Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q00613 (HSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Protein existenceEvidence 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.19

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.19 Ref.27

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.21

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. Phosphorylation on Ser-326 plays an important role in heat activation of HSF1 transcriptional activity. Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20

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.20

Sequence similarities

Belongs to the HSF family.

Ontologies

Keywords
   Biological processStress response
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to heat

Inferred from direct assay PubMed 17897941. Source: UniProtKB

defense response

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

embryonic process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

female meiotic division

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10561509. Source: MGI

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of spindle checkpoint

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

pronucleus

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA 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: Ensembl

protein binding

Inferred from physical interaction PubMed 11005381PubMed 17897941. Source: UniProtKB

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

MAPKAPK2P491375EBI-719620,EBI-993299
PRKCQQ047592EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Heat shock factor protein 1
PRO_0000124567

Regions

DNA binding15 – 120106 By similarity
Region130 – 20374Hydrophobic repeat HR-A/B
Region221 – 31090Regulatory domain
Region371 – 529159Transactivation domain
Region384 – 40926Hydrophobic repeat HR-C
Motif412 – 42099aaTAD

Amino acid modifications

Modified residue11N-acetylmethionine Ref.24
Modified residue1211Phosphoserine; by MAPKAPK2 Ref.17 Ref.19
Modified residue1421Phosphothreonine; by CK2 Ref.14
Modified residue2301Phosphoserine Ref.7 Ref.17
Modified residue2921Phosphoserine Ref.17
Modified residue3031Phosphoserine Ref.7 Ref.9 Ref.10 Ref.15 Ref.17 Ref.20
Modified residue3071Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.17
Modified residue3141Phosphoserine Ref.17 Ref.22 Ref.25 Ref.26
Modified residue3231Phosphothreonine Ref.18 Ref.25
Modified residue3261Phosphoserine Ref.17 Ref.25 Ref.26
Modified residue3441Phosphoserine Ref.17
Modified residue3631Phosphoserine Ref.17 Ref.23
Modified residue4191Phosphoserine Ref.17
Modified residue4441Phosphoserine Ref.17
Cross-link298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.12 Ref.15 Ref.20

Natural variations

Alternative sequence462 – 48928GKQLV…SNDLP → AGALHSAAAVPAGPRLRGHR EQRPAGAV in isoform Short.
VSP_002414
Alternative sequence490 – 52940Missing in isoform Short.
VSP_002415

Experimental info

Mutagenesis911K → R: No effect on sumoylation. Ref.15
Mutagenesis1201T → A: No effect on binding HSE nor on transcriptional activity. Ref.19
Mutagenesis1211S → A: Increased binding HSE and transcriptional activity. Greatly reduced binding to HSP90AA1. No effect on MAPKAPK2 binding. Ref.19
Mutagenesis1211S → D: Some inhibition of binding HSE and transcriptional activity. No change in binding HSP90AA1. Inhibits MAPKAPK2 binding. Ref.19
Mutagenesis1231S → A: No effect on binding HSE nor on transcriptional activity. Ref.19
Mutagenesis1241T → A: No effect on binding HSE nor on transcriptional activity. Ref.19
Mutagenesis1261K → R: No effect on sumoylation. Ref.15
Mutagenesis1421T → A: Reduced promoter activity by about 90%. Almost no transcriptional activity when coexpressed with CK2. Ref.14
Mutagenesis1501K → R: No effect on sumoylation. Ref.15
Mutagenesis1621K → R: No effect on sumoylation. Ref.15
Mutagenesis2301S → A: No phosphorylation. Impaired transcriptional activity. No change in inducible DNA-binding activity. Ref.7 Ref.15
Mutagenesis2301S → D: Mimics phosphorylation. No effect on transcriptional activity. Ref.7 Ref.15
Mutagenesis2751S → A: Reduced increase in heat-induced transcriptional activity. Ref.11
Mutagenesis2961R → A: No effect on repression of transcriptional activity at control temperature. Ref.9
Mutagenesis2971V → A: Slight effect on repression of transcriptional activity at control temperature. Ref.9
Mutagenesis2981K → A: Derepression of transcriptional activity at control temperature by 18.5%. Ref.9 Ref.12 Ref.15
Mutagenesis2981K → 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
Mutagenesis2991E → A: No effect on repression of transcriptional activity at control temperature. Ref.9
Mutagenesis3001E → A: Derepression of transcriptional activity at control temperature by 11%. Ref.9
Mutagenesis3031S → 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
Mutagenesis3031S → 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
Mutagenesis3071S → 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
Mutagenesis3091R → A: No effect on repression of transcriptional activity at control temperature. Ref.9
Mutagenesis3111E → A: No effect on repression of transcriptional activity at control temperature. Ref.9
Mutagenesis3261S → A: No phosphorylation. Significant decrease in transcriptional activity by heat stress. Ref.17
Mutagenesis3631S → A: No effect on sumoylation. Ref.15
Mutagenesis3811K → R: No effect on sumoylation. Ref.15
Mutagenesis5271T → A: No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-529. Ref.19
Mutagenesis5291S → A: No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-527. Ref.19

Secondary structure

..................... 529
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 735074507C954365

FASTA52957,260
        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 

« Hide

Isoform Short [UniParc].

Checksum: FD6694B6D3927639
Show »

FASTA48952,881

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress."
Guettouche T., Boellmann F., Lane W.S., Voellmy R.
BMC Biochem. 6:4-4(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-121; SER-230; SER-292; SER-303; SER-307; SER-314; SER-326; SER-344; SER-363; SER-419 AND SER-444, MUTAGENESIS OF SER-326, IDENTIFICATION BY MASS SPECTROMETRY.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[20]"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.
[21]"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.
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"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.
[28]"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.
CCDSCCDS6419.1. [Q00613-1]
PIRA41137.
RefSeqNP_005517.1. NM_005526.2. [Q00613-1]
UniGeneHs.530227.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDUNMR-A10-123[»]
ProteinModelPortalQ00613.
SMRQ00613. Positions 10-123.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109530. 79 interactions.
DIPDIP-35670N.
IntActQ00613. 12 interactions.
MINTMINT-230849.
STRING9606.ENSP00000332698.

Chemistry

BindingDBQ00613.
ChEMBLCHEMBL5869.

PTM databases

PhosphoSiteQ00613.

Polymorphism databases

DMDM462333.

Proteomic databases

MaxQBQ00613.
PaxDbQ00613.
PRIDEQ00613.

Protocols and materials databases

DNASU3297.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000528838; ENSP00000431512; ENSG00000185122. [Q00613-1]
ENST00000570268; ENSP00000455432; ENSG00000261132. [Q00613-1]
GeneID3297.
KEGGhsa:3297.
UCSCuc003zbt.4. human. [Q00613-1]

Organism-specific databases

CTD3297.
GeneCardsGC08P145515.
HGNCHGNC:5224. HSF1.
HPACAB004239.
HPA008888.
MIM140580. gene.
neXtProtNX_Q00613.
PharmGKBPA29493.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5169.
HOGENOMHOG000253917.
HOVERGENHBG005999.
InParanoidQ00613.
KOK09414.
OMALFLVDPG.
PhylomeDBQ00613.
TreeFamTF330401.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkQ00613.

Gene expression databases

ArrayExpressQ00613.
BgeeQ00613.
CleanExHS_HSF1.
GenevestigatorQ00613.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR027072. HSF1.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR010542. Vert_HSTF_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR10015. PTHR10015. 1 hit.
PTHR10015:SF142. PTHR10015:SF142. 1 hit.
PfamPF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 1 hit.
[Graphical view]
PRINTSPR00056. HSFDOMAIN.
SMARTSM00415. HSF. 1 hit.
[Graphical view]
PROSITEPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSF1. human.
GeneWikiHSF1.
GenomeRNAi3297.
NextBio13075.
PROQ00613.
SOURCESearch...

Entry information

Entry nameHSF1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM