HSF1

Heat shock factor protein 1 ;
HSF 1 ;
Heat shock transcription factor 1 ;
HSTF 1 ;

function: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. ,PTM: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. ,PTM:Sumoylated BY 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. ,similarity:Belongs to the HSF family. ,subcellular location:Cytoplasmic during normal growth. On activation , translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules. ,subunit: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. ,

in utero embryonic development , regulation of cytokine production , negative regulation of cytokine production ,placenta development , embryonic placenta development , response to molecule of bacterial origin , transcription ,regulation of transcription , DNA-dependent , protein amino acid phosphorylation , phosphorus metabolic process ,phosphate metabolic process , defense response , gamete generation , spermatogenesis , female pregnancy , negative regulation of cell proliferation , response to temperature stimulus , response to heat , response to bacterium , response to abiotic stimulus , embryonic development ending in birth or egg hatching , response to organic substance ,phosphorylation , sexual reproduction , response to lipopolysaccharide , multicellular organism reproduction , regulation of tumor necrosis factor production , negative regulation of tumor necrosis factor production , regulation of growth ,regulation of multicellular organism growth , positive regulation of multicellular organism growth , regulation of cell proliferation , chordate embryonic development , regulation of transcription , positive regulation of growth , male gamete generation , embryonic organ development , reproductive process in a multicellular organism , positive regulation of multicellular organismal process , negative regulation of multicellular organismal process , regulation of RNA metabolic process , embryonic process involved in female pregnancy ,

Nucleus . Cytoplasm . Nucleus , nucleoplasm . Cytoplasm , perinuclear region . Cytoplasm , cytoskeleton , spindle pole . Cytoplasm , cytoskeleton , microtubule organizing center , centrosome . Chromosome , centromere , kinetochore . The monomeric form is cytoplasmic in unstressed cells (PubMed:8455624 , PubMed:26159920) . Predominantly nuclear protein in both unstressed and heat shocked cells (PubMed:10413683 , PubMed:10359787) . Translocates in the nucleus upon heat shock (PubMed:8455624) . Nucleocytoplasmic shuttling protein (PubMed:26159920) . Colocalizes with IER5 in the nucleus (PubMed:27354066) . Colocalizes with BAG3 to the nucleus upon heat stress (PubMed:8455624 , PubMed:26159920) . Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock (PubMed:11447121 , PubMed:11514557 , PubMed:10359787 , PubMed:25963659 , PubMed:10747973 , PubMed:24581496 , PubMed:19229036) . Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock (PubMed:11447121 , PubMed:12665592 , PubMed:11514557 , PubMed:14707147 , PubMed:10359787) . Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock (PubMed:21085490) . Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response (PubMed:26159920) . Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner (PubMed:12917326) . Together with histone H2AX , redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) (PubMed:26359349) . Colocalizes with calcium-responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes (PubMed:18794143) . Colocalizes with gamma tubulin at centrosome (PubMed:18794143) . Localizes at spindle pole in metaphase (PubMed:18794143) . Colocalizes with PLK1 at spindle poles during prometaphase (PubMed:18794143) . .