Heat shock factor protein 1

Details

Name
Heat shock factor protein 1
Kind
protein
Synonyms
  • Heat shock transcription factor 1
  • HSF 1
  • HSTF 1
  • HSTF1
Gene Name
HSF1
UniProtKB Entry
Q00613Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0006786|Heat shock factor protein 1
MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKY
FKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVT
SVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHA
QQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPY
SAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEE
PPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGR
PPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLSSHGFSVDTSALLDLFSP
SVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGS
VDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS
Number of residues
529
Molecular Weight
57259.87
Theoretical pI
4.81
GO Classification
Functions
chromatin DNA binding / DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / DNA-binding transcription factor activity / DNA-binding transcription factor activity, RNA polymerase II-specific / DNA-binding transcription repressor activity, RNA polymerase II-specific / general transcription initiation factor binding / heat shock protein binding / Hsp90 protein binding / identical protein binding / promoter-specific chromatin binding / protein heterodimerization activity / protein kinase binding / RNA polymerase II cis-regulatory region sequence-specific DNA binding / sequence-specific DNA binding / sequence-specific double-stranded DNA binding / sequence-specific single stranded DNA binding / STAT family protein binding / transcription cis-regulatory region binding / translation elongation factor binding
Processes
cellular response to angiotensin / cellular response to cadmium ion / cellular response to copper ion / cellular response to diamide / cellular response to estradiol stimulus / cellular response to gamma radiation / cellular response to hydrogen peroxide / cellular response to L-glutamine / cellular response to lipopolysaccharide / cellular response to nitroglycerin / cellular response to potassium ion / cellular response to sodium arsenite / cellular response to unfolded protein / cellular response to xenobiotic stimulus / DNA repair / MAPK cascade / mRNA processing / mRNA transport / negative regulation of cardiac muscle cell apoptotic process / negative regulation of double-strand break repair via nonhomologous end joining / negative regulation of gene expression / negative regulation of inclusion body assembly / negative regulation of protein-containing complex assembly / negative regulation of transcription by RNA polymerase II / positive regulation of apoptotic DNA fragmentation / positive regulation of cold-induced thermogenesis / positive regulation of DNA-binding transcription factor activity / positive regulation of gene expression / positive regulation of inclusion body assembly / positive regulation of macrophage differentiation / positive regulation of mitotic cell cycle / positive regulation of stress granule assembly / positive regulation of transcription by RNA polymerase II / positive regulation of tyrosine phosphorylation of STAT protein / protein-containing complex assembly / regulation of transcription by RNA polymerase II / response to activity / response to hypobaric hypoxia / response to nutrient / response to peptide / response to psychosocial stress / response to testosterone
Components
centrosome / chromatin / euchromatin / heterochromatin / kinetochore / mitotic spindle pole / nuclear stress granule / nucleus / perinuclear region of cytoplasm / PML body / protein folding chaperone complex / ribonucleoprotein complex
General Function
Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:11447121, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:11583998, PubMed:16278218, PubMed:9727490). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:9499401, PubMed:9727490). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925)
Specific Function
chromatin DNA binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0012449|Heat shock factor protein 1 (HSF1)
ATGGATCTGCCCGTGGGCCCCGGCGCGGCGGGGCCCAGCAACGTCCCGGCCTTCCTGACC
AAGCTGTGGACCCTCGTGAGCGACCCGGACACCGACGCGCTCATCTGCTGGAGCCCGAGC
GGGAACAGCTTCCACGTGTTCGACCAGGGCCAGTTTGCCAAGGAGGTGCTGCCCAAGTAC
TTCAAGCACAACAACATGGCCAGCTTCGTGCGGCAGCTCAACATGTATGGCTTCCGGAAA
GTGGTCCACATCGAGCAGGGCGGCCTGGTCAAGCCAGAGAGAGACGACACGGAGTTCCAG
CACCCATGCTTCCTGCGTGGCCAGGAGCAGCTCCTTGAGAACATCAAGAGGAAAGTGACC
AGTGTGTCCACCCTGAAGAGTGAAGACATAAAGATCCGCCAGGACAGCGTCACCAAGCTG
CTGACGGACGTGCAGCTGATGAAGGGGAAGCAGGAGTGCATGGACTCCAAGCTCCTGGCC
ATGAAGCATGAGAATGAGGCTCTGTGGCGGGAGGTGGCCAGCCTTCGGCAGAAGCATGCC
CAGCAACAGAAAGTCGTCAACAAGCTCATTCAGTTCCTGATCTCACTGGTGCAGTCAAAC
CGGATCCTGGGGGTGAAGAGAAAGATCCCCCTGATGCTGAACGACAGTGGCTCAGCACAT
TCCATGCCCAAGTATAGCCGGCAGTTCTCCCTGGAGCACGTCCACGGCTCGGGCCCCTAC
TCGGCCCCCTCCCCAGCCTACAGCAGCTCCAGCCTCTACGCCCCTGATGCTGTGGCCAGC
TCTGGACCCATCATCTCCGACATCACCGAGCTGGCTCCTGCCAGCCCCATGGCCTCCCCC
GGCGGGAGCATAGACGAGAGGCCCCTATCCAGCAGCCCCCTGGTGCGTGTCAAGGAGGAG
CCCCCCAGCCCGCCTCAGAGCCCCCGGGTAGAGGAGGCGAGTCCCGGGCGCCCATCTTCC
GTGGACACCCTCTTGTCCCCGACCGCCCTCATTGACTCCATCCTGCGGGAGAGTGAACCT
GCCCCCGCCTCCGTCACAGCCCTCACGGACGCCAGGGGCCACACGGACACCGAGGGCCGG
CCTCCCTCCCCCCCGCCCACCTCCACCCCTGAAAAGTGCCTCAGCGTAGCCTGCCTGGAC
AAGAATGAGCTCAGTGACCACTTGGATGCTATGGACTCCAACCTGGATAACCTGCAGACC
ATGCTGAGCAGCCACGGCTTCAGCGTGGACACCAGTGCCCTGCTGGACCTGTTCAGCCCC
TCGGTGACCGTGCCCGACATGAGCCTGCCTGACCTTGACAGCAGCCTGGCCAGTATCCAA
GAGCTCCTGTCTCCCCAGGAGCCCCCCAGGCCTCCCGAGGCAGAGAACAGCAGCCCGGAT
TCAGGGAAGCAGCTGGTGCACTACACAGCGCAGCCGCTGTTCCTGCTGGACCCCGGCTCC
GTGGACACCGGGAGCAACGACCTGCCGGTGCTGTTTGAGCTGGGAGAGGGCTCCTACTTC
TCCGAAGGGGACGGCTTCGCCGAGGACCCCACCATCTCCCTGCTGACAGGCTCGGAGCCT
CCCAAAGCCAAGGACCCCACTGTCTCCTAG
Chromosome Location
8
Locus
8q24.3
External Identifiers
ResourceLink
UniProtKB IDQ00613
UniProtKB Entry NameHSF1_HUMAN
GenBank Gene IDBC014638
GeneCard IDHSF1
GenAtlas IDHSF1
HGNC IDHGNC:5224
PDB ID(s)2LDU, 5D5U, 5D5V, 5HDG, 5HDN, 7DCJ, 7DCS, 7DCT
KEGG IDhsa:3297
NCBI Gene ID3297
General References
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  5. Schuetz TJ, Gallo GJ, Sheldon L, Tempst P, Kingston RE: Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):6911-5. [Article]
  6. Holmberg CI, Hietakangas V, Mikhailov A, Rantanen JO, Kallio M, Meinander A, Hellman J, Morrice N, MacKintosh C, Morimoto RI, Eriksson JE, Sistonen L: Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1. EMBO J. 2001 Jul 16;20(14):3800-10. [Article]
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  24. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
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  28. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
BimoclomolinvestigationalunknowntargetDetails