Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q00613

- HSF1_HUMAN

UniProt

Q00613 - HSF1_HUMAN

Protein

Heat shock factor protein 1

Gene

HSF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. chromatin binding Source: Ensembl
    2. protein binding Source: UniProtKB
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
    5. RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding Source: MGI
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. cellular response to heat Source: UniProtKB
    2. defense response Source: Ensembl
    3. embryonic placenta development Source: Ensembl
    4. embryonic process involved in female pregnancy Source: Ensembl
    5. female meiotic division Source: Ensembl
    6. negative regulation of cell proliferation Source: Ensembl
    7. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    8. negative regulation of tumor necrosis factor production Source: Ensembl
    9. positive regulation of multicellular organism growth Source: Ensembl
    10. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    11. protein phosphorylation Source: Ensembl
    12. regulation of spindle checkpoint Source: Ensembl
    13. response to lipopolysaccharide Source: Ensembl
    14. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_200624. Attenuation phase.
    REACT_200744. HSF1 activation.
    REACT_200775. HSF1-dependent transactivation.
    REACT_200780. 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: 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

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA
    3. pronucleus Source: Ensembl
    4. protein complex Source: Ensembl

    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.

    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 MAPKAPK23 Publications
    Modified residuei142 – 1421Phosphothreonine; by CK22 Publications
    Modified residuei230 – 2301Phosphoserine3 Publications
    Modified residuei292 – 2921Phosphoserine2 Publications
    Cross-linki298 – 298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei303 – 3031Phosphoserine7 Publications
    Modified residuei307 – 3071Phosphoserine6 Publications
    Modified residuei314 – 3141Phosphoserine5 Publications
    Modified residuei323 – 3231Phosphothreonine3 Publications
    Modified residuei326 – 3261Phosphoserine4 Publications
    Modified residuei344 – 3441Phosphoserine2 Publications
    Modified residuei363 – 3631Phosphoserine3 Publications
    Modified residuei419 – 4191Phosphoserine2 Publications
    Modified residuei444 – 4441Phosphoserine2 Publications

    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.11 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

    ArrayExpressiQ00613.
    BgeeiQ00613.
    CleanExiHS_HSF1.
    GenevestigatoriQ00613.

    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
    PRKCQQ047592EBI-719620,EBI-374762

    Protein-protein interaction databases

    BioGridi109530. 79 interactions.
    DIPiDIP-35670N.
    IntActiQ00613. 22 interactions.
    MINTiMINT-230849.
    STRINGi9606.ENSP00000332698.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000253917.
    HOVERGENiHBG005999.
    InParanoidiQ00613.
    KOiK09414.
    OMAiLFLVDPG.
    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. Align

    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

    MDLPVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG    50
    QFAKEVLPKY FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ 100
    HPCFLRGQEQ LLENIKRKVT SVSTLKSEDI KIRQDSVTKL LTDVQLMKGK 150
    QECMDSKLLA MKHENEALWR EVASLRQKHA QQQKVVNKLI QFLISLVQSN 200
    RILGVKRKIP LMLNDSGSAH SMPKYSRQFS LEHVHGSGPY SAPSPAYSSS 250
    SLYAPDAVAS SGPIISDITE LAPASPMASP GGSIDERPLS SSPLVRVKEE 300
    PPSPPQSPRV EEASPGRPSS VDTLLSPTAL IDSILRESEP APASVTALTD 350
    ARGHTDTEGR PPSPPPTSTP EKCLSVACLD KNELSDHLDA MDSNLDNLQT 400
    MLSSHGFSVD TSALLDLFSP SVTVPDMSLP DLDSSLASIQ ELLSPQEPPR 450
    PPEAENSSPD SGKQLVHYTA QPLFLLDPGS VDTGSNDLPV LFELGEGSYF 500
    SEGDGFAEDP TISLLTGSEP PKAKDPTVS 529
    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:
    EMBL
    GenBank
    DDBJ
    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. [Q00613-1]
    GeneIDi3297.
    KEGGihsa:3297.
    UCSCiuc003zbt.4. human. [Q00613-1]

    Polymorphism databases

    DMDMi462333.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6419.1. [Q00613-1 ]
    PIRi A41137.
    RefSeqi NP_005517.1. NM_005526.2. [Q00613-1 ]
    UniGenei Hs.530227.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LDU NMR - A 10-123 [» ]
    ProteinModelPortali Q00613.
    SMRi Q00613. Positions 10-123.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109530. 79 interactions.
    DIPi DIP-35670N.
    IntActi Q00613. 22 interactions.
    MINTi MINT-230849.
    STRINGi 9606.ENSP00000332698.

    Chemistry

    BindingDBi Q00613.
    ChEMBLi CHEMBL5869.

    PTM databases

    PhosphoSitei Q00613.

    Polymorphism databases

    DMDMi 462333.

    Proteomic databases

    MaxQBi Q00613.
    PaxDbi Q00613.
    PRIDEi Q00613.

    Protocols and materials databases

    DNASUi 3297.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000528838 ; ENSP00000431512 ; ENSG00000185122 . [Q00613-1 ]
    GeneIDi 3297.
    KEGGi hsa:3297.
    UCSCi uc003zbt.4. human. [Q00613-1 ]

    Organism-specific databases

    CTDi 3297.
    GeneCardsi GC08P145515.
    HGNCi HGNC:5224. HSF1.
    HPAi CAB004239.
    HPA008888.
    MIMi 140580. gene.
    neXtProti NX_Q00613.
    PharmGKBi PA29493.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5169.
    HOGENOMi HOG000253917.
    HOVERGENi HBG005999.
    InParanoidi Q00613.
    KOi K09414.
    OMAi LFLVDPG.
    PhylomeDBi Q00613.
    TreeFami TF330401.

    Enzyme and pathway databases

    Reactomei REACT_200624. Attenuation phase.
    REACT_200744. HSF1 activation.
    REACT_200775. HSF1-dependent transactivation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    SignaLinki Q00613.

    Miscellaneous databases

    ChiTaRSi HSF1. human.
    GeneWikii HSF1.
    GenomeRNAii 3297.
    NextBioi 13075.
    PROi Q00613.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00613.
    Bgeei Q00613.
    CleanExi HS_HSF1.
    Genevestigatori Q00613.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR027072. HSF1.
    IPR000232. HSF_DNA-bd.
    IPR027725. HSF_fam.
    IPR010542. Vert_HSTF_C.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10015. PTHR10015. 1 hit.
    PTHR10015:SF142. PTHR10015:SF142. 1 hit.
    Pfami PF00447. HSF_DNA-bind. 1 hit.
    PF06546. Vert_HS_TF. 1 hit.
    [Graphical view ]
    PRINTSi PR00056. HSFDOMAIN.
    SMARTi SM00415. HSF. 1 hit.
    [Graphical view ]
    PROSITEi PS00434. HSF_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 142 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