热休克因子1重组兔单抗

HSF1

Heat shock factor protein 1

Monomer. Under normal conditions, interacts with HSP90AA1in the HSP90 multichaperone complex; the interaction preventstrimerization and activation of HSF1. On activation by heat-stressor by other factors such as metal ions, HSF1 is released from thecomplex, homotrimerizes, is hyperphosphorylated and translocated tothe nucleus where, subsequently, it can activate transcription.Binds the complex through the regulatory domain. Interacts withSYMPK and CSTF2 in heat-stressed cells. Interacts with FKBP4 in theHSP90 multichaperone complex; the interaction is independent of thephosphorylation state of HSF1. Interacts with MAPKAPK2.

Cytoplasm. Nucleus. Note=Cytoplasmic duringnormal growth. On activation, translocates to nuclear stressgranules. Colocalizes with SUMO1 in nuclear stress granules.

Phosphorylated on multiple serine residues, a subset of whichare involved in stress-related regulation of transcriptionactivation. Constitutive phosphorylation represses transcriptionalactivity at normal temperatures. Levels increase on specificresidues heat-shock and enhance HSF1 transactivation activity.Phosphorylation on Ser-307 derepresses activation on heat-stressand in combination with Ser-303 phosphorylation appears to beinvolved in recovery after heat-stress. Phosphorylated on Ser-230by CAMK2, in vitro. Cadmium also enhances phosphorylation at thissite. Phosphorylation on Ser-303 is a prerequisite for HSF1sumoylation. Phosphorylation on Ser-121 inhibits transactivationand promotes HSP90 binding. Phosphorylation on Thr-142 alsomediates transcriptional activity induced by heat.

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.
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.

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.
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.

Belongs to the HSF family.

DNA-binding protein that specifically binds heat shockpromoter elements (HSE) and activates transcription. In highereukaryotes, HSF is unable to bind to the HSE unless the cells areheat shocked.