Reviewed, UniProtKB/Swiss-Prot Q00613 (HSF1_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 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. Ref.12 Ref.18 Ref.15
Subcellular location	Cytoplasm. Nucleus. Note: Cytoplasmic during normal growth. On activation, translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules. Ref.6 Ref.14
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.6 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.18 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Sumoylated BY 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.14 Ref.19 Ref.11
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	Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	protein binding Ref.18 Inferred from physical interaction. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro transcription factor activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAPKAPK2	P49137	4	EBI-719620,EBI-993299

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
Amino acid modifications
	Modified residue	121	1	Phosphoserine; by MAPKAPK2 Ref.18
	Modified residue	142	1	Phosphothreonine; by CK2 Ref.13
	Modified residue	230	1	Phosphoserine Ref.6
	Modified residue	292	1	Phosphoserine
	Modified residue	303	1	Phosphoserine Ref.6 Ref.8 Ref.9 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22
	Modified residue	307	1	Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10 Ref.16 Ref.17 Ref.22
	Modified residue	314	1	Phosphoserine Ref.21
	Modified residue	323	1	Phosphothreonine Ref.17 Ref.21
	Modified residue	326	1	Phosphoserine Ref.21
	Modified residue	344	1	Phosphoserine
	Modified residue	363	1	Phosphoserine Ref.17 Ref.22
	Modified residue	369	1	Phosphothreonine 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.14 Ref.19 Ref.11
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.14
	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.14
	Mutagenesis	142	1	T → A: Reduced promoter activity by about 90%. Almost no transcriptional activity when coexpressed with CK2. Ref.13
	Mutagenesis	150	1	K → R: No effect on sumoylation. Ref.14
	Mutagenesis	162	1	K → R: No effect on sumoylation. Ref.14
	Mutagenesis	230	1	S → A: No phosphorylation. Impaired transcriptional activity. No change in inducible DNA-binding activity. Ref.6 Ref.14
	Mutagenesis	230	1	S → D: Mimics phosphorylation. No effect on transcriptional activity. Ref.6 Ref.14
	Mutagenesis	275	1	S → A: Reduced increase in heat-induced transcriptional activity. Ref.10
	Mutagenesis	296	1	R → A: No effect on repression of transcriptional activity at control temperature. Ref.8
	Mutagenesis	297	1	V → A: Slight effect on repression of transcriptional activity at control temperature. Ref.8
	Mutagenesis	298	1	K → A: Derepression of transcriptional activity at control temperature by 18.5%. Ref.8 Ref.14 Ref.11
	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.8 Ref.14 Ref.11
	Mutagenesis	299	1	E → A: No effect on repression of transcriptional activity at control temperature. Ref.8
	Mutagenesis	300	1	E → A: Derepression of transcriptional activity at control temperature by 11%. Ref.8
	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.8 Ref.9 Ref.10 Ref.14
	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.8 Ref.9 Ref.10 Ref.14
	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.8 Ref.9 Ref.10 Ref.14
	Mutagenesis	309	1	R → A: No effect on repression of transcriptional activity at control temperature. Ref.8
	Mutagenesis	311	1	E → A: No effect on repression of transcriptional activity at control temperature. Ref.8
	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.14
	Mutagenesis	381	1	K → R: No effect on sumoylation. Ref.14
	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

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. 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: 1871105] [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: 14702039] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). Tissue: Muscle.
[5]	"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: 1871106] [Abstract] Cited for: PROTEIN SEQUENCE OF 73-79; 81-93; 97-106; 163-170 AND 337-352.
[6]	"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: 11447121] [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.
[7]	"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: 7760831] [Abstract] Cited for: DOMAINS.
[8]	"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: 8946918] [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.
[9]	"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: 9121459] [Abstract] Cited for: PHOSPHORYLATION AT SER-303 AND SER-307, FUNCTION, MUTAGENESIS OF SER-303 AND SER-307.
[10]	"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: 9535852] [Abstract] Cited for: PHOSPHORYLATION AT SER-307, FUNCTION, MUTAGENESIS OF SER-275; SER-303 AND SER-307.
[11]	"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: 11514557] [Abstract] Cited for: SUMOYLATION AT LYS-298, MUTAGENESIS OF LYS-298.
[12]	"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: 11583998] [Abstract] Cited for: INTERACTION WITH FKBP4 AND HSP90AA1 IN THE HSP90 MULTICHAPERONE COMPLEX, SUBUNIT, PHOSPHPORYLATION, FUNCTION.
[13]	"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: 12659875] [Abstract] Cited for: PHOSPHORYLATION AT THR-142, FUNCTION, MUTAGENESIS OF THR-142.
[14]	"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: 12665592] [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.
[15]	"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: 14707147] [Abstract] Cited for: INTERACTION WITH SYMPK AND CSTF2.
[16]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-307, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-307; THR-323 AND SER-363, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16278218] [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: 16371476] [Abstract] Cited for: SUMOYLATION AT LYS-298, PHOSPHORYLATION AT SER-303.
[20]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, MASS SPECTROMETRY.
[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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; THR-323 AND SER-326, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-307; SER-363 AND THR-369, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M64673 mRNA. Translation: AAA52695.1. AK290975 mRNA. Translation: BAF83664.1. BT007351 mRNA. Translation: AAP36015.1. BC014638 mRNA. Translation: AAH14638.1.
IPI	IPI00024071. IPI00218507.
PIR	A41137.
RefSeq	NP_005517.1.
UniGene	Hs.530227 Hs.571397
3D structure databases
HSSP	HSSP built from PDB template 1HKT based on UniProtKB P22813.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q00613. 2 interactions.
PTM databases
PhosphoSite	Q00613.
Proteomic databases
PRIDE	Q00613.
Genome annotation databases
Ensembl	ENSG00000185122. Homo sapiens. [Contig view]
GeneID	3297.
KEGG	hsa:3297.
Organism-specific databases
GeneCards	GC08P145486. GC08P145487.
H-InvDB	HIX0007849.
HGNC	HGNC:5224. HSF1.
HPA	CAB004239. HPA008888.
MIM	140580. gene.
PharmGKB	PA29493.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q00613.
HOVERGEN	Q00613.
OMA	Q00613. ACLDKTE.
Gene expression databases
Bgee	Q00613.
CleanEx	HS_HSF1.
GermOnline	ENSG00000185122. Homo sapiens.
Family and domain databases
InterPro	IPR000232. HSF_DNA_bd. IPR010542. Vert_HS_TF. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF00447. HSF_DNA-bind. 1 hit. PF06546. Vert_HS_TF. 1 hit. [Graphical view]
PRINTS	PR00056. HSFDOMAIN.
ProDom	PD001788. HSF_DNA_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00415. HSF. 1 hit. [Graphical view]
PROSITE	PS00434. HSF_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	13075.
SOURCE	Search...

Entry information

Entry name

HSF1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	June 16, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)