HSF1_MOUSE
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 03-AUG-2022, entry version 188.
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 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 insults' damage. In unstressed cells, is present in
CC a HSP90-containing multichaperone complex that maintains it in a non-
CC DNA-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. Also serves several other
CC functions independently of its transcriptional activity. Involved in
CC the repression of Ras-induced transcriptional activation of the c-fos
CC gene in heat-stressed cells. Positively regulates pre-mRNA 3'-end
CC processing and polyadenylation of HSP70 mRNA upon heat-stressed cells
CC in a symplekin (SYMPK)-dependent manner. Plays a role in nuclear export
CC of stress-induced HSP70 mRNA. Plays a role in the regulation of mitotic
CC progression. Also plays a role as a negative regulator of non-
CC homologous end joining (NHEJ) repair activity in a DNA damage-dependent
CC manner. Involved in stress-induced cancer cell proliferation in a IER5-
CC dependent manner. {ECO:0000250|UniProtKB:Q00613}.
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 IntAct; P38532; 13.
DR MINT; P38532; -.
DR STRING; 10090.ENSMUSP00000072617; -.
DR BindingDB; P38532; -.
DR ChEMBL; CHEMBL5313; -.
DR iPTMnet; P38532; -.
DR PhosphoSitePlus; P38532; -.
DR jPOST; P38532; -.
DR MaxQB; P38532; -.
DR PaxDb; P38532; -.
DR PeptideAtlas; P38532; -.
DR PRIDE; P38532; -.
DR ProteomicsDB; 273389; -. [P38532-1]
DR ProteomicsDB; 273390; -. [P38532-2]
DR Antibodypedia; 1848; 1788 antibodies from 50 providers.
DR DNASU; 15499; -.
DR Ensembl; ENSMUST00000072838; ENSMUSP00000072617; ENSMUSG00000022556. [P38532-2]
DR Ensembl; ENSMUST00000227478; ENSMUSP00000154602; ENSMUSG00000022556. [P38532-1]
DR GeneID; 15499; -.
DR KEGG; mmu:15499; -.
DR UCSC; uc056yzg.1; mouse. [P38532-1]
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 PhylomeDB; P38532; -.
DR TreeFam; TF330401; -.
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 BioGRID-ORCS; 15499; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Hsf1; mouse.
DR PRO; PR:P38532; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P38532; protein.
DR Bgee; ENSMUSG00000022556; Expressed in animal zygote and 255 other tissues.
DR ExpressionAtlas; P38532; baseline and differential.
DR Genevisible; P38532; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0101031; C:chaperone complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
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: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:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
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:MGI.
DR GO; GO:0098847; F:sequence-specific single stranded DNA binding; ISO:MGI.
DR GO; GO:0097677; F:STAT family protein binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0061770; F:translation elongation factor binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:MGI.
DR GO; GO:1904385; P:cellular response to angiotensin; ISO:MGI.
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:MGI.
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:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0071478; P:cellular response to radiation; ISO:MGI.
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:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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:0050673; P:epithelial cell proliferation; IGI:MGI.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009299; P:mRNA transcription; ISO:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
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:1902512; P:positive regulation of apoptotic DNA fragmentation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CACAO.
DR GO; GO:0090261; P:positive regulation of inclusion body assembly; ISO:MGI.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:MGI.
DR GO; GO:1904528; P:positive regulation of microtubule binding; ISO:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; ISS:UniProtKB.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0032355; P:response to estradiol; ISO:MGI.
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:MGI.
DR GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR010542; Vert_HSTF_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 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; SSF46785; 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 340..360
FT /note="Polar 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
