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RecName: Full=Heat shock factor protein 1; Short=HSF 1; AltName: Full=Heat shock transcription factor 1; Short=HSTF 1

UniProtKB/Swiss-Prot: Q00613.1

Identical Proteins FASTA Graphics 

LOCUS       HSF1_HUMAN               529 aa            linear   PRI 27-NOV-2024
DEFINITION  RecName: Full=Heat shock factor protein 1; Short=HSF 1; AltName:
            Full=Heat shock transcription factor 1; Short=HSTF 1.
ACCESSION   Q00613
VERSION     Q00613.1
DBSOURCE    UniProtKB: locus HSF1_HUMAN, accession Q00613;
            class: standard.
            extra accessions:A8K4L0,A8MW26,Q53XT4
            created: Feb 1, 1994.
            sequence updated: Feb 1, 1994.
            annotation updated: Nov 27, 2024.
            xrefs: M64673.1, AAA52695.1, AK290975.1, BAF83664.1, BT007351.1,
            AAP36015.1, AC110280.8, AF205589.5, BC014638.1, AAH14638.1, A41137,
            NP_005517.1, XP_016868866.1, 2LDU_A, 5D5U_B, 5D5V_B, 5D5V_D,
            5HDG_A, 5HDN_A, 5HDN_B, 5HDN_C, 5HDN_D, 7DCJ_A, 7DCJ_B, 7DCS_A,
            7DCS_B, 7DCS_C, 7DCS_D, 7DCS_E, 7DCS_F, 7DCT_A, 7DCT_B, 7DCT_C,
            7DCT_D, 7DCT_E, 7DCT_F
            xrefs (non-sequence databases): CCDS:CCDS6419.1, PDBsum:2LDU,
            PDBsum:5D5U, PDBsum:5D5V, PDBsum:5HDG, PDBsum:5HDN, PDBsum:7DCJ,
            PDBsum:7DCS, PDBsum:7DCT, AlphaFoldDB:Q00613, BMRB:Q00613,
            SMR:Q00613, BioGRID:109530, CORUM:Q00613, DIP:DIP-35670N,
            IntAct:Q00613, MINT:Q00613, STRING:9606.ENSP00000431512,
            BindingDB:Q00613, ChEMBL:CHEMBL5869, DrugBank:DB06258,
            MoonDB:Q00613, GlyGen:Q00613, iPTMnet:Q00613, MetOSite:Q00613,
            PhosphoSitePlus:Q00613, BioMuta:HSF1, DMDM:462333, jPOST:Q00613,
            MassIVE:Q00613, PaxDb:9606-ENSP00000431512, PeptideAtlas:Q00613,
            ProteomicsDB:57864, ProteomicsDB:57865, Pumba:Q00613,
            Antibodypedia:1848, DNASU:3297, Ensembl:ENST00000528838.6,
            Ensembl:ENSP00000431512.1, Ensembl:ENSG00000185122.11,
            Ensembl:ENST00000646252.2, Ensembl:ENSP00000493830.1,
            Ensembl:ENSG00000284774.2, GeneID:3297, KEGG:hsa:3297,
            MANE-Select:ENST00000528838.6, UCSC:uc003zbt.5, AGR:HGNC:5224,
            CTD:3297, DisGeNET:3297, GeneCards:HSF1, HGNC:5224,
            HPA:ENSG00000185122, MIM 140580, neXtProt:NX_Q00613,
            OpenTargets:ENSG00000185122, PharmGKB:PA29493,
            VEuPathDB:HostDB:ENSG00000185122, eggNOG:KOG0627,
            GeneTree:ENSGT00940000158421, HOGENOM:CLU_038829_2_0_1,
            InParanoid:Q00613, OMA:MPIFFEL, OrthoDB:1117127at2759,
            PhylomeDB:Q00613, TreeFam:TF330401, PathwayCommons:Q00613,
            Reactome:R-HSA-3371453, Reactome:R-HSA-3371511,
            Reactome:R-HSA-3371568, Reactome:R-HSA-3371571,
            Reactome:R-HSA-9646399, SignaLink:Q00613, SIGNOR:Q00613,
            BioGRID-ORCS:3297, ChiTaRS:HSF1, EvolutionaryTrace:Q00613,
            GeneWiki:HSF1, GenomeRNAi:3297, Pharos:Q00613, PRO:PR:Q00613,
            Proteomes:UP000005640, RNAct:Q00613, Bgee:ENSG00000185122,
            ExpressionAtlas:Q00613, GO:0005813, GO:0000785, GO:0005737,
            GO:0005829, GO:0000791, GO:0000792, GO:0000776, GO:0097431,
            GO:0097165, GO:0005654, GO:0005634, GO:0048471, GO:0016605,
            GO:0101031, GO:1990904, GO:0031490, GO:0003677, GO:0001228,
            GO:0003700, GO:0000981, GO:0001227, GO:0140296, GO:0031072,
            GO:0051879, GO:0042802, GO:1990841, GO:0046982, GO:0019901,
            GO:0000978, GO:0001162, GO:0043565, GO:1990837, GO:0098847,
            GO:0097677, GO:0000976, GO:0061770, GO:1904385, GO:0071276,
            GO:0071280, GO:0072738, GO:0071392, GO:0071480, GO:0034605,
            GO:0070301, GO:1904845, GO:0071222, GO:1904843, GO:0035865,
            GO:1903936, GO:0034620, GO:0071466, GO:0006952, GO:0006281,
            GO:0000165, GO:0006397, GO:0051028, GO:0010667, GO:2001033,
            GO:0010629, GO:0090084, GO:0031333, GO:0000122, GO:1902512,
            GO:0120162, GO:0051091, GO:0010628, GO:0090261, GO:0045651,
            GO:0045931, GO:0062029, GO:0045944, GO:0065003, GO:1900034,
            GO:0006357, GO:0014823, GO:1990910, GO:0007584, GO:1901652,
            GO:1990911, GO:0033574, FunFam:1.10.10.10:FF:000027,
            Gene3D:1.10.10.10, IDEAL:IID00461, InterPro:IPR000232,
            InterPro:IPR027725, InterPro:IPR010542, InterPro:IPR036388,
            InterPro:IPR036390, PANTHER:PTHR10015:SF274, PANTHER:PTHR10015,
            Pfam:PF00447, Pfam:PF06546, PRINTS:PR00056, SMART:SM00415,
            SUPFAM:SSF46785, PROSITE:PS00434
KEYWORDS    3D-structure; Acetylation; Activator; Alternative splicing;
            Centromere; Chromosome; Cytoplasm; Cytoskeleton; Direct protein
            sequencing; DNA damage; DNA repair; DNA-binding; Host-virus
            interaction; Isopeptide bond; Kinetochore; mRNA processing; mRNA
            transport; Nucleus; Phosphoprotein; Proteomics identification;
            Reference proteome; Stress response; Transcription; Transcription
            regulation; Transport; Ubl conjugation.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Rabindran,S.K., Giorgi,G., Clos,J. and Wu,C.
  TITLE     Molecular cloning and expression of a human heat shock factor, HSF1
  JOURNAL   Proc Natl Acad Sci U S A 88 (16), 6906-6910 (1991)
   PUBMED   1871105
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DNA-BINDING.
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Kalnine,N., Chen,X., Rolfs,A., Halleck,A., Hines,L., Eisenstein,S.,
            Koundinya,M., Raphael,J., Moreira,D., Kelley,T., LaBaer,J., Lin,Y.,
            Phelan,M. and Farmer,A.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-MAY-2003) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Nusbaum,C., Mikkelsen,T.S., Zody,M.C., Asakawa,S., Taudien,S.,
            Garber,M., Kodira,C.D., Schueler,M.G., Shimizu,A., Whittaker,C.A.,
            Chang,J.L., Cuomo,C.A., Dewar,K., FitzGerald,M.G., Yang,X.,
            Allen,N.R., Anderson,S., Asakawa,T., Blechschmidt,K., Bloom,T.,
            Borowsky,M.L., Butler,J., Cook,A., Corum,B., DeArellano,K.,
            DeCaprio,D., Dooley,K.T., Dorris,L. III, Engels,R., Glockner,G.,
            Hafez,N., Hagopian,D.S., Hall,J.L., Ishikawa,S.K., Jaffe,D.B.,
            Kamat,A., Kudoh,J., Lehmann,R., Lokitsang,T., Macdonald,P.,
            Major,J.E., Matthews,C.D., Mauceli,E., Menzel,U., Mihalev,A.H.,
            Minoshima,S., Murayama,Y., Naylor,J.W., Nicol,R., Nguyen,C.,
            O'Leary,S.B., O'Neill,K., Parker,S.C., Polley,A., Raymond,C.K.,
            Reichwald,K., Rodriguez,J., Sasaki,T., Schilhabel,M., Siddiqui,R.,
            Smith,C.L., Sneddon,T.P., Talamas,J.A., Tenzin,P., Topham,K.,
            Venkataraman,V., Wen,G., Yamazaki,S., Young,S.K., Zeng,Q.,
            Zimmer,A.R., Rosenthal,A., Birren,B.W., Platzer,M., Shimizu,N. and
            Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 8
  JOURNAL   Nature 439 (7074), 331-335 (2006)
   PUBMED   16421571
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).;
            TISSUE=Muscle
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Schuetz,T.J., Gallo,G.J., Sheldon,L., Tempst,P. and Kingston,R.E.
  TITLE     Isolation of a cDNA for HSF2: evidence for two heat shock factor
            genes in humans
  JOURNAL   Proc Natl Acad Sci U S A 88 (16), 6911-6915 (1991)
   PUBMED   1871106
  REMARK    PROTEIN SEQUENCE OF 73-79; 81-93; 97-106; 163-170 AND 337-352.
REFERENCE   7  (residues 1 to 529)
  AUTHORS   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. and Sistonen,L.
  TITLE     Phosphorylation of serine 230 promotes inducible transcriptional
            activity of heat shock factor 1
  JOURNAL   EMBO J 20 (14), 3800-3810 (2001)
   PUBMED   11447121
  REMARK    PROTEIN SEQUENCE OF 228-241 AND 297-310, PHOSPHORYLATION AT SER-230
            BY CAMK2, PHOSPHORYLATION AT SER-303 AND SER-307, FUNCTION,
            SUBCELLULAR LOCATION, MUTAGENESIS OF SER-230, DOMAIN, AND
            IDENTIFICATION BY MASS SPECTROMETRY.
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Abravaya,K., Phillips,B. and Morimoto,R.I.
  TITLE     Heat shock-induced interactions of heat shock transcription factor
            and the human hsp70 promoter examined by in vivo footprinting
  JOURNAL   Mol Cell Biol 11 (1), 586-592 (1991)
   PUBMED   1986252
  REMARK    FUNCTION, AND DNA-BINDING.
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Baler,R., Dahl,G. and Voellmy,R.
  TITLE     Activation of human heat shock genes is accompanied by
            oligomerization, modification, and rapid translocation of heat
            shock transcription factor HSF1
  JOURNAL   Mol Cell Biol 13 (4), 2486-2496 (1993)
   PUBMED   8455624
  REMARK    FUNCTION, DNA-BINDING, SUBUNIT, AND SUBCELLULAR LOCATION.
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Rabindran,S.K., Wisniewski,J., Li,L., Li,G.C. and Wu,C.
  TITLE     Interaction between heat shock factor and hsp70 is insufficient to
            suppress induction of DNA-binding activity in vivo
  JOURNAL   Mol Cell Biol 14 (10), 6552-6560 (1994)
   PUBMED   7935376
  REMARK    SUBUNIT, AND INTERACTION WITH HSPA1A.
REFERENCE   11 (residues 1 to 529)
  AUTHORS   Zuo,J., Baler,R., Dahl,G. and Voellmy,R.
  TITLE     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
  JOURNAL   Mol Cell Biol 14 (11), 7557-7568 (1994)
   PUBMED   7935471
  REMARK    FUNCTION, DNA-BINDING, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-140;
            MET-147; LEU-189; LEU-193; MET-391 AND LEU-395.
REFERENCE   12 (residues 1 to 529)
  AUTHORS   Green,M., Schuetz,T.J., Sullivan,E.K. and Kingston,R.E.
  TITLE     A heat shock-responsive domain of human HSF1 that regulates
            transcription activation domain function
  JOURNAL   Mol Cell Biol 15 (6), 3354-3362 (1995)
   PUBMED   7760831
  REMARK    FUNCTION, AND DOMAIN.
REFERENCE   13 (residues 1 to 529)
  AUTHORS   Zuo,J., Rungger,D. and Voellmy,R.
  TITLE     Multiple layers of regulation of human heat shock transcription
            factor 1
  JOURNAL   Mol Cell Biol 15 (8), 4319-4330 (1995)
   PUBMED   7623826
  REMARK    FUNCTION, SUBUNIT, DNA-BINDING, SUBCELLULAR LOCATION, DOMAIN, AND
            MUTAGENESIS OF LEU-140; MET-147; LEU-189 AND MET-391.
REFERENCE   14 (residues 1 to 529)
  AUTHORS   Baler,R., Zou,J. and Voellmy,R.
  TITLE     Evidence for a role of Hsp70 in the regulation of the heat shock
            response in mammalian cells
  JOURNAL   Cell Stress Chaperones 1 (1), 33-39 (1996)
   PUBMED   9222587
  REMARK    SUBUNIT, AND INTERACTION WITH HSPA1A.
REFERENCE   15 (residues 1 to 529)
  AUTHORS   Knauf,U., Newton,E.M., Kyriakis,J. and Kingston,R.E.
  TITLE     Repression of human heat shock factor 1 activity at control
            temperature by phosphorylation
  JOURNAL   Genes Dev 10 (21), 2782-2793 (1996)
   PUBMED   8946918
  REMARK    PHOSPHORYLATION AT SER-303 AND SER-307, FUNCTION, DOMAIN,
            MUTAGENESIS OF ARG-296; VAL-297; LYS-298; GLU-299; GLU-300;
            SER-303; SER-307; ARG-309 AND GLU-311, AND IDENTIFICATION BY MASS
            SPECTROMETRY.
REFERENCE   16 (residues 1 to 529)
  AUTHORS   Chu,B., Soncin,F., Price,B.D., Stevenson,M.A. and Calderwood,S.K.
  TITLE     Sequential phosphorylation by mitogen-activated protein kinase and
            glycogen synthase kinase 3 represses transcriptional activation by
            heat shock factor-1
  JOURNAL   J Biol Chem 271 (48), 30847-30857 (1996)
   PUBMED   8940068
  REMARK    PHOSPHORYLATION AT SER-275; SER-303 BY GSK3B AND SER-307 BY MAPK3,
            FUNCTION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, AND
            MUTAGENESIS OF SER-275; SER-303 AND SER-307.
REFERENCE   17 (residues 1 to 529)
  AUTHORS   Chen,C., Xie,Y., Stevenson,M.A., Auron,P.E. and Calderwood,S.K.
  TITLE     Heat shock factor 1 represses Ras-induced transcriptional
            activation of the c-fos gene
  JOURNAL   J Biol Chem 272 (43), 26803-26806 (1997)
   PUBMED   9341107
  REMARK    FUNCTION, AND MUTAGENESIS OF LEU-22.
REFERENCE   18 (residues 1 to 529)
  AUTHORS   Kline,M.P. and Morimoto,R.I.
  TITLE     Repression of the heat shock factor 1 transcriptional activation
            domain is modulated by constitutive phosphorylation
  JOURNAL   Mol Cell Biol 17 (4), 2107-2115 (1997)
   PUBMED   9121459
  REMARK    PHOSPHORYLATION AT SER-303 AND SER-307, FUNCTION, DOMAIN,
            MUTAGENESIS OF SER-303 AND SER-307, AND IDENTIFICATION BY MASS
            SPECTROMETRY.
REFERENCE   19 (residues 1 to 529)
  AUTHORS   Zou,J., Guo,Y., Guettouche,T., Smith,D.F. and Voellmy,R.
  TITLE     Repression of heat shock transcription factor HSF1 activation by
            HSP90 (HSP90 complex) that forms a stress-sensitive complex with
            HSF1
  JOURNAL   Cell 94 (4), 471-480 (1998)
   PUBMED   9727490
  REMARK    FUNCTION, SUBUNIT, AND INTERACTION WITH HSP90 PROTEINS.
REFERENCE   20 (residues 1 to 529)
  AUTHORS   Shi,Y., Mosser,D.D. and Morimoto,R.I.
  TITLE     Molecular chaperones as HSF1-specific transcriptional repressors
  JOURNAL   Genes Dev 12 (5), 654-666 (1998)
   PUBMED   9499401
  REMARK    INTERACTION WITH DNAJB1; HSPA1A AND HSPA8, FUNCTION, DNA-BINDING,
            AND PHOSPHORYLATION.
REFERENCE   21 (residues 1 to 529)
  AUTHORS   Xia,W., Guo,Y., Vilaboa,N., Zuo,J. and Voellmy,R.
  TITLE     Transcriptional activation of heat shock factor HSF1 probed by
            phosphopeptide analysis of factor 32P-labeled in vivo
  JOURNAL   J Biol Chem 273 (15), 8749-8755 (1998)
   PUBMED   9535852
  REMARK    PHOSPHORYLATION AT SER-307, FUNCTION, MUTAGENESIS OF SER-275;
            SER-303 AND SER-307, AND IDENTIFICATION BY MASS SPECTROMETRY.
REFERENCE   22 (residues 1 to 529)
  AUTHORS   Mercier,P.A., Winegarden,N.A. and Westwood,J.T.
  TITLE     Human heat shock factor 1 is predominantly a nuclear protein before
            and after heat stress
  JOURNAL   J Cell Sci 112 (Pt 16), 2765-2774 (1999)
   PUBMED   10413683
  REMARK    SUBCELLULAR LOCATION.
REFERENCE   23 (residues 1 to 529)
  AUTHORS   Jolly,C., Usson,Y. and Morimoto,R.I.
  TITLE     Rapid and reversible relocalization of heat shock factor 1 within
            seconds to nuclear stress granules
  JOURNAL   Proc Natl Acad Sci U S A 96 (12), 6769-6774 (1999)
   PUBMED   10359787
  REMARK    FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND DNA-BINDING.
REFERENCE   24 (residues 1 to 529)
  AUTHORS   Yuan,C.X. and Gurley,W.B.
  TITLE     Potential targets for HSF1 within the preinitiation complex
  JOURNAL   Cell Stress Chaperones 5 (3), 229-242 (2000)
   PUBMED   11005381
  REMARK    INTERACTION WITH GTF2A2; GTF2B AND TBP.
REFERENCE   25 (residues 1 to 529)
  AUTHORS   Dai,R., Frejtag,W., He,B., Zhang,Y. and Mivechi,N.F.
  TITLE     c-Jun NH2-terminal kinase targeting and phosphorylation of heat
            shock factor-1 suppress its transcriptional activity
  JOURNAL   J Biol Chem 275 (24), 18210-18218 (2000)
   PUBMED   10747973
  REMARK    INTERACTION WITH MAPK3 AND MAPK8, PHOSPHORYLATION AT SER-363 BY
            MAPK8, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF SER-363, AND
            IDENTIFICATION BY MASS SPECTROMETRY.
REFERENCE   26 (residues 1 to 529)
  AUTHORS   Hong,Y., Rogers,R., Matunis,M.J., Mayhew,C.N., Goodson,M.L.,
            Park-Sarge,O.K. and Sarge,K.D.
  TITLE     Regulation of heat shock transcription factor 1 by stress-induced
            SUMO-1 modification
  JOURNAL   J Biol Chem 276 (43), 40263-40267 (2001)
   PUBMED   11514557
  REMARK    SUMOYLATION AT LYS-298, MUTAGENESIS OF LYS-298, AND SUBCELLULAR
            LOCATION.
            Erratum:[J Biol Chem 2002 Jul 19;277(29):26708. Goodson M
            [corrected to Goodson ML]]
REFERENCE   27 (residues 1 to 529)
  AUTHORS   Guo,Y., Guettouche,T., Fenna,M., Boellmann,F., Pratt,W.B.,
            Toft,D.O., Smith,D.F. and Voellmy,R.
  TITLE     Evidence for a mechanism of repression of heat shock factor 1
            transcriptional activity by a multichaperone complex
  JOURNAL   J Biol Chem 276 (49), 45791-45799 (2001)
   PUBMED   11583998
  REMARK    COMPONENT OF A CHAPERONE COMPLEX, INTERACTION WITH FKBP4 AND HSP90
            PROTEINS, SUBUNIT, PHOSPHORYLATION, FUNCTION, AND DNA-BINDING.
REFERENCE   28 (residues 1 to 529)
  AUTHORS   Hilgarth,R.S., Hong,Y., Park-Sarge,O.K. and Sarge,K.D.
  TITLE     Insights into the regulation of heat shock transcription factor 1
            SUMO-1 modification
  JOURNAL   Biochem Biophys Res Commun 303 (1), 196-200 (2003)
   PUBMED   12646186
  REMARK    PHOSPHORYLATION AT SER-307, SUMOYLATION, AND MUTAGENESIS OF
            LYS-298; SER-303 AND SER-307.
REFERENCE   29 (residues 1 to 529)
  AUTHORS   Soncin,F., Zhang,X., Chu,B., Wang,X., Asea,A., Ann Stevenson,M.,
            Sacks,D.B. and Calderwood,S.K.
  TITLE     Transcriptional activity and DNA binding of heat shock factor-1
            involve phosphorylation on threonine 142 by CK2
  JOURNAL   Biochem Biophys Res Commun 303 (2), 700-706 (2003)
   PUBMED   12659875
  REMARK    PHOSPHORYLATION AT THR-142 BY CK2, FUNCTION, MUTAGENESIS OF
            THR-142, AND IDENTIFICATION BY MASS SPECTROMETRY.
REFERENCE   30 (residues 1 to 529)
  AUTHORS   Hietakangas,V., Ahlskog,J.K., Jakobsson,A.M., Hellesuo,M.,
            Sahlberg,N.M., Holmberg,C.I., Mikhailov,A., Palvimo,J.J.,
            Pirkkala,L. and Sistonen,L.
  TITLE     Phosphorylation of serine 303 is a prerequisite for the
            stress-inducible SUMO modification of heat shock factor 1
  JOURNAL   Mol Cell Biol 23 (8), 2953-2968 (2003)
   PUBMED   12665592
  REMARK    SUMOYLATION AT LYS-298, PHOSPHORYLATION AT SER-303, SUBCELLULAR
            LOCATION, MUTAGENESIS OF LYS-91; LYS-126; LYS-150; LYS-162;
            SER-230; LYS-298; SER-303; SER-307; SER-363 AND LYS-381, AND
            IDENTIFICATION BY MASS SPECTROMETRY.
REFERENCE   31 (residues 1 to 529)
  AUTHORS   Wang,X., Grammatikakis,N., Siganou,A. and Calderwood,S.K.
  TITLE     Regulation of molecular chaperone gene transcription involves the
            serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic
            sequestration of heat shock factor 1
  JOURNAL   Mol Cell Biol 23 (17), 6013-6026 (2003)
   PUBMED   12917326
  REMARK    FUNCTION, DNA-BINDING, INTERACTION WITH YWHAE, PHOSPHORYLATION,
            SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-303 AND SER-307.
REFERENCE   32 (residues 1 to 529)
  AUTHORS   Xing,H., Mayhew,C.N., Cullen,K.E., Park-Sarge,O.K. and Sarge,K.D.
  TITLE     HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with
            symplekin
  JOURNAL   J Biol Chem 279 (11), 10551-10555 (2004)
   PUBMED   14707147
  REMARK    FUNCTION, INTERACTION WITH SYMPK AND CSTF2, SUBCELLULAR LOCATION,
            AND MUTAGENESIS OF LEU-22.
REFERENCE   33 (residues 1 to 529)
  AUTHORS   Boellmann,F., Guettouche,T., Guo,Y., Fenna,M., Mnayer,L. and
            Voellmy,R.
  TITLE     DAXX interacts with heat shock factor 1 during stress activation
            and enhances its transcriptional activity
  JOURNAL   Proc Natl Acad Sci U S A 101 (12), 4100-4105 (2004)
   PUBMED   15016915
  REMARK    FUNCTION, INTERACTION WITH DAXX, IDENTIFICATION IN A
            RIBONUCLEOPROTEIN COMPLEX, AND MUTAGENESIS OF LYS-298 AND SER-326.
REFERENCE   34 (residues 1 to 529)
  AUTHORS   Guettouche,T., Boellmann,F., Lane,W.S. and Voellmy,R.
  TITLE     Analysis of phosphorylation of human heat shock factor 1 in cells
            experiencing a stress
  JOURNAL   BMC Biochem 6, 4 (2005)
   PUBMED   15760475
  REMARK    PHOSPHORYLATION AT SER-121; SER-230; SER-292; SER-303; SER-307;
            SER-314; SER-319; SER-326; SER-344; SER-363; SER-419 AND SER-444,
            MUTAGENESIS OF SER-326, AND IDENTIFICATION BY MASS SPECTROMETRY.
            Publication Status: Online-Only
REFERENCE   35 (residues 1 to 529)
  AUTHORS   Kim,S.A., Yoon,J.H., Lee,S.H. and Ahn,S.G.
  TITLE     Polo-like kinase 1 phosphorylates heat shock transcription factor 1
            and mediates its nuclear translocation during heat stress
  JOURNAL   J Biol Chem 280 (13), 12653-12657 (2005)
   PUBMED   15661742
  REMARK    INTERACTION WITH PLK1 AND HSP90 PROTEINS, PHOSPHORYLATION AT
            SER-419 BY PLK1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-292;
            SER-314; SER-319; SER-326 AND SER-419.
REFERENCE   36 (residues 1 to 529)
  AUTHORS   Olsen,J.V., Blagoev,B., Gnad,F., Macek,B., Kumar,C., Mortensen,P.
            and Mann,M.
  TITLE     Global, in vivo, and site-specific phosphorylation dynamics in
            signaling networks
  JOURNAL   Cell 127 (3), 635-648 (2006)
   PUBMED   17081983
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-323, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Cervix carcinoma
REFERENCE   37 (residues 1 to 529)
  AUTHORS   Wang,X., Khaleque,M.A., Zhao,M.J., Zhong,R., Gaestel,M. and
            Calderwood,S.K.
  TITLE     Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on
            serine 121, inhibits transcriptional activity and promotes HSP90
            binding
  JOURNAL   J Biol Chem 281 (2), 782-791 (2006)
   PUBMED   16278218
  REMARK    PHOSPHORYLATION AT SER-121 BY MAPKAPK2, FUNCTION, INTERACTION WITH
            HSP90 PROTEINS AND MAPKAPK2, MUTAGENESIS OF THR-120; SER-121;
            SER-123; THR-124; THR-527 AND SER-529, AND IDENTIFICATION BY MASS
            SPECTROMETRY.
REFERENCE   38 (residues 1 to 529)
  AUTHORS   Hietakangas,V., Anckar,J., Blomster,H.A., Fujimoto,M.,
            Palvimo,J.J., Nakai,A. and Sistonen,L.
  TITLE     PDSM, a motif for phosphorylation-dependent SUMO modification
  JOURNAL   Proc Natl Acad Sci U S A 103 (1), 45-50 (2006)
   PUBMED   16371476
  REMARK    SUMOYLATION AT LYS-298, AND PHOSPHORYLATION AT SER-303.
REFERENCE   39 (residues 1 to 529)
  AUTHORS   Shamovsky,I., Ivannikov,M., Kandel,E.S., Gershon,D. and Nudler,E.
  TITLE     RNA-mediated response to heat shock in mammalian cells
  JOURNAL   Nature 440 (7083), 556-560 (2006)
   PUBMED   16554823
  REMARK    INTERACTION WITH EEF1A PROTEINS, AND IDENTIFICATION IN A
            RIBONUCLEOPROTEIN COMPLEX.
REFERENCE   40 (residues 1 to 529)
  AUTHORS   Piskacek,S., Gregor,M., Nemethova,M., Grabner,M., Kovarik,P. and
            Piskacek,M.
  TITLE     Nine-amino-acid transactivation domain: establishment and
            prediction utilities
  JOURNAL   Genomics 89 (6), 756-768 (2007)
   PUBMED   17467953
  REMARK    DOMAIN.
REFERENCE   41 (residues 1 to 529)
  AUTHORS   Skaggs,H.S., Xing,H., Wilkerson,D.C., Murphy,L.A., Hong,Y.,
            Mayhew,C.N. and Sarge,K.D.
  TITLE     HSF1-TPR interaction facilitates export of stress-induced HSP70
            mRNA
  JOURNAL   J Biol Chem 282 (47), 33902-33907 (2007)
   PUBMED   17897941
  REMARK    FUNCTION IN STRESS-INDUCED NUCLEAR MRNA EXPORT, AND INTERACTION
            WITH TPR.
REFERENCE   42 (residues 1 to 529)
  AUTHORS   Lee,Y.J., Kim,E.H., Lee,J.S., Jeoung,D., Bae,S., Kwon,S.H. and
            Lee,Y.S.
  TITLE     HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is
            essential for mitotic progression
  JOURNAL   Cancer Res 68 (18), 7550-7560 (2008)
   PUBMED   18794143
  REMARK    FUNCTION IN MITOTIC PROGRESSION REGULATION, INTERACTION WITH BTRC;
            CDC20; MAD2L1 AND PLK1, PHOSPHORYLATION AT SER-216 BY PLK1,
            SUBCELLULAR LOCATION, UBIQUITINATION, PROTEASOMAL DEGRADATION, AND
            MUTAGENESIS OF SER-216; SER-230; SER-303; SER-307 AND SER-419.
REFERENCE   43 (residues 1 to 529)
  AUTHORS   Xu,D., Zalmas,L.P. and La Thangue,N.B.
  TITLE     A transcription cofactor required for the heat-shock response
  JOURNAL   EMBO Rep 9 (7), 662-669 (2008)
   PUBMED   18451878
  REMARK    FUNCTION, AND INTERACTION WITH TTC5 AND EP300.
REFERENCE   44 (residues 1 to 529)
  AUTHORS   Cantin,G.T., Yi,W., Lu,B., Park,S.K., Xu,T., Lee,J.D. and
            Yates,J.R. III.
  TITLE     Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
            efficient phosphoproteomic analysis
  JOURNAL   J Proteome Res 7 (3), 1346-1351 (2008)
   PUBMED   18220336
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Cervix carcinoma
REFERENCE   45 (residues 1 to 529)
  AUTHORS   Dephoure,N., Zhou,C., Villen,J., Beausoleil,S.A., Bakalarski,C.E.,
            Elledge,S.J. and Gygi,S.P.
  TITLE     A quantitative atlas of mitotic phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 105 (31), 10762-10767 (2008)
   PUBMED   18669648
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Cervix carcinoma
REFERENCE   46 (residues 1 to 529)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
            MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE   47 (residues 1 to 529)
  AUTHORS   Mayya,V., Lundgren,D.H., Hwang,S.I., Rezaul,K., Wu,L., Eng,J.K.,
            Rodionov,V. and Han,D.K.
  TITLE     Quantitative phosphoproteomic analysis of T cell receptor signaling
            reveals system-wide modulation of protein-protein interactions
  JOURNAL   Sci Signal 2 (84), ra46 (2009)
   PUBMED   19690332
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; THR-323 AND
            SER-326, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
            ANALYSIS].;
            TISSUE=Leukemic T-cell
            Publication Status: Online-Only
REFERENCE   48 (residues 1 to 529)
  AUTHORS   Westerheide,S.D., Anckar,J., Stevens,S.M. Jr., Sistonen,L. and
            Morimoto,R.I.
  TITLE     Stress-inducible regulation of heat shock factor 1 by the
            deacetylase SIRT1
  JOURNAL   Science 323 (5917), 1063-1066 (2009)
   PUBMED   19229036
  REMARK    DEACETYLATION AT LYS-80 BY SIRT1, ACETYLATION AT LYS-80,
            SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
            MUTAGENESIS OF LYS-80.
            Erratum:[Science. 2013 Nov 22;342(6161):931]
REFERENCE   49 (residues 1 to 529)
  AUTHORS   Murshid,A., Chou,S.D., Prince,T., Zhang,Y., Bharti,A. and
            Calderwood,S.K.
  TITLE     Protein kinase A binds and activates heat shock factor 1
  JOURNAL   PLoS One 5 (11), e13830 (2010)
   PUBMED   21085490
  REMARK    INTERACTION WITH PRKACA, PHOSPHORYLATION AT SER-320 BY PRKACA,
            SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
            MUTAGENESIS OF SER-320.
            Publication Status: Online-Only
REFERENCE   50 (residues 1 to 529)
  AUTHORS   Olsen,J.V., Vermeulen,M., Santamaria,A., Kumar,C., Miller,M.L.,
            Jensen,L.J., Gnad,F., Cox,J., Jensen,T.S., Nigg,E.A., Brunak,S. and
            Mann,M.
  TITLE     Quantitative phosphoproteomics reveals widespread full
            phosphorylation site occupancy during mitosis
  JOURNAL   Sci Signal 3 (104), ra3 (2010)
   PUBMED   20068231
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-326, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Cervix carcinoma
            Publication Status: Online-Only
REFERENCE   51 (residues 1 to 529)
  AUTHORS   Kaitsuka,T., Tomizawa,K. and Matsushita,M.
  TITLE     Transformation of eEF1Bdelta into heat-shock response transcription
            factor by alternative splicing
  JOURNAL   EMBO Rep 12 (7), 673-681 (2011)
   PUBMED   21597468
  REMARK    INTERACTION WITH EEF1D.
            Publication Status: Online-Only
REFERENCE   52 (residues 1 to 529)
  AUTHORS   Rigbolt,K.T., Prokhorova,T.A., Akimov,V., Henningsen,J.,
            Johansen,P.T., Kratchmarova,I., Kassem,M., Mann,M., Olsen,J.V. and
            Blagoev,B.
  TITLE     System-wide temporal characterization of the proteome and
            phosphoproteome of human embryonic stem cell differentiation
  JOURNAL   Sci Signal 4 (164), rs3 (2011)
   PUBMED   21406692
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
            Publication Status: Online-Only
REFERENCE   53 (residues 1 to 529)
  AUTHORS   Zhou,H., Di Palma,S., Preisinger,C., Peng,M., Polat,A.N., Heck,A.J.
            and Mohammed,S.
  TITLE     Toward a comprehensive characterization of a human cancer cell
            phosphoproteome
  JOURNAL   J Proteome Res 12 (1), 260-271 (2013)
   PUBMED   23186163
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-307 AND
            SER-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
            ANALYSIS].;
            TISSUE=Cervix carcinoma, and Erythroleukemia
REFERENCE   54 (residues 1 to 529)
  AUTHORS   Raychaudhuri,S., Loew,C., Korner,R., Pinkert,S., Theis,M.,
            Hayer-Hartl,M., Buchholz,F. and Hartl,F.U.
  TITLE     Interplay of acetyltransferase EP300 and the proteasome system in
            regulating heat shock transcription factor 1
  JOURNAL   Cell 156 (5), 975-985 (2014)
   PUBMED   24581496
  REMARK    ACETYLATION AT LYS-80; LYS-91; LYS-118; LYS-150; LYS-188; LYS-208;
            LYS-298 AND LYS-524, PHOSPHORYLATION, UBIQUITINATION, PROTEASOMAL
            DEGRADATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-80; LYS-118;
            LYS-208 AND LYS-298, AND IDENTIFICATION BY MASS SPECTROMETRY.
REFERENCE   55 (residues 1 to 529)
  AUTHORS   Bian,Y., Song,C., Cheng,K., Dong,M., Wang,F., Huang,J., Sun,D.,
            Wang,L., Ye,M. and Zou,H.
  TITLE     An enzyme assisted RP-RPLC approach for in-depth analysis of human
            liver phosphoproteome
  JOURNAL   J Proteomics 96, 253-262 (2014)
   PUBMED   24275569
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-363, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver
REFERENCE   56 (residues 1 to 529)
  AUTHORS   Jin,Y.H., Ahn,S.G. and Kim,S.A.
  TITLE     BAG3 affects the nucleocytoplasmic shuttling of HSF1 upon heat
            stress
  JOURNAL   Biochem Biophys Res Commun 464 (2), 561-567 (2015)
   PUBMED   26159920
  REMARK    INTERACTION WITH BAG3, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND
            NUCLEOCYTOPLASMIC SHUTTLING.
REFERENCE   57 (residues 1 to 529)
  AUTHORS   Ishikawa,Y., Kawabata,S. and Sakurai,H.
  TITLE     HSF1 transcriptional activity is modulated by IER5 and PP2A/B55
  JOURNAL   FEBS Lett 589 (10), 1150-1155 (2015)
   PUBMED   25816751
  REMARK    INTERACTION WITH IER5.
REFERENCE   58 (residues 1 to 529)
  AUTHORS   Kawabata,S., Ishita,Y., Ishikawa,Y. and Sakurai,H.
  TITLE     Immediate-early response 5 (IER5) interacts with protein
            phosphatase 2A and regulates the phosphorylation of ribosomal
            protein S6 kinase and heat shock factor 1
  JOURNAL   FEBS Lett 589 (23), 3679-3685 (2015)
   PUBMED   26496226
  REMARK    INTERACTION WITH IER5.
REFERENCE   59 (residues 1 to 529)
  AUTHORS   Budzynski,M.A., Puustinen,M.C., Joutsen,J. and Sistonen,L.
  TITLE     Uncoupling Stress-Inducible Phosphorylation of Heat Shock Factor 1
            from Its Activation
  JOURNAL   Mol Cell Biol 35 (14), 2530-2540 (2015)
   PUBMED   25963659
  REMARK    FUNCTION, DNA-BINDING, CHROMATIN BINDING, SUBCELLULAR LOCATION, AND
            PHOSPHORYLATIONS.
REFERENCE   60 (residues 1 to 529)
  AUTHORS   Kang,G.Y., Kim,E.H., Lee,H.J., Gil,N.Y., Cha,H.J. and Lee,Y.S.
  TITLE     Heat shock factor 1, an inhibitor of non-homologous end joining
            repair
  JOURNAL   Oncotarget 6 (30), 29712-29724 (2015)
   PUBMED   26359349
  REMARK    FUNCTION IN DNA REPAIR, INTERACTION WITH XRCC5 AND XRCC6,
            SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-80; SER-216; LYS-298;
            SER-326 AND SER-419.
REFERENCE   61 (residues 1 to 529)
  AUTHORS   Prince,T.L., Kijima,T., Tatokoro,M., Lee,S., Tsutsumi,S., Yim,K.,
            Rivas,C., Alarcon,S., Schwartz,H., Khamit-Kush,K., Scroggins,B.T.,
            Beebe,K., Trepel,J.B. and Neckers,L.
  TITLE     Client Proteins and Small Molecule Inhibitors Display Distinct
            Binding Preferences for Constitutive and Stress-Induced HSP90
            Isoforms and Their Conformationally Restricted Mutants
  JOURNAL   PLoS One 10 (10), e0141786 (2015)
   PUBMED   26517842
  REMARK    INTERACTION WITH HSP90AA1 AND HSP90AB1.
            Publication Status: Online-Only
REFERENCE   62 (residues 1 to 529)
  AUTHORS   Dayalan Naidu,S., Sutherland,C., Zhang,Y., Risco,A., de la Vega,L.,
            Caunt,C.J., Hastie,C.J., Lamont,D.J., Torrente,L., Chowdhry,S.,
            Benjamin,I.J., Keyse,S.M., Cuenda,A. and Dinkova-Kostova,A.T.
  TITLE     Heat Shock Factor 1 Is a Substrate for p38 Mitogen-Activated
            Protein Kinases
  JOURNAL   Mol Cell Biol 36 (18), 2403-2417 (2016)
   PUBMED   27354066
  REMARK    PHOSPHORYLATION AT SER-326 BY MAPK12, SUBCELLULAR LOCATION, AND
            MUTAGENESIS OF SER-326.
            Publication Status: Online-Only
REFERENCE   63 (residues 1 to 529)
  AUTHORS   Asano,Y., Kawase,T., Okabe,A., Tsutsumi,S., Ichikawa,H., Tatebe,S.,
            Kitabayashi,I., Tashiro,F., Namiki,H., Kondo,T., Semba,K.,
            Aburatani,H., Taya,Y., Nakagama,H. and Ohki,R.
  TITLE     IER5 generates a novel hypo-phosphorylated active form of HSF1 and
            contributes to tumorigenesis
  JOURNAL   Sci Rep 6, 19174 (2016)
   PUBMED   26754925
  REMARK    DEPHOSPHORYLATION AT SER-121; SER-307; SER-314; THR-323 AND THR-367
            BY PPP2CA, ACETYLATION AT LYS-118, IDENTIFICATION IN COMPLEX WITH
            IER5 AND PPP2CA, INTERACTION WITH HSP90AA1 AND IER5, FUNCTION,
            SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF SER-121; SER-307; SER-314;
            THR-323 AND THR-367.
            Publication Status: Online-Only
REFERENCE   64 (residues 1 to 529)
  AUTHORS   Pan,X.Y., Zhao,W., Zeng,X.Y., Lin,J., Li,M.M., Shen,X.T. and
            Liu,S.W.
  TITLE     Heat Shock Factor 1 Mediates Latent HIV Reactivation
  JOURNAL   Sci Rep 6, 26294 (2016)
   PUBMED   27189267
  REMARK    FUNCTION IN LATENT HIV-1 TRANSCRIPTIONAL REACTIVATION (MICROBIAL
            INFECTION), INTERACTION WITH CDK9; CCNT1 AND EP300, PHOSPHORYLATION
            AT SER-320, ACETYLATION, AND SUBCELLULAR LOCATION.
            Publication Status: Online-Only
REFERENCE   65 (residues 1 to 529)
  AUTHORS   Hendriks,I.A., Lyon,D., Young,C., Jensen,L.J., Vertegaal,A.C. and
            Nielsen,M.L.
  TITLE     Site-specific mapping of the human SUMO proteome reveals
            co-modification with phosphorylation
  JOURNAL   Nat Struct Mol Biol 24 (3), 325-336 (2017)
   PUBMED   28112733
  REMARK    SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-126; LYS-131;
            LYS-208; LYS-224 AND LYS-298, AND IDENTIFICATION BY MASS
            SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE   66 (residues 1 to 529)
  AUTHORS   Mota,A., Waxman,H.K., Hong,R., Lagani,G.D., Niu,S.Y.,
            Bertherat,F.L., Wolfe,L., Malicdan,C.M., Markello,T.C., Adams,D.R.,
            Gahl,W.A., Cheng,C.S., Beffert,U. and Ho,A.
  TITLE     FOXR1 regulates stress response pathways and is necessary for
            proper brain development
  JOURNAL   PLoS Genet 17 (11), e1009854 (2021)
   PUBMED   34723967
  REMARK    FUNCTION.
            Publication Status: Online-Only
REFERENCE   67 (residues 1 to 529)
  AUTHORS   Neudegger,T., Verghese,J., Hayer-Hartl,M., Hartl,F.U. and
            Bracher,A.
  TITLE     Structure of human heat-shock transcription factor 1 in complex
            with DNA
  JOURNAL   Nat Struct Mol Biol 23 (2), 140-146 (2016)
   PUBMED   26727489
  REMARK    X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-120 IN COMPLEX WITH
            DNA, DNA-BINDING, SUBUNIT, AND FUNCTION.
COMMENT     On or before Dec 1, 2006 this sequence version replaced
            gi:74740826, gi:87630.
            [FUNCTION] Functions as a stress-inducible and DNA-binding
            transcription factor that plays a central role in the
            transcriptional activation of the heat shock response (HSR),
            leading to the expression of a large class of molecular chaperones,
            heat shock proteins (HSPs), that protect cells from cellular insult
            damage (PubMed:11447121, PubMed:12659875, PubMed:12917326,
            PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252,
            PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831,
            PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107,
            PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed
            cells, is present in a HSP90-containing multichaperone complex that
            maintains it in a non-DNA-binding inactivated monomeric form
            (PubMed:11583998, PubMed:16278218, PubMed:9727490). Upon exposure
            to heat and other stress stimuli, undergoes homotrimerization and
            activates HSP gene transcription through binding to site-specific
            heat shock elements (HSEs) present in the promoter regions of HSP
            genes (PubMed:10359787, PubMed:11583998, PubMed:12659875,
            PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659,
            PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624,
            PubMed:8940068, PubMed:9499401, PubMed:9727490). Upon heat shock
            stress, forms a chromatin-associated complex with TTC5/STRAP and
            p300/EP300 to stimulate HSR transcription, therefore increasing
            cell survival (PubMed:18451878). Activation is reversible, and
            during the attenuation and recovery phase period of the HSR,
            returns to its unactivated form (PubMed:11583998, PubMed:16278218).
            Binds to inverted 5'-NGAAN-3' pentamer DNA sequences
            (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock
            gene promoters (PubMed:25963659). Activates transcription of
            transcription factor FOXR1 which in turn activates transcription of
            the heat shock chaperones HSPA1A and HSPA6 and the antioxidant
            NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves
            several other functions independently of its transcriptional
            activity. Involved in the repression of Ras-induced transcriptional
            activation of the c-fos gene in heat-stressed cells
            (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing
            and polyadenylation of HSP70 mRNA upon heat-stressed cells in a
            symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role
            in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941).
            Plays a role in the regulation of mitotic progression
            (PubMed:18794143). Also plays a role as a negative regulator of
            non-homologous end joining (NHEJ) repair activity in a DNA
            damage-dependent manner (PubMed:26359349). Involved in
            stress-induced cancer cell proliferation in a IER5-dependent manner
            (PubMed:26754925). {ECO:0000269|PubMed:10359787,
            ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11583998,
            ECO:0000269|PubMed:12659875, ECO:0000269|PubMed:12917326,
            ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:15016915,
            ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:17897941,
            ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:1871105,
            ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:1986252,
            ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26359349,
            ECO:0000269|PubMed:26727489, ECO:0000269|PubMed:26754925,
            ECO:0000269|PubMed:34723967, ECO:0000269|PubMed:7623826,
            ECO:0000269|PubMed:7760831, ECO:0000269|PubMed:7935471,
            ECO:0000269|PubMed:8455624, ECO:0000269|PubMed:8940068,
            ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459,
            ECO:0000269|PubMed:9341107, ECO:0000269|PubMed:9499401,
            ECO:0000269|PubMed:9535852, ECO:0000269|PubMed:9727490}.
            [FUNCTION] (Microbial infection) Plays a role in latent human
            immunodeficiency virus (HIV-1) transcriptional reactivation. Binds
            to the HIV-1 long terminal repeat promoter (LTR) to reactivate
            viral transcription by recruiting cellular transcriptional
            elongation factors, such as CDK9, CCNT1 and EP300.
            {ECO:0000269|PubMed:27189267}.
            [SUBUNIT] Monomer; cytoplasmic latent and transcriptionally
            inactive monomeric form in unstressed cells (PubMed:11583998,
            PubMed:7623826, PubMed:7935376, PubMed:7935471, PubMed:8455624,
            PubMed:9222587, PubMed:9727490). Homotrimer; in response to stress,
            such as heat shock, homotrimerizes and translocates into the
            nucleus, binds to heat shock element (HSE) sequences in promoter of
            heat shock protein (HSP) genes and acquires transcriptional ability
            (PubMed:11583998, PubMed:26727489, PubMed:26754925, PubMed:7623826,
            PubMed:7935471, PubMed:8455624, PubMed:9222587, PubMed:9727490).
            Interacts (via monomeric form) with FKBP4; this interaction occurs
            in unstressed cells (PubMed:11583998). Associates (via monomeric
            form) with HSP90 proteins in a multichaperone complex in
            unnstressed cell; this association maintains HSF1 in a
            non-DNA-binding and transcriptional inactive form by preventing
            HSF1 homotrimerization (PubMed:11583998, PubMed:15661742,
            PubMed:16278218, PubMed:9727490). Homotrimeric transactivation
            activity is modulated by protein-protein interactions and
            post-translational modifications (PubMed:11583998, PubMed:15016915,
            PubMed:16554823, PubMed:26754925). Interacts with HSP90AA1; this
            interaction is decreased in a IER5-dependent manner, promoting HSF1
            accumulation in the nucleus, homotrimerization and DNA-binding
            activities (PubMed:26754925). Part (via regulatory domain in the
            homotrimeric form) of a large heat shock-induced HSP90-dependent
            multichaperone complex at least composed of FKBP4, FKBP5, HSP90
            proteins, PPID, PPP5C and PTGES3; this association maintains the
            HSF1 homotrimeric DNA-bound form in a transcriptionally inactive
            form (PubMed:11583998, PubMed:16278218, PubMed:9727490). Interacts
            with BAG3 (via BAG domain); this interaction occurs in normal and
            heat-shocked cells promoting nuclear shuttling of HSF1 in a
            BAG3-dependent manner (PubMed:26159920). Interacts (via
            homotrimeric and hyperphosphorylated form) with FKBP4; this
            interaction occurs upon heat shock in a HSP90-dependent
            multichaperone complex (PubMed:11583998). Interacts (via
            homotrimeric form preferentially) with EEF1A proteins
            (PubMed:15016915). In heat shocked cells, stress-denatured proteins
            compete with HSF1 homotrimeric DNA-bound form for association of
            the HSP90-dependent multichaperone complex, and hence alleviating
            repression of HSF1-mediated transcriptional activity
            (PubMed:11583998). Interacts (via homotrimeric form preferentially)
            with DAXX; this interaction relieves homotrimeric HSF1 from
            repression of its transcriptional activity by HSP90-dependent
            multichaperone complex upon heat shock (PubMed:15016915). Interacts
            (via D domain and preferentially with hyperphosphorylated form)
            with JNK1; this interaction occurs under both normal growth
            conditions and immediately upon heat shock (PubMed:10747973).
            Interacts (via D domain and preferentially with hyperphosphorylated
            form) with MAPK3; this interaction occurs upon heat shock
            (PubMed:10747973). Interacts with IER5 (via central region); this
            interaction promotes PPP2CA-induced dephosphorylation on Ser-121,
            Ser-307, Ser-314, Thr-323 and Thr-367 and HSF1 transactivation
            activity (PubMed:25816751, PubMed:26496226, PubMed:26754925). Found
            in a ribonucleoprotein complex composed of the HSF1 homotrimeric
            form, translation elongation factor eEF1A proteins and non-coding
            RNA heat shock RNA-1 (HSR1); this complex occurs upon heat shock
            and stimulates HSF1 DNA-binding activity (PubMed:16554823).
            Interacts (via transactivation domain) with HSPA1A/HSP70 and
            DNAJB1; these interactions result in the inhibition of heat shock-
            and HSF1-induced transcriptional activity during the attenuation
            and recovery phase from heat shock (PubMed:7935376, PubMed:9222587,
            PubMed:9499401). Interacts (via Ser-303 and Ser-307 phosphorylated
            form) with YWHAE; this interaction promotes HSF1 sequestration in
            the cytoplasm in an ERK-dependent manner (PubMed:12917326). Found
            in a complex with IER5 and PPP2CA (PubMed:26754925). Interacts with
            TPR; this interaction increases upon heat shock and stimulates
            export of HSP70 mRNA (PubMed:17897941). Interacts with SYMPK (via
            N-terminus) and CSTF2; these interactions occur upon heat shock
            (PubMed:14707147). Interacts (via transactivation domain) with
            HSPA8 (PubMed:9499401). Interacts with EEF1D; this interaction
            occurs at heat shock promoter element (HSE) sequences
            (PubMed:21597468). Interacts with MAPKAPK2 (PubMed:16278218).
            Interacts with PRKACA/PKA (PubMed:21085490). Interacts (via
            transactivation domain) with GTF2A2 (PubMed:11005381). Interacts
            (via transactivation domain) with GTF2B (PubMed:11005381).
            Interacts (via transactivation domain) with TBP (PubMed:11005381).
            Interacts with CDK9, CCNT1 and EP300 (PubMed:27189267). Interacts
            (via N-terminus) with XRCC5 (via N-terminus) and XRCC6 (via
            N-terminus); these interactions are direct and prevent XRCC5/XRCC6
            heterodimeric binding and non-homologous end joining (NHEJ) repair
            activities induced by ionizing radiation (IR) (PubMed:26359349).
            Interacts with PLK1; this interaction occurs during the early
            mitotic period, increases upon heat shock but does not modulate
            neither HSF1 homotrimerization and DNA-binding activities
            (PubMed:15661742, PubMed:18794143). Interacts (via Ser-216
            phosphorylated form) with CDC20; this interaction occurs in mitosis
            in a MAD2L1-dependent manner and prevents PLK1-stimulated
            degradation of HSF1 by blocking the recruitment of the SCF(BTRC)
            ubiquitin ligase complex (PubMed:18794143). Interacts with MAD2L1;
            this interaction occurs in mitosis (PubMed:18794143). Interacts
            with BTRC; this interaction occurs during mitosis, induces its
            ubiquitin-dependent degradation following stimulus-dependent
            phosphorylation at Ser-216, a process inhibited by CDC20
            (PubMed:18794143). Interacts with HSP90AA1 and HSP90AB1
            (PubMed:26517842). Forms a complex with TTC5/STRAP and p300/EP300;
            these interactions augment chromatin-bound HSF1 and p300/EP300
            histone acetyltransferase activity (PubMed:18451878).
            {ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11005381,
            ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12917326,
            ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:15016915,
            ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:16278218,
            ECO:0000269|PubMed:16554823, ECO:0000269|PubMed:17897941,
            ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:18794143,
            ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:21597468,
            ECO:0000269|PubMed:25816751, ECO:0000269|PubMed:26159920,
            ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:26496226,
            ECO:0000269|PubMed:26517842, ECO:0000269|PubMed:26727489,
            ECO:0000269|PubMed:26754925, ECO:0000269|PubMed:27189267,
            ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:7935376,
            ECO:0000269|PubMed:7935471, ECO:0000269|PubMed:8455624,
            ECO:0000269|PubMed:9222587, ECO:0000269|PubMed:9499401,
            ECO:0000269|PubMed:9727490, ECO:0000305|PubMed:15016915}.
            [INTERACTION] Q00613; Q00613: HSF1; NbExp=2; IntAct=EBI-719620,
            EBI-719620; Q00613; Q03933: HSF2; NbExp=11; IntAct=EBI-719620,
            EBI-2556750; Q00613; Q5VY09: IER5; NbExp=3; IntAct=EBI-719620,
            EBI-1774000; Q00613; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-719620,
            EBI-712105; Q00613; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-719620,
            EBI-2796400; Q00613; Q14693: LPIN1; NbExp=3; IntAct=EBI-719620,
            EBI-5278370; Q00613; P49137: MAPKAPK2; NbExp=5; IntAct=EBI-719620,
            EBI-993299; Q00613; Q8N4C8: MINK1; NbExp=2; IntAct=EBI-719620,
            EBI-2133481; Q00613; Q04759: PRKCQ; NbExp=2; IntAct=EBI-719620,
            EBI-374762; Q00613; O14744: PRMT5; NbExp=3; IntAct=EBI-719620,
            EBI-351098; Q00613; Q96CM3: RPUSD4; NbExp=3; IntAct=EBI-719620,
            EBI-7825200; Q00613; P11684: SCGB1A1; NbExp=3; IntAct=EBI-719620,
            EBI-7797649; Q00613; P63165: SUMO1; NbExp=2; IntAct=EBI-719620,
            EBI-80140; Q00613; Q8NFB2: TMEM185A; NbExp=3; IntAct=EBI-719620,
            EBI-21757569; Q00613; Q6ZMY6-2: WDR88; NbExp=3; IntAct=EBI-719620,
            EBI-25857007; Q00613; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-719620,
            EBI-749023.
            [SUBCELLULAR LOCATION] Nucleus {ECO:0000269|PubMed:10413683,
            ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11447121,
            ECO:0000269|PubMed:11514557, ECO:0000269|PubMed:12665592,
            ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147,
            ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:19229036,
            ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:25963659,
            ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27189267,
            ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:7623826,
            ECO:0000269|PubMed:8455624}. Cytoplasm
            {ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973,
            ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:15661742,
            ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:26159920,
            ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27354066,
            ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:8455624}. Nucleus,
            nucleoplasm {ECO:0000269|PubMed:10359787}. Cytoplasm, perinuclear
            region {ECO:0000269|PubMed:21085490}. Cytoplasm, cytoskeleton,
            spindle pole {ECO:0000269|PubMed:18794143}. Cytoplasm,
            cytoskeleton, microtubule organizing center, centrosome
            {ECO:0000269|PubMed:18794143}. Chromosome, centromere, kinetochore
            {ECO:0000269|PubMed:18794143}. Note=The monomeric form is
            cytoplasmic in unstressed cells (PubMed:26159920, PubMed:8455624).
            Predominantly nuclear protein in both unstressed and heat shocked
            cells (PubMed:10359787, PubMed:10413683). Translocates in the
            nucleus upon heat shock (PubMed:8455624). Nucleocytoplasmic
            shuttling protein (PubMed:26159920). Colocalizes with IER5 in the
            nucleus (PubMed:27354066). Colocalizes with BAG3 to the nucleus
            upon heat stress (PubMed:26159920, PubMed:8455624). Localizes in
            subnuclear granules called nuclear stress bodies (nSBs) upon heat
            shock (PubMed:10359787, PubMed:10747973, PubMed:11447121,
            PubMed:11514557, PubMed:19229036, PubMed:24581496,
            PubMed:25963659). Colocalizes with SYMPK and SUMO1 in nSBs upon
            heat shock (PubMed:10359787, PubMed:11447121, PubMed:11514557,
            PubMed:12665592, PubMed:14707147). Colocalizes with PRKACA/PKA in
            the nucleus and nSBs upon heat shock (PubMed:21085490). Relocalizes
            from the nucleus to the cytoplasm during the attenuation and
            recovery phase period of the heat shock response (PubMed:26159920).
            Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent
            manner (PubMed:12917326). Together with histone H2AX, redistributed
            in discrete nuclear DNA damage-induced foci after ionizing
            radiation (IR) (PubMed:26359349). Colocalizes with
            calcium-responsive transactivator SS18L1 at kinetochore region on
            the mitotic chromosomes (PubMed:18794143). Colocalizes with gamma
            tubulin at centrosome (PubMed:18794143). Localizes at spindle pole
            in metaphase (PubMed:18794143). Colocalizes with PLK1 at spindle
            poles during prometaphase (PubMed:18794143).
            {ECO:0000269|PubMed:10359787, ECO:0000269|PubMed:10413683,
            ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11447121,
            ECO:0000269|PubMed:11514557, ECO:0000269|PubMed:12665592,
            ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147,
            ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:21085490,
            ECO:0000269|PubMed:24581496, ECO:0000269|PubMed:25963659,
            ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:26359349,
            ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:8455624}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=Long; IsoId=Q00613-1; Sequence=Displayed;
            Name=Short; IsoId=Q00613-2; Sequence=VSP_002414, VSP_002415.
            [DOMAIN] In unstressed cells, spontaneous homotrimerization is
            inhibited (PubMed:7760831, PubMed:7935471). Intramolecular
            interactions between the hydrophobic repeat HR-A/B and HR-C regions
            are necessary to maintain HSF1 in the inactive, monomeric
            conformation (PubMed:7623826, PubMed:7935471). Furthermore,
            intramolecular interactions between the regulatory domain and the
            nonadjacent transactivation domain prevents transcriptional
            activation, a process that is relieved upon heat shock
            (PubMed:7760831). The regulatory domain is necessary for full
            repression of the transcriptional activation domain in unstressed
            cells through its phosphorylation on Ser-303 and Ser-307
            (PubMed:8946918, PubMed:9121459). In heat stressed cells, HSF1
            homotrimerization occurs through formation of a three-stranded
            coiled-coil structure generated by intermolecular interactions
            between HR-A/B regions allowing DNA-binding activity
            (PubMed:7935471). The D domain is necessary for translocation to
            the nucleus, interaction with JNK1 and MAPK3 and efficient JNK1-
            and MAPK3-dependent phosphorylation (PubMed:10747973). The
            regulatory domain confers heat shock inducibility on the
            transcriptional transactivation domain (PubMed:7760831). The
            regulatory domain is necessary for transcriptional activation
            through its phosphorylation on Ser-230 upon heat shock
            (PubMed:11447121). 9aaTAD is a transactivation motif present in a
            large number of yeast and animal transcription factors
            (PubMed:17467953). {ECO:0000269|PubMed:10747973,
            ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:17467953,
            ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:7760831,
            ECO:0000269|PubMed:7935471, ECO:0000269|PubMed:8946918,
            ECO:0000269|PubMed:9121459}.
            [PTM] Phosphorylated (PubMed:10359787, PubMed:11583998,
            PubMed:26159920, PubMed:9499401). Phosphorylated in unstressed
            cells; this phosphorylation is constitutive and implicated in the
            repression of HSF1 transcriptional activity (PubMed:16278218,
            PubMed:8940068, PubMed:8946918, PubMed:9121459). Phosphorylated on
            Ser-121 by MAPKAPK2; this phosphorylation promotes interaction with
            HSP90 proteins and inhibits HSF1 homotrimerization, DNA-binding and
            transactivation activities (PubMed:16278218). Phosphorylation on
            Ser-303 by GSK3B/GSK3-beta and on Ser-307 by MAPK3 within the
            regulatory domain is involved in the repression of HSF1
            transcriptional activity and occurs in a RAF1-dependent manner
            (PubMed:10747973, PubMed:12646186, PubMed:8940068, PubMed:8946918,
            PubMed:9121459, PubMed:9535852). Phosphorylation on Ser-303 and
            Ser-307 increases HSF1 nuclear export in a YWHAE- and
            XPO1/CRM1-dependent manner (PubMed:12917326). Phosphorylation on
            Ser-307 is a prerequisite for phosphorylation on Ser-303
            (PubMed:8940068). According to PubMed:9535852, Ser-303 is not
            phosphorylated in unstressed cells. Phosphorylated on Ser-419 by
            PLK1; phosphorylation promotes nuclear translocation upon heat
            shock (PubMed:15661742). Hyperphosphorylated upon heat shock and
            during the attenuation and recovery phase period of the heat shock
            response (PubMed:11447121, PubMed:12659875, PubMed:24581496).
            Phosphorylated on Thr-142; this phosphorylation increases HSF1
            transactivation activity upon heat shock (PubMed:12659875).
            Phosphorylation on Ser-230 by CAMK2A; this phosphorylation enhances
            HSF1 transactivation activity upon heat shock (PubMed:11447121).
            Phosphorylation on Ser-326 by MAPK12; this phosphorylation enhances
            HSF1 nuclear translocation, homotrimerization and transactivation
            activities upon heat shock (PubMed:15760475, PubMed:27354066).
            Phosphorylated on Ser-320 by PRKACA/PKA; this phosphorylation
            promotes nuclear localization and transcriptional activity upon
            heat shock (PubMed:21085490). Phosphorylated on Ser-363 by MAPK8;
            this phosphorylation occurs upon heat shock, induces HSF1
            translocation into nuclear stress bodies and negatively regulates
            transactivation activity (PubMed:10747973). Neither basal nor
            stress-inducible phosphorylation on Ser-230, Ser-292, Ser-303,
            Ser-307, Ser-314, Ser-319, Ser-320, Thr-323, Ser-326, Ser-338,
            Ser-344, Ser-363, Thr-367, Ser-368 and Thr-369 within the
            regulatory domain is involved in the regulation of HSF1 subcellular
            localization or DNA-binding activity; however, it negatively
            regulates HSF1 transactivation activity (PubMed:25963659).
            Phosphorylated on Ser-216 by PLK1 in the early mitotic period; this
            phosphorylation regulates HSF1 localization to the spindle pole,
            the recruitment of the SCF(BTRC) ubiquitin ligase complex inducing
            HSF1 degradation, and hence mitotic progression (PubMed:18794143).
            Dephosphorylated on Ser-121, Ser-307, Ser-314, Thr-323 and Thr-367
            by phosphatase PPP2CA in an IER5-dependent manner, leading to
            HSF1-mediated transactivation activity (PubMed:26754925).
            {ECO:0000269|PubMed:10359787, ECO:0000269|PubMed:10747973,
            ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11583998,
            ECO:0000269|PubMed:12646186, ECO:0000269|PubMed:12659875,
            ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:15760475,
            ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:18794143,
            ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:24581496,
            ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26159920,
            ECO:0000269|PubMed:26754925, ECO:0000269|PubMed:27354066,
            ECO:0000269|PubMed:8940068, ECO:0000269|PubMed:8946918,
            ECO:0000269|PubMed:9121459, ECO:0000269|PubMed:9499401,
            ECO:0000269|PubMed:9535852}.
            [PTM] Sumoylated with SUMO1 and SUMO2 upon heat shock in a
            ERK2-dependent manner (PubMed:12646186, PubMed:12665592).
            Sumoylated by SUMO1 on Lys-298; sumoylation occurs upon heat shock
            and promotes its localization to nuclear stress bodies and
            DNA-binding activity (PubMed:11514557). Phosphorylation on Ser-303
            and Ser-307 is probably a prerequisite for sumoylation
            (PubMed:12646186, PubMed:12665592). {ECO:0000269|PubMed:11514557,
            ECO:0000269|PubMed:12646186, ECO:0000269|PubMed:12665592}.
            [PTM] Acetylated on Lys-118; this acetylation is decreased in a
            IER5-dependent manner (PubMed:26754925). Acetylated on Lys-118,
            Lys-208 and Lys-298; these acetylations occur in a EP300-dependent
            manner (PubMed:24581496, PubMed:27189267). Acetylated on Lys-80;
            this acetylation inhibits DNA-binding activity upon heat shock
            (PubMed:19229036). Deacetylated on Lys-80 by SIRT1; this
            deacetylation increases DNA-binding activity (PubMed:19229036).
            {ECO:0000269|PubMed:19229036, ECO:0000269|PubMed:24581496,
            ECO:0000269|PubMed:26754925, ECO:0000269|PubMed:27189267}.
            [PTM] Ubiquitinated by SCF(BTRC) and degraded following
            stimulus-dependent phosphorylation at Ser-216 by PLK1 in mitosis
            (PubMed:18794143). Polyubiquitinated (PubMed:24581496). Undergoes
            proteasomal degradation upon heat shock and during the attenuation
            and recovery phase period of the heat shock response
            (PubMed:24581496). {ECO:0000269|PubMed:18794143,
            ECO:0000269|PubMed:24581496}.
            [SIMILARITY] Belongs to the HSF family. {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..529
                     /gene="HSF1"
                     /gene_synonym="HSTF1"
     Protein         1..529
                     /product="Heat shock factor protein 1"
                     /note="HSF 1; Heat shock transcription factor 1; HSTF 1"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..529
                     /region_name="Mature chain"
                     /note="Heat shock factor protein 1. /id=PRO_0000124567."
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330."
     Region          14..118
                     /region_name="HSF"
                     /note="heat shock factor; smart00415"
                     /db_xref="CDD:214654"
     Region          15..120
                     /region_name="Region of interest in the sequence"
                     /note="DNA-binding domain.
                     /evidence=ECO:0000269|PubMed:26727489,
                     ECO:0000269|PubMed:7935471."
     Region          17..27
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Site            22
                     /site_type="mutagenized"
                     /note="L->A: Inhibits HSE DNA-binding activity and
                     transcriptional activation.
                     /evidence=ECO:0000269|PubMed:9341107."
     Region          29..31
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Region          32..34
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Region          35..37
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Region          39..42
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5D5U."
     Region          44..47
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Region          49..55
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Region          57..60
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Region          66..75
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Region          79..83
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Site            80
                     /site_type="mutagenized"
                     /note="K->Q: Loss of nuclear stress bodies localization.
                     Loss of DNA-binding and transcriptional activities upon
                     heat shock. No change in homotrimerization upon heat
                     shock. /evidence=ECO:0000269|PubMed:19229036,
                     ECO:0000269|PubMed:24581496."
     Site            80
                     /site_type="mutagenized"
                     /note="K->R: Does not change interaction with XRCC5 and
                     XRCC6. Loss of nuclear stress bodies localization.
                     Decreased nuclear stress bodies localization. Loss of
                     DNA-binding and transcriptional activities upon heat
                     shock. /evidence=ECO:0000269|PubMed:19229036,
                     ECO:0000269|PubMed:24581496, ECO:0000269|PubMed:26359349."
     Site            80
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:19229036,
                     ECO:0000269|PubMed:24581496."
     Region          87..89
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:7DCJ."
     Bond            bond(91)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO2); alternate.
                     /evidence=ECO:0007744|PubMed:28112733."
     Site            91
                     /site_type="mutagenized"
                     /note="K->R: No effect on sumoylation.
                     /evidence=ECO:0000269|PubMed:12665592."
     Site            91
                     /site_type="acetylation"
                     /note="N6-acetyllysine; alternate.
                     /evidence=ECO:0000269|PubMed:24581496."
     Region          96..100
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Region          109..114
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:5HDN."
     Site            118
                     /site_type="mutagenized"
                     /note="K->Q: Loss of nuclear stress bodies localization.
                     No change in protein abundance.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            118
                     /site_type="mutagenized"
                     /note="K->R: No change in nuclear stress bodies
                     localization. /evidence=ECO:0000269|PubMed:24581496."
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24581496,
                     ECO:0000269|PubMed:26754925."
     Site            120
                     /site_type="mutagenized"
                     /note="T->A: No effect on binding HSE nor on
                     transcriptional activity.
                     /evidence=ECO:0000269|PubMed:16278218."
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by MAPKAPK2.
                     /evidence=ECO:0000269|PubMed:15760475,
                     ECO:0000269|PubMed:16278218."
     Site            121
                     /site_type="mutagenized"
                     /note="S->A: Increased binding HSE and transcriptional
                     activity. Greatly reduced binding to HSP90AA1. No effect
                     on MAPKAPK2 binding.
                     /evidence=ECO:0000269|PubMed:16278218."
     Site            121
                     /site_type="mutagenized"
                     /note="S->D: Some inhibition of binding HSE and
                     transcriptional activity. No change in binding HSP90AA1.
                     Inhibits MAPKAPK2 binding. Decreased HSF1-induced
                     expression of HSPA1A mRNA in a IER5-dependent manner; when
                     associated with D-307; D-314; D-323 and D-367.
                     /evidence=ECO:0000269|PubMed:16278218,
                     ECO:0000269|PubMed:26754925."
     Site            123
                     /site_type="mutagenized"
                     /note="S->A: No effect on binding HSE nor on
                     transcriptional activity.
                     /evidence=ECO:0000269|PubMed:16278218."
     Site            124
                     /site_type="mutagenized"
                     /note="T->A: No effect on binding HSE nor on
                     transcriptional activity.
                     /evidence=ECO:0000269|PubMed:16278218."
     Bond            bond(126)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO2). /evidence=ECO:0007744|PubMed:28112733."
     Site            126
                     /site_type="mutagenized"
                     /note="K->R: No effect on sumoylation.
                     /evidence=ECO:0000269|PubMed:12665592."
     Region          130..203
                     /region_name="Region of interest in the sequence"
                     /note="Hydrophobic repeat HR-A/B.
                     /evidence=ECO:0000269|PubMed:7935471."
     Bond            bond(131)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO2). /evidence=ECO:0007744|PubMed:28112733."
     Site            140
                     /site_type="mutagenized"
                     /note="L->K: Leads to constitutive homotrimerization and
                     DNA-binding activities at 20 degrees Celsius. Does not
                     lead to constitutive transactivation activity at 20
                     degrees Celsius. Decreased DNA-binding activity at 37
                     degrees Celsius. /evidence=ECO:0000269|PubMed:7623826,
                     ECO:0000269|PubMed:7935471."
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphothreonine; by CK2.
                     /evidence=ECO:0000269|PubMed:12659875."
     Site            142
                     /site_type="mutagenized"
                     /note="T->A: Reduced promoter activity by about 90%.
                     Almost no transcriptional activity when coexpressed with
                     CK2. /evidence=ECO:0000269|PubMed:12659875."
     Site            147
                     /site_type="mutagenized"
                     /note="M->A: Leads to constitutive homotrimerization and
                     DNA-binding activities at 20 degrees Celsius. Does not
                     lead to constitutive transactivation activity at 20
                     degrees Celsius. No effect on DNA-binding activity at 37
                     degrees Celsius. /evidence=ECO:0000269|PubMed:7623826,
                     ECO:0000269|PubMed:7935471."
     Site            147
                     /site_type="mutagenized"
                     /note="M->E: Does not lead to constitutive
                     homotrimerization and DNA-binding activities at 20 degrees
                     Celsius. Loss of DNA-binding activity at 37 degrees
                     Celsius. /evidence=ECO:0000269|PubMed:7935471."
     Site            147
                     /site_type="mutagenized"
                     /note="M->K: Does not lead to constitutive
                     homotrimerization and DNA-binding activities at 20 degrees
                     Celsius. Loss of DNA-binding activity at 37 degrees
                     Celsius. /evidence=ECO:0000269|PubMed:7935471."
     Site            150
                     /site_type="mutagenized"
                     /note="K->R: No effect on sumoylation.
                     /evidence=ECO:0000269|PubMed:12665592."
     Site            150
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            162
                     /site_type="mutagenized"
                     /note="K->R: No effect on sumoylation.
                     /evidence=ECO:0000269|PubMed:12665592."
     Site            188
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            189
                     /site_type="mutagenized"
                     /note="L->A: Does not lead to constitutive
                     homotrimerization and DNA-binding activities at 20 degrees
                     Celsius. Leads to constitutive homotrimerization and
                     DNA-binding activities at 30 degrees Celsius. No effect on
                     DNA-binding activity at 37 degrees Celsius.
                     /evidence=ECO:0000269|PubMed:7935471."
     Site            189
                     /site_type="mutagenized"
                     /note="L->E: Leads to constitutive homotrimerization,
                     DNA-binding and transactivation activities at 20 degrees
                     Celsius. Decreased DNA-binding activity at 37 degrees
                     Celsius. /evidence=ECO:0000269|PubMed:7623826,
                     ECO:0000269|PubMed:7935471."
     Site            189
                     /site_type="mutagenized"
                     /note="L->K: Leads to constitutive homotrimerization and
                     DNA-binding activities at 20 degrees Celsius. No effect on
                     DNA-binding activity at 37 degrees Celsius.
                     /evidence=ECO:0000269|PubMed:7935471."
     Site            193
                     /site_type="mutagenized"
                     /note="L->A: Does not lead to constitutive
                     homotrimerization and DNA-binding activities at 20 degrees
                     Celsius. Leads to constitutive homotrimerization and
                     DNA-binding activities at 30 degrees Celsius. No effect on
                     DNA-binding activity at 37 degrees Celsius.
                     /evidence=ECO:0000269|PubMed:7935471."
     Site            193
                     /site_type="mutagenized"
                     /note="L->E: Leads to constitutive homotrimerization and
                     DNA-binding activities at 20 degrees Celsius. Decreased
                     DNA-binding activity at 37 degrees Celsius.
                     /evidence=ECO:0000269|PubMed:7935471."
     Site            193
                     /site_type="mutagenized"
                     /note="L->K: Leads to constitutive homotrimerization and
                     DNA-binding activities at 20 degrees Celsius. Loss of
                     DNA-binding activity at 37 degrees Celsius.
                     /evidence=ECO:0000269|PubMed:7935471."
     Region          203..224
                     /region_name="Region of interest in the sequence"
                     /note="D domain. /evidence=ECO:0000269|PubMed:10747973."
     Bond            bond(208)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO2); alternate.
                     /evidence=ECO:0007744|PubMed:28112733."
     Site            208
                     /site_type="mutagenized"
                     /note="K->Q: No change in nuclear stress bodies
                     localization. Increased protein abundance.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            208
                     /site_type="mutagenized"
                     /note="K->R: No change in nuclear stress bodies
                     localization. No change in protein abundance.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine; alternate.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by PLK1.
                     /evidence=ECO:0000269|PubMed:18794143."
     Site            216
                     /site_type="mutagenized"
                     /note="S->A: Does not change interaction with XRCC5 and
                     XRCC6. No PLK1-induced phosphorylation in mitosis.
                     Inhibits PLK1-stimulated ubiquitinylation. Increased
                     protein stability. /evidence=ECO:0000269|PubMed:18794143,
                     ECO:0000269|PubMed:26359349."
     Site            216
                     /site_type="mutagenized"
                     /note="S->E: Does not change interaction with XRCC5 and
                     XRCC6. No change in spindle pole localization. Increases
                     weakly PLK1-stimulated ubiquitinylation. No change in
                     protein stability. Increased interaction with BTRC.
                     /evidence=ECO:0000269|PubMed:18794143,
                     ECO:0000269|PubMed:26359349."
     Site            216
                     /site_type="mutagenized"
                     /note="S->N: Decreased spindle pole localization.
                     Decreased interaction with BTRC. Increased protein
                     stability. /evidence=ECO:0000269|PubMed:18794143."
     Region          221..310
                     /region_name="Region of interest in the sequence"
                     /note="Regulatory domain.
                     /evidence=ECO:0000269|PubMed:7760831."
     Bond            bond(224)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO2). /evidence=ECO:0007744|PubMed:28112733."
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by CAMK2A.
                     /evidence=ECO:0000269|PubMed:11447121,
                     ECO:0000269|PubMed:15760475."
     Site            230
                     /site_type="mutagenized"
                     /note="S->A: No phosphorylation. No change in PLK1-induced
                     phosphorylation in mitosis. No change in DNA-binding
                     activity upon heat shock. Decreased transcriptional
                     activity upon heat shock.
                     /evidence=ECO:0000269|PubMed:11447121,
                     ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:18794143."
     Site            230
                     /site_type="mutagenized"
                     /note="S->D: Mimics phosphorylation. No effect on
                     transcriptional activity upon heat shock.
                     /evidence=ECO:0000269|PubMed:11447121,
                     ECO:0000269|PubMed:12665592."
     Region          252..529
                     /region_name="Vert_HS_TF"
                     /note="Vertebrate heat shock transcription factor;
                     pfam06546"
                     /db_xref="CDD:461944"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8940068."
     Site            275
                     /site_type="mutagenized"
                     /note="S->A: Reduced increase in heat-induced
                     transcriptional activity.
                     /evidence=ECO:0000269|PubMed:9535852."
     Site            275
                     /site_type="mutagenized"
                     /note="S->G: Leads to weak constitutive transactivation
                     activity at room temperature.
                     /evidence=ECO:0000269|PubMed:8940068."
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15760475."
     Site            292
                     /site_type="mutagenized"
                     /note="S->A: Weak decreased PLK1-induced phosphorylation.
                     Increased nuclear localization upon heat shock.
                     /evidence=ECO:0000269|PubMed:15661742."
     Region          295..324
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            296
                     /site_type="mutagenized"
                     /note="R->A: No effect neither on repression of
                     transcriptional activity at control temperature nor on
                     transcriptional activation upon heat shock.
                     /evidence=ECO:0000269|PubMed:8946918."
     Site            297
                     /site_type="mutagenized"
                     /note="V->A: Slight effect on derepression of
                     transcriptional activity at control temperature and on
                     transcriptional activation upon heat shock.
                     /evidence=ECO:0000269|PubMed:8946918."
     Bond            bond(298)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO); alternate.
                     /evidence=ECO:0000269|PubMed:11514557,
                     ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:16371476."
     Bond            bond(298)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO2); alternate.
                     /evidence=ECO:0007744|PubMed:28112733."
     Site            298
                     /site_type="mutagenized"
                     /note="K->A: Induces derepression of transcriptional
                     activity at control temperature.
                     /evidence=ECO:0000269|PubMed:12665592,
                     ECO:0000269|PubMed:8946918."
     Site            298
                     /site_type="mutagenized"
                     /note="K->Q: No change in nuclear stress bodies
                     localization. Increased protein abundance.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            298
                     /site_type="mutagenized"
                     /note="K->R: Abolishes sumoylation. No effect on
                     phosphorylation of S-303 nor of S-307. No change in
                     subcellular location to nuclear stress granules upon heat
                     shock. Loss of colocalization with SUMO1 to nuclear stress
                     granules upon heat shock. Does not change interaction with
                     XRCC5 and XRCC6. No effect on binding to HSE nor on
                     transactivation of HSP70. Increases transcriptional
                     activity in a DAXX-dependent manner. No change in protein
                     abundance. /evidence=ECO:0000269|PubMed:11514557,
                     ECO:0000269|PubMed:12646186, ECO:0000269|PubMed:12665592,
                     ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:24581496,
                     ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:8946918."
     Site            298
                     /site_type="acetylation"
                     /note="N6-acetyllysine; alternate.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            299
                     /site_type="mutagenized"
                     /note="E->A: No effect on repression of transcriptional
                     activity at control temperature.
                     /evidence=ECO:0000269|PubMed:8946918."
     Site            300
                     /site_type="mutagenized"
                     /note="E->A: Induces derepression of transcriptional
                     activity at control temperature.
                     /evidence=ECO:0000269|PubMed:8946918."
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:11447121,
                     ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:15760475,
                     ECO:0000269|PubMed:16371476, ECO:0000269|PubMed:8940068,
                     ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569."
     Site            303
                     /site_type="mutagenized"
                     /note="S->A: No phosphorylation nor sumoylation. No change
                     in nuclear stress granules subcellular location upon heat
                     shock. Loss of colocalization with SUMO1 to nuclear stress
                     granules upon heat shock. Slight decrease in
                     transcriptional activity on heat treatment. No change in
                     PLK1-induced phosphorylation in mitosis, induces
                     derepression of transcription activation at control
                     temperature, abolishes sumoylation and induces 2.5-fold
                     increase in transcriptional activity on heat treatment;
                     when associated with A-307.
                     /evidence=ECO:0000269|PubMed:12646186,
                     ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:18794143,
                     ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459,
                     ECO:0000269|PubMed:9535852."
     Site            303
                     /site_type="mutagenized"
                     /note="S->D: Mimics phosphorylation. No effect on in vitro
                     sumoylation. Greatly increased transcriptional activity on
                     heat induction. 5-fold derepression of transcriptional
                     activity at control temperature; when associated with
                     D-307. /evidence=ECO:0000269|PubMed:12665592,
                     ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459,
                     ECO:0000269|PubMed:9535852."
     Site            303
                     /site_type="mutagenized"
                     /note="S->G: Leads to constitutive transactivation
                     activity at room temperature. Inhibits interaction with
                     YWHAE and increases cytoplasmic localization; when
                     associated with G-307.
                     /evidence=ECO:0000269|PubMed:12917326,
                     ECO:0000269|PubMed:8940068."
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by MAPK3.
                     /evidence=ECO:0000269|PubMed:11447121,
                     ECO:0000269|PubMed:15760475, ECO:0000269|PubMed:8940068,
                     ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459,
                     ECO:0000269|PubMed:9535852, ECO:0007744|PubMed:23186163."
     Site            307
                     /site_type="mutagenized"
                     /note="S->A: No phosphorylation. Does not reduce Ser-303
                     phosphorylation. 1.5% increase in transcriptional activity
                     on heat-treatment. No change in PLK1-induced
                     phosphorylation in mitosis, induces derepression of
                     transcription activation at control temperature, abolishes
                     sumoylation and induces 2.5-fold increase in
                     transcriptional activity on heat treatment; when
                     associated with A-303.
                     /evidence=ECO:0000269|PubMed:12646186,
                     ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:18794143,
                     ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459,
                     ECO:0000269|PubMed:9535852."
     Site            307
                     /site_type="mutagenized"
                     /note="S->D: 5-fold derepression of transcriptional
                     activity at control temperature; when associated with
                     D-303. Decreased HSF1-induced expression of HSPA1A mRNA in
                     a IER5-dependent manner; when associated with D-121;
                     D-314; D-323 and D-367.
                     /evidence=ECO:0000269|PubMed:26754925,
                     ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459."
     Site            307
                     /site_type="mutagenized"
                     /note="S->G: Leads to constitutive transactivation
                     activity at room temperature. Inhibits interaction with
                     YWHAE and increases cytoplasmic localization; when
                     associated with G-303.
                     /evidence=ECO:0000269|PubMed:12917326,
                     ECO:0000269|PubMed:8940068."
     Site            309
                     /site_type="mutagenized"
                     /note="R->A: No effect on repression of transcriptional
                     activity at control temperature.
                     /evidence=ECO:0000269|PubMed:8946918."
     Site            311
                     /site_type="mutagenized"
                     /note="E->A: No effect neither on repression of
                     transcriptional activity at control temperature nor on
                     transcriptional activation upon heat shock.
                     /evidence=ECO:0000269|PubMed:8946918."
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15760475,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231."
     Site            314
                     /site_type="mutagenized"
                     /note="S->A: Weak decreased PLK1-induced phosphorylation.
                     /evidence=ECO:0000269|PubMed:15661742."
     Site            314
                     /site_type="mutagenized"
                     /note="S->D: Decreased HSF1-induced expression of HSPA1A
                     mRNA in a IER5-dependent manner; when associated with
                     D-121; D-307; D-323 and D-367.
                     /evidence=ECO:0000269|PubMed:26754925."
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15760475."
     Site            319
                     /site_type="mutagenized"
                     /note="S->A: Weak decreased PLK1-induced phosphorylation.
                     /evidence=ECO:0000269|PubMed:15661742."
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by PKA.
                     /evidence=ECO:0000269|PubMed:21085490,
                     ECO:0000269|PubMed:27189267."
     Site            320
                     /site_type="mutagenized"
                     /note="S->A: Decreased nuclear localization and
                     transcriptional activity upon heat shock.
                     /evidence=ECO:0000269|PubMed:21085490."
     Site            320
                     /site_type="mutagenized"
                     /note="S->D: Increased nuclear localization and
                     transcriptional activity upon heat shock.
                     /evidence=ECO:0000269|PubMed:21085490."
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332."
     Site            323
                     /site_type="mutagenized"
                     /note="T->D: Decreased HSF1-induced expression of HSPA1A
                     mRNA in a IER5-dependent manner; when associated with
                     D-121; D-307; D-314 and D-367.
                     /evidence=ECO:0000269|PubMed:26754925."
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by MAPK12.
                     /evidence=ECO:0000269|PubMed:15760475,
                     ECO:0000269|PubMed:27354066, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231."
     Site            326
                     /site_type="mutagenized"
                     /note="S->A: No phosphorylation. Increased nuclear
                     localization upon heat shock. No effect on
                     oligomerization, DNA-binding activities and nuclear
                     localization. Significant decrease in transcriptional
                     activity by heat shock. Decreases transcriptional activity
                     in a DAXX-dependent manner. Does not change interaction
                     with XRCC5 and XRCC6. Weak decreased PLK1-induced
                     phosphorylation. /evidence=ECO:0000269|PubMed:15016915,
                     ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:15760475,
                     ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27354066."
     Site            326
                     /site_type="mutagenized"
                     /note="S->E: Does not change interaction with XRCC5 and
                     XRCC6. /evidence=ECO:0000269|PubMed:26359349."
     Region          336..372
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15760475."
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by MAPK8.
                     /evidence=ECO:0000269|PubMed:10747973,
                     ECO:0000269|PubMed:15760475, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569."
     Site            363
                     /site_type="mutagenized"
                     /note="S->A: Decreases MAPK8-induced phosphorylation and
                     does not negatively regulates transactivating activity
                     upon heat shock. No effect on sumoylation.
                     /evidence=ECO:0000269|PubMed:10747973,
                     ECO:0000269|PubMed:12665592."
     Site            367
                     /site_type="mutagenized"
                     /note="T->D: Decreased HSF1-induced expression of HSPA1A
                     mRNA in a IER5-dependent manner; when associated with
                     D-121; D-307; D-314 and D-323.
                     /evidence=ECO:0000269|PubMed:26754925."
     Region          371..529
                     /region_name="Region of interest in the sequence"
                     /note="Transactivation domain.
                     /evidence=ECO:0000269|PubMed:7623826,
                     ECO:0000269|PubMed:7760831."
     Site            381
                     /site_type="mutagenized"
                     /note="K->R: No effect on sumoylation.
                     /evidence=ECO:0000269|PubMed:12665592."
     Region          384..409
                     /region_name="Region of interest in the sequence"
                     /note="Hydrophobic repeat HR-C.
                     /evidence=ECO:0000269|PubMed:7935471."
     Site            391
                     /site_type="mutagenized"
                     /note="M->A: Does not lead to constitutive DNA-binding
                     activity at 20 degrees Celsius. Leads to weak constitutive
                     DNA-binding and homotrimerization activities at 30 degrees
                     Celsius. Decreased DNA-binding activity at 37 degrees
                     Celsius. /evidence=ECO:0000269|PubMed:7935471."
     Site            391
                     /site_type="mutagenized"
                     /note="M->E: Leads to constitutive DNA-binding and
                     homotrimerization activities at 20 degrees Celsius. Does
                     not lead to constitutive transactivation activity at 20
                     degrees Celsius. No effect on DNA-binding activity at 37
                     degrees Celsius. /evidence=ECO:0000269|PubMed:7623826,
                     ECO:0000269|PubMed:7935471."
     Site            391
                     /site_type="mutagenized"
                     /note="M->K: Leads to constitutive DNA-binding and
                     homotrimerization activities at 20 degrees Celsius. No
                     effect on DNA-binding activity at 37 degrees Celsius.
                     /evidence=ECO:0000269|PubMed:7935471."
     Site            395
                     /site_type="mutagenized"
                     /note="L->E: Leads to constitutive DNA-binding and
                     homotrimerization activities at 20 degrees Celsius. No
                     effect on DNA-binding activity at 37 degrees Celsius.
                     /evidence=ECO:0000269|PubMed:7935471."
     Site            395
                     /site_type="mutagenized"
                     /note="L->K: Leads to constitutive DNA-binding and
                     homotrimerization activities at 20 degrees Celsius. No
                     effect on DNA-binding activity at 37 degrees Celsius.
                     /evidence=ECO:0000269|PubMed:7935471."
     Region          412..420
                     /region_name="Short sequence motif of biological interest"
                     /note="9aaTAD. /evidence=ECO:0000303|PubMed:17467953."
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by PLK1.
                     /evidence=ECO:0000269|PubMed:15661742."
     Site            419
                     /site_type="mutagenized"
                     /note="S->A: Does not change interaction with XRCC5 and
                     XRCC6. Decreased nuclear localization upon heat shock.
                     Strongly decreases PLK1-induced phosphorylation. No change
                     in PLK1-induced phosphorylation in mitosis.
                     /evidence=ECO:0000269|PubMed:15661742,
                     ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:26359349."
     Site            419
                     /site_type="mutagenized"
                     /note="S->E: Does not change interaction with XRCC5 and
                     XRCC6. /evidence=ECO:0000269|PubMed:26359349."
     Region          444..463
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15760475."
     Region          462..489
                     /region_name="Splicing variant"
                     /note="GKQLVHYTAQPLFLLDPGSVDTGSNDLP ->
                     AGALHSAAAVPAGPRLRGHREQRPAGAV (in isoform Short).
                     /evidence=ECO:0000305. /id=VSP_002414."
     Region          490..529
                     /region_name="Splicing variant"
                     /note="Missing (in isoform Short). /evidence=ECO:0000305.
                     /id=VSP_002415."
     Region          502..529
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            524
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24581496."
     Site            527
                     /site_type="mutagenized"
                     /note="T->A: No change in binding HSE nor on
                     transcriptional activity. Decreased binding HSE; when
                     associated with A-529.
                     /evidence=ECO:0000269|PubMed:16278218."
     Site            529
                     /site_type="mutagenized"
                     /note="S->A: No change in binding HSE nor on
                     transcriptional activity. Decreased binding HSE; when
                     associated with A-527.
                     /evidence=ECO:0000269|PubMed:16278218."
ORIGIN      
        1 mdlpvgpgaa gpsnvpaflt klwtlvsdpd tdalicwsps gnsfhvfdqg qfakevlpky
       61 fkhnnmasfv rqlnmygfrk vvhieqgglv kperddtefq hpcflrgqeq llenikrkvt
      121 svstlksedi kirqdsvtkl ltdvqlmkgk qecmdsklla mkhenealwr evaslrqkha
      181 qqqkvvnkli qflislvqsn rilgvkrkip lmlndsgsah smpkysrqfs lehvhgsgpy
      241 sapspaysss slyapdavas sgpiisdite lapaspmasp ggsiderpls ssplvrvkee
      301 ppsppqsprv eeaspgrpss vdtllsptal idsilresep apasvtaltd arghtdtegr
      361 ppsppptstp ekclsvacld knelsdhlda mdsnldnlqt mlsshgfsvd tsalldlfsp
      421 svtvpdmslp dldsslasiq ellspqeppr ppeaensspd sgkqlvhyta qplflldpgs
      481 vdtgsndlpv lfelgegsyf segdgfaedp tislltgsep pkakdptvs
//
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