ID  Q00613;
PN  Heat shock factor protein 1;
GN  HSF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11514557, ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:19229036, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27189267, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:8455624}. Cytoplasm {ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:8455624}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10359787}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21085490}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18794143}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18794143}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18794143}. Note=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). {ECO:0000269|PubMed:10359787, ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11514557, ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:24581496, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:8455624}.
DR  UNIPROT: Q00613;
DR  UNIPROT: A8K4L0;
DR  UNIPROT: A8MW26;
DR  UNIPROT: Q53XT4;
DR  PDB: 2LDU;
DR  PDB: 5D5U;
DR  PDB: 5D5V;
DR  PDB: 5HDG;
DR  PDB: 5HDN;
DR  PDB: 7DCJ;
DR  PDB: 7DCS;
DR  PDB: 7DCT;
DR  Pfam: PF00447;
DR  Pfam: PF06546;
DR  PROSITE: PS00434;
DR  OMIM: 140580;
DR  DisGeNET: 3297;
DE  Function: 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 insult 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, PubMed:18451878). 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). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). 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). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). 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 (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). Also plays 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). {ECO:0000269|PubMed:10359787, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12659875, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:1871105, ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:1986252, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:26727489, ECO:0000269|PubMed:26754925, ECO:0000269|PubMed:34723967, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:7760831, ECO:0000269|PubMed:7935471, ECO:0000269|PubMed:8455624, ECO:0000269|PubMed:8940068, ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459, ECO:0000269|PubMed:9341107, ECO:0000269|PubMed:9499401, ECO:0000269|PubMed:9535852, ECO:0000269|PubMed:9727490}. (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. {ECO:0000269|PubMed:27189267}.
DE  Reference Proteome: Yes;
DE  Interaction: O60271; IntAct: EBI-11911387; Score: 0.00
DE  Interaction: P02545; IntAct: EBI-10682932; Score: 0.35
DE  Interaction: P22392; IntAct: EBI-9394221; Score: 0.35
DE  Interaction: P63165; IntAct: EBI-15799774; Score: 0.44
DE  Interaction: P09104; IntAct: EBI-734427; Score: 0.00
DE  Interaction: Q9UNE7; IntAct: EBI-7902188; Score: 0.40
DE  Interaction: P49137; IntAct: EBI-993295; Score: 0.60
DE  Interaction: Q8N0Z6; IntAct: EBI-7909995; Score: 0.40
DE  Interaction: Q9CQU5; IntAct: EBI-2556745; Score: 0.40
DE  Interaction: Q81JT7; IntAct: EBI-2832104; Score: 0.00
DE  Interaction: Q81VE1; IntAct: EBI-2832111; Score: 0.00
DE  Interaction: P62258; IntAct: EBI-6994351; Score: 0.53
DE  Interaction: O43529; IntAct: EBI-3910513; Score: 0.37
DE  Interaction: P26641; IntAct: EBI-6954536; Score: 0.40
DE  Interaction: Q00534; IntAct: EBI-5293131; Score: 0.44
DE  Interaction: Q04759; IntAct: EBI-6512722; Score: 0.54
DE  Interaction: O00505; IntAct: EBI-9394221; Score: 0.64
DE  Interaction: O95817; IntAct: EBI-9394221; Score: 0.64
DE  Interaction: O95757; IntAct: EBI-9394221; Score: 0.35
DE  Interaction: Q9NZL4; IntAct: EBI-9394221; Score: 0.64
DE  Interaction: Q03933; IntAct: EBI-9394221; Score: 0.73
DE  Interaction: P04792; IntAct: EBI-9394221; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-9394221; Score: 0.64
DE  Interaction: Q9ULV5; IntAct: EBI-9394268; Score: 0.35
DE  Interaction: P14618; IntAct: EBI-9355222; Score: 0.44
DE  Interaction: P54645; IntAct: EBI-10682831; Score: 0.40
DE  Interaction: Q8N4C8; IntAct: EBI-10816412; Score: 0.54
DE  Interaction: Q5VY09; IntAct: EBI-10816421; Score: 0.59
DE  Interaction: Q9UKX3; IntAct: EBI-11141047; Score: 0.35
DE  Interaction: Q53FA3; IntAct: EBI-12450308; Score: 0.35
DE  Interaction: Q8NET4; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: Q5VZK9; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: P34931; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: O43683; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: Q96SB8; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: Q15029; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: Q8NEH6; IntAct: EBI-12451193; Score: 0.51
DE  Interaction: P53350; IntAct: EBI-12451475; Score: 0.51
DE  Interaction: Q9UKN8; IntAct: EBI-11911558; Score: 0.00
DE  Interaction: Q9UBC2; IntAct: EBI-11911549; Score: 0.00
DE  Interaction: Q15555; IntAct: EBI-11911495; Score: 0.00
DE  Interaction: Q14C86; IntAct: EBI-11911477; Score: 0.00
DE  Interaction: Q14683; IntAct: EBI-11911468; Score: 0.00
DE  Interaction: Q14566; IntAct: EBI-11911459; Score: 0.00
DE  Interaction: P61962; IntAct: EBI-11911450; Score: 0.00
DE  Interaction: P51157; IntAct: EBI-11911432; Score: 0.00
DE  Interaction: P49736; IntAct: EBI-11911423; Score: 0.00
DE  Interaction: P33991; IntAct: EBI-11911405; Score: 0.00
DE  Interaction: Q9Y4E8; IntAct: EBI-11911567; Score: 0.00
DE  Interaction: Q9Y6Y0; IntAct: EBI-11911585; Score: 0.00
DE  Interaction: Q9Y6A4; IntAct: EBI-11911576; Score: 0.00
DE  Interaction: Q8IV03; IntAct: EBI-21503643; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21714606; Score: 0.35
DE  Interaction: O95429; IntAct: EBI-21788135; Score: 0.35
DE  Interaction: Q00613; IntAct: EBI-16190425; Score: 0.57
DE  Interaction: P45983; IntAct: EBI-16203579; Score: 0.35
DE  Interaction: Q96MT8; IntAct: EBI-21379247; Score: 0.00
DE  Interaction: Q6ZMY6; IntAct: EBI-25869741; Score: 0.56
DE  Interaction: Q96CM3; IntAct: EBI-25869733; Score: 0.56
DE  Interaction: Q8NFB2; IntAct: EBI-25869723; Score: 0.56
DE  Interaction: Q9UIH9; IntAct: EBI-25869715; Score: 0.56
DE  Interaction: Q13352; IntAct: EBI-25869705; Score: 0.56
DE  Interaction: Q14693; IntAct: EBI-25869697; Score: 0.56
DE  Interaction: O14744; IntAct: EBI-25869689; Score: 0.56
DE  Interaction: Q9UNY5; IntAct: EBI-25869681; Score: 0.56
DE  Interaction: P11684; IntAct: EBI-25869673; Score: 0.56
GO  GO:0005813;
GO  GO:0101031;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000791;
GO  GO:0000792;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0097165;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:1990904;
GO  GO:0031490;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0003700;
GO  GO:0000981;
GO  GO:0001227;
GO  GO:0140296;
GO  GO:0031072;
GO  GO:0051879;
GO  GO:0042802;
GO  GO:1990841;
GO  GO:0046982;
GO  GO:0019901;
GO  GO:0043621;
GO  GO:0000978;
GO  GO:0001162;
GO  GO:0043565;
GO  GO:1990837;
GO  GO:0098847;
GO  GO:0097677;
GO  GO:0000976;
GO  GO:0061770;
GO  GO:1904385;
GO  GO:0071276;
GO  GO:0071280;
GO  GO:0072738;
GO  GO:0071392;
GO  GO:0071480;
GO  GO:0034605;
GO  GO:0070301;
GO  GO:1904845;
GO  GO:0071222;
GO  GO:1904843;
GO  GO:0035865;
GO  GO:1903936;
GO  GO:0034620;
GO  GO:0071466;
GO  GO:0006952;
GO  GO:0006281;
GO  GO:0000165;
GO  GO:0006397;
GO  GO:0009299;
GO  GO:0051028;
GO  GO:0010667;
GO  GO:2001033;
GO  GO:0010629;
GO  GO:0090084;
GO  GO:1901215;
GO  GO:0031333;
GO  GO:0000122;
GO  GO:1902512;
GO  GO:0120162;
GO  GO:0043280;
GO  GO:0051091;
GO  GO:0010628;
GO  GO:0090261;
GO  GO:0045651;
GO  GO:1904528;
GO  GO:0045931;
GO  GO:1900365;
GO  GO:0045944;
GO  GO:0042531;
GO  GO:0065003;
GO  GO:1900034;
GO  GO:0006357;
GO  GO:0014823;
GO  GO:1990910;
GO  GO:0007584;
GO  GO:1990911;
GO  GO:0033574;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRK
SQ  VVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLA
SQ  MKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPY
SQ  SAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSS
SQ  VDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQT
SQ  MLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGS
SQ  VDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS
//