National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory
Protein Information |
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|---|---|
| Protein Name | Heat shock factor protein 1 |
| Accession Code | P38529 |
| Gene | HSF1 |
| Organism | Gallus gallus | Chicken (Taxonomy: 9031) |
| Part of Reference Proteome? | Yes |
| Sequence (Length: 491) |
Description |
Position in the Nuclear Envelope |
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|---|---|---|
| Location | Location ID | Description |
| Perinuclear Region | SL-0198 | The perinuclear region is the cytoplasmic region just around the nucleus. | Membrane Topology |
| Topology | Source | Annotation Type |
| Unknown | UniProt | Sequence Analysis | Assigned Ontology terms |
Description |
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|---|---|
| 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 insults' damage (PubMed:8455593). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form. 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. Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (By similarity). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to chromatin at heat shock gene promoters. 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. Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells. Plays a role in nuclear export of stress-induced mRNA. Plays a role in the regulation of mitotic progression. Also plays a role as a negative regulator of non- homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner. Involved in stress-induced cancer cell proliferation. {By SimilarityUniProtKB:Q00613, Experimental EvidencePubMed:8455593}. | Assigned Ontology terms |
National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory