Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heat shock factor protein 1

Gene

HSF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi15 – 120106By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_264071. HSF1 activation.
REACT_264075. Attenuation phase.
REACT_264164. HSF1-dependent transactivation.
REACT_264487. Regulation of HSF1-mediated heat shock response.
SignaLinkiQ00613.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock factor protein 1
Short name:
HSF 1
Alternative name(s):
Heat shock transcription factor 1
Short name:
HSTF 1
Gene namesi
Name:HSF1
Synonyms:HSTF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:5224. HSF1.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Cytoplasmic during normal growth. On activation, translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 911K → R: No effect on sumoylation. 1 Publication
Mutagenesisi120 – 1201T → A: No effect on binding HSE nor on transcriptional activity. 1 Publication
Mutagenesisi121 – 1211S → A: Increased binding HSE and transcriptional activity. Greatly reduced binding to HSP90AA1. No effect on MAPKAPK2 binding. 1 Publication
Mutagenesisi121 – 1211S → D: Some inhibition of binding HSE and transcriptional activity. No change in binding HSP90AA1. Inhibits MAPKAPK2 binding. 1 Publication
Mutagenesisi123 – 1231S → A: No effect on binding HSE nor on transcriptional activity. 1 Publication
Mutagenesisi124 – 1241T → A: No effect on binding HSE nor on transcriptional activity. 1 Publication
Mutagenesisi126 – 1261K → R: No effect on sumoylation. 1 Publication
Mutagenesisi142 – 1421T → A: Reduced promoter activity by about 90%. Almost no transcriptional activity when coexpressed with CK2. 1 Publication
Mutagenesisi150 – 1501K → R: No effect on sumoylation. 1 Publication
Mutagenesisi162 – 1621K → R: No effect on sumoylation. 1 Publication
Mutagenesisi230 – 2301S → A: No phosphorylation. Impaired transcriptional activity. No change in inducible DNA-binding activity. 2 Publications
Mutagenesisi230 – 2301S → D: Mimics phosphorylation. No effect on transcriptional activity. 2 Publications
Mutagenesisi275 – 2751S → A: Reduced increase in heat-induced transcriptional activity. 1 Publication
Mutagenesisi296 – 2961R → A: No effect on repression of transcriptional activity at control temperature. 1 Publication
Mutagenesisi297 – 2971V → A: Slight effect on repression of transcriptional activity at control temperature. 1 Publication
Mutagenesisi298 – 2981K → A: Derepression of transcriptional activity at control temperature by 18.5%. 3 Publications
Mutagenesisi298 – 2981K → 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. 3 Publications
Mutagenesisi299 – 2991E → A: No effect on repression of transcriptional activity at control temperature. 1 Publication
Mutagenesisi300 – 3001E → A: Derepression of transcriptional activity at control temperature by 11%. 1 Publication
Mutagenesisi303 – 3031S → 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. 4 Publications
Mutagenesisi303 – 3031S → 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. 4 Publications
Mutagenesisi307 – 3071S → 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. 4 Publications
Mutagenesisi309 – 3091R → A: No effect on repression of transcriptional activity at control temperature. 1 Publication
Mutagenesisi311 – 3111E → A: No effect on repression of transcriptional activity at control temperature. 1 Publication
Mutagenesisi326 – 3261S → A: No phosphorylation. Significant decrease in transcriptional activity by heat stress. 1 Publication
Mutagenesisi363 – 3631S → A: No effect on sumoylation. 1 Publication
Mutagenesisi381 – 3811K → R: No effect on sumoylation. 1 Publication
Mutagenesisi527 – 5271T → A: No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-529. 1 Publication
Mutagenesisi529 – 5291S → A: No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-527. 1 Publication

Organism-specific databases

PharmGKBiPA29493.

Polymorphism and mutation databases

BioMutaiHSF1.
DMDMi462333.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Heat shock factor protein 1PRO_0000124567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei121 – 1211Phosphoserine; by MAPKAPK22 Publications
Modified residuei142 – 1421Phosphothreonine; by CK21 Publication
Modified residuei230 – 2301Phosphoserine2 Publications
Modified residuei292 – 2921Phosphoserine1 Publication
Cross-linki298 – 298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei303 – 3031Phosphoserine7 Publications
Modified residuei307 – 3071Phosphoserine5 Publications
Modified residuei314 – 3141Phosphoserine4 Publications
Modified residuei323 – 3231Phosphothreonine2 Publications
Modified residuei326 – 3261Phosphoserine3 Publications
Modified residuei344 – 3441Phosphoserine1 Publication
Modified residuei363 – 3631Phosphoserine3 Publications
Modified residuei419 – 4191Phosphoserine1 Publication
Modified residuei444 – 4441Phosphoserine1 Publication

Post-translational modificationi

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.9 Publications
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.6 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ00613.
PaxDbiQ00613.
PRIDEiQ00613.

PTM databases

PhosphoSiteiQ00613.

Expressioni

Gene expression databases

BgeeiQ00613.
CleanExiHS_HSF1.
ExpressionAtlasiQ00613. baseline and differential.
GenevisibleiQ00613. HS.

Organism-specific databases

HPAiCAB004239.
HPA008888.

Interactioni

Subunit structurei

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).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPKAPK2P491375EBI-719620,EBI-993299
MINK1Q8N4C82EBI-719620,EBI-2133481
PRKCQQ047592EBI-719620,EBI-374762

Protein-protein interaction databases

BioGridi109530. 83 interactions.
DIPiDIP-35670N.
IntActiQ00613. 26 interactions.
MINTiMINT-230849.
STRINGi9606.ENSP00000431512.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2711Combined sources
Turni29 – 346Combined sources
Beta strandi35 – 373Combined sources
Beta strandi41 – 466Combined sources
Helixi49 – 6012Combined sources
Helixi66 – 7510Combined sources
Beta strandi79 – 824Combined sources
Beta strandi87 – 915Combined sources
Beta strandi97 – 1004Combined sources
Helixi109 – 1113Combined sources
Turni112 – 1143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDUNMR-A10-123[»]
ProteinModelPortaliQ00613.
SMRiQ00613. Positions 10-123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 20374Hydrophobic repeat HR-A/BAdd
BLAST
Regioni221 – 31090Regulatory domainAdd
BLAST
Regioni371 – 529159Transactivation domainAdd
BLAST
Regioni384 – 40926Hydrophobic repeat HR-CAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi412 – 42099aaTAD

Domaini

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.2 Publications

Sequence similaritiesi

Belongs to the HSF family.Curated

Phylogenomic databases

eggNOGiCOG5169.
GeneTreeiENSGT00390000001182.
HOGENOMiHOG000253917.
HOVERGENiHBG005999.
InParanoidiQ00613.
KOiK09414.
OMAiQFSLEHV.
PhylomeDBiQ00613.
TreeFamiTF330401.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR027072. HSF1.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR010542. Vert_HSTF_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 1 hit.
PTHR10015:SF142. PTHR10015:SF142. 1 hit.
PfamiPF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q00613-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDLPVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG
60 70 80 90 100
QFAKEVLPKY FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ
110 120 130 140 150
HPCFLRGQEQ LLENIKRKVT SVSTLKSEDI KIRQDSVTKL LTDVQLMKGK
160 170 180 190 200
QECMDSKLLA MKHENEALWR EVASLRQKHA QQQKVVNKLI QFLISLVQSN
210 220 230 240 250
RILGVKRKIP LMLNDSGSAH SMPKYSRQFS LEHVHGSGPY SAPSPAYSSS
260 270 280 290 300
SLYAPDAVAS SGPIISDITE LAPASPMASP GGSIDERPLS SSPLVRVKEE
310 320 330 340 350
PPSPPQSPRV EEASPGRPSS VDTLLSPTAL IDSILRESEP APASVTALTD
360 370 380 390 400
ARGHTDTEGR PPSPPPTSTP EKCLSVACLD KNELSDHLDA MDSNLDNLQT
410 420 430 440 450
MLSSHGFSVD TSALLDLFSP SVTVPDMSLP DLDSSLASIQ ELLSPQEPPR
460 470 480 490 500
PPEAENSSPD SGKQLVHYTA QPLFLLDPGS VDTGSNDLPV LFELGEGSYF
510 520
SEGDGFAEDP TISLLTGSEP PKAKDPTVS
Length:529
Mass (Da):57,260
Last modified:February 1, 1994 - v1
Checksum:i735074507C954365
GO
Isoform Short (identifier: Q00613-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:489
Mass (Da):52,881
Checksum:iFD6694B6D3927639
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei462 – 48928GKQLV…SNDLP → AGALHSAAAVPAGPRLRGHR EQRPAGAV in isoform Short. CuratedVSP_002414Add
BLAST
Alternative sequencei490 – 52940Missing in isoform Short. CuratedVSP_002415Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6419.1. [Q00613-1]
PIRiA41137.
RefSeqiNP_005517.1. NM_005526.2. [Q00613-1]
UniGeneiHs.530227.

Genome annotation databases

EnsembliENST00000528838; ENSP00000431512; ENSG00000185122.
GeneIDi3297.
KEGGihsa:3297.
UCSCiuc003zbt.4. human. [Q00613-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6419.1. [Q00613-1]
PIRiA41137.
RefSeqiNP_005517.1. NM_005526.2. [Q00613-1]
UniGeneiHs.530227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDUNMR-A10-123[»]
ProteinModelPortaliQ00613.
SMRiQ00613. Positions 10-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109530. 83 interactions.
DIPiDIP-35670N.
IntActiQ00613. 26 interactions.
MINTiMINT-230849.
STRINGi9606.ENSP00000431512.

Chemistry

BindingDBiQ00613.
ChEMBLiCHEMBL5869.

PTM databases

PhosphoSiteiQ00613.

Polymorphism and mutation databases

BioMutaiHSF1.
DMDMi462333.

Proteomic databases

MaxQBiQ00613.
PaxDbiQ00613.
PRIDEiQ00613.

Protocols and materials databases

DNASUi3297.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000528838; ENSP00000431512; ENSG00000185122.
GeneIDi3297.
KEGGihsa:3297.
UCSCiuc003zbt.4. human. [Q00613-1]

Organism-specific databases

CTDi3297.
GeneCardsiGC08P145515.
HGNCiHGNC:5224. HSF1.
HPAiCAB004239.
HPA008888.
MIMi140580. gene.
neXtProtiNX_Q00613.
PharmGKBiPA29493.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5169.
GeneTreeiENSGT00390000001182.
HOGENOMiHOG000253917.
HOVERGENiHBG005999.
InParanoidiQ00613.
KOiK09414.
OMAiQFSLEHV.
PhylomeDBiQ00613.
TreeFamiTF330401.

Enzyme and pathway databases

ReactomeiREACT_264071. HSF1 activation.
REACT_264075. Attenuation phase.
REACT_264164. HSF1-dependent transactivation.
REACT_264487. Regulation of HSF1-mediated heat shock response.
SignaLinkiQ00613.

Miscellaneous databases

ChiTaRSiHSF1. human.
GeneWikiiHSF1.
GenomeRNAii3297.
NextBioi13075.
PROiQ00613.
SOURCEiSearch...

Gene expression databases

BgeeiQ00613.
CleanExiHS_HSF1.
ExpressionAtlasiQ00613. baseline and differential.
GenevisibleiQ00613. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR027072. HSF1.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR010542. Vert_HSTF_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 1 hit.
PTHR10015:SF142. PTHR10015:SF142. 1 hit.
PfamiPF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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. 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. 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].
  29. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHSF1_HUMAN
AccessioniPrimary (citable) accession number: Q00613
Secondary accession number(s): A8K4L0, A8MW26, Q53XT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 22, 2015
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.