
AC   T01042
AS   T00383.
XX
ID   T01042
XX
DT   21.02.1994 (created); ewi.
DT   19.02.2013 (updated); mkl.
CO   Copyright (C), QIAGEN.
XX
FA   HSF1-L
XX
SY   heat shock (transcription) factor 1; heat shock factor 1; heat shock transcription factor 1; hHSF1; HSF; HSF 1; HSF1; HSTF; HSTF 1; HSTF1; HTF.
XX
OS   human, Homo sapiens
OC   eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates
XX
GE   G004875 HSF1; HGNC: HSF1.
XX
HO   heat-induced factor.
XX
CL   C0050; HSF; 3.4.1.0.1.1.
XX
SZ   529 AA; 57.3 kDa (cDNA) (calc.), 83 kDa (SDS), 4-5S (inactive), 8S (active) 83 kDa (SDS) [12]
XX
SQ   MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKY
SQ   FKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVT
SQ   SVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHA
SQ   QQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPY
SQ   SAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEE
SQ   PPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGR
SQ   PPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLSSHGFSVDTSALLDLFSP
SQ   SVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGS
SQ   VDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS
XX
SC   Swiss-Prot#Q00613-1
XX
FT       14    118    SM00415; HSF.
FT       16    211
   SM00415; HSF.
FT       16    211    PF00447; HSF-type DNA-binding.
FT       18     85
   PF00447; HSF-type DNA-binding.
FT       18     85    PS50140; HSF_ETS.
FT      137    197
   PS50140; HSF_ETS.
FT      137    197    hydrophobic repeat [12].
FT      142    142
   hydrophobic repeat [12].
FT      142    142    Threonine 142, phosphorylated by CK2 [25].
FT      221    310
   Threonine 142, phosphorylated by CK2 [25].
FT      221    310    regulatory domain [19].
FT      230    230
   regulatory domain [19].
FT      230    230    Serine 230, phosphorylation site [19].
FT      246    529
   Serine 230, phosphorylation site [19].
FT      246    529    PF06546; Vertebrate heat shock transcription fact.
FT      298    298
   PF06546; Vertebrate heat shock transcription fact.
FT      298    298    Lysine 298 is a site of SUMO-1 modification in vivo [28].
FT      384    488
   Lysine 298 is a site of SUMO-1 modification in vivo [28].
FT      384    488    repressing region [17].
FT      463    474
   repressing region [17].
FT      463    474    region of homology with HSF2 [17].
   region of homology with HSF2 [17].
 XX
SF   phosphorylation;
SF   2 open reading frames encode a long and a short form (possibly splice variants): inactive HSF sediments with 4-5S, the active form with 8S [2];
SF   trimerization occurs after activation [17];
SF   the C-terminal part represses multimerization [17];
SF   here, one subregion is a hydrophobic repeat which may form intramolecular coiled-coil with those close to the DNA-binding domain, while the other is a HSF2-homologous region [16] [17];
SF   regulatory domain aa221-310 [19];
XX
CP   (HeLa).
XX
FF   binds to DNA, not to nucleosome-assembled DNA unless TBP was present during assembly;
FF   activator, mediating response of heat shock genes to heat and stress factors [15] [6];
FF   being constitutively transcribed, HSF1 requires activation by heat induction to bind to DNA [15] [6];
FF   other inducing factors (besides heat) are heavy metals, oxidizing agents, teratogens, hypoxia, and arachidonate [18] [11];
FF   inducing signals cause transition of HSF1 from inactive monomeric to active trimeric state [17];
FF   phosphorylation appears to modulate the trans-activation potential by HSF1 [6];
FF   induced by following stress factors: heat, hydrogen peroxide, osmotic stress [22];
FF   DNA binding may be increased by DeltaN p73alpha T06002 [23];
FF   HSF1 builds a subcellular structure (granules) in the nuclei of stressed cells [26];
FF   HSF1 granules associate in vivo with chromosome 9q11-9q12 during heat stress [24];
FF   aaT142 is phosphorylated by CK2 [25];
FF   phosphorylation at T142 is essential for activation of HSF1 by heat shock [25];
FF   HSF1  associates with HSF2 T01043 in vitro and in vivo, binding is enhanced by heat shock [27];
FF   colocalizes with the SUMO-1 protein in nuclear granules under heat stress and heavy metal (cadmium) stress [28];
FF   Lysine 298 is a site of SUMO-1 (small ubiquitin related protein) modification in vivo [28];
FF   associates with the BRG1, the ATPase subunit of the ATP-dependant chromatin remodeling complex SWI/SNF at the transcriptional domain [29];
FF   exists in unstressed cells in a heterodimeric complex with the Heat Shock Protein Hsp70 [30];
FF   interacts with Hsp90-Immunophilin-p23 complexes [31];
FF   interacts with Hsp90 with both, trimeric and nontrimeric forms [31];
FF   is associated with the Hsp90-Immunophilin(FKBP52)-p23 complex in a trimeric, but transcriptionally inactive, form;
FF   overexpression of a competing protein to the Hsp90-Immunophilin(FKBP52)-p23 complex alleviates the repression, the presence of stress-denatured proteins has the same effect [31];
FF   Hsp90-Immunophilin(FKBP52)-p23 complex binds to the regulatory domain of HSF1 [31];
FF   serine 230 is a phosphorylation site in the regulatory domain [19];
FF   a mutation S230A impairs the transcriptional activity of HSF1 [19];
FF   the phosphorylation of serine 230 contributes to the stress-induced transcriptional activity of HSF1 [19];
XX
IN   T08796 ASC-2; human, Homo sapiens.
IN   T09410 C/EBPbeta; Mammalia.
IN   T15118 CBP; Mammalia.
IN   T02944 Daxx; human, Homo sapiens.
IN   T01042 HSF1-L; human, Homo sapiens.
IN   T09196 HSF2A; human, Homo sapiens.
IN   T16186 HSF2B; human, Homo sapiens.
IN   T01264 HST; yeast, Kluyveromyces lactis.
IN   T09092 PC4; human, Homo sapiens.
IN   T09238 TAFII55; human, Homo sapiens.
IN   T08520 TBP-isoform1; human, Homo sapiens.
IN   T09237 TFIIA-gamma; human, Homo sapiens.
IN   T08496 TFIIB; human, Homo sapiens.
XX
MX   M00146 V$HSF1_01.
MX   M07259 V$HSF1_Q5.
MX   M07459 V$HSF1_Q5_01.
MX   M01023 V$HSF1_Q6.
MX   M02017 V$HSF1_Q6_01.
MX   M00641 V$HSF_Q6.
XX
BS   R01925.
BS   R03331.
BS   R03624.
BS   R00754.
BS   R00756.
BS   R00773.
BS   R00762.
BS   R00763.
BS   R00764.
BS   R04287.
BS   R02181.
BS   R15803.
BS   R15806.
BS   R15816.
BS   R15817.
BS   R15818.
BS   R15819.
BS   R15820.
BS   R15797.
BS   R15740.
BS   R15766.
XX
DR   TRANSPATH: MO000006878.
DR   EMBL: M64673;
DR   UniProtKB: Q00613-1;
XX
RN   [1]; RE0000170.
RX   PUBMED: 2018972.
RA   Sorger P. K.
RT   Heat shock factor and the heat shock response
RL   Cell 65:363-366 (1991).
RN   [2]; RE0000284.
RX   PUBMED: 1913856.
RA   Kimura Y., Taniguchi T., Yahara I.
RT   An alteration in molecular form associated with activation of human heat shock factor
RL   Cell Struct. Funct. 16:263-271 (1991).
RN   [3]; RE0000760.
RX   PUBMED: 2065977.
RA   Taylor I. C. A., Workman J. L., Schuetz T. J., Kingston R. E.
RT   Facilitated binding of GAL4 and heat shock factor to nucleosomal templates: differential function of DNA-binding domains
RL   Genes Dev. 5:1285-1298 (1991).
RN   [4]; RE0000851.
RX   PUBMED: 3198647.
RA   Goldenberg C. J., Luo Y., Fenna M., Baler R., Weinmann R., Voellmy R.
RT   Purified Human Factor Activates Heat Shock Promoter in a HeLa Cell-free Transcription System
RL   J. Biol. Chem. 263:19734-19739 (1988).
RN   [5]; RE0001284.
RX   PUBMED: 3561411.
RA   Morgan W. D., Williams G. T., Morimoto R. I., Greene J., Kingston R. E., Tjian R.
RT   Two transcriptional activators, CCAAT-box-binding transcription factor and heat shock transcription factor, interact with a human hsp70 gene promoter
RL   Mol. Cell. Biol. 7:1129-1138 (1987).
RN   [6]; RE0001285.
RX   PUBMED: 3600634.
RA   Kingston R. E., Schuetz T. J., Larin Z.
RT   Heat-Inducible Human Factor That Binds to a Human hsp70 Promoter
RL   Mol. Cell. Biol. 7:1530-1534 (1987).
RN   [7]; RE0001286.
RX   PUBMED: 3211126.
RA   Mosser D. D., Theodorakis N. G., Morimoto R. I.
RT   Coordinate Changes in Heat Shock Element-Binding Acitvity and HSP70 Gene Transcription Rates in Human Cells
RL   Mol. Cell. Biol. 8:4736-4744 (1988).
RN   [8]; RE0001575.
RX   PUBMED: 1986252.
RA   Abravaya K., Phillips B., Morimoto R. I.
RT   Heat shock-induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting
RL   Mol. Cell. Biol. 11:586-592 (1991).
RN   [9]; RE0001657.
RX   PUBMED: 1904540.
RA   Cunniff N. F. A., Wagner J., Morgan W. D.
RT   Modular recognition of 5-base-pair DNA sequence motifs by human heat shock transcription factor
RL   Mol. Cell. Biol. 11:3504-3514 (1991).
RN   [10]; RE0001793.
RX   PUBMED: 3419505.
RA   Larson J. S., Schuetz T. J., Kingston R. E.
RT   Activation in vitro of sequence-specific DNA binding by a human regulatory factor
RL   Nature 335:372-375 (1988).
RN   [11]; RE0002440.
RX   PUBMED: 1696723.
RA   Benjamin I. J., Kroeger B., Williams R. S.
RT   Activation of the heat shock transcription factor by hypoxia in mammalian cells
RL   Proc. Natl. Acad. Sci. USA 87:6263-6267 (1990).
RN   [12]; RE0002538.
RX   PUBMED: 1871105.
RA   Rabindran S. K., Giorgi G., Clos J., Wu C.
RT   Molecular cloning and expression of a human heat shock factor, HSF1
RL   Proc. Natl. Acad. Sci. USA 88:6906-6910 (1991).
RN   [13]; RE0002871.
RX   PUBMED: 1936996.
RA   Abravaya K., Phillips B., Morimoto R. I.
RT   Attenuation of the heat shock response in HeLa cells is mediated  by the release of bound heat shock transcription factor and is modulated by changes in growth and in heat shock temperatures
RL   Genes Dev. 5:2117-2127 (1991).
RN   [14]; RE0003104.
RX   PUBMED: 1508207.
RA   Sistonen L., Sarge K. D., Phillips B., Abravaya K., Morimoto R. I.
RT   Activation of heat shock factor 2 during hemin-induced differentiation of human erythroleukemia cells
RL   Mol. Cell. Biol. 12:4104-4111 (1992).
RN   [15]; RE0005275.
RX   PUBMED: 3306402.
RA   Sorger P. K., Lewis M. J., Pelham H. R. B.
RT   Heat shock factor is regulated differently in yeast and HeLa cells
RL   Nature 329:81-84 (1987).
RN   [16]; RE0005278.
RX   PUBMED: 7935471.
RA   Zuo J., Baler R., Dahl G., Voellmy R.
RT   Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure
RL   Mol. Cell. Biol. 14:7557-7568 (1994).
RN   [17]; RE0005280.
RX   PUBMED: 8421783.
RA   Rabindran S. K., Haroun R. I., Clos J., Wisniewski J., Wu C.
RT   Regulation of heat shock factor trimer formation: role of a conserved leucine zipper
RL   Science 259:230-234 (1993).
RN   [18]; RE0005282.
RX   PUBMED: 8134388.
RA   Jurivich D. A., Sistonen L., Sarge K. D., Morimoto R. I.
RT   Arachidonate is a potent modulator of human heat shock gene transcription
RL   Proc. Natl. Acad. Sci. USA 91:2280-2284 (1994).
RN   [19]; RE0018120.
RX   PUBMED: 11447121.
RA   Holmberg C. I., Hietakangas V., Mikhailov A., Rantanen J. O., Kallio M., Meinander A., Hellman J., Morrice N., MacKintosh C., Morimoto R. I., Eriksson J. E., Sistonen L.
RT   Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1.
RL   EMBO J. 20:3800-3810 (2001).
RN   [20]; RE0023682.
RX   PUBMED: 7999960.
RA   Wu C., Clos J., Giorgi G, Haroun R., Kim S, Rabindran S., Westwood T., Wisniewski J., Yim G.
RT   Structure and Regulation of Heat Shock Transcription Factor
RL   The Biology of Heat Shock Proteins and Molecular Chaperones 5:395-400 (1994).
RN   [21]; RE0023684.
RA   Morimoto R., Jurivich D., Kroeger P., Mathur S., Murphy S., Nakai A., Sarge K., Abravaya K., Sistonen L.
RT   Regulation of Heat Shock Gene Transcription by a Family of Heat Shock Factors
RL   The Biology of Heat Shock Proteins and Molecular Chaperones :417-455 (1994).
RN   [22]; RE0023693.
RX   PUBMED: 10547058.
RA   Nakai A.
RT   New aspects in the vertebrate heat shock factor system: Hsf3 and Hsf4.
RL   Cell Stress Chaperones 4:86-93 (1999).
RN   [23]; RE0024793.
RX   PUBMED: 15081420.
RA   Tanaka Y., Kameoka M., Itaya A., Ota K., Yoshihara K.
RT   Regulation of HSF1-responsive gene expression by N-terminal truncated form of p73alpha.
RL   Biochem. Biophys. Res. Commun. 317:865-872 (2004).
RN   [24]; RE0024938.
RX   PUBMED: 11877455.
RA   Jolly C., Konecny L., Grady D. L., Kutskova Y. A., Cotto J. J., Morimoto R. I., Vourc'h C.
RT   In vivo binding of active heat shock transcription factor 1 to human chromosome 9 heterochromatin during stress.
RL   J. Cell Biol. 156:775-781 (2002).
RN   [25]; RE0024949.
RX   PUBMED: 12659875.
RA   Soncin F., Zhang X., Chu B., Wang X., Asea A., Ann Stevenson M., Sacks D. B., Calderwood S. K.
RT   Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2.
RL   Biochem. Biophys. Res. Commun. 303:700-706 (2003).
RN   [26]; RE0024960.
RX   PUBMED: 9359875.
RA   Cotto J., Fox S., Morimoto R.
RT   HSF1 granules: a novel stress-induced nuclear compartment of human cells.
RL   J. Cell Sci. 110:2925-2934 (1997).
RN   [27]; RE0025006.
RX   PUBMED: 12813038.
RA   He H., Soncin F., Grammatikakis N., Li Y., Siganou A., Gong J., Brown S. A., Kingston R. E., Calderwood S. K.
RT   Elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress.
RL   J. Biol. Chem. 278:35465-35475 (2003).
RN   [28]; RE0025037.
RX   PUBMED: 11514557.
RA   Hong Y., Rogers R., Matunis M. J., Mayhew C. N., Goodson M. L., Park-Sarge O. K., Sarge K. D., Goodson M.
RT   Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification.
RL   J. Biol. Chem. 276:40263-40267 (2001).
RN   [29]; RE0025039.
RX   PUBMED: 11486022.
RA   Sullivan E. K., Weirich C. S., Guyon J. R., Sif S., Kingston R. E.
RT   Transcriptional activation domains of human heat shock factor 1 recruit human SWI/SNF.
RL   Mol. Cell. Biol. 21:5826-5837 (2001).
RN   [30]; RE0025041.
RX   PUBMED: 9222587.
RA   Baler R., Zou J., Voellmy R.
RT   Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells.
RL   Cell Stress Chaperones 1:33-39 (1996).
RN   [31]; RE0025042.
RX   PUBMED: 11583998.
RA   Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W. B., Toft D. O., Smith D. F., Voellmy R.
RT   Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex.
RL   J. Biol. Chem. 276:45791-45799 (2001).
RN   [32]; RE0031850.
RX   PUBMED: 11005381.
RA   Yuan C. X., Gurley W. B.
RT   Potential targets for HSF1 within the preinitiation complex.
RL   Cell Stress Chaperones 5:229-42 (2000).
RN   [33]; RE0047991.
RX   PUBMED: 11801594.
RA   Xie Y., Chen C., Stevenson M. A., Auron P. E., Calderwood S. K.
RT   Heat shock factor 1 represses transcription of the IL-1beta gene through physical interaction with the nuclear factor of interleukin 6.
RL   J. Biol. Chem. 277:11802-11810 (2002).
RN   [34]; RE0048044.
RX   PUBMED: 14960326.
RA   Hong S., Kim S. H., Heo M. A., Choi Y. H., Park M. J., Yoo M. A., Kim H. D., Kang H. S., Cheong J.
RT   Coactivator ASC-2 mediates heat shock factor 1-mediated transactivation dependent on heat shock.
RL   FEBS Lett. 559:165-170 (2004).
RN   [35]; RE0048049.
RX   PUBMED: 12621024.
RA   Hu Y., Mivechi N. F.
RT   HSF-1 interacts with Ral-binding protein 1 in a stress-responsive, multiprotein complex with HSP90 in vivo.
RL   J. Biol. Chem. 278:17299-17306 (2003).
RN   [36]; RE0048789.
RX   PUBMED: 12665592.
RA   Hietakangas V., Ahlskog J. K., Jakobsson A. M., Hellesuo M., Sahlberg N. M., Holmberg C. I., Mikhailov A., Palvimo J. J., Pirkkala L., Sistonen L.
RT   Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1.
RL   Mol. Cell. Biol. 23:2953-2968 (2003).
RN   [37]; RE0048834.
RX   PUBMED: 15016915.
RA   Boellmann F., Guettouche T., Guo Y., Fenna M., Mnayer L., Voellmy R.
RT   DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity.
RL   Proc. Natl. Acad. Sci. USA 101:4100-4105 (2004).
XX
//
XX
SF   phosphorylation;
SF   2 open reading frames encode a long and a short form (possibly splice variants): inactive HSF sediments with 4-5S, the active form with 8S [2];
SF   trimerization occurs after activation [17];
SF   the C-terminal part represses multimerization [17];
SF   here, one subregion is a hydrophobic repeat which may form intramolecular coiled-coil with those close to the DNA-binding domain, while the other is a HSF2-homologous region [16] [17];
SF   regulatory domain aa221-310 [19];
XX
CP   (HeLa).
XX
FF   binds to DNA, not to nucleosome-assembled DNA unless TBP was present during assembly;
FF   activator, mediating response of heat shock genes to heat and stress factors [15] [6];
FF   being constitutively transcribed, HSF1 requires activation by heat induction to bind to DNA [15] [6];
FF   other inducing factors (besides heat) are heavy metals, oxidizing agents, teratogens, hypoxia, and arachidonate [18] [11];
FF   inducing signals cause transition of HSF1 from inactive monomeric to active trimeric state [17];
FF   phosphorylation appears to modulate the trans-activation potential by HSF1 [6];
FF   induced by following stress factors: heat, hydrogen peroxide, osmotic stress [22];
FF   DNA binding may be increased by DeltaN p73alpha T06002 [23];
FF   HSF1 builds a subcellular structure (granules) in the nuclei of stressed cells [26];
FF   HSF1 granules associate in vivo with chromosome 9q11-9q12 during heat stress [24];
FF   aaT142 is phosphorylated by CK2 [25];
FF   phosphorylation at T142 is essential for activation of HSF1 by heat shock [25];
FF   HSF1  associates with HSF2 T01043 in vitro and in vivo, binding is enhanced by heat shock [27];
FF   colocalizes with the SUMO-1 protein in nuclear granules under heat stress and heavy metal (cadmium) stress [28];
FF   Lysine 298 is a site of SUMO-1 (small ubiquitin related protein) modification in vivo [28];
FF   associates with the BRG1, the ATPase subunit of the ATP-dependant chromatin remodeling complex SWI/SNF at the transcriptional domain [29];
FF   exists in unstressed cells in a heterodimeric complex with the Heat Shock Protein Hsp70 [30];
FF   interacts with Hsp90-Immunophilin-p23 complexes [31];
FF   interacts with Hsp90 with both, trimeric and nontrimeric forms [31];
FF   is associated with the Hsp90-Immunophilin(FKBP52)-p23 complex in a trimeric, but transcriptionally inactive, form;
FF   overexpression of a competing protein to the Hsp90-Immunophilin(FKBP52)-p23 complex alleviates the repression, the presence of stress-denatured proteins has the same effect [31];
FF   Hsp90-Immunophilin(FKBP52)-p23 complex binds to the regulatory domain of HSF1 [31];
FF   serine 230 is a phosphorylation site in the regulatory domain [19];
FF   a mutation S230A impairs the transcriptional activity of HSF1 [19];
FF   the phosphorylation of serine 230 contributes to the stress-induced transcriptional activity of HSF1 [19];
XX
IN   T08796 ASC-2; human, Homo sapiens.
IN   T09410 C/EBPbeta; Mammalia.
IN   T15118 CBP; Mammalia.
IN   T02944 Daxx; human, Homo sapiens.
IN   T01042 HSF1-L; human, Homo sapiens.
IN   T09196 HSF2A; human, Homo sapiens.
IN   T16186 HSF2B; human, Homo sapiens.
IN   T01264 HST; yeast, Kluyveromyces lactis.
IN   T09092 PC4; human, Homo sapiens.
IN   T09238 TAFII55; human, Homo sapiens.
IN   T08520 TBP-isoform1; human, Homo sapiens.
IN   T09237 TFIIA-gamma; human, Homo sapiens.
IN   T08496 TFIIB; human, Homo sapiens.
XX
MX   M00146 V$HSF1_01.
MX   M07259 V$HSF1_Q5.
MX   M07459 V$HSF1_Q5_01.
MX   M01023 V$HSF1_Q6.
MX   M02017 V$HSF1_Q6_01.
MX   M00641 V$HSF_Q6.
XX
BS   R01925.
BS   R03331.
BS   R03624.
BS   R00754.
BS   R00756.
BS   R00773.
BS   R00762.
BS   R00763.
BS   R00764.
BS   R04287.
BS   R02181.
BS   R15803.
BS   R15806.
BS   R15816.
BS   R15817.
BS   R15818.
BS   R15819.
BS   R15820.
BS   R15797.
BS   R15740.
BS   R15766.
XX
DR   TRANSPATH: MO000006878.
DR   EMBL: M64673;
DR   UniProtKB: Q00613-1;
XX
RN   [1]; RE0000170.
RX   PUBMED: 2018972.
RA   Sorger P. K.
RT   Heat shock factor and the heat shock response
RL   Cell 65:363-366 (1991).
RN   [2]; RE0000284.
RX   PUBMED: 1913856.
RA   Kimura Y., Taniguchi T., Yahara I.
RT   An alteration in molecular form associated with activation of human heat shock factor
RL   Cell Struct. Funct. 16:263-271 (1991).
RN   [3]; RE0000760.
RX   PUBMED: 2065977.
RA   Taylor I. C. A., Workman J. L., Schuetz T. J., Kingston R. E.
RT   Facilitated binding of GAL4 and heat shock factor to nucleosomal templates: differential function of DNA-binding domains
RL   Genes Dev. 5:1285-1298 (1991).
RN   [4]; RE0000851.
RX   PUBMED: 3198647.
RA   Goldenberg C. J., Luo Y., Fenna M., Baler R., Weinmann R., Voellmy R.
RT   Purified Human Factor Activates Heat Shock Promoter in a HeLa Cell-free Transcription System
RL   J. Biol. Chem. 263:19734-19739 (1988).
RN   [5]; RE0001284.
RX   PUBMED: 3561411.
RA   Morgan W. D., Williams G. T., Morimoto R. I., Greene J., Kingston R. E., Tjian R.
RT   Two transcriptional activators, CCAAT-box-binding transcription factor and heat shock transcription factor, interact with a human hsp70 gene promoter
RL   Mol. Cell. Biol. 7:1129-1138 (1987).
RN   [6]; RE0001285.
RX   PUBMED: 3600634.
RA   Kingston R. E., Schuetz T. J., Larin Z.
RT   Heat-Inducible Human Factor That Binds to a Human hsp70 Promoter
RL   Mol. Cell. Biol. 7:1530-1534 (1987).
RN   [7]; RE0001286.
RX   PUBMED: 3211126.
RA   Mosser D. D., Theodorakis N. G., Morimoto R. I.
RT   Coordinate Changes in Heat Shock Element-Binding Acitvity and HSP70 Gene Transcription Rates in Human Cells
RL   Mol. Cell. Biol. 8:4736-4744 (1988).
RN   [8]; RE0001575.
RX   PUBMED: 1986252.
RA   Abravaya K., Phillips B., Morimoto R. I.
RT   Heat shock-induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting
RL   Mol. Cell. Biol. 11:586-592 (1991).
RN   [9]; RE0001657.
RX   PUBMED: 1904540.
RA   Cunniff N. F. A., Wagner J., Morgan W. D.
RT   Modular recognition of 5-base-pair DNA sequence motifs by human heat shock transcription factor
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