a transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription. Induced in response to heat, heavy metals, and oxidative stress. In higher eukaryotes, HSF is unable to bind to HSEs unless the cells are stressed. Becomes phosphorylated in response to stress, forming homotrimers that bind DNA and activate transcription. Phosphorylation by PLK1 enhances nuclear translocation, and phosphorylation by CaMKII enhances transactivation. Phosphorylation by GSK3 and ERK1 induces binding by 14-3-3 and sequestration in the cytoplasm. In addition, during attenuation from the heat shock response, HSF1 is repressed by direct binding of Hsp70, HSP40, and HSF binding protein 1 (HSBP1). Four alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Transcription factor; DNA binding protein
Chromosomal Location of Human Ortholog: 8q24.3
Cellular Component: nucleoplasm; protein complex; pronucleus; cytoplasm; cytosol
Molecular Function: protein binding; chromatin binding; transcription factor activity
Biological Process: negative regulation of cell proliferation; embryonic placenta development; transcription, DNA-dependent; embryonic process involved in female pregnancy; female meiosis; defense response; response to lipopolysaccharide; positive regulation of transcription from RNA polymerase II promoter; spermatogenesis; negative regulation of tumor necrosis factor production; negative regulation of transcription from RNA polymerase II promoter; positive regulation of multicellular organism growth; protein amino acid phosphorylation
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.