HSF1 information

HSF1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2LDU, 5D5U, 5D5V
Identifiers
Aliases	HSF1, HSTF1, heat shock transcription factor 1
External IDs	OMIM: 140580; MGI: 96238; HomoloGene: 74556; GeneCards: HSF1; OMA:HSF1 - orthologs
Gene location (Human)
Chr.	Chromosome 8 (human)
End	144,314,720 bp
RNA expression pattern
	Top expressed in
	left ventricle; ; stromal cell of endometrium; ; gastrocnemius muscle; ; popliteal artery; ; fundus; ; body of stomach; ; skeletal muscle tissue; ; right coronary artery; ; prostate; ; body of pancreas;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	DNA-binding transcription factor activity; chromatin binding; DNA-binding transcription repressor activity, RNA polymerase II-specific; protein binding; RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; sequence-specific single stranded DNA binding; DNA binding; protein kinase binding; heat shock protein binding; chromatin DNA binding; identical protein binding; sequence-specific DNA binding; protein self-association; protein heterodimerization activity; Hsp90 protein binding; translation elongation factor binding; promoter-specific chromatin binding; RNA polymerase II cis-regulatory region sequence-specific DNA binding; DNA-binding transcription factor activity, RNA polymerase II-specific; STAT family protein binding;
Cellular component	cytoplasm; pronucleus; euchromatin; heterochromatin; nucleus; centrosome; cytosol; PML body; nuclear stress granule; mitotic spindle pole; ribonucleoprotein complex; chromosome, centromeric region; kinetochore; spindle pole; nucleoplasm; chromosome; microtubule organizing center; cytoskeleton; perinuclear region of cytoplasm; protein-containing complex;
Biological process	defense response; regulation of transcription, DNA-templated; embryonic placenta development; mRNA transcription; in utero embryonic development; negative regulation of transcription by RNA polymerase II; response to heat; female meiotic nuclear division; transcription, DNA-templated; embryonic process involved in female pregnancy; protein phosphorylation; response to lipopolysaccharide; spermatogenesis; positive regulation of multicellular organism growth; negative regulation of tumor necrosis factor production; positive regulation of transcription by RNA polymerase II; negative regulation of cell population proliferation; response to organonitrogen compound; cellular response to lipopolysaccharide; negative regulation of gene expression; cellular response to amino acid stimulus; cellular response to hydrogen peroxide; positive regulation of microtubule binding; response to peptide; cellular response to nitroglycerin; negative regulation of cardiac muscle cell apoptotic process; response to estradiol; cellular response to organic cyclic compound; positive regulation of gene expression; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; cellular response to potassium ion; response to amino acid; negative regulation of inclusion body assembly; positive regulation of apoptotic DNA fragmentation; cellular response to L-glutamine; response to psychosocial stress; response to organic cyclic compound; negative regulation of neuron death; response to nutrient; cellular response to angiotensin; response to testosterone; response to hypobaric hypoxia; response to activity; cellular response to radiation; cellular response to estradiol stimulus; positive regulation of inclusion body assembly; MAPK cascade; positive regulation of cell population proliferation; cellular response to heat; Unfolded Protein Response; regulation of protein heterodimerization activity; positive regulation of mitotic cell cycle; protein homooligomerization; positive regulation of transcription from RNA polymerase II promoter in response to heat stress; protein homotrimerization; cellular response to cadmium ion; cellular response to copper ion; cellular response to gamma radiation; cellular response to diamide; regulation of cellular response to heat; positive regulation of mRNA polyadenylation; cellular response to sodium arsenite; negative regulation of double-strand break repair via nonhomologous end joining; DNA repair; mRNA processing; cellular response to DNA damage stimulus; mRNA transport; positive regulation of tyrosine phosphorylation of STAT protein; positive regulation of cold-induced thermogenesis;
	Sources:Amigo / QuickGO
Orthologs
	3297
	15499
	ENSG00000185122; ENSG00000284774
	ENSMUSG00000022556
	Q00613
	P38532
	NM_005526
	NM_008296
	NP_005517
	NP_001318081; NP_001318082; NP_001318083; NP_001318143; NP_032322
	Wikidata
View/Edit Human	View/Edit Mouse

Heat shock factor 1 (HSF 1) is a protein that in humans is encoded by the HSF1 gene.^[4] HSF1 is highly conserved in eukaryotes and is the primary mediator of transcriptional responses to proteotoxic stress with important roles in non-stress regulation such as development and metabolism.^[5]

^ ^a ^b ^c ENSG00000284774 GRCh38: Ensembl release 89: ENSG00000185122, ENSG00000284774 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Rabindran SK, Giorgi G, Clos J, Wu C (August 1991). "Molecular cloning and expression of a human heat shock factor, HSF1". Proceedings of the National Academy of Sciences of the United States of America. 88 (16): 6906–10. Bibcode:1991PNAS...88.6906R. doi:10.1073/pnas.88.16.6906. PMC 52202. PMID 1871105.
^ Vihervaara A, Sistonen L (January 2014). "HSF1 at a glance". Journal of Cell Science. 127 (Pt 2): 261–6. doi:10.1242/jcs.132605. PMID 24421309.

[refGRCh38Ensembl-1] ENSG00000284774 GRCh38: Ensembl release 89: ENSG00000185122, ENSG00000284774 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid18711052-4] Rabindran SK, Giorgi G, Clos J, Wu C (August 1991). "Molecular cloning and expression of a human heat shock factor, HSF1". Proceedings of the National Academy of Sciences of the United States of America. 88 (16): 6906–10. Bibcode:1991PNAS...88.6906R. doi:10.1073/pnas.88.16.6906. PMC 52202. PMID 1871105.

[5] Vihervaara A, Sistonen L (January 2014). "HSF1 at a glance". Journal of Cell Science. 127 (Pt 2): 261–6. doi:10.1242/jcs.132605. PMID 24421309.

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