Hsf1 (heat shock transcription factor 1) - Rat Genome Database

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Gene: Hsf1 (heat shock transcription factor 1) Rattus norvegicus
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Symbol: Hsf1
Name: heat shock transcription factor 1
RGD ID: 620913
Description: Enables several functions, including STAT family protein binding activity; promoter-specific chromatin binding activity; and sequence-specific single stranded DNA binding activity. Involved in several processes, including regulation of apoptotic process; regulation of inclusion body assembly; and regulation of macromolecule metabolic process. Located in euchromatin and heterochromatin. Used to study Parkinson's disease; muscular atrophy; and transient cerebral ischemia. Biomarker of Alzheimer's disease; Parkinson's disease; congestive heart failure; cryptorchidism; and transient cerebral ischemia. Human ortholog(s) of this gene implicated in Huntington's disease. Orthologous to human HSF1 (heat shock transcription factor 1); INTERACTS WITH (+)-schisandrin B; (R)-adrenaline; (Z)-ligustilide.
Type: protein-coding
RefSeq Status: VALIDATED
Previously known as: heat shock factor protein 1
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Black Rat
Alliance Orthologs
More Info more info ...
Latest Assembly: GRCr8 - GRCr8 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr87110,076,710 - 110,103,665 (+)NCBIGRCr8GRCr8GRCr8
GRCr8 Ensembl7110,076,710 - 110,103,665 (+)EnsemblGRCr8
mRatBN7.27108,196,040 - 108,223,011 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl7108,196,056 - 108,223,011 (+)EnsemblmRatBN7.2
UTH_Rnor_SHR_Utx7109,940,443 - 109,967,383 (+)NCBIUTH_Rnor_SHR_UtxUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.07112,164,140 - 112,191,080 (+)NCBIUTH_Rnor_SHRSP_BbbUtx_1.0UTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.07112,122,490 - 112,149,447 (+)NCBIUTH_Rnor_WKY_Bbb_1.0UTH_Rnor_WKY_Bbb_1.0
Rnor_6.07117,538,523 - 117,565,478 (+)NCBIRnor_6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl7117,538,523 - 117,565,478 (+)Ensemblrn6Rnor6.0
Rnor_5.07117,526,154 - 117,553,109 (+)NCBIRnor_5.0Rnor_5.0rn5
RGSC_v3.47114,524,211 - 114,551,166 (+)NCBIRGSC_v3.4RGSC_v3.4rn4
Celera7104,547,683 - 104,574,508 (+)NCBICelera
RGSC_v3.17114,580,681 - 114,585,056 (+)NCBI
Cytogenetic Map7q34NCBI
JBrowse:




Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(+)-schisandrin B  (EXP)
(20S)-ginsenoside Rg3  (ISO)
(R)-adrenaline  (EXP)
(R,S)-Scoulerine  (ISO)
(Z)-ligustilide  (EXP)
1,3,5-trinitro-1,3,5-triazinane  (EXP)
1-naphthyl isothiocyanate  (ISO)
15-deoxy-Delta(12,14)-prostaglandin J2  (ISO)
17alpha-ethynylestradiol  (EXP)
17beta-estradiol  (ISO)
17beta-hydroxy-17-methylestra-4,9,11-trien-3-one  (ISO)
2,2',4,4'-Tetrabromodiphenyl ether  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,4-dinitrotoluene  (EXP)
2-nitrofluorene  (EXP)
2-tert-butylhydroquinone  (ISO)
4-(N-nitrosomethylamino)-1-(3-pyridyl)butan-1-one  (EXP)
4-hydroxyphenyl retinamide  (ISO)
5-azacytidine  (ISO)
6-propyl-2-thiouracil  (ISO)
7H-xanthine  (EXP)
9H-xanthine  (EXP)
acetaldehyde  (ISO)
acetate ester  (ISO)
acetylsalicylic acid  (ISO)
acrolein  (ISO)
acrylamide  (ISO)
actinomycin D  (ISO)
afimoxifene  (ISO)
aflatoxin B1  (EXP,ISO)
albendazole  (ISO)
aldehydo-D-glucose  (ISO)
all-trans-retinoic acid  (ISO)
allyl alcohol  (ISO)
alpha-D-galactose  (ISO)
alpha-pinene  (ISO)
ammonium chloride  (EXP)
amphibole asbestos  (ISO)
anthra[1,9-cd]pyrazol-6(2H)-one  (ISO)
apratoxin A  (ISO)
arsane  (ISO)
arsenic atom  (ISO)
arsenite(3-)  (EXP,ISO)
arsenous acid  (ISO)
Aurin  (ISO)
azathioprine  (ISO)
Bardoxolone methyl  (ISO)
benzene  (ISO)
benzo[a]pyrene  (EXP,ISO)
beta-lapachone  (ISO)
bisphenol A  (EXP,ISO)
bisphenol F  (ISO)
bortezomib  (ISO)
C.I. Natural Red 20  (ISO)
cadmium atom  (ISO)
cadmium dichloride  (EXP,ISO)
cadmium sulfate  (ISO)
caffeine  (ISO)
Calcimycin  (ISO)
capsaicin  (EXP)
carbamazepine  (ISO)
carbonyl cyanide p-trifluoromethoxyphenylhydrazone  (ISO)
ceftazidime pentahydrate  (ISO)
celastrol  (EXP,ISO)
chelidonine  (ISO)
chlorphenamine  (ISO)
cisplatin  (ISO)
clotrimazole  (ISO)
cobalt atom  (ISO)
cobalt dichloride  (ISO)
cocaine  (EXP)
coumarin  (ISO)
curcumin  (EXP,ISO)
cycloheximide  (ISO)
cyclosporin A  (ISO)
cylindrospermopsin  (ISO)
cypermethrin  (ISO)
cyproheptadine  (ISO)
D-glucose  (ISO)
dactolisib  (ISO)
dexamethasone  (ISO)
diarsenic trioxide  (ISO)
diazinon  (ISO)
dibutyl phthalate  (ISO)
diclofenac  (ISO)
dicrotophos  (ISO)
diethylstilbestrol  (EXP,ISO)
diltiazem  (ISO)
dioxygen  (ISO)
disodium selenite  (ISO)
doxorubicin  (ISO)
ebselen  (ISO)
elesclomol  (ISO)
epoxiconazole  (ISO)
epoxomicin  (ISO)
etacrynic acid  (ISO)
ethanol  (ISO)
ethyl methanesulfonate  (ISO)
fenbendazole  (ISO)
fenofibrate  (EXP)
fenthion  (ISO)
fipronil  (EXP)
flavonoids  (EXP)
formaldehyde  (ISO)
fotemustine  (ISO)
FR900359  (ISO)
fulvestrant  (ISO)
furosemide  (ISO)
galactose  (ISO)
geldanamycin  (ISO)
geneticin  (ISO)
gentamycin  (EXP,ISO)
glucose  (ISO)
gold atom  (ISO)
gold(0)  (ISO)
GSK-J4  (ISO)
hemin  (ISO)
homocysteic acid  (EXP)
hydrogen chloride  (ISO)
hydrogen peroxide  (EXP,ISO)
ibuprofen  (ISO)
imipramine  (ISO)
indole-3-methanol  (ISO)
indometacin  (ISO)
L-serine  (ISO)
lactacystin  (ISO)
lead diacetate  (EXP,ISO)
lead(0)  (EXP)
linalool  (ISO)
LY294002  (ISO)
maneb  (ISO)
manganese atom  (ISO)
manganese(0)  (ISO)
manganese(II) chloride  (ISO)
melatonin  (ISO)
menadione  (ISO)
mercury atom  (ISO)
mercury dichloride  (ISO)
mercury(0)  (ISO)
mesalamine  (ISO)
methapyrilene  (EXP)
methidathion  (ISO)
methyl methanesulfonate  (ISO)
mifepristone  (ISO)
mometasone furoate  (ISO)
monohexyl phthalate  (ISO)
N-acetyl-L-cysteine  (ISO)
N-benzyloxycarbonyl-L-leucyl-L-leucyl-L-leucinal  (ISO)
N-ethyl-N-nitrosourea  (ISO)
N-nitrosodiethylamine  (EXP)
N-nitrosodimethylamine  (EXP)
nickel sulfate  (ISO)
nifedipine  (ISO)
nimesulide  (ISO)
nitrates  (ISO)
nitrofurantoin  (ISO)
oxaprozin  (ISO)
oxyphenbutazone  (ISO)
ozone  (ISO)
papaverine  (ISO)
paracetamol  (EXP,ISO)
paraquat  (ISO)
parthenolide  (ISO)
PD 0325901  (ISO)
pevonedistat  (ISO)
Phenoxybenzamine  (ISO)
phenprocoumon  (ISO)
phosphocholine  (ISO)
phosphorylcholine chloride  (ISO)
piperidones  (ISO)
piperonyl butoxide  (EXP)
pirinixic acid  (EXP,ISO)
PLX-4720  (ISO)
promegestone  (ISO)
promethazine  (ISO)
pyocyanine  (EXP)
pyridine  (ISO)
quercetin  (ISO)
resveratrol  (ISO)
rivastigmine  (ISO)
rotenone  (EXP,ISO)
SB 203580  (EXP)
Securinine  (ISO)
senecionine  (ISO)
Shikonin  (ISO)
silver atom  (ISO)
silver(0)  (ISO)
silver(1+) nitrate  (ISO)
simvastatin  (ISO)
Siomycin A  (ISO)
sirolimus  (ISO)
sodium arsenite  (ISO)
Sodium salicylate  (ISO)
solanesol  (ISO)
sphingosine 1-phosphate  (ISO)
sulforaphane  (ISO)
sulindac  (ISO)
sunitinib  (ISO)
tanespimycin  (ISO)
teprenone  (ISO)
teriflunomide  (ISO)
tetrachloroethene  (ISO)
tetrachloromethane  (EXP)
thalidomide  (ISO)
thiazoles  (ISO)
thioacetamide  (EXP)
thiopental  (ISO)
thiram  (ISO)
titanium dioxide  (ISO)
trichostatin A  (ISO)
triphenyl phosphate  (ISO)
valproic acid  (ISO)
withaferin A  (ISO)
wortmannin  (ISO)
zinc atom  (ISO)
zinc oxide  (ISO)
zinc pyrithione  (ISO)
zinc sulfate  (ISO)
zinc(0)  (ISO)

Gene Ontology Annotations     Click to see Annotation Detail View

Biological Process
cellular response to amino acid stimulus  (IDA,IEP)
cellular response to angiotensin  (IDA)
cellular response to cadmium ion  (IEA,ISO)
cellular response to copper ion  (IEA,ISO)
cellular response to diamide  (IEA,ISO)
cellular response to estradiol stimulus  (IDA)
cellular response to gamma radiation  (IEA,ISO)
cellular response to heat  (IEA,IMP,ISO)
cellular response to hydrogen peroxide  (IMP)
cellular response to L-glutamine  (IEP)
cellular response to lipopolysaccharide  (IEP)
cellular response to nitroglycerin  (IEP)
cellular response to potassium ion  (IEP)
cellular response to radiation  (IDA)
cellular response to sodium arsenite  (IEA,ISO)
cellular response to unfolded protein  (IEA,ISO)
cellular response to xenobiotic stimulus  (IEP)
defense response  (IDA)
DNA-templated transcription  (IEA)
embryonic placenta development  (ISO)
embryonic process involved in female pregnancy  (ISO)
female meiotic nuclear division  (ISO)
in utero embryonic development  (ISO)
MAPK cascade  (IEA,ISO)
negative regulation of cardiac muscle cell apoptotic process  (IMP)
negative regulation of cell population proliferation  (ISO)
negative regulation of cellular process  (IMP)
negative regulation of double-strand break repair via nonhomologous end joining  (IEA,ISO)
negative regulation of gene expression  (IMP)
negative regulation of inclusion body assembly  (IMP)
negative regulation of protein-containing complex assembly  (IEA,ISO)
negative regulation of transcription by RNA polymerase II  (IEA,ISO)
negative regulation of tumor necrosis factor production  (ISO)
positive regulation of apoptotic DNA fragmentation  (IMP)
positive regulation of apoptotic signaling pathway  (IMP)
positive regulation of cold-induced thermogenesis  (IEA,ISO,ISS)
positive regulation of gene expression  (IEA,IMP,ISO)
positive regulation of inclusion body assembly  (IMP)
positive regulation of macrophage differentiation  (IEA,ISO)
positive regulation of mitotic cell cycle  (IEA,ISO)
positive regulation of multicellular organism growth  (ISO)
positive regulation of protein modification process  (IMP)
positive regulation of stress granule assembly  (IMP)
positive regulation of transcription by RNA polymerase II  (IEA,ISO)
protein phosphorylation  (ISO)
protein-containing complex assembly  (IEA,ISO)
regulation of cellular response to heat  (IEA,ISO)
regulation of DNA-templated transcription  (IEA,TAS)
regulation of transcription by RNA polymerase II  (IEA,ISO)
response to activity  (IEP)
response to amino acid  (IEP)
response to estradiol  (IDA)
response to heat  (ISO)
response to hypobaric hypoxia  (IEP)
response to lipopolysaccharide  (ISO)
response to nutrient  (IEP)
response to peptide  (IEP)
response to psychosocial stress  (IEP)
response to testosterone  (IDA)
spermatogenesis  (ISO)

Cellular Component

References

References - curated
# Reference Title Reference Citation
1. During ischemia-reperfusion in rat kidneys, heat shock response is not regulated by expressional changes of heat shock factor 1. Akcetin Z, etal., Transpl Int 2000;13(4):297-302.
2. Hsp90 chaperone inhibitor 17-AAG attenuates Abeta-induced synaptic toxicity and memory impairment. Chen Y, etal., J Neurosci. 2014 Feb 12;34(7):2464-70. doi: 10.1523/JNEUROSCI.0151-13.2014.
3. The A2A adenosine receptor rescues the urea cycle deficiency of Huntington's disease by enhancing the activity of the ubiquitin-proteasome system. Chiang MC, etal., Hum Mol Genet. 2009 Aug 15;18(16):2929-42. doi: 10.1093/hmg/ddp230. Epub 2009 May 14.
4. The administration of renoprotective agents extends warm ischemia in a rat model. Cohen J, etal., J Endourol. 2013 Mar;27(3):343-8. doi: 10.1089/end.2012.0194. Epub 2013 Feb 25.
5. Tissue-specific Gene Expression in Rat Hearts and Aortas in a Model of Vascular Nitrate Tolerance. Csont T, etal., J Cardiovasc Pharmacol. 2015 May;65(5):485-93. doi: 10.1097/FJC.0000000000000218.
6. Expression and localization of heat shock factor (Hsf) 1 in the rodent cochlea. Fairfield DA, etal., Hear Res 2002 Nov;173(1-2):109-18.
7. Heat shock factor 1 regulates the expression of the TRPV1 gene in the rat preoptic-anterior hypothalamus area during lipopolysaccharide-induced fever. Fan-xin M, etal., Exp Physiol. 2012 Jun;97(6):730-40. doi: 10.1113/expphysiol.2011.064204. Epub 2012 Mar 16.
8. Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models. Fujimoto M, etal., J Biol Chem. 2005 Oct 14;280(41):34908-16. Epub 2005 Jul 28.
9. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, etal., Brief Bioinform. 2011 Sep;12(5):449-62. doi: 10.1093/bib/bbr042. Epub 2011 Aug 27.
10. Rat ISS GO annotations from GOA human gene data--August 2006 GOA data from the GO Consortium
11. Characterizing HSF1 Binding and Post-Translational Modifications of hsp70 Promoter in Cultured Cortical Neurons: Implications in the Heat-Shock Response. Gomez AV, etal., PLoS One. 2015 Jun 8;10(6):e0129329. doi: 10.1371/journal.pone.0129329. eCollection 2015.
12. Glutamine induces heat shock protein 70 expression via O-GlcNAc modification and subsequent increased expression and transcriptional activity of heat shock factor-1. Gong J and Jing L, Minerva Anestesiol. 2011 May;77(5):488-95.
13. Celastrol overcomes HSP72 gene silencing-mediated muscle atrophy and induces myofiber preservation. Gwag T, etal., J Physiol Pharmacol. 2015 Apr;66(2):273-83.
14. ANG II promotes IGF-IIR expression and cardiomyocyte apoptosis by inhibiting HSF1 via JNK activation and SIRT1 degradation. Huang CY, etal., Cell Death Differ. 2014 Aug;21(8):1262-74. doi: 10.1038/cdd.2014.46. Epub 2014 May 2.
15. Polyamines mediate glutamine-dependent induction of the intestinal epithelial heat shock response. Iwashita Y, etal., Am J Physiol Gastrointest Liver Physiol. 2011 Jul;301(1):G181-7. doi: 10.1152/ajpgi.00054.2011. Epub 2011 Apr 21.
16. Differential hypoxic tolerance is mediated by activation of heat shock response and nitric oxide pathway. Jain K, etal., Cell Stress Chaperones. 2014 Nov;19(6):801-12. doi: 10.1007/s12192-014-0504-9. Epub 2014 Mar 4.
17. Neonatal capsaicin treatment in rats affects TRPV1-related noxious heat sensation and circadian body temperature rhythm. Jeong KY and Seong J, J Neurol Sci. 2014 Jun 15;341(1-2):58-63. doi: 10.1016/j.jns.2014.03.054. Epub 2014 Apr 3.
18. Increased heat shock transcription factor 1 in the cerebellum reverses the deficiency of Purkinje cells in Alzheimer's disease. Jiang YQ, etal., Brain Res. 2013 Jun 26;1519:105-11. doi: 10.1016/j.brainres.2013.04.059. Epub 2013 May 9.
19. Hypothermia and rewarming induce gene expression and multiplication of cells in healthy rat prostate tissue. Kaija H, etal., PLoS One. 2015 May 21;10(5):e0127854. doi: 10.1371/journal.pone.0127854. eCollection 2015.
20. The effect of glutamine on cerebral ischaemic injury after cardiac arrest. Kim KS, etal., Resuscitation. 2013 Sep;84(9):1285-90. doi: 10.1016/j.resuscitation.2013.03.019. Epub 2013 Mar 22.
21. The heat shock paradox and cardiac myocytes: role of heat shock factor. Kobba S, etal., Shock. 2011 May;35(5):478-84. doi: 10.1097/SHK.0b013e3182094a0b.
22. The role of heat shock protein 70 in the protective effect of YC-1 on heat stroke rats. Lam KK, etal., Eur J Pharmacol. 2013 Jan 15;699(1-3):67-73. doi: 10.1016/j.ejphar.2012.11.044. Epub 2012 Dec 5.
23. Biphasic stress response in the soleus during reloading after hind limb unloading. Lawler JM, etal., Med Sci Sports Exerc. 2012 Apr;44(4):600-9. doi: 10.1249/MSS.0b013e31823ab37a.
24. Amlodipine besylate and amlodipine camsylate prevent cortical neuronal cell death induced by oxidative stress. Lee YJ, etal., J Neurochem. 2011 Dec;119(6):1262-70. doi: 10.1111/j.1471-4159.2011.07529.x. Epub 2011 Nov 3.
25. P53 is transported into the nucleus via an Hsf1-dependent nuclear localization mechanism. Li Q and Martinez JD, Mol Carcinog. 2011 Feb;50(2):143-52. doi: 10.1002/mc.20713. Epub 2010 Dec 10.
26. The therapeutic efficacy of glutamine for rats with smoking inhalation injury. Li W, etal., Int Immunopharmacol. 2013 Jun;16(2):248-53. doi: 10.1016/j.intimp.2013.02.022. Epub 2013 Mar 14.
27. Expression of Hsf1, Hsf2, and Phlda1 in cells undergoing cryptorchid-induced apoptosis in rat testes. Liu F, etal., Mol Reprod Dev. 2011 Apr;78(4):283-91. doi: 10.1002/mrd.21304. Epub 2011 Apr 8.
28. Heat stress activates ER stress signals which suppress the heat shock response, an effect occurring preferentially in the cortex in rats. Liu Y, etal., Mol Biol Rep. 2012 Apr;39(4):3987-93. doi: 10.1007/s11033-011-1179-2. Epub 2011 Jul 21.
29. RNA interference may suppress stress granule formation by preventing argonaute 2 recruitment. Lou Q, etal., Am J Physiol Cell Physiol. 2019 Jan 1;316(1):C81-C91. doi: 10.1152/ajpcell.00251.2018. Epub 2018 Nov 7.
30. Association of Stat3 with HSF1 plays a critical role in G-CSF-induced cardio-protection against ischemia/reperfusion injury. Ma H, etal., J Mol Cell Cardiol. 2012 Jun;52(6):1282-90. doi: 10.1016/j.yjmcc.2012.02.011. Epub 2012 Mar 6.
31. Celastrol Protects against Obesity and Metabolic Dysfunction through Activation of a HSF1-PGC1alpha Transcriptional Axis. Ma X, etal., Cell Metab. 2015 Oct 6;22(4):695-708. doi: 10.1016/j.cmet.2015.08.005. Epub 2015 Sep 3.
32. Dexamethasone induces heat shock response and slows down disease progression in mouse and fly models of Huntington's disease. Maheshwari M, etal., Hum Mol Genet. 2014 May 15;23(10):2737-51. doi: 10.1093/hmg/ddt667. Epub 2013 Dec 30.
33. Possible involvement of HSP90-HSF1 multichaperone complex in impairment of HSP72 induction in the failing heart following myocardial infarction in rats. Marunouchi T, etal., J Pharmacol Sci. 2013;123(4):336-46. Epub 2013 Nov 27.
34. Exposure of Wistar rats to 24-h psycho-social stress alters gene expression in the inferior colliculus. Mazurek B, etal., Neurosci Lett. 2012 Oct 3;527(1):40-5. doi: 10.1016/j.neulet.2012.08.019. Epub 2012 Aug 17.
35. Methyl-deficient diet promotes colitis and SIRT1-mediated endoplasmic reticulum stress. Melhem H, etal., Gut. 2015 Jan 20. pii: gutjnl-2014-307030. doi: 10.1136/gutjnl-2014-307030.
36. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
37. Whey protein hydrolysate enhances HSP90 but does not alter HSP60 and HSP25 in skeletal muscle of rats. Moura CS, etal., PLoS One. 2014 Jan 20;9(1):e83437. doi: 10.1371/journal.pone.0083437. eCollection 2014.
38. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
39. Fibronectin-integrin signaling is required for L-glutamine's protection against gut injury. Niederlechner S, etal., PLoS One. 2012;7(11):e50185. doi: 10.1371/journal.pone.0050185. Epub 2012 Nov 20.
40. The activation of heat shock transcription factor 1 is differentially regulated in the brain of estrogen- and testosterone-treated heat-shocked rats. Papasozomenos SCh and Papasozomenos H, J Alzheimers Dis. 2008 Nov;15(3):375-90.
41. Redox signaling of cardiac HSF1 DNA binding. Paroo Z, etal., Am J Physiol Cell Physiol 2002 Aug;283(2):C404-11.
42. L-glutamine supplementations enhance liver glutamine-glutathione axis and heat shock factor-1 expression in endurance-exercise trained rats. Petry ER, etal., Int J Sport Nutr Exerc Metab. 2015 Apr;25(2):188-97. doi: 10.1123/ijsnem.2014-0131. Epub 2014 Sep 8.
43. [Effect of microwave irradiation on expression of heat shock proteins family in primary cultured rat hippocampal neurons]. Qu MY, etal., Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi. 2010 Dec;28(12):909-13.
44. GOA pipeline RGD automated data pipeline
45. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
46. 17beta-Estradiol, aging, inflammation, and the stress response in the female heart. Stice JP, etal., Endocrinology. 2011 Apr;152(4):1589-98. doi: 10.1210/en.2010-0627. Epub 2011 Feb 8.
47. Development-dependent regulation of molecular chaperones after hypoxia-ischemia. Sun X, etal., Neurobiol Dis. 2015 Jun 9;82:123-131. doi: 10.1016/j.nbd.2015.06.001.
48. Gastric ulcers induced by systemic hypoxia. Syam AF, etal., Acta Med Indones. 2011 Oct;43(4):243-8.
49. The induction levels of heat shock protein 70 differentiate the vulnerabilities to mutant huntingtin among neuronal subtypes. Tagawa K, etal., J Neurosci. 2007 Jan 24;27(4):868-80.
50. Modulatory effects of sodium salicylate on the factors affecting protein aggregation during rotenone induced Parkinson's disease pathology. Thakur P and Nehru B, Neurochem Int. 2014 Sep;75:1-10. doi: 10.1016/j.neuint.2014.05.002. Epub 2014 May 19.
51. Long-term heat shock proteins (HSPs) induction by carbenoxolone improves hallmark features of Parkinson's disease in a rotenone-based model. Thakur P and Nehru B, Neuropharmacology. 2014 Apr;79:190-200. doi: 10.1016/j.neuropharm.2013.11.016. Epub 2013 Dec 1.
52. HSF1 protects neurons through a novel trimerization- and HSP-independent mechanism. Verma P, etal., J Neurosci. 2014 Jan 29;34(5):1599-612. doi: 10.1523/JNEUROSCI.3039-13.2014.
53. The systemic amyloid precursor transthyretin (TTR) behaves as a neuronal stress protein regulated by HSF1 in SH-SY5Y human neuroblastoma cells and APP23 Alzheimer's disease model mice. Wang X, etal., J Neurosci. 2014 May 21;34(21):7253-65. doi: 10.1523/JNEUROSCI.4936-13.2014.
54. Celastrol prevents circulatory failure via induction of heme oxygenase-1 and heat shock protein 70 in endotoxemic rats. Wang YL, etal., J Ethnopharmacol. 2015 Mar 13;162:168-75. doi: 10.1016/j.jep.2014.12.062. Epub 2015 Jan 5.
55. HSF1 and NF-kappaB p65 participate in the process of exercise preconditioning attenuating pressure overload-induced pathological cardiac hypertrophy. Xu T, etal., Biochem Biophys Res Commun. 2015 May 8;460(3):622-7. doi: 10.1016/j.bbrc.2015.03.079. Epub 2015 Mar 21.
56. Glutamine-mediated dual regulation of heat shock transcription factor-1 activation and expression. Xue H, etal., J Biol Chem. 2012 Nov 23;287(48):40400-13. doi: 10.1074/jbc.M112.410712. Epub 2012 Oct 10.
57. Protective HSP70 Induction by Z-Ligustilide against Oxygen-Glucose Deprivation Injury via Activation of the MAPK Pathway but Not of HSF1. Yu J, etal., Biol Pharm Bull. 2015 Oct 1;38(10):1564-72. doi: 10.1248/bpb.b15-00352. Epub 2015 Jul 22.
58. Protein kinase A regulates molecular chaperone transcription and protein aggregation. Zhang Y, etal., PLoS One. 2011;6(12):e28950. doi: 10.1371/journal.pone.0028950. Epub 2011 Dec 22.
59. Involvement of fibrinolytic regulators in adhesion of monocytes to vascular endothelial cells induced by glycated LDL and to aorta from diabetic mice. Zhao R, etal., J Leukoc Biol. 2014 Jun;95(6):941-9. doi: 10.1189/jlb.0513262. Epub 2014 Feb 4.
Additional References at PubMed
PMID:7760831   PMID:7935471   PMID:8455624   PMID:8926278   PMID:9222587   PMID:9341107   PMID:9499401   PMID:9727490   PMID:10359787   PMID:10413683   PMID:10545106   PMID:10561509  
PMID:10747973   PMID:11032181   PMID:11514557   PMID:11583998   PMID:12659875   PMID:12665592   PMID:12917326   PMID:14707147   PMID:14766729   PMID:14994269   PMID:15016915   PMID:15483628  
PMID:15877948   PMID:16278218   PMID:16554823   PMID:16889897   PMID:16990482   PMID:17095722   PMID:17536178   PMID:17589386   PMID:17785525   PMID:17897941   PMID:18242848   PMID:18398426  
PMID:18434628   PMID:18755693   PMID:18794143   PMID:19910575   PMID:20426530   PMID:21085490   PMID:21098017   PMID:21597468   PMID:21690297   PMID:22246807   PMID:23587726   PMID:23769970  
PMID:23902977   PMID:24065656   PMID:25109347   PMID:25963659   PMID:26159920   PMID:26251235   PMID:26359349   PMID:26436502   PMID:26719858   PMID:26727490   PMID:26754925   PMID:27216364  
PMID:28383811   PMID:29257252   PMID:29997244   PMID:30143534   PMID:30467350   PMID:31522994   PMID:32457290   PMID:33989081   PMID:34530848   PMID:36741074  


Genomics

Comparative Map Data
Hsf1
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr87110,076,710 - 110,103,665 (+)NCBIGRCr8GRCr8GRCr8
GRCr8 Ensembl7110,076,710 - 110,103,665 (+)EnsemblGRCr8
mRatBN7.27108,196,040 - 108,223,011 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl7108,196,056 - 108,223,011 (+)EnsemblmRatBN7.2
UTH_Rnor_SHR_Utx7109,940,443 - 109,967,383 (+)NCBIUTH_Rnor_SHR_UtxUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.07112,164,140 - 112,191,080 (+)NCBIUTH_Rnor_SHRSP_BbbUtx_1.0UTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.07112,122,490 - 112,149,447 (+)NCBIUTH_Rnor_WKY_Bbb_1.0UTH_Rnor_WKY_Bbb_1.0
Rnor_6.07117,538,523 - 117,565,478 (+)NCBIRnor_6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl7117,538,523 - 117,565,478 (+)Ensemblrn6Rnor6.0
Rnor_5.07117,526,154 - 117,553,109 (+)NCBIRnor_5.0Rnor_5.0rn5
RGSC_v3.47114,524,211 - 114,551,166 (+)NCBIRGSC_v3.4RGSC_v3.4rn4
Celera7104,547,683 - 104,574,508 (+)NCBICelera
RGSC_v3.17114,580,681 - 114,585,056 (+)NCBI
Cytogenetic Map7q34NCBI
HSF1
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh388144,291,604 - 144,314,720 (+)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl8144,291,529 - 144,314,727 (+)Ensemblhg38GRCh38
GRCh378145,515,286 - 145,538,383 (+)NCBIGRCh37GRCh37hg19GRCh37
Build 368145,486,078 - 145,509,193 (+)NCBIBuild 36Build 36hg18NCBI36
Build 348145,486,090 - 145,509,187NCBI
Celera8141,707,360 - 141,713,153 (+)NCBICelera
Cytogenetic Map8q24.3NCBI
HuRef8140,629,839 - 140,652,904 (+)NCBIHuRef
CHM1_18145,553,452 - 145,576,661 (+)NCBICHM1_1
T2T-CHM13v2.08145,460,056 - 145,483,355 (+)NCBIT2T-CHM13v2.0
Hsf1
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm391576,361,562 - 76,385,355 (+)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl1576,361,622 - 76,386,113 (+)EnsemblGRCm39 EnsemblGRCm39
GRCm381576,477,362 - 76,501,155 (+)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl1576,477,422 - 76,501,913 (+)Ensemblmm10GRCm38
MGSCv371576,307,875 - 76,331,402 (+)NCBIMGSCv37MGSCv37mm9NCBIm37
MGSCv361576,304,700 - 76,328,227 (+)NCBIMGSCv36mm8
Celera1577,977,956 - 78,001,512 (+)NCBICelera
Cytogenetic Map15D3NCBI
cM Map1535.95NCBI
Hsf1
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_0049554542,907,265 - 2,932,351 (+)Ensembl
ChiLan1.0NW_0049554542,907,265 - 2,932,352 (+)NCBIChiLan1.0ChiLan1.0
HSF1
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1-v27161,778,661 - 161,801,822 (+)NCBINHGRI_mPanPan1-v2
NHGRI_mPanPan18137,308,606 - 137,331,773 (+)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v08141,055,310 - 141,078,360 (+)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.18144,062,137 - 144,067,725 (+)NCBIPanPan1.1PanPan1.1panPan2
PanPan1.1 Ensembl8144,062,137 - 144,067,866 (+)EnsemblpanPan2panpan1.1
HSF1
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.11337,724,741 - 37,745,259 (+)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl1337,724,759 - 37,745,252 (+)EnsemblcanFam3CanFam3.1
Dog10K_Boxer_Tasha1337,688,336 - 37,708,839 (+)NCBIDog10K_Boxer_TashaDog10K_Boxer_Tasha
ROS_Cfam_1.01338,200,982 - 38,221,480 (+)NCBIROS_Cfam_1.0ROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl1338,200,916 - 38,221,478 (+)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.11337,893,218 - 37,913,632 (+)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.01338,001,763 - 38,022,270 (+)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.01338,478,086 - 38,498,596 (+)NCBIUU_Cfam_GSD_1.0UU_Cfam_GSD_1.0
Hsf1
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_024405303501,635 - 524,700 (-)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_0049364707,928,095 - 7,933,337 (-)EnsemblSpeTri2.0 Ensembl
SpeTri2.0NW_0049364707,927,734 - 7,950,805 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
HSF1
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl4463,393 - 486,473 (-)EnsemblsusScr11Sscrofa11.1
Sscrofa11.14463,531 - 486,483 (-)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.24610,323 - 633,482 (-)NCBISscrofa10.2Sscrofa10.2susScr3
HSF1
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.18138,503,836 - 138,529,562 (+)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl8138,503,831 - 138,529,165 (+)EnsemblChlSab1.1 EnsemblchlSab2Vervet-AGM
Vero_WHO_p1.0NW_0236660391,334,097 - 1,360,855 (-)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Hsf1
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_00462473512,537,128 - 12,562,644 (-)EnsemblHetGla_female_1.0 EnsemblhetGla2HetGla_female_1.0 Ensembl
HetGla 1.0NW_00462473512,536,818 - 12,562,643 (-)NCBIHetGla 1.0HetGla 1.0hetGla2
Hsf1
(Rattus rattus - black rat)
Black Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Rrattus_CSIRO_v11248,809,178 - 248,834,596 (+)NCBIRrattus_CSIRO_v1

Variants

.
Variants in Hsf1
231 total Variants
miRNA Target Status (No longer updated)

Predicted Target Of
Summary Value
Count of predictions:73
Count of miRNA genes:60
Interacting mature miRNAs:69
Transcripts:ENSRNOT00000050108
Prediction methods:Miranda, Rnahybrid, Targetscan
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (http://mirgate.bioinfo.cnio.es/).
For more information about miRGate, see PMID:25858286 or access the full paper here.


QTLs in Region (GRCr8)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
1300179Kidm5Kidney mass QTL 53.51kidney mass (VT:0002707)left kidney wet weight (CMO:0000083)792388565119280177Rat
1331728Bp214Blood pressure QTL 2142.825arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)782111245123048330Rat
1331731Bp216Blood pressure QTL 2162.851arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)7104186212135371468Rat
1358361Sradr5Stress Responsive Adrenal Weight QTL 55.55adrenal gland mass (VT:0010420)both adrenal glands wet weight (CMO:0000164)731770293110435881Rat
1357338Stl17Serum triglyceride level QTL 173.23blood triglyceride amount (VT:0002644)serum triglyceride level (CMO:0000360)771621154114982716Rat
70159Bp61Blood pressure QTL 610.0001arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)773618702118618702Rat
631687Hcas1Hepatocarcinoma susceptibility QTL 13.90.001liver integrity trait (VT:0010547)liver tumorous lesion volume to total liver volume ratio (CMO:0001082)793302009131686183Rat
61397Bw17Body weight QTL 176.3body mass (VT:0001259)body weight (CMO:0000012)795485047137014596Rat
631504Cm27Cardiac mass QTL 273.45heart left ventricle mass (VT:0007031)heart left ventricle wet weight (CMO:0000071)746307490127866166Rat
634322Bw12Body weight QTL 120body mass (VT:0001259)body weight (CMO:0000012)785043242130043242Rat
70173Niddm19Non-insulin dependent diabetes mellitus QTL 194.330.00005blood glucose amount (VT:0000188)blood glucose level area under curve (AUC) (CMO:0000350)785497398130497398Rat
1549899Stresp8Stress response QTL 84.370.0008stress-related behavior trait (VT:0010451)defensive burying duration (CMO:0001961)792362341137014596Rat
2317052Aia17Adjuvant induced arthritis QTL 172.13joint integrity trait (VT:0010548)left rear ankle joint diameter (CMO:0002149)783626689128626689Rat
1331723Bw25Body weight QTL 253.348body mass (VT:0001259)body weight (CMO:0000012)796700404111672180Rat
631529Tls2T-lymphoma susceptibility QTL 200.001thymus integrity trait (VT:0010555)percentage of study population developing T-cell lymphomas during a period of time (CMO:0001911)782111382132099989Rat
731176Glom5Glomerulus QTL 52.50.0035kidney glomerulus morphology trait (VT:0005325)count of superficial glomeruli not directly contacting the kidney surface (CMO:0001002)798549867137014596Rat
7411607Foco15Food consumption QTL 150.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)777807807122807807Rat
631201Panci1Pancreas inflammation QTL 100.001pancreas integrity trait (VT:0010560)percentage of study population displaying chronic pancreatitis at a point in time (CMO:0001214)773557047118557047Rat
634336Anxrr17Anxiety related response QTL 173.66locomotor behavior trait (VT:0001392)number of entries into a discrete space in an experimental apparatus (CMO:0000960)71509236116977875Rat
1331768Kidm10Kidney mass QTL 104.62096kidney mass (VT:0002707)left kidney wet weight (CMO:0000083)782111245123048330Rat
61357Bp38Blood pressure QTL 381.60.052arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)740540077123682549Rat
2313102Bmd79Bone mineral density QTL 792.30.0001tibia mineral mass (VT:1000283)total volumetric bone mineral density (CMO:0001728)796700404118618702Rat
2316947Rf58Renal function QTL 587.8kidney glomerulus morphology trait (VT:0005325)index of glomerular damage (CMO:0001135)749682832115766396Rat
10450862Kidm55Kidney mass QTL 554.9kidney mass (VT:0002707)kidney weight (CMO:0000081)772725037117725037Rat
61428Scl3Serum cholesterol level QTL 33.2blood cholesterol amount (VT:0000180)serum total cholesterol level (CMO:0000363)7100548246137014596Rat
1331746Kidm9Kidney mass QTL 93.934kidney mass (VT:0002707)right kidney wet weight (CMO:0000082)782111245134948181Rat
10450856Livw4Liver weight QTL 43.8liver mass (VT:0003402)liver weight (CMO:0000092)772725037117725037Rat
7411654Foco25Food consumption QTL 259.30.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)777807807122807807Rat
2316955Stl24Serum triglyceride level QTL 247.1blood triglyceride amount (VT:0002644)plasma triglyceride level (CMO:0000548)749682832115766396Rat
10402855Bp379Blood pressure QTL 3790.21arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)778682549123682549Rat
2316952Pur22Proteinuria QTL 225.2urine protein amount (VT:0005160)urine protein level (CMO:0000591)749682832115766396Rat
631540Bw9Body weight QTL 94.5body mass (VT:0001259)body weight (CMO:0000012)771621154119349044Rat
1358891Bp265Blood pressure QTL 2652.21arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)771827901136544683Rat

Markers in Region
Hsf1  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr87110,100,693 - 110,100,991 (+)Marker Load Pipeline
mRatBN7.27108,220,039 - 108,220,337 (+)MAPPERmRatBN7.2
Rnor_6.07117,562,507 - 117,562,804NCBIRnor6.0
Rnor_5.07117,550,138 - 117,550,435UniSTSRnor5.0
Celera7104,571,538 - 104,571,835UniSTS
Cytogenetic Map7q34UniSTS


Expression

RNA-SEQ Expression

alimentary part of gastrointestinal system
appendage
circulatory system
ectoderm
endocrine system
endoderm
exocrine system
hemolymphoid system
hepatobiliary system
integumental system
mesenchyme
mesoderm
musculoskeletal system
nervous system
renal system
reproductive system
respiratory system
sensory system
visual system
16 12 67 163 91 90 59 92 59 6 356 192 11 142 81 92 31 17 17

Sequence


Ensembl Acc Id: ENSRNOT00000050108   ⟹   ENSRNOP00000047030
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8 Ensembl7110,076,710 - 110,103,665 (+)Ensembl
mRatBN7.2 Ensembl7108,196,056 - 108,223,011 (+)Ensembl
Rnor_6.0 Ensembl7117,538,523 - 117,565,478 (+)Ensembl
Ensembl Acc Id: ENSRNOT00000098804   ⟹   ENSRNOP00000091032
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl7108,196,056 - 108,222,720 (+)Ensembl
Ensembl Acc Id: ENSRNOT00000101096   ⟹   ENSRNOP00000090341
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8 Ensembl7110,076,727 - 110,103,375 (+)Ensembl
mRatBN7.2 Ensembl7108,196,056 - 108,223,011 (+)Ensembl
Ensembl Acc Id: ENSRNOT00000106601   ⟹   ENSRNOP00000076751
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8 Ensembl7110,076,727 - 110,103,375 (+)Ensembl
mRatBN7.2 Ensembl7108,217,511 - 108,223,011 (+)Ensembl
RefSeq Acc Id: NM_024393   ⟹   NP_077369
RefSeq Status: VALIDATED
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr87110,076,710 - 110,103,665 (+)NCBI
mRatBN7.27108,196,056 - 108,223,011 (+)NCBI
Rnor_6.07117,538,523 - 117,565,478 (+)NCBI
Rnor_5.07117,526,154 - 117,553,109 (+)NCBI
RGSC_v3.47114,524,211 - 114,551,166 (+)RGD
Celera7104,547,683 - 104,574,508 (+)RGD
Sequence:
RefSeq Acc Id: XM_006241888   ⟹   XP_006241950
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr87110,076,890 - 110,103,376 (+)NCBI
mRatBN7.27108,196,042 - 108,222,779 (+)NCBI
Rnor_6.07117,538,538 - 117,565,246 (+)NCBI
Rnor_5.07117,526,154 - 117,553,109 (+)NCBI
Sequence:
RefSeq Acc Id: XM_006241889   ⟹   XP_006241951
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr87110,076,890 - 110,103,433 (+)NCBI
mRatBN7.27108,196,040 - 108,222,671 (+)NCBI
Rnor_6.07117,538,537 - 117,565,246 (+)NCBI
Rnor_5.07117,526,154 - 117,553,109 (+)NCBI
Sequence:
RefSeq Acc Id: XM_006241890   ⟹   XP_006241952
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr87110,076,890 - 110,103,376 (+)NCBI
mRatBN7.27108,196,042 - 108,222,779 (+)NCBI
Rnor_6.07117,538,538 - 117,565,246 (+)NCBI
Rnor_5.07117,526,154 - 117,553,109 (+)NCBI
Sequence:
RefSeq Acc Id: XM_006241891   ⟹   XP_006241953
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr87110,076,890 - 110,103,376 (+)NCBI
mRatBN7.27108,196,043 - 108,222,779 (+)NCBI
Rnor_6.07117,538,539 - 117,565,246 (+)NCBI
Rnor_5.07117,526,154 - 117,553,109 (+)NCBI
Sequence:
RefSeq Acc Id: XM_063264288   ⟹   XP_063120358
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr87110,076,890 - 110,103,376 (+)NCBI
RefSeq Acc Id: XM_063264289   ⟹   XP_063120359
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr87110,076,890 - 110,103,376 (+)NCBI
RefSeq Acc Id: NP_077369   ⟸   NM_024393
- UniProtKB: A0A8I5Y5J6 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: XP_006241951   ⟸   XM_006241889
- Peptide Label: isoform X2
- UniProtKB: A0A8I5Y5J6 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: XP_006241950   ⟸   XM_006241888
- Peptide Label: isoform X1
- UniProtKB: F1MAF1 (UniProtKB/TrEMBL),   A0A8I5Y5J6 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: XP_006241952   ⟸   XM_006241890
- Peptide Label: isoform X3
- UniProtKB: A0A8I6AMW4 (UniProtKB/TrEMBL),   A0A8I5Y5J6 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: XP_006241953   ⟸   XM_006241891
- Peptide Label: isoform X5
- UniProtKB: A0A8I5Y5J6 (UniProtKB/TrEMBL)
- Sequence:
Ensembl Acc Id: ENSRNOP00000047030   ⟸   ENSRNOT00000050108
Ensembl Acc Id: ENSRNOP00000090341   ⟸   ENSRNOT00000101096
Ensembl Acc Id: ENSRNOP00000091032   ⟸   ENSRNOT00000098804
Ensembl Acc Id: ENSRNOP00000076751   ⟸   ENSRNOT00000106601
RefSeq Acc Id: XP_063120358   ⟸   XM_063264288
- Peptide Label: isoform X4
- UniProtKB: A0A8I5Y5J6 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063120359   ⟸   XM_063264289
- Peptide Label: isoform X6
- UniProtKB: A0A8I5Y5J6 (UniProtKB/TrEMBL)
Protein Domains
HSF-type DNA-binding   Vertebrate heat shock transcription factor C-

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-F1MAF1-F1-model_v2 AlphaFold F1MAF1 1-525 view protein structure

Transcriptome

eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen

Promoters
RGD ID:13695425
Promoter ID:EPDNEW_R5948
Type:initiation region
Name:Hsf1_1
Description:heat shock transcription factor 1
SO ACC ID:SO:0000170
Source:EPDNEW (Eukaryotic Promoter Database, http://epd.vital-it.ch/)
Experiment Methods:Single-end sequencing.
Position:
Rat AssemblyChrPosition (strand)Source
Rnor_6.07117,538,570 - 117,538,630EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:620913 AgrOrtholog
BioCyc Gene G2FUF-32926 BioCyc
Ensembl Genes ENSRNOG00000021732 Ensembl, ENTREZGENE, UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000050108 ENTREZGENE
  ENSRNOT00000050108.5 UniProtKB/TrEMBL
  ENSRNOT00000101096 ENTREZGENE
  ENSRNOT00000101096.2 UniProtKB/TrEMBL
  ENSRNOT00000106601 ENTREZGENE
  ENSRNOT00000106601.2 UniProtKB/TrEMBL
Gene3D-CATH 1.10.10.10 UniProtKB/TrEMBL
InterPro HSF_DNA-bd UniProtKB/TrEMBL
  Vert_HS_TF UniProtKB/TrEMBL
  WH-like_DNA-bd_sf UniProtKB/TrEMBL
  WH_DNA-bd_sf UniProtKB/TrEMBL
NCBI Gene 79245 ENTREZGENE
PANTHER HEAT SHOCK FACTOR PROTEIN 1 UniProtKB/TrEMBL
  PTHR10015 UniProtKB/TrEMBL
Pfam HSF_DNA-bind UniProtKB/TrEMBL
  Vert_HS_TF UniProtKB/TrEMBL
PhenoGen Hsf1 PhenoGen
PRINTS HSFDOMAIN UniProtKB/TrEMBL
PROSITE HSF_DOMAIN UniProtKB/TrEMBL
RatGTEx ENSRNOG00000021732 RatGTEx
SMART HSF UniProtKB/TrEMBL
Superfamily-SCOP SSF46785 UniProtKB/TrEMBL
UniProt A0A8I5Y5J6 ENTREZGENE, UniProtKB/TrEMBL
  A0A8I6AMW4 ENTREZGENE, UniProtKB/TrEMBL
  F1MAF1 ENTREZGENE, UniProtKB/TrEMBL
  Q63717_RAT UniProtKB/TrEMBL


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2004-02-26 Hsf1  heat shock transcription factor 1      Symbol and Name status set to approved 625702 APPROVED
2002-08-07 Hsf1  heat shock transcription factor 1      Symbol and Name status set to provisional 70820 PROVISIONAL

RGD Curation Notes
Note Type Note Reference
gene_regulation activated by hyperphosphorylation following heat shock 708322
gene_regulation heat shock and exercise promotes Hsf1-heat shock element (HSE) DNA binding in the myocardium in the absence of changes in reduced glutathione (GSH) 625653