Q00613 (HSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heat shock factor protein 1
Short name=HSF 1

Alternative name(s):
Heat shock transcription factor 1
Short name=HSTF 1

Gene names

Name:	HSF1
Synonyms:	HSTF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.18
Subunit structure	Monomer. Under normal conditions, interacts with HSP90AA1 in the HSP90 multichaperone complex; the interaction prevents trimerization and activation of HSF1. On activation by heat-stress or by other factors such as metal ions, HSF1 is released from the complex, homotrimerizes, is hyperphosphorylated and translocated to the nucleus where, subsequently, it can activate transcription. Binds the complex through the regulatory domain. Interacts with SYMPK and CSTF2 in heat-stressed cells. Interacts with FKBP4 in the HSP90 multichaperone complex; the interaction is independent of the phosphorylation state of HSF1. Interacts with MAPKAPK2. Interacts with EEF1D at heat shock promoter elements (HSE). Ref.13 Ref.16 Ref.18 Ref.25
Subcellular location	Cytoplasm. Nucleus. Note: Cytoplasmic during normal growth. On activation, translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules. Ref.7 Ref.15
Domain	the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.8 Ref.20
Post-translational modification	Phosphorylated on multiple serine residues, a subset of which are involved in stress-related regulation of transcription activation. Constitutive phosphorylation represses transcriptional activity at normal temperatures. Levels increase on specific residues heat-shock and enhance HSF1 transactivation activity. Phosphorylation on Ser-307 derepresses activation on heat-stress and in combination with Ser-303 phosphorylation appears to be involved in recovery after heat-stress. Phosphorylated on Ser-230 by CAMK2, in vitro. Cadmium also enhances phosphorylation at this site. Phosphorylation on Ser-303 is a prerequisite for HSF1 sumoylation. Phosphorylation on Ser-121 inhibits transactivation and promotes HSP90 binding. Phosphorylation on Thr-142 also mediates transcriptional activity induced by heat. Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Sumoylated with SUMO1 and SUMO2 on heat-shock. Heat-inducible sumoylation occurs after 15 min of heat-shock, after which levels decrease and at 4 hours, levels return to control levels. Sumoylation has no effect on HSE binding nor on transcriptional activity. Phosphorylation on Ser-303 is a prerequisite for sumoylation. Ref.12 Ref.15 Ref.19
Sequence similarities	Belongs to the HSF family.

Ontologies

Keywords
Biological process	Stress response Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to heat Inferred from direct assay PubMed 17897941. Source: UniProtKB embryonic placenta development Inferred from electronic annotation. Source: Compara embryonic process involved in female pregnancy Inferred from electronic annotation. Source: Compara female meiosis Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of tumor necrosis factor production Inferred from electronic annotation. Source: Compara positive regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 10561509. Source: MGI protein phosphorylation Inferred from electronic annotation. Source: Compara regulation of spindle checkpoint Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA pronucleus Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding Inferred from direct assay PubMed 10561509. Source: MGI chromatin binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 10821850Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAPKAPK2	P49137	5	EBI-719620,EBI-993299
PRKCQ	Q04759	2	EBI-719620,EBI-374762

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q00613-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: Q00613-2)

The sequence of this isoform differs from the canonical sequence as follows:
     462-489: GKQLVHYTAQPLFLLDPGSVDTGSNDLP → AGALHSAAAVPAGPRLRGHREQRPAGAV
     490-529: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 529

529

Heat shock factor protein 1

PRO_0000124567

Regions

DNA binding

15 – 120

106

By similarity

Region

130 – 203

74

Hydrophobic repeat HR-A/B

Region

221 – 310

90

Regulatory domain

Region

371 – 529

159

Transactivation domain

Region

384 – 409

26

Hydrophobic repeat HR-C

Motif

412 – 420

9

9aaTAD

Amino acid modifications

Modified residue

121

1

Phosphoserine; by MAPKAPK2 Ref.18

Modified residue

142

1

Phosphothreonine; by CK2 Ref.14

Modified residue

230

1

Phosphoserine Ref.7

Modified residue

292

1

Phosphoserine

Modified residue

303

1

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.15 Ref.19

Modified residue

307

1

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11

Modified residue

314

1

Phosphoserine Ref.21 Ref.23 Ref.24

Modified residue

323

1

Phosphothreonine Ref.17 Ref.23

Modified residue

326

1

Phosphoserine Ref.23 Ref.24

Modified residue

344

1

Phosphoserine

Modified residue

363

1

Phosphoserine Ref.22

Modified residue

419

1

Phosphoserine

Modified residue

444

1

Phosphoserine

Cross-link

298

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.12 Ref.15 Ref.19

Natural variations

Alternative sequence

462 – 489

28

GKQLV…SNDLP → AGALHSAAAVPAGPRLRGHR EQRPAGAV in isoform Short.

VSP_002414

Alternative sequence

490 – 529

40

Missing in isoform Short.

VSP_002415

Experimental info

Mutagenesis

91

1

K → R: No effect on sumoylation. Ref.15

Mutagenesis

120

1

T → A: No effect on binding HSE nor on transcriptional activity. Ref.18

Mutagenesis

121

1

S → A: Increased binding HSE and transcriptional activity. Greatly reduced binding to HSP90AA1. No effect on MAPKAPK2 binding. Ref.18

Mutagenesis

121

1

S → D: Some inhibition of binding HSE and transcriptional activity. No change in binding HSP90AA1. Inhibits MAPKAPK2 binding. Ref.18

Mutagenesis

123

1

S → A: No effect on binding HSE nor on transcriptional activity. Ref.18

Mutagenesis

124

1

T → A: No effect on binding HSE nor on transcriptional activity. Ref.18

Mutagenesis

126

1

K → R: No effect on sumoylation. Ref.15

Mutagenesis

142

1

T → A: Reduced promoter activity by about 90%. Almost no transcriptional activity when coexpressed with CK2. Ref.14

Mutagenesis

150

1

K → R: No effect on sumoylation. Ref.15

Mutagenesis

162

1

K → R: No effect on sumoylation. Ref.15

Mutagenesis

230

1

S → A: No phosphorylation. Impaired transcriptional activity. No change in inducible DNA-binding activity. Ref.7 Ref.15

Mutagenesis

230

1

S → D: Mimics phosphorylation. No effect on transcriptional activity. Ref.7 Ref.15

Mutagenesis

275

1

S → A: Reduced increase in heat-induced transcriptional activity. Ref.11

Mutagenesis

296

1

R → A: No effect on repression of transcriptional activity at control temperature. Ref.9

Mutagenesis

297

1

V → A: Slight effect on repression of transcriptional activity at control temperature. Ref.9

Mutagenesis

298

1

K → A: Derepression of transcriptional activity at control temperature by 18.5%. Ref.9 Ref.12 Ref.15

Mutagenesis

298

1

K → R: Abolishes sumoylation. No effect on phosphorylation of S-303 nor of S-307. No effect on binding to HSE nor on transactivation of HSP70. Ref.9 Ref.12 Ref.15

Mutagenesis

299

1

E → A: No effect on repression of transcriptional activity at control temperature. Ref.9

Mutagenesis

300

1

E → A: Derepression of transcriptional activity at control temperature by 11%. Ref.9

Mutagenesis

303

1

S → A: No phosphorylation nor sumoylation. No change in subcellular location to nuclear stress granules. Slight decrease in transcriptional activity on heat treatment. 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-303. Ref.9 Ref.10 Ref.11 Ref.15

Mutagenesis

303

1

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 A-307. Ref.9 Ref.10 Ref.11 Ref.15

Mutagenesis

307

1

S → A: No phosphorylation. 5-fold derepression of transcriptional activity at control temperature; when associated with A-303. 1.5% increase in transcriptional activity on heat-treatment. 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-303. Ref.9 Ref.10 Ref.11 Ref.15

Mutagenesis

309

1

R → A: No effect on repression of transcriptional activity at control temperature. Ref.9

Mutagenesis

311

1

E → A: No effect on repression of transcriptional activity at control temperature. Ref.9

Mutagenesis

326

1

S → A: Significant increase in transcriptional activity. No effect on DNA binding nor on nuclear translocation.

Mutagenesis

363

1

S → A: No effect on sumoylation. Ref.15

Mutagenesis

381

1

K → R: No effect on sumoylation. Ref.15

Mutagenesis

527

1

T → A: No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-529. Ref.18

Mutagenesis

529

1

S → A: No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-527. Ref.18

Secondary structure

1

.

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529

Helix Strand Turn

Details...

Helix

17 – 27

11

Turn

29 – 34

6

Beta strand

35 – 37

3

Beta strand

41 – 46

6

Helix

49 – 60

12

Helix

66 – 75

10

Beta strand

79 – 82

4

Beta strand

87 – 91

5

Beta strand

97 – 100

4

Helix

109 – 111

3

Turn

112 – 114

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 735074507C954365	FASTA	529	57,260
	10 20 30 40 50 60 MDLPVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG QFAKEVLPKY 70 80 90 100 110 120 FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ HPCFLRGQEQ LLENIKRKVT 130 140 150 160 170 180 SVSTLKSEDI KIRQDSVTKL LTDVQLMKGK QECMDSKLLA MKHENEALWR EVASLRQKHA 190 200 210 220 230 240 QQQKVVNKLI QFLISLVQSN RILGVKRKIP LMLNDSGSAH SMPKYSRQFS LEHVHGSGPY 250 260 270 280 290 300 SAPSPAYSSS SLYAPDAVAS SGPIISDITE LAPASPMASP GGSIDERPLS SSPLVRVKEE 310 320 330 340 350 360 PPSPPQSPRV EEASPGRPSS VDTLLSPTAL IDSILRESEP APASVTALTD ARGHTDTEGR 370 380 390 400 410 420 PPSPPPTSTP EKCLSVACLD KNELSDHLDA MDSNLDNLQT MLSSHGFSVD TSALLDLFSP 430 440 450 460 470 480 SVTVPDMSLP DLDSSLASIQ ELLSPQEPPR PPEAENSSPD SGKQLVHYTA QPLFLLDPGS 490 500 510 520 VDTGSNDLPV LFELGEGSYF SEGDGFAEDP TISLLTGSEP PKAKDPTVS
	Isoform Short [UniParc]. Checksum: FD6694B6D3927639	FASTA	489	52,881
	10 20 30 40 50 60 MDLPVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG QFAKEVLPKY 70 80 90 100 110 120 FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ HPCFLRGQEQ LLENIKRKVT 130 140 150 160 170 180 SVSTLKSEDI KIRQDSVTKL LTDVQLMKGK QECMDSKLLA MKHENEALWR EVASLRQKHA 190 200 210 220 230 240 QQQKVVNKLI QFLISLVQSN RILGVKRKIP LMLNDSGSAH SMPKYSRQFS LEHVHGSGPY 250 260 270 280 290 300 SAPSPAYSSS SLYAPDAVAS SGPIISDITE LAPASPMASP GGSIDERPLS SSPLVRVKEE 310 320 330 340 350 360 PPSPPQSPRV EEASPGRPSS VDTLLSPTAL IDSILRESEP APASVTALTD ARGHTDTEGR 370 380 390 400 410 420 PPSPPPTSTP EKCLSVACLD KNELSDHLDA MDSNLDNLQT MLSSHGFSVD TSALLDLFSP 430 440 450 460 470 480 SVTVPDMSLP DLDSSLASIQ ELLSPQEPPR PPEAENSSPD SAGALHSAAA VPAGPRLRGH REQRPAGAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of a human heat shock factor, HSF1." Rabindran S.K., Giorgi G., Clos J., Wu C. Proc. Natl. Acad. Sci. U.S.A. 88:6906-6910(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[4]	"DNA sequence and analysis of human chromosome 8." 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., Gloeckner 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.J., 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., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). Tissue: Muscle.
[6]	"Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans." Schuetz T.J., Gallo G.J., Sheldon L., Tempst P., Kingston R.E. Proc. Natl. Acad. Sci. U.S.A. 88:6911-6915(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 73-79; 81-93; 97-106; 163-170 AND 337-352.
[7]	"Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1." Holmberg C.I., Hietakangas V., Mikhailov A., Rantanen J.O., Kallio M., Meinander A., Hellman J., Morrice N., MacKintosh C., Morimoto R.I., Eriksson J.E., Sistonen L. EMBO J. 20:3800-3810(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 228-241 AND 297-310, PHOSPHORYLATION AT SER-230; SER-303 AND SER-307, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-230.
[8]	"A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function." Green M., Schuetz T.J., Sullivan E.K., Kingston R.E. Mol. Cell. Biol. 15:3354-3362(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAINS.
[9]	"Repression of human heat shock factor 1 activity at control temperature by phosphorylation." Knauf U., Newton E.M., Kyriakis J., Kingston R.E. Genes Dev. 10:2782-2793(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-303 AND SER-307, FUNCTION, MUTAGENESIS OF ARG-296; VAL-297; LYS-298; GLU-299; GLU-300; SER-303; SER-307; ARG-309 AND GLU-311.
[10]	"Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation." Kline M.P., Morimoto R.I. Mol. Cell. Biol. 17:2107-2115(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-303 AND SER-307, FUNCTION, MUTAGENESIS OF SER-303 AND SER-307.
[11]	"Transcriptional activation of heat shock factor HSF1 probed by phosphopeptide analysis of factor 32P-labeled in vivo." Xia W., Guo Y., Vilaboa N., Zuo J., Voellmy R. J. Biol. Chem. 273:8749-8755(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-307, FUNCTION, MUTAGENESIS OF SER-275; SER-303 AND SER-307.
[12]	"Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification." Hong Y., Rogers R., Matunis M.J., Mayhew C.N., Goodson M.L., Park-Sarge O.K., Sarge K.D. J. Biol. Chem. 276:40263-40267(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-298, MUTAGENESIS OF LYS-298.
[13]	"Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex." Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O., Smith D.F., Voellmy R. J. Biol. Chem. 276:45791-45799(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FKBP4 AND HSP90AA1 IN THE HSP90 MULTICHAPERONE COMPLEX, SUBUNIT, PHOSPHORYLATION, FUNCTION.
[14]	"Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2." Soncin F., Zhang X., Chu B., Wang X., Asea A., Ann Stevenson M., Sacks D.B., Calderwood S.K. Biochem. Biophys. Res. Commun. 303:700-706(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-142, FUNCTION, MUTAGENESIS OF THR-142.
[15]	"Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1." Hietakangas V., Ahlskog J.K., Jakobsson A.M., Hellesuo M., Sahlberg N.M., Holmberg C.I., Mikhailov A., Palvimo J.J., Pirkkala L., Sistonen L. Mol. Cell. Biol. 23:2953-2968(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-298, PHOSPHORYLATION AT SER-303, FUNCTION, 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.
[16]	"HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin." Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D. J. Biol. Chem. 279:10551-10555(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYMPK AND CSTF2.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-323, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding." Wang X., Khaleque M.A., Zhao M.J., Zhong R., Gaestel M., Calderwood S.K. J. Biol. Chem. 281:782-791(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-121, FUNCTION, INTERACTION WITH HSP90AA1 AND MAPKAPK2, MUTAGENESIS OF THR-120; SER-121; SER-123; THR-124; THR-527 AND SER-529, MASS SPECTROMETRY.
[19]	"PDSM, a motif for phosphorylation-dependent SUMO modification." Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J., Nakai A., Sistonen L. Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-298, PHOSPHORYLATION AT SER-303.
[20]	"Nine-amino-acid transactivation domain: establishment and prediction utilities." Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M. Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
[21]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; THR-323 AND SER-326, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[24]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-326, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Transformation of eEF1Bdelta into heat-shock response transcription factor by alternative splicing." Kaitsuka T., Tomizawa K., Matsushita M. EMBO Rep. 12:673-681(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EEF1D.
[26]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M64673 mRNA. Translation: AAA52695.1.
AK290975 mRNA. Translation: BAF83664.1.
BT007351 mRNA. Translation: AAP36015.1.
AC110280 Genomic DNA. No translation available.
AF205589 Genomic DNA. No translation available.
BC014638 mRNA. Translation: AAH14638.1.

IPI

IPI00024071.
IPI00218507.

PIR

A41137.

RefSeq

NP_005517.1. NM_005526.2.

UniGene

Hs.530227.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LDU	NMR	-	A	10-123	[»]

ProteinModelPortal

Q00613.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35670N.

IntAct

Q00613. 8 interactions.

MINT

MINT-230849.

STRING

9606.ENSP00000332698.

PTM databases

PhosphoSite

Q00613.

Polymorphism databases

DMDM

462333.

Proteomic databases

PaxDb

Q00613.

PRIDE

Q00613.

Protocols and materials databases

DNASU

3297.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000528838; ENSP00000431512; ENSG00000185122.
ENST00000570268; ENSP00000455432; ENSG00000261132.

GeneID

3297.

KEGG

hsa:3297.

UCSC

uc003zbt.4. human.

Organism-specific databases

CTD

3297.

GeneCards

GC08P145515.

HGNC

HGNC:5224. HSF1.

HPA

CAB004239.
HPA008888.

MIM

140580. gene.

neXtProt

NX_Q00613.

PharmGKB

PA29493.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5169.

HOGENOM

HOG000253917.

HOVERGEN

HBG005999.

InParanoid

Q00613.

KO

K09414.

OMA

SPLVRVK.

OrthoDB

EOG4VMFFN.

PhylomeDB

Q00613.

Enzyme and pathway databases

SignaLink

Q00613.

Gene expression databases

ArrayExpress

Q00613.

Bgee

Q00613.

CleanEx

HS_HSF1.

Genevestigator

Q00613.

GermOnline

ENSG00000185122. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR027072. HSF1.
IPR000232. HSF_DNA-bd.
IPR010542. Vert_HS_TF.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

PANTHER

PTHR10015:SF42. PTHR10015:SF42. 1 hit.

Pfam

PF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 1 hit.
[Graphical view]

PRINTS

PR00056. HSFDOMAIN.

SMART

SM00415. HSF. 1 hit.
[Graphical view]

PROSITE

PS00434. HSF_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q00613.

ChEMBL

CHEMBL5869.

ChiTaRS

HSF1. human.

GenomeRNAi

3297.

NextBio

13075.

SOURCE

Search...

Entry information

Entry name

HSF1_HUMAN

Accession

Primary (citable) accession number: Q00613
Secondary accession number(s): A8K4L0, A8MW26, Q53XT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 29, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.