17-like protein, a participant in reactive
RT   oxygen species metabolism.";
RL   Mol. Cell. Biol. 30:2306-2315(2010).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=26159920; DOI=10.1016/j.bbrc.2015.07.006;
RA   Jin Y.H., Ahn S.G., Kim S.A.;
RT   "BAG3 affects the nucleocytoplasmic shuttling of HSF1 upon heat stress.";
RL   Biochem. Biophys. Res. Commun. 464:561-567(2015).
CC   -!- FUNCTION: Functions as a stress-inducible and DNA-binding transcription
CC       factor that plays a central role in the transcriptional activation of
CC       the heat shock response (HSR), leading to the expression of a large
CC       class of molecular chaperones, heat shock proteins (HSPs), that protect
CC       cells from cellular insult damage. In unstressed cells, is present in a
CC       HSP90-containing multichaperone complex that maintains it in a non-DNA-
CC       binding inactivated monomeric form. Upon exposure to heat and other
CC       stress stimuli, undergoes homotrimerization and activates HSP gene
CC       transcription through binding to site-specific heat shock elements
CC       (HSEs) present in the promoter regions of HSP genes. Upon heat shock
CC       stress, forms a chromatin-associated complex with TTC5/STRAP and
CC       p300/EP300 to stimulate HSR transcription, therefore increasing cell
CC       survival. Activation is reversible, and during the attenuation and
CC       recovery phase period of the HSR, returns to its unactivated form.
CC       Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to
CC       chromatin at heat shock gene promoters. Activates transcription of
CC       transcription factor FOXR1 which in turn activates transcription of the
CC       heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-
CC       dependent reductase DHRS2 (By similarity). Binds the promoter region
CC       upstream of exon 1 of Mpv17l to activate expression of the M-LPS
CC       isoform which is involved in metabolism of reactive oxygen species
CC       (PubMed:20231359). Also serves several other functions independently of
CC       its transcriptional activity. Involved in the repression of Ras-induced
CC       transcriptional activation of the c-fos gene in heat-stressed cells.
CC       Positively regulates pre-mRNA 3'-end processing and polyadenylation of
CC       HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent
CC       manner. Plays a role in nuclear export of stress-induced HSP70 mRNA.
CC       Plays a role in the regulation of mitotic progression. Also plays a
CC       role as a negative regulator of non-homologous end joining (NHEJ)
CC       repair activity in a DNA damage-dependent manner. Involved in stress-
CC       induced cancer cell proliferation in a IER5-dependent manner.
CC       {ECO:0000250|UniProtKB:Q00613, ECO:0000269|PubMed:20231359}.
CC   -!- SUBUNIT: Monomer; cytoplasmic latent and transcriptionally inactive
CC       monomeric form in unstressed cells. Homotrimer; in response to stress,
CC       such as heat shock, homotrimerizes and translocates into the nucleus,
CC       binds to heat shock element (HSE) sequences in promoter of heat shock
CC       protein (HSP) genes and acquires transcriptional ability. Interacts
CC       (via monomeric form) with FKBP4; this interaction occurs in unstressed
CC       cells. Associates (via monomeric form) with HSP90 proteins in a
CC       multichaperone complex in unnstressed cell; this association maintains
CC       HSF1 in a non-DNA-binding and transcriptional inactive form by
CC       preventing HSF1 homotrimerization. Homotrimeric transactivation
CC       activity is modulated by protein-protein interactions and post-
CC       translational modifications. Interacts with HSP90AA1; this interaction
CC       is decreased in a IER5-dependent manner, promoting HSF1 accumulation in
CC       the nucleus, homotrimerization and DNA-binding activities. Part (via
CC       regulatory domain in the homotrimeric form) of a large heat shock-
CC       induced HSP90-dependent multichaperone complex at least composed of
CC       FKBP4, FKBP5, HSP90 proteins, PPID, PPP5C and PTGES3; this association
CC       maintains the HSF1 homotrimeric DNA-bound form in a transcriptionally
CC       inactive form. Interacts with BAG3 (via BAG domain); this interaction
CC       occurs in normal and heat-shocked cells promoting nuclear shuttling of
CC       HSF1 in a BAG3-dependent manner. Interacts (via homotrimeric and
CC       hyperphosphorylated form) with FKBP4; this interaction occurs upon heat
CC       shock in a HSP90-dependent multichaperone complex. Interacts (via
CC       homotrimeric form preferentially) with EEF1A proteins. In heat shocked
CC       cells, stress-denatured proteins compete with HSF1 homotrimeric DNA-
CC       bound form for association of the HSP90-dependent multichaperone
CC       complex, and hence alleviating repression of HSF1-mediated
CC       transcriptional activity. Interacts (via homotrimeric form
CC       preferentially) with DAXX; this interaction relieves homotrimeric HSF1
CC       from repression of its transcriptional activity by HSP90-dependent
CC       multichaperone complex upon heat shock. Interacts (via D domain and
CC       preferentially with hyperphosphorylated form) with JNK1; this
CC       interaction occurs under both normal growth conditions and immediately
CC       upon heat shock. Interacts (via D domain and preferentially with
CC       hyperphosphorylated form) with MAPK3; this interaction occurs upon heat
CC       shock. Interacts with IER5 (via central region); this interaction
CC       promotes PPP2CA-induced dephosphorylation on Ser-121, Ser-307, Ser-314
CC       and Thr-323 and HSF1 transactivation activity. Found in a
CC       ribonucleoprotein complex composed of the HSF1 homotrimeric form,
CC       translation elongation factor eEF1A proteins and non-coding RNA heat
CC       shock RNA-1 (HSR1); this complex occurs upon heat shock and stimulates
CC       HSF1 DNA-binding activity. Interacts (via transactivation domain) with
CC       HSPA1A/HSP70 and DNAJB1; these interactions result in the inhibition of
CC       heat shock- and HSF1-induced transcriptional activity during the
CC       attenuation and recovery phase from heat shock. Interacts (via Ser-303
CC       and Ser-307 phosphorylated form) with YWHAE; this interaction promotes
CC       HSF1 sequestration in the cytoplasm in an ERK-dependent manner. Found
CC       in a complex with IER5 and PPP2CA. Interacts with TPR; this interaction
CC       increases upon heat shock and stimulates export of HSP70 mRNA.
CC       Interacts with SYMPK (via N-terminus) and CSTF2; these interactions
CC       occur upon heat shock. Interacts (via transactivation domain) with
CC       HSPA8. Interacts with EEF1D; this interaction occurs at heat shock
CC       promoter element (HSE) sequences. Interacts with MAPKAPK2. Interacts
CC       with PRKACA/PKA. Interacts (via transactivation domain) with GTF2A2.
CC       Interacts (via transactivation domain) with GTF2B. Interacts (via
CC       transactivation domain) with TBP. Interacts with CDK9, CCNT1 and EP300.
CC       Interacts (via N-terminus) with XRCC5 (via N-terminus) and XRCC6 (via
CC       N-terminus); these interactions are direct and prevent XRCC5/XRCC6
CC       heterodimeric binding and non-homologous end joining (NHEJ) repair
CC       activities induced by ionizing radiation (IR). Interacts with PLK1;
CC       this interaction occurs during the early mitotic period, increases upon
CC       heat shock but does not modulate neither HSF1 homotrimerization and
CC       DNA-binding activities. Interacts (via Ser-216 phosphorylated form)
CC       with CDC20; this interaction occurs in mitosis in a MAD2L1-dependent
CC       manner and prevents PLK1-stimulated degradation of HSF1 by blocking the
CC       recruitment of the SCF(BTRC) ubiquitin ligase complex. Interacts with
CC       MAD2L1; this interaction occurs in mitosis. Interacts with BTRC; this
CC       interaction occurs during mitosis, induces its ubiquitin-dependent
CC       degradation following stimulus-dependent phosphorylation at Ser-216, a
CC       process inhibited by CDC20. Interacts with HSP90AA1 and HSP90AB1. Forms
CC       a complex with TTC5/STRAP and p300/EP300; these interactions augment
CC       chromatin-bound HSF1 and p300/EP300 histone acetyltransferase activity
CC       (By similarity). {ECO:0000250|UniProtKB:Q00613}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26159920}. Cytoplasm
CC       {ECO:0000269|PubMed:26159920}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q00613}.
CC       Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00613}.
CC       Note=The monomeric form is cytoplasmic in unstressed cells
CC       (PubMed:26159920). Predominantly nuclear protein in both unstressed and
CC       heat shocked cells. Translocates in the nucleus upon heat shock.
CC       Nucleocytoplasmic shuttling protein. Colocalizes with IER5 in the
CC       nucleus. Colocalizes with BAG3 to the nucleus upon heat stress.
CC       Localizes in subnuclear granules called nuclear stress bodies (nSBs)
CC       upon heat shock. Colocalizes with SYMPK and SUMO1 in nSBs upon heat
CC       shock. Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat
CC       shock. Relocalizes from the nucleus to the cytoplasm during the
CC       attenuation and recovery phase period of the heat shock response.
CC       Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent
CC       manner. Together with histone H2AX, redistributed in discrete nuclear
CC       DNA damage-induced foci after ionizing radiation (IR). Colocalizes with
CC       calcium-responsive transactivator SS18L1 at kinetochore region on the
CC       mitotic chromosomes. Colocalizes with gamma tubulin at centrosome.
CC       Localizes at spindle pole in metaphase. Colocalizes with PLK1 at
CC       spindle poles during prometaphase. {ECO:0000250|UniProtKB:Q00613,
CC       ECO:0000269|PubMed:26159920}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=P38532-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=P38532-2; Sequence=VSP_002416;
CC   -!- DOMAIN: In unstressed cells, spontaneous homotrimerization is
CC       inhibited. Intramolecular interactions between the hydrophobic repeat
CC       HR-A/B and HR-C regions are necessary to maintain HSF1 in the inactive,
CC       monomeric conformation. Furthermore, intramolecular interactions
CC       between the regulatory domain and the nonadjacent transactivation
CC       domain prevents transcriptional activation, a process that is relieved
CC       upon heat shock. The regulatory domain is necessary for full repression
CC       of the transcriptional activation domain in unstressed cells through
CC       its phosphorylation on Ser-303 and Ser-307. In heat stressed cells,
CC       HSF1 homotrimerization occurs through formation of a three-stranded
CC       coiled-coil structure generated by intermolecular interactions between
CC       HR-A/B regions allowing DNA-binding activity. The D domain is necessary
CC       for translocation to the nucleus, interaction with JNK1 and MAPK3 and
CC       efficient JNK1- and MAPK3-dependent phosphorylation. The regulatory
CC       domain confers heat shock inducibility on the transcriptional
CC       transactivation domain. The regulatory domain is necessary for
CC       transcriptional activation through its phosphorylation on Ser-230 upon
CC       heat shock. 9aaTAD is a transactivation motif present in a large number
CC       of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:Q00613}.
CC   -!- PTM: Phosphorylated. Phosphorylated in unstressed cells; this
CC       phosphorylation is constitutive and implicated in the repression of
CC       HSF1 transcriptional activity. Phosphorylated on Ser-121 by MAPKAPK2;
CC       this phosphorylation promotes interaction with HSP90 proteins and
CC       inhibits HSF1 homotrimerization, DNA-binding and transactivation
CC       activities. Phosphorylation on Ser-303 by GSK3B/GSK3-beat and on Ser-
CC       307 by MAPK3 within the regulatory domain is involved in the repression
CC       of HSF1 transcriptional activity and occurs in a RAF1-dependent manner.
CC       Phosphorylation on Ser-303 and Ser-307 increases HSF1 nuclear export in
CC       a YWHAE- and XPO1/CRM1-dependent manner. Phosphorylation on Ser-307 is
CC       a prerequisite for phosphorylation on Ser-303. According to, Ser-303 is
CC       not phosphorylated in unstressed cells. Phosphorylated on Ser-415 by
CC       PLK1; phosphorylation promotes nuclear translocation upon heat shock.
CC       Hyperphosphorylated upon heat shock and during the attenuation and
CC       recovery phase period of the heat shock response. Phosphorylated on
CC       Thr-142; this phosphorylation increases HSF1 transactivation activity
CC       upon heat shock. Phosphorylation on Ser-230 by CAMK2A; this
CC       phosphorylation enhances HSF1 transactivation activity upon heat shock.
CC       Phosphorylation on Ser-326 by MAPK12; this phosphorylation enhances
CC       HSF1 nuclear translocation, homotrimerization and transactivation
CC       activities upon heat shock. Phosphorylated on Ser-320 by PRKACA/PKA;
CC       this phosphorylation promotes nuclear localization and transcriptional
CC       activity upon heat shock. Phosphorylated by MAPK8; this phosphorylation
CC       occurs upon heat shock, induces HSF1 translocation into nuclear stress
CC       bodies and negatively regulates transactivation activity. Neither basal
CC       nor stress-inducible phosphorylation on Ser-230, Ser-292, Ser-303, Ser-
CC       307, Ser-314, Ser-319, Ser-320, Thr-323, Ser-326, Ser-338, Ser-345,
CC       Ser-364 and Thr-365 within the regulatory domain is involved in the
CC       regulation of HSF1 subcellular localization or DNA-binding activity;
CC       however, it negatively regulates HSF1 transactivation activity.
CC       Phosphorylated on Ser-216 by PLK1 in the early mitotic period; this
CC       phosphorylation regulates HSF1 localization to the spindle pole, the
CC       recruitment of the SCF(BTRC) ubiquitin ligase complex inducing HSF1
CC       degradation, and hence mitotic progression. Dephosphorylated on Ser-
CC       121, Ser-307, Ser-314 and Thr-323 by phosphatase PPP2CA in an IER5-
CC       dependent manner, leading to HSF1-mediated transactivation activity.
CC       {ECO:0000250|UniProtKB:Q00613}.
CC   -!- PTM: Sumoylated with SUMO1 and SUMO2 upon heat shock in a ERK2-
CC       dependent manner. Sumoylated by SUMO1 on Lys-298; sumoylation occurs
CC       upon heat shock and promotes its localization to nuclear stress bodies
CC       and DNA-binding activity. Phosphorylation on Ser-303 and Ser-307 is
CC       probably a prerequisite for sumoylation.
CC       {ECO:0000250|UniProtKB:Q00613}.
CC   -!- PTM: Acetylated on Lys-118; this acetylation is decreased in a IER5-
CC       dependent manner. Acetylated on Lys-118, Lys-208 and Lys-298; these
CC       acetylations occur in a EP300-dependent manner. Acetylated on Lys-80;
CC       this acetylation inhibits DNA-binding activity upon heat shock.
CC       Deacetylated on Lys-80 by SIRT1; this deacetylation increases DNA-
CC       binding activity. {ECO:0000250|UniProtKB:Q00613}.
CC   -!- PTM: Ubiquitinated by SCF(BTRC) and degraded following stimulus-
CC       dependent phosphorylation at Ser-216 by PLK1 in mitosis.
CC       Polyubiquitinated. Undergoes proteasomal degradation upon heat shock
CC       and during the attenuation and recovery phase period of the heat shock
CC       response. {ECO:0000250|UniProtKB:Q00613}.
CC   -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR   EMBL; X61753; CAA43892.1; -; mRNA.
DR   EMBL; BC013716; AAH13716.1; -; mRNA.
DR   EMBL; AF059275; AAC80425.1; -; Genomic_DNA.
DR   CCDS; CCDS27572.1; -. [P38532-2]
DR   CCDS; CCDS88787.1; -. [P38532-1]
DR   PIR; A40583; A40583.
DR   RefSeq; NP_001318083.1; NM_001331154.1. [P38532-1]
DR   RefSeq; NP_032322.1; NM_008296.3. [P38532-2]
DR   AlphaFoldDB; P38532; -.
DR   BMRB; P38532; -.
DR   SMR; P38532; -.
DR   BioGRID; 200443; 14.
DR   FunCoup; P38532; 1621.
DR   IntAct; P38532; 16.
DR   MINT; P38532; -.
DR   STRING; 10090.ENSMUSP00000072617; -.
DR   ChEMBL; CHEMBL5313; -.
DR   GlyGen; P38532; 5 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P38532; -.
DR   PhosphoSitePlus; P38532; -.
DR   jPOST; P38532; -.
DR   PaxDb; 10090-ENSMUSP00000072617; -.
DR   PeptideAtlas; P38532; -.
DR   ProteomicsDB; 273389; -. [P38532-1]
DR   ProteomicsDB; 273390; -. [P38532-2]
DR   Pumba; P38532; -.
DR   Antibodypedia; 1848; 1729 antibodies from 54 providers.
DR   DNASU; 15499; -.
DR   Ensembl; ENSMUST00000072838.6; ENSMUSP00000072617.6; ENSMUSG00000022556.12. [P38532-2]
DR   Ensembl; ENSMUST00000227478.2; ENSMUSP00000154602.2; ENSMUSG00000022556.12. [P38532-1]
DR   GeneID; 15499; -.
DR   KEGG; mmu:15499; -.
DR   UCSC; uc056yzg.1; mouse. [P38532-1]
DR   AGR; MGI:96238; -.
DR   CTD; 3297; -.
DR   MGI; MGI:96238; Hsf1.
DR   VEuPathDB; HostDB:ENSMUSG00000022556; -.
DR   eggNOG; KOG0627; Eukaryota.
DR   GeneTree; ENSGT00940000158421; -.
DR   HOGENOM; CLU_038829_2_0_1; -.
DR   InParanoid; P38532; -.
DR   OMA; LICWSPQ; -.
DR   OrthoDB; 60033at2759; -.
DR   PhylomeDB; P38532; -.
DR   Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-MMU-3371511; HSF1 activation.
DR   Reactome; R-MMU-3371568; Attenuation phase.
DR   Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR   Reactome; R-MMU-9841251; Mitochondrial unfolded protein response (UPRmt).
DR   BioGRID-ORCS; 15499; 5 hits in 81 CRISPR screens.
DR   PRO; PR:P38532; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P38532; protein.
DR   Bgee; ENSMUSG00000022556; Expressed in animal zygote and 258 other cell types or tissues.
DR   ExpressionAtlas; P38532; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0000791; C:euchromatin; ISO:GO_Central.
DR   GO; GO:0000792; C:heterochromatin; ISO:GO_Central.
DR   GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR   GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR   GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR   GO; GO:0045120; C:pronucleus; IDA:MGI.
DR   GO; GO:0101031; C:protein folding chaperone complex; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:GO_Central.
DR   GO; GO:0140296; F:general transcription initiation factor binding; ISO:GO_Central.
DR   GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR   GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISO:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISO:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:GO_Central.
DR   GO; GO:0098847; F:sequence-specific single stranded DNA binding; ISO:GO_Central.
DR   GO; GO:0097677; F:STAT family protein binding; ISO:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:GO_Central.
DR   GO; GO:0061770; F:translation elongation factor binding; ISS:UniProtKB.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:GO_Central.
DR   GO; GO:1904385; P:cellular response to angiotensin; ISO:GO_Central.
DR   GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
DR   GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB.
DR   GO; GO:0072738; P:cellular response to diamide; ISS:UniProtKB.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:GO_Central.
DR   GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:GO_Central.
DR   GO; GO:0071478; P:cellular response to radiation; ISO:GO_Central.
DR   GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB.
DR   GO; GO:0034620; P:cellular response to unfolded protein; ISS:UniProtKB.
DR   GO; GO:0006952; P:defense response; ISO:GO_Central.
DR   GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR   GO; GO:0060136; P:embryonic process involved in female pregnancy; IMP:MGI.
DR   GO; GO:0007143; P:female meiotic nuclear division; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IDA:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:GO_Central.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:GO_Central.
DR   GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:GO_Central.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:MGI.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI.
DR   GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; ISO:GO_Central.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:GO_Central.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:CACAO.
DR   GO; GO:0090261; P:positive regulation of inclusion body assembly; ISO:GO_Central.
DR   GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:GO_Central.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0031401; P:positive regulation of protein modification process; ISO:GO_Central.
DR   GO; GO:0062029; P:positive regulation of stress granule assembly; ISO:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:1900034; P:regulation of cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:GO_Central.
DR   GO; GO:0032355; P:response to estradiol; ISO:GO_Central.
DR   GO; GO:0009408; P:response to heat; IMP:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0033574; P:response to testosterone; ISO:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR   DisProt; DP03368; -. [P38532-2]
DR   FunFam; 1.10.10.10:FF:000027; Heat shock transcription factor 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000232; HSF_DNA-bd.
DR   InterPro; IPR010542; Vert_HSTF_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10015:SF274; HEAT SHOCK FACTOR PROTEIN 1; 1.
DR   PANTHER; PTHR10015; HEAT SHOCK TRANSCRIPTION FACTOR; 1.
DR   Pfam; PF00447; HSF_DNA-bind; 1.
DR   Pfam; PF06546; Vert_HS_TF; 1.
DR   PRINTS; PR00056; HSFDOMAIN.
DR   SMART; SM00415; HSF; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00434; HSF_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; Centromere; Chromosome;
KW   Cytoplasm; Cytoskeleton; DNA damage; DNA repair; DNA-binding;
KW   Isopeptide bond; Kinetochore; mRNA processing; mRNA transport; Nucleus;
KW   Phosphoprotein; Reference proteome; Stress response; Transcription;
KW   Transcription regulation; Transport; Ubl conjugation.
FT   CHAIN           1..525
FT                   /note="Heat shock factor protein 1"
FT                   /id="PRO_0000124568"
FT   REGION          15..120
FT                   /note="DNA-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   REGION          130..203
FT                   /note="Hydrophobic repeat HR-A/B"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   REGION          203..224
FT                   /note="D domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   REGION          221..310
FT                   /note="Regulatory domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   REGION          272..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..525
FT                   /note="Transactivation domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   REGION          380..405
FT                   /note="Hydrophobic repeat HR-C"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   REGION          441..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           408..416
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   COMPBIAS        343..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         80
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         91
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         118
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         121
FT                   /note="Phosphoserine; by MAPKAPK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         142
FT                   /note="Phosphothreonine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         150
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         188
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         208
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         216
FT                   /note="Phosphoserine; by PLK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         230
FT                   /note="Phosphoserine; by CAMK2A"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         298
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         320
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         323
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         326
FT                   /note="Phosphoserine; by MAPK12"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         415
FT                   /note="Phosphoserine; by PLK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   MOD_RES         520
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   CROSSLNK        91
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   CROSSLNK        126
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   CROSSLNK        131
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   CROSSLNK        208
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   CROSSLNK        224
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   CROSSLNK        298
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   CROSSLNK        298
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00613"
FT   VAR_SEQ         413..434
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:1717345"
FT                   /id="VSP_002416"
SQ   SEQUENCE   525 AA;  57223 MW;  DCB6418FC12F5F43 CRC64;
     MDLAVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG QFAKEVLPKY
     FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ HPCFLRGQEQ LLENIKRKVT
     SVSTLKSEDI KIRQDSVTRL LTDVQLMKGK QECMDSKLLA MKHENEALWR EVASLRQKHA
     QQQKVVNKLI QFLISLVQSN RILGVKRKIP LMLSDSNSAH SVPKYGRQYS LEHVHGPGPY
     SAPSPAYSSS SLYSSDAVTS SGPIISDITE LAPTSPLASP GRSIDERPLS SSTLVRVKQE
     PPSPPHSPRV LEASPGRPSS MDTPLSPTAF IDSILRESEP TPAASNTAPM DTTGAQAPAL
     PTPSTPEKCL SVACLDKNEL SDHLDAMDSN LDNLQTMLTS HGFSVDTSAL LDLFSPSVTM
     PDMSLPDLDS SLASIQELLS PQEPPRPIEA ENSNPDSGKQ LVHYTAQPLF LLDPDAVDTG
     SSELPVLFEL GESSYFSEGD DYTDDPTISL LTGTEPHKAK DPTVS
//