Localization
Nucleus,Cytoplasm,Nucleus,Nucleoplasm,Cytoplasm,Perinuclear region,Cytoplasm,Cytoskeleton,Spindle pole,Cytoplasm,Cytoskeleton,Microtubule organizing center,Centrosome,Chromosome,Centromere,Kinetochore;
Function
Function 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:1871105, PubMed:11447121, PubMed:1986252, PubMed:7760831, PubMed:7623826, PubMed:8946918, PubMed:8940068, PubMed:9341107, PubMed:9121459, PubMed:9727490, PubMed:9499401, PubMed:9535852, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:25963659, PubMed:26754925). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:9727490, PubMed:11583998, PubMed:16278218). 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 (PubMed:1871105, PubMed:1986252, PubMed:8455624, PubMed:7935471, PubMed:7623826, PubMed:8940068, PubMed:9727490, PubMed:9499401, PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:25963659, PubMed:26754925). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Plays also 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 (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Plays also a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925).(Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300.
Gene Ontology
GO:0005813; GO:0000777; GO:0005737; GO:0005829; GO:0000791; GO:0000792; GO:0000776; GO:0097431; GO:0097165; GO:0005654; GO:0005634; GO:0048471; GO:0016605; GO:0045120; GO:1990904; GO:0031490; GO:0003677; GO:0003700; GO:0000981; GO:0001227; GO:0031072; GO:0051879; GO:0042802; GO:1990841; GO:0046982; GO:0019901; GO:0043621; GO:0001162; GO:0000978; GO:0043565; GO:0098847; GO:0097677; GO:0061770; GO:0034622; GO:1904385; GO:0071276; GO:0071280; GO:0072738; GO:0071392; GO:0071480; GO:0034605; GO:0070301; GO:1904845; GO:0071222; GO:1904843; GO:0035865; GO:1903936; GO:0034620; GO:0006952; GO:0006281; GO:0001892; GO:0060136; GO:0007143; GO:0000165; GO:0006397; GO:0009299; GO:0051028; GO:0010667; GO:0008285; GO:2001033; GO:0090084; GO:1901215; GO:0000122; GO:0032720; GO:1902512; GO:0008284; GO:0120162; GO:0043280; GO:0090261; GO:1904528; GO:0045931; GO:1900365; GO:0040018; GO:0045944; GO:0061408; GO:0042531; GO:0051260; GO:0070207; GO:1900034; GO:0043497; GO:0014823; GO:1990910; GO:1990911; GO:0033574; GO:0007283