Hspa8 (heat shock protein family A (Hsp70) member 8) - Rat Genome Database

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Gene: Hspa8 (heat shock protein family A (Hsp70) member 8) Rattus norvegicus
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Symbol: Hspa8
Name: heat shock protein family A (Hsp70) member 8
RGD ID: 621725
Description: Enables several functions, including A1 adenosine receptor binding activity; ATP hydrolysis activity; and adenyl ribonucleotide binding activity. Involved in several processes, including brain development; establishment of protein localization to organelle; and protein-containing complex disassembly. Acts upstream of or within protein-containing complex disassembly. Located in several cellular components, including dendrite; polymeric cytoskeletal fiber; and vacuole. Part of messenger ribonucleoprotein complex. Is active in several cellular components, including glutamatergic synapse; glycinergic synapse; and postsynaptic density. Biomarker of Parkinson's disease; acute kidney failure; brain ischemia (multiple); disease of metabolism; and graft-versus-host disease. Human ortholog(s) of this gene implicated in Parkinson's disease and renal hypertension. Orthologous to human HSPA8 (heat shock protein family A (Hsp70) member 8); PARTICIPATES IN androgen signaling pathway; chaperone mediated autophagy pathway; clathrin-dependent synaptic vesicle endocytosis; INTERACTS WITH (+)-schisandrin B; (R)-adrenaline; 1,1,1-Trichloro-2-(o-chlorophenyl)-2-(p-chlorophenyl)ethane.
Type: protein-coding
RefSeq Status: VALIDATED
Previously known as: heat shock 70 kDa protein 8; heat shock 70kD protein 8; heat shock 70kDa protein 8; heat shock cognate 71 kDa protein; Heat shock cognate protein 70; heat shock protein 8; heat shock protein A8; Hsc70; MGC114311
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Alliance Genes
More Info more info ...
Related Pseudogenes: Hspa8-ps1   Hspa8-ps14  
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
NCBI Annotation Information: Note: The functional gene for Hspa8 is located on Rno8. It was incorrectly placed on Rno5 on the reference assembly for NCBI Build 4.1 at the location of one of its pseudogenes. The correct GeneID for the pseudogene is geneID:100190885. [17 Jun 2014]
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.2841,183,397 - 41,187,260 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl841,183,264 - 41,187,259 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx846,682,619 - 46,686,480 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0844,961,220 - 44,965,081 (+)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0842,828,805 - 42,832,666 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0844,989,401 - 44,993,261 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl844,990,014 - 44,993,179 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0843,478,238 - 43,480,456 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
Rnor_5.0846,005,304 - 46,006,864 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4843,784,035 - 43,787,760 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1843,792,829 - 43,796,525 (+)NCBI
Celera840,782,916 - 40,786,778 (+)NCBICelera
Cytogenetic Map8q22NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(+)-schisandrin B  (EXP)
(-)-alpha-phellandrene  (ISO)
(2,4,5-trichlorophenoxy)acetic acid  (ISO)
(R)-adrenaline  (EXP)
(S)-amphetamine  (ISO)
1,1,1-Trichloro-2-(o-chlorophenyl)-2-(p-chlorophenyl)ethane  (EXP,ISO)
1,2-dimethylhydrazine  (ISO)
1-chloro-2,4-dinitrobenzene  (ISO)
1-naphthyl isothiocyanate  (EXP)
17alpha-ethynylestradiol  (EXP,ISO)
17beta-estradiol  (ISO)
17beta-estradiol 3-benzoate  (EXP)
1H-pyrazole  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,4,6-trinitrotoluene  (EXP)
2,4-dibromophenyl 2,4,5-tribromophenyl ether  (EXP,ISO)
2,4-dinitrotoluene  (EXP)
2-hydroxypropanoic acid  (ISO)
2-methylcholine  (ISO)
3'-amino-3'-deoxy-N(6),N(6)-dimethyladenosine  (EXP)
3,3',4,4',5-pentachlorobiphenyl  (EXP)
3,4-methylenedioxymethamphetamine  (ISO)
3-chloropropane-1,2-diol  (EXP)
3-methylcholanthrene  (EXP)
3-phenylprop-2-enal  (ISO)
4,4'-sulfonyldiphenol  (ISO)
4-amino-2,6-dinitrotoluene  (EXP)
4-hydroxyphenyl retinamide  (ISO)
5-aza-2'-deoxycytidine  (ISO)
5-fluorouracil  (ISO)
6-propyl-2-thiouracil  (EXP)
7,12-dimethyltetraphene  (ISO)
7H-xanthine  (EXP)
8-Br-cAMP  (ISO)
9H-xanthine  (EXP)
acrolein  (ISO)
acrylamide  (EXP,ISO)
afimoxifene  (ISO)
albendazole  (ISO)
aldrin  (ISO)
all-trans-retinoic acid  (ISO)
alpha-naphthoflavone  (EXP)
alpha-phellandrene  (ISO)
alpha-pinene  (ISO)
AM-251  (ISO)
ammonium chloride  (EXP)
amphibole asbestos  (ISO)
amphotericin B  (ISO)
antimonite  (ISO)
apigenin  (ISO)
Aroclor 1254  (ISO)
arsane  (ISO)
arsenic atom  (ISO)
arsenite(3-)  (ISO)
arsenous acid  (ISO)
astemizole  (EXP)
atrazine  (ISO)
azoxystrobin  (ISO)
bathocuproine disulfonic acid  (ISO)
benzene  (ISO)
benzo[a]pyrene  (ISO)
Benzo[ghi]perylene  (ISO)
bifenthrin  (ISO)
bis(2-chloroethyl) sulfide  (ISO)
bis(2-ethylhexyl) phthalate  (EXP,ISO)
bisphenol A  (EXP,ISO)
Bisphenol B  (ISO)
bisphenol F  (ISO)
bromobenzene  (EXP)
C60 fullerene  (EXP)
cadmium atom  (ISO)
cadmium dichloride  (ISO)
cadmium sulfate  (ISO)
cannabidiol  (ISO)
carbon nanotube  (ISO)
carbonyl cyanide p-trifluoromethoxyphenylhydrazone  (ISO)
casticin  (ISO)
ceruletide  (EXP)
CGP 52608  (ISO)
chlordecone  (ISO)
chloromethylisothiazolinone  (ISO)
chloropicrin  (ISO)
chloroprene  (ISO)
chloroquine  (ISO)
chlorpyrifos  (ISO)
choline  (ISO)
ciguatoxin CTX1B  (ISO)
cisplatin  (ISO)
cobalt dichloride  (EXP,ISO)
copper atom  (ISO)
copper(0)  (ISO)
copper(II) sulfate  (ISO)
coumarin  (ISO)
crocidolite asbestos  (ISO)
CU-O LINKAGE  (ISO)
Cuprizon  (ISO)
cyclophosphamide  (ISO)
cyclosporin A  (ISO)
deguelin  (ISO)
deoxynivalenol  (ISO)
dexamethasone  (ISO)
dextran sulfate  (ISO)
diallyl trisulfide  (ISO)
diarsenic trioxide  (ISO)
dibutyl phthalate  (ISO)
diclofenac  (EXP,ISO)
dicrotophos  (ISO)
diethyl maleate  (ISO)
dihydroartemisinin  (ISO)
dimethylarsinic acid  (ISO)
dioxygen  (ISO)
dipotassium bis[mu-tartrato(4-)]diantimonate(2-) trihydrate  (ISO)
disodium selenite  (ISO)
disulfiram  (ISO)
diuron  (EXP,ISO)
doxorubicin  (ISO)
endosulfan  (EXP)
enzyme inhibitor  (ISO)
ethanol  (EXP,ISO)
ethyl methanesulfonate  (ISO)
fenofibrate  (ISO)
fenvalerate  (EXP)
ferric oxide  (ISO)
flutamide  (EXP)
folic acid  (ISO)
folpet  (ISO)
formaldehyde  (ISO)
formetanate  (ISO)
fulvestrant  (ISO)
furan  (EXP,ISO)
gallic acid  (ISO)
gamma-poly(L-glutamic acid) macromolecule  (EXP)
gentamycin  (EXP)
glyphosate  (ISO)
gold atom  (ISO)
gold(0)  (ISO)
hyaluronic acid  (EXP)
hydralazine  (ISO)
hydrogen peroxide  (EXP,ISO)
hydroxyurea  (ISO)
ibuprofen  (ISO)
imipramine  (EXP)
Indeno[1,2,3-cd]pyrene  (ISO)
indometacin  (ISO)
iodide salt  (EXP)
ionomycin  (ISO)
iron atom  (EXP)
iron dichloride  (ISO)
iron(0)  (EXP)
isobutanol  (ISO)
isoprenaline  (ISO)
ivermectin  (ISO)
L-methionine  (ISO)
lead diacetate  (ISO)
leflunomide  (ISO)
Licochalcone B  (ISO)
lipopolysaccharide  (ISO)
lovastatin  (ISO)
maneb  (ISO)
manganese atom  (ISO)
manganese(0)  (ISO)
mercury dichloride  (ISO)
methamphetamine  (EXP)
methapyrilene  (EXP)
methomyl  (ISO)
methotrexate  (ISO)
methoxyacetic acid  (ISO)
methyl methanesulfonate  (ISO)
methylarsonic acid  (ISO)
microcystin-LR  (ISO)
mitomycin C  (ISO)
monocrotaline  (ISO)
morphine  (EXP)
N-benzyloxycarbonyl-L-leucyl-L-leucyl-L-leucinal  (ISO)
N-methylformamide  (ISO)
N-nitrosomorpholine  (EXP)
nefazodone  (EXP)
nickel atom  (EXP)
nickel dichloride  (EXP,ISO)
nimesulide  (EXP)
nitric oxide  (EXP)
nitrofurantoin  (EXP)
ochratoxin A  (EXP)
oxidopamine  (EXP,ISO)
ozone  (ISO)
p-toluidine  (EXP)
paracetamol  (ISO)
paraquat  (ISO)
pentachlorophenol  (ISO)
perfluorododecanoic acid  (EXP)
perfluorooctane-1-sulfonic acid  (EXP)
perfluorooctanoic acid  (EXP,ISO)
phenobarbital  (EXP,ISO)
phenytoin  (ISO)
PhIP  (EXP)
phlorizin  (ISO)
phorbol 13-acetate 12-myristate  (ISO)
phorone  (EXP)
pirimicarb  (ISO)
pirinixic acid  (EXP,ISO)
poly(I:C)  (EXP)
pregnenolone 16alpha-carbonitrile  (EXP)
progesterone  (EXP)
propiconazole  (ISO)
Propiverine  (EXP)
prostaglandin A1  (ISO)
pyrimidifen  (ISO)
pyrogallol  (ISO)
pyrrolidine dithiocarbamate  (ISO)
quercetin  (EXP,ISO)
quercitrin  (ISO)
quinolin-8-ol  (ISO)
quizartinib  (ISO)
rac-lactic acid  (ISO)
raloxifene  (ISO)
rifampicin  (ISO)
rotenone  (EXP,ISO)
S-butyl-DL-homocysteine (S,R)-sulfoximine  (EXP,ISO)
sarin  (EXP)
sertraline  (EXP,ISO)
sevoflurane  (EXP)
silicon dioxide  (ISO)
silver atom  (ISO)
silver(0)  (ISO)
simvastatin  (EXP)
sodium arsenate  (ISO)
sodium arsenite  (EXP,ISO)
sodium fluoride  (ISO)
T-2 toxin  (EXP)
tacrolimus hydrate  (EXP)
tamoxifen  (ISO)
testosterone  (EXP)
tetrachloromethane  (EXP)
tetraphene  (ISO)
thapsigargin  (EXP,ISO)
thifluzamide  (ISO)
thioacetamide  (EXP)
thiostrepton  (ISO)
thymol  (ISO)
thymol sulfate(1-)  (ISO)
titanium dioxide  (ISO)
triadimefon  (ISO)
tributylstannane  (ISO)
Tributyltin oxide  (EXP)
trichloroethene  (EXP,ISO)
triphenylstannane  (ISO)
triptonide  (ISO)
troglitazone  (ISO)
tungsten  (EXP)
tunicamycin  (ISO)
urethane  (ISO)
valproic acid  (EXP,ISO)
vorinostat  (ISO)
warfarin  (ISO)
Yessotoxin  (ISO)
zinc pyrithione  (ISO)
zinc sulfate  (ISO)

Gene Ontology Annotations     Click to see Annotation Detail View

Biological Process
ATP metabolic process  (ISO)
axo-dendritic transport  (IEP)
cellular response to cadmium ion  (IEP)
cellular response to heat  (IEP)
cellular response to hydrogen peroxide  (IEP)
cerebellum development  (IEP)
chaperone cofactor-dependent protein refolding  (IBA,IEA,ISO)
chaperone-mediated autophagy  (IDA,IGI)
chaperone-mediated autophagy translocation complex disassembly  (IBA,IDA)
chaperone-mediated protein folding  (IDA,ISO)
clathrin coat disassembly  (IBA,IDA,IEA,ISO)
estrous cycle  (IEP)
forebrain development  (IEP)
G1/S transition of mitotic cell cycle  (IEP)
kidney development  (IEP)
late endosomal microautophagy  (IBA,IEA,ISO)
maintenance of postsynaptic specialization structure  (EXP,IDA,IMP)
modulation by host of viral process  (ISO)
mRNA processing  (IEA)
negative regulation of cardiac muscle cell apoptotic process  (IMP)
negative regulation of DNA-templated transcription  (ISO,ISS)
negative regulation of NLRP3 inflammasome complex assembly  (ISO)
negative regulation of supramolecular fiber organization  (ISO)
positive regulation by host of viral genome replication  (IEA,ISO)
positive regulation of catalytic activity  (IMP)
positive regulation of gene expression  (IMP)
positive regulation of lysosomal membrane permeability  (IMP)
positive regulation of mRNA splicing, via spliceosome  (IEA,ISO)
positive regulation of phagocytosis  (IMP)
positive regulation of protein refolding  (IDA)
positive regulation of proteolysis  (IDA)
positive regulation of T cell mediated cytotoxicity  (IMP)
protein autophosphorylation  (IDA)
protein folding  (IEA,ISO)
protein import into nucleus  (IMP)
protein refolding  (IBA,ISO,ISS)
protein targeting to lysosome involved in chaperone-mediated autophagy  (IBA,ISO,ISS)
protein transmembrane import into intracellular organelle  (IEP)
protein-containing complex disassembly  (IMP)
regulation of cell cycle  (IEA,ISO)
regulation of postsynapse organization  (IEA,ISO)
regulation of protein complex stability  (IDA)
regulation of protein stability  (ISO)
response to activity  (IEP)
response to estradiol  (IEP)
response to ethanol  (IEP)
response to nickel cation  (IEP)
response to odorant  (IEP)
response to progesterone  (IEP)
response to starvation  (IEP)
response to xenobiotic stimulus  (IEP)
RNA splicing  (IEA)
skeletal muscle tissue development  (IEP)
slow axonal transport  (IBA,IEP)
synaptic vesicle uncoating  (IDA)

References

References - curated
# Reference Title Reference Citation
1. Chaperone-mediated autophagy markers in Parkinson disease brains. Alvarez-Erviti L, etal., Arch Neurol. 2010 Dec;67(12):1464-72. Epub 2010 Aug 9.
2. Antisense oligonucleotide to the 70-kDa heat shock cognate protein inhibits synthesis of myelin basic protein. Aquino DA, etal., Neurochem Res. 1996 Apr;21(4):417-22.
3. Chaperone-assisted selective autophagy is essential for muscle maintenance. Arndt V, etal., Curr Biol. 2010 Jan 26;20(2):143-8. doi: 10.1016/j.cub.2009.11.022. Epub 2010 Jan 7.
4. The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Bandyopadhyay U, etal., Mol Cell Biol. 2008 Sep;28(18):5747-63. doi: 10.1128/MCB.02070-07. Epub 2008 Jul 21.
5. Slow axonal transport of the cytosolic chaperonin CCT with Hsc73 and actin in motor neurons. Bourke GJ, etal., J Neurosci Res. 2002 Apr 1;68(1):29-35.
6. Essential role of the redox-sensitive kinase p66shc in determining energetic and oxidative status and cell fate in neuronal preconditioning. Brown JE, etal., J Neurosci. 2010 Apr 14;30(15):5242-52. doi: 10.1523/JNEUROSCI.6366-09.2010.
7. In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state. Calabrese V, etal., J Neurochem. 2007 May;101(3):709-17. Epub 2007 Jan 4.
8. Odorants as cell-type specific activators of a heat shock response in the rat olfactory mucosa. Carr VM, etal., J Comp Neurol. 2001 Apr 16;432(4):425-39.
9. Splicing and beyond: the many faces of the Prp19 complex. Chanarat S and Strasser K, Biochim Biophys Acta. 2013 Oct;1833(10):2126-34. doi: 10.1016/j.bbamcr.2013.05.023. Epub 2013 Jun 3.
10. The effect of mutating arginine-469 on the substrate binding and refolding activities of 70-kDa heat shock cognate protein. Chang TC, etal., Arch Biochem Biophys. 2001 Feb 1;386(1):30-6.
11. Association of heat shock proteins and neuronal membrane components with lipid rafts from the rat brain. Chen S, etal., J Neurosci Res. 2005 Aug 15;81(4):522-9.
12. Autoantibodies against HSP70 family proteins were detected in the cerebrospinal fluid from patients with multiple sclerosis. Chiba S, etal., J Neurol Sci. 2006 Feb 15;241(1-2):39-43. Epub 2005 Nov 21.
13. Chaperone-mediated autophagy: roles in disease and aging. Cuervo AM and Wong E, Cell Res. 2014 Jan;24(1):92-104. doi: 10.1038/cr.2013.153. Epub 2013 Nov 26.
14. A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. Cuervo AM, etal., J Biol Chem. 1997 Feb 28;272(9):5606-15.
15. Direct lysosomal uptake of alpha 2-microglobulin contributes to chemically induced nephropathy. Cuervo AM, etal., Kidney Int. 1999 Feb;55(2):529-45.
16. Constitutive expression of heat shock proteins Hsp90, Hsc70, Hsp70 and Hsp60 in neural and non-neural tissues of the rat during postnatal development. D'Souza SM and Brown IR, Cell Stress Chaperones. 1998 Sep;3(3):188-99.
17. Constitutive and inducible heat shock protein 70 immunoreactivity in the normal rat eye. Dean DO, etal., Invest Ophthalmol Vis Sci. 1999 Nov;40(12):2952-62.
18. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Demand J, etal., Mol Cell Biol 1998 Apr;18(4):2023-8.
19. The effects of exercise duration on adrenal HSP72/73 induction in rats. Demirel HA, etal., Acta Physiol Scand. 1999 Nov;167(3):227-31.
20. Identification in the rat brain of a set of nuclear proteins interacting with H1 degrees mRNA. Di Liegro CM, etal., Neuroscience. 2013 Jan 15;229:71-6. doi: 10.1016/j.neuroscience.2012.10.072. Epub 2012 Nov 14.
21. STUB1/CHIP is required for HIF1A degradation by chaperone-mediated autophagy. Ferreira JV, etal., Autophagy. 2013 Sep;9(9):1349-66. doi: 10.4161/auto.25190. Epub 2013 Jun 7.
22. 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.
23. Characteristics of the interaction between Hsc70 and the transferrin receptor in exosomes released during reticulocyte maturation. Geminard C, etal., J Biol Chem. 2001 Mar 30;276(13):9910-6. Epub 2000 Dec 22.
24. Rat ISS GO annotations from GOA human gene data--August 2006 GOA data from the GO Consortium
25. Expression of 70-kDa heat-shock protein during acute graft-versus-host disease. Goral J, etal., Clin Immunol Immunopathol. 1998 Mar;86(3):252-8.
26. Beta-internexin is a microtubule-associated protein identical to the 70-kDa heat-shock cognate protein and the clathrin uncoating ATPase. Green LA and Liem RK, J Biol Chem. 1989 Sep 15;264(26):15210-5.
27. Effects of nickel poisoning on expression pattern of the 72/73 and 94 kDa stress proteins in rat organs and in the COS-7, HepG2, and A549 cell lines. Hfaiedh N, etal., J Biochem Mol Toxicol. 2005;19(1):12-8.
28. Cathepsin C propeptide interacts with intestinal alkaline phosphatase and heat shock cognate protein 70 in human Caco-2 cells. Hirasaka K, etal., J Physiol Sci. 2008 Apr;58(2):105-11. doi: 10.2170/physiolsci.RP013007. Epub 2008 Mar 1.
29. Assembly of proteins to postsynaptic densities after transient cerebral ischemia. Hu BR, etal., J Neurosci. 1998 Jan 15;18(2):625-33.
30. Involvement of the 10-kDa C-terminal fragment of hsc70 in complexing with unfolded protein. Hu SM and Wang C, Arch Biochem Biophys. 1996 Aug 1;332(1):163-9.
31. Aspartyl residue 10 is essential for ATPase activity of rat hsc70. Huang SP, etal., J Biol Chem. 1993 Jan 25;268(3):2063-8.
32. Involvement of heat shock elements and basal transcription elements in the differential induction of the 70-kDa heat shock protein and its cognate by cadmium chloride in 9L rat brain tumor cells. Hung JJ, etal., J Cell Biochem. 1998 Oct 1;71(1):21-35.
33. Serum level of soluble 70-kD heat shock protein is associated with high mortality in patients with colorectal cancer without distant metastasis. Kocsis J, etal., Cell Stress Chaperones. 2010 Mar;15(2):143-51. Epub 2009 Jul 4.
34. Constitutive upregulation of chaperone-mediated autophagy in Huntington's disease. Koga H, etal., J Neurosci. 2011 Dec 14;31(50):18492-505.
35. Intracellular localization of HSP73 and HSP90 in rat kidneys with acute lysosomal thesaurismosis. Komatsuda A, etal., Pathol Int. 1999 Jun;49(6):513-8.
36. The 70-kDa heat shock cognate protein (Hsc73) gene is enhanced by ovarian hormones in the ventromedial hypothalamus. Krebs CJ, etal., Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1686-91.
37. Evidence for the existence of a novel mechanism for the nuclear import of Hsc70. Lamian V, etal., Exp Cell Res. 1996 Oct 10;228(1):84-91.
38. Association of neovascular age-related macular degeneration with specific gene expression patterns in peripheral white blood cells. Lederman M, etal., Invest Ophthalmol Vis Sci. 2010 Jan;51(1):53-8. Epub 2009 Aug 13.
39. Induction of molecular chaperones in carbon tetrachloride-treated rat liver: implications in protection against liver damage. Lee KJ, etal., Cell Stress Chaperones. 2004 Mar;9(1):58-68.
40. Hereditary sensory neuropathy is caused by a mutation in the delta subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct4 ) gene. Lee MJ, etal., Hum Mol Genet 2003 Aug 1;12(15):1917-25.
41. Integrity of intermediate filaments is associated with the development of acquired thermotolerance in 9L rat brain tumor cells. Lee YC and Lai YK, J Cell Biochem. 1995 Jan;57(1):150-62.
42. Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions. Liou ST and Wang C, Arch Biochem Biophys. 2005 Mar 15;435(2):253-63.
43. Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease. Lo Bianco C, etal., J Clin Invest. 2008 Sep;118(9):3087-97.
44. Diagnostic protein marker patterns in squamous cervical cancer. Lomnytska MI, etal., Proteomics Clin Appl. 2010 Jan;4(1):17-31. doi: 10.1002/prca.200900086. Epub 2009 Nov 11.
45. Constitutive heat shock protein 70 interacts with alpha-enolase and protects cardiomyocytes against oxidative stress. Luo Q, etal., Free Radic Res. 2011 Nov;45(11-12):1355-65. doi: 10.3109/10715762.2011.627330.
46. Heat shock cognate protein 70 regulates gephyrin clustering. Machado P, etal., J Neurosci. 2011 Jan 5;31(1):3-14. doi: 10.1523/JNEUROSCI.2533-10.2011.
47. Molecular composition of staufen2-containing ribonucleoproteins in embryonic rat brain. Maher-Laporte M, etal., PLoS One. 2010 Jun 28;5(6):e11350. doi: 10.1371/journal.pone.0011350.
48. Tumor necrosis factor alpha and inflammation disrupt the polarity complex in intestinal epithelial cells by a posttranslational mechanism. Mashukova A, etal., Mol Cell Biol. 2011 Feb;31(4):756-65. Epub 2010 Dec 6.
49. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
50. 73-kDa molecular chaperone HSP73 is a direct target of antibiotic gentamicin. Miyazaki T, etal., J Biol Chem. 2004 Apr 23;279(17):17295-300. Epub 2004 Feb 13.
51. Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses. Moon IS, etal., Cereb Cortex. 2001 Mar;11(3):238-48.
52. Induction of heat-shock proteins HSP73 and HSP90 in rat kidneys after ischemia. Morita K, etal., Ren Fail. 1995 Jul;17(4):405-19.
53. 73-kDa heat shock cognate protein interacts directly with P27Kip1, a cyclin-dependent kinase inhibitor, during G1/S transition. Nakamura S, etal., Biochem Biophys Res Commun. 1999 Apr 13;257(2):340-3.
54. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
55. Increased striatal mRNA and protein levels of the immunophilin FKBP-12 in experimental Parkinson's disease and identification of FKBP-12-binding proteins. Nilsson A, etal., J Proteome Res. 2007 Oct;6(10):3952-61. Epub 2007 Sep 18.
56. Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like protein. O'Malley K, etal., Mol Cell Biol 1985 Dec;5(12):3476-83.
57. Endogenous expression and developmental changes of HSP72 in rat skeletal muscles. Ogata T, etal., J Appl Physiol (1985). 2003 Sep;95(3):1279-86.
58. Association of polymorphisms of THBS2 and HSPA8 with hypertension in Japanese individuals with chronic kidney disease. Oguri M, etal., Mol Med Rep. 2009 Mar-Apr;2(2):205-11. doi: 10.3892/mmr_00000085.
59. Cloning and characterization of a novel GRP78-binding protein in the rat brain. Oh-hashi K, etal., J Biol Chem 2003 Mar 21;278(12):10531-7. Epub 2003 Jan 3.
60. Cancer-associated retinopathy induced by both anti-recoverin and anti-hsc70 antibodies in vivo. Ohguro H, etal., Invest Ophthalmol Vis Sci. 1999 Dec;40(13):3160-7.
61. Muscle type-specific response of HSP60, HSP72, and HSC73 during recovery after elevation of muscle temperature. Oishi Y, etal., J Appl Physiol (1985). 2002 Mar;92(3):1097-103.
62. Redox regulation of cellular stress response in multiple sclerosis. Pennisi G, etal., Biochem Pharmacol. 2011 Nov 15;82(10):1490-9. Epub 2011 Jul 30.
63. Clathrin-coated pit-associated proteins are required for alveolar macrophage phagocytosis. Perry DG, etal., J Immunol. 1999 Jan 1;162(1):380-6.
64. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
65. Molecular chaperones throughout the life cycle of the androgen receptor. Prescott J and Coetzee GA, Cancer Lett. 2006 Jan 8;231(1):12-9.
66. The molecular chaperone Hsc70 interacts with the vesicular monoamine transporter-2. Requena DF, etal., J Neurochem. 2009 Jul;110(2):581-94. Epub 2009 Apr 30.
67. GOA pipeline RGD automated data pipeline
68. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
69. Synaptic vesicle endocytosis. Saheki Y and De Camilli P, Cold Spring Harb Perspect Biol. 2012 Sep 1;4(9):a005645. doi: 10.1101/cshperspect.a005645.
70. PSMD11, PTPRM and PTPRB as novel biomarkers of pancreatic cancer progression. Sahni S, etal., Biochim Biophys Acta Gen Subj. 2020 Nov;1864(11):129682. doi: 10.1016/j.bbagen.2020.129682. Epub 2020 Jul 12.
71. The heat shock cognate protein hsc73 assembles with A(1) adenosine receptors to form functional modules in the cell membrane. Sarrio S, etal., Mol Cell Biol. 2000 Jul;20(14):5164-74.
72. Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells. Sorger PK and Pelham HR, EMBO J 1987 Apr;6(4):993-8.
73. A physiologically relevant hyperthermia selectively activates constitutive hsp70 in H9c2 cardiac myoblasts and confers oxidative protection. Su CY, etal., J Mol Cell Cardiol. 1999 Apr;31(4):845-55.
74. Presence of molecular chaperones, heat shock cognate (Hsc) 70 and heat shock proteins (Hsp) 40, in the postsynaptic structures of rat brain. Suzuki T, etal., Brain Res. 1999 Jan 16;816(1):99-110.
75. Involvement of peptide antigens in the cytotoxicity between 70-kDa heat shock cognate protein-like molecule and CD3+, CD4-, CD8-, TCR-alpha beta- killer T cells. Takashima S, etal., J Immunol. 1996 Oct 15;157(8):3391-5.
76. 70 kDa heat shock cognate protein is a transformation-associated antigen and a possible target for the host's anti-tumor immunity. Tamura Y, etal., J Immunol. 1993 Nov 15;151(10):5516-24.
77. Altered chaperone and protein turnover regulators expression in cultured skin fibroblasts from type 1 diabetes mellitus with nephropathy. Tessari P, etal., J Proteome Res. 2007 Mar;6(3):976-86.
78. Altered gene expression pattern in peripheral blood leukocytes from patients with arterial hypertension. Timofeeva AV, etal., Ann N Y Acad Sci. 2006 Dec;1091:319-35.
79. Stress response caused by chronic alcohol intake in aged rat brain. Unno K, etal., Alcohol Clin Exp Res. 2002 Jul;26(7):1017-23.
80. Increase in basal level of Hsp70, consisting chiefly of constitutively expressed Hsp70 (Hsc70) in aged rat brain. Unno K, etal., J Gerontol A Biol Sci Med Sci. 2000 Jul;55(7):B329-35.
81. Differential expression of heat shock 70 proteins in primary cultures from rat cerebellum. Voisin PJ, etal., Brain Res. 1996 Nov 11;739(1-2):215-34.
82. High-level expression of soluble rat hsc70 in Escherichia coli: purification and characterization of the cloned enzyme. Wang C and Lee MR, Biochem J. 1993 Aug 15;294 ( Pt 1):69-77.
83. Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins. Wilhelm BG, etal., Science. 2014 May 30;344(6187):1023-8. doi: 10.1126/science.1252884.
84. Chaperone mediated autophagy to the rescue: A new-fangled target for the treatment of neurodegenerative diseases. Xilouri M and Stefanis L, Mol Cell Neurosci. 2015 May;66(Pt A):29-36. doi: 10.1016/j.mcn.2015.01.003. Epub 2015 Feb 25.
85. Identification of a novel splice variant of heat shock cognate protein 70 after chronic antidepressant treatment in rat frontal cortex. Yamada M, etal., Biochem Biophys Res Commun. 1999 Aug 2;261(2):541-5.
86. Proteomic identification of protein targets for 15-deoxy-Delta(12,14)-prostaglandin J2 in neuronal plasma membrane. Yamamoto Y, etal., PLoS One. 2011 Mar 18;6(3):e17552. doi: 10.1371/journal.pone.0017552.
87. Immunohistochemical studies on the expression pattern of molecular chaperones HSC70 and HSP25 and cell cycle-related proteins cyclin D1 and PCNA in rat liver after thioacetamide intoxication. Zborek A, etal., Histochem Cell Biol. 2002 Oct;118(4):311-9. Epub 2002 Sep 5.
88. Nuclear translocation of stress protein Hsc70 during S phase in rat C6 glioma cells. Zeise E, etal., Cell Stress Chaperones. 1998 Jun;3(2):94-9.
89. Irreversible aggregation of protein synthesis machinery after focal brain ischemia. Zhang F, etal., J Neurochem. 2006 Jul;98(1):102-12.
90. Critical role of extracellular heat shock cognate protein 70 in the myocardial inflammatory response and cardiac dysfunction after global ischemia-reperfusion. Zou N, etal., Am J Physiol Heart Circ Physiol. 2008 Jun;294(6):H2805-13. Epub 2008 Apr 25.
Additional References at PubMed
PMID:8535066   PMID:9122205   PMID:9920933   PMID:10373374   PMID:10567422   PMID:10722728   PMID:11891788   PMID:12150907   PMID:12426384   PMID:12477932   PMID:12588994   PMID:12773536  
PMID:12878599   PMID:14627652   PMID:14644449   PMID:14681019   PMID:14978028   PMID:15215316   PMID:15489334   PMID:15543931   PMID:15972823   PMID:16207813   PMID:16502470   PMID:16854843  
PMID:16903783   PMID:16906134   PMID:17182002   PMID:17289661   PMID:17441507   PMID:17634366   PMID:17636261   PMID:17979815   PMID:18310515   PMID:18378183   PMID:19028452   PMID:19056867  
PMID:19199708   PMID:19388598   PMID:19551494   PMID:19724054   PMID:19946888   PMID:20160091   PMID:20176811   PMID:20458337   PMID:20884878   PMID:21151134   PMID:21231916   PMID:21235781  
PMID:21238931   PMID:21362503   PMID:21423176   PMID:21423662   PMID:21482805   PMID:21697503   PMID:21811788   PMID:22082260   PMID:22206666   PMID:22516433   PMID:22658674   PMID:22681889  
PMID:22871113   PMID:23106098   PMID:23376485   PMID:23533145   PMID:23636947   PMID:23762333   PMID:23904609   PMID:23921388   PMID:23979707   PMID:24030972   PMID:24616664   PMID:24625528  
PMID:25281747   PMID:25468996   PMID:25719862   PMID:25891763   PMID:26212789   PMID:26316108   PMID:26323693   PMID:26581985   PMID:27365397   PMID:28234934   PMID:28559423   PMID:29339092  
PMID:29476059   PMID:29875314   PMID:31506297   PMID:31904090   PMID:32336545   PMID:32360748   PMID:32873086   PMID:34362408   PMID:37947174  


Genomics

Comparative Map Data
Hspa8
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.2841,183,397 - 41,187,260 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl841,183,264 - 41,187,259 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx846,682,619 - 46,686,480 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0844,961,220 - 44,965,081 (+)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0842,828,805 - 42,832,666 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0844,989,401 - 44,993,261 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl844,990,014 - 44,993,179 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0843,478,238 - 43,480,456 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
Rnor_5.0846,005,304 - 46,006,864 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4843,784,035 - 43,787,760 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1843,792,829 - 43,796,525 (+)NCBI
Celera840,782,916 - 40,786,778 (+)NCBICelera
Cytogenetic Map8q22NCBI
HSPA8
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh3811123,057,489 - 123,062,462 (-)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl11123,057,489 - 123,063,230 (-)EnsemblGRCh38hg38GRCh38
GRCh3711122,928,197 - 122,932,844 (-)NCBIGRCh37GRCh37hg19GRCh37
Build 3611122,433,410 - 122,438,054 (-)NCBINCBI36Build 36hg18NCBI36
Build 3411122,433,410 - 122,438,054NCBI
Celera11120,087,529 - 120,092,173 (-)NCBICelera
Cytogenetic Map11q24.1NCBI
HuRef11118,870,278 - 118,875,122 (-)NCBIHuRef
CHM1_111122,814,192 - 122,819,035 (-)NCBICHM1_1
T2T-CHM13v2.011123,086,071 - 123,093,285 (-)NCBIT2T-CHM13v2.0
Hspa8
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm39940,712,572 - 40,716,498 (+)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl940,712,280 - 40,721,383 (+)EnsemblGRCm39 Ensembl
GRCm38940,801,276 - 40,805,202 (+)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl940,800,984 - 40,810,087 (+)EnsemblGRCm38mm10GRCm38
MGSCv37940,609,356 - 40,613,282 (+)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv3658,102,053 - 8,104,168 (+)NCBIMGSCv36mm8
MGSCv36940,552,355 - 40,556,269 (+)NCBIMGSCv36mm8
Celera938,034,609 - 38,038,251 (+)NCBICelera
Cytogenetic Map9A5.1NCBI
cM Map921.55NCBI
Hspa8
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_00495541223,862,590 - 23,867,984 (-)EnsemblChiLan1.0
ChiLan1.0NW_00495541223,863,513 - 23,867,984 (-)NCBIChiLan1.0ChiLan1.0
HSPA8
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan111124,863,401 - 124,868,370 (-)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v011117,890,545 - 117,895,262 (-)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.111121,809,800 - 121,814,628 (-)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl11121,809,800 - 121,815,773 (-)Ensemblpanpan1.1panPan2
HSPA8
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.1511,292,219 - 11,296,851 (+)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl511,292,262 - 11,296,797 (+)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha511,348,073 - 11,352,702 (+)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.0511,243,037 - 11,247,671 (+)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl511,242,826 - 11,307,583 (+)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.1511,346,458 - 11,351,078 (+)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.0511,279,270 - 11,283,884 (+)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.0511,323,539 - 11,328,166 (+)NCBIUU_Cfam_GSD_1.0
Hspa8
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_024404947104,655,786 - 104,660,238 (-)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_0049365427,577,149 - 7,581,923 (-)EnsemblSpeTri2.0SpeTri2.0 Ensembl
SpeTri2.0NW_0049365427,577,192 - 7,581,598 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
HSPA8
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl949,982,284 - 49,990,508 (-)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.1949,982,278 - 49,986,760 (-)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.2955,405,395 - 55,409,839 (+)NCBISscrofa10.2Sscrofa10.2susScr3
HSPA8
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.11114,447,348 - 114,452,693 (-)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl1114,446,544 - 114,451,562 (-)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_02366604311,677,166 - 11,681,993 (+)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Hspa8
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_0046248802,070,523 - 2,079,421 (+)EnsemblHetGla_female_1.0HetGla_female_1.0 EnsemblhetGla2
HetGla 1.0NW_0046248802,070,410 - 2,075,069 (+)NCBIHetGla_female_1.0HetGla 1.0hetGla2

Variants

.
Variants in Hspa8
23 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:116
Count of miRNA genes:77
Interacting mature miRNAs:79
Transcripts:ENSRNOT00000013159, ENSRNOT00000041306, ENSRNOT00000044608
Prediction methods:Microtar, Miranda, Rnahybrid
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 (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
12880023Bw184Body weight QTL 1840.001body mass (VT:0001259)body weight (CMO:0000012)8209764047097640Rat
12880025Cm102Cardiac mass QTL 1020.044heart mass (VT:0007028)heart wet weight to body weight ratio (CMO:0002408)8209764047097640Rat
12880028Cm103Cardiac mass QTL 1030.02heart left ventricle mass (VT:0007031)heart left ventricle weight to body weight ratio (CMO:0000530)8209764047097640Rat
12880044Am9Aortic mass QTL 90.007aorta mass (VT:0002845)aorta weight to aorta length to body weight ratio (CMO:0002722)8209764047097640Rat
2317032Ginf2Gastrointestinal inflammation QTL 23.210.005liver integrity trait (VT:0010547)liver granuloma severity score (CMO:0002157)8470581049705810Rat
2317036Livw3Liver weight QTL 32.430.01liver mass (VT:0003402)liver weight to body weight ratio (CMO:0000633)8470581049705810Rat
2317048Ginf1Gastrointestinal inflammation QTL 13.520.005cecum mucosa thickness (VT:0010234)enterocolitis severity score (CMO:0002138)8470581049705810Rat
2301416Bp315Blood pressure QTL 3150.008arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)8767057852670578Rat
1354595Despr4Despair related QTL 42.160.0036locomotor behavior trait (VT:0001392)amount of time spent in voluntary immobility (CMO:0001043)8768895552688955Rat
1354627Despr14Despair related QTL 140.0056locomotor behavior trait (VT:0001392)amount of experiment time spent in a discrete space in an experimental apparatus (CMO:0000958)8768895552688955Rat
1581557Eae16Experimental allergic encephalomyelitis QTL 163.8nervous system integrity trait (VT:0010566)experimental autoimmune encephalomyelitis incidence/prevalence measurement (CMO:0001046)88462195110921472Rat
2317030Wbc5White blood cell count QTL 53.210.005leukocyte quantity (VT:0000217)white blood cell count (CMO:0000027)8873663553736635Rat
2317051Aia18Adjuvant induced arthritis QTL 182.42joint integrity trait (VT:0010548)left rear ankle joint diameter (CMO:0002149)8873663553736635Rat
1598824Memor4Memory QTL 42.5exploratory behavior trait (VT:0010471)total horizontal distance resulting from voluntary locomotion in an experimental apparatus (CMO:0001443)8971222053356647Rat
1357398Slep3Serum leptin concentration QTL 33.43blood leptin amount (VT:0005667)serum leptin level (CMO:0000780)8971246341866876Rat
2302367Slep5Serum leptin concentration QTL 53.43blood leptin amount (VT:0005667)serum leptin level (CMO:0000780)8971246341866876Rat
631650Stl6Serum triglyceride level QTL 640.0019blood triglyceride amount (VT:0002644)plasma triglyceride level (CMO:0000548)810378157112202585Rat
1558646Swd5Spike wave discharge measurement QTL 53.450.00036brain electrophysiology trait (VT:0010557)brain spike-and-wave discharge frequency (CMO:0001742)81490675159906751Rat
61373Mcs4Mammary carcinoma susceptibility QTL 41.1mammary gland integrity trait (VT:0010552)mammary tumor number (CMO:0000343)81629044461290444Rat
631271Lecl1Lens clarity QTL 10.001lens clarity trait (VT:0001304)age of onset/diagnosis of cataract (CMO:0001584)81898416884531599Rat
731182Uae24Urinary albumin excretion QTL 246.4urine albumin amount (VT:0002871)urine albumin excretion rate (CMO:0000757)81933115293965294Rat
631842Inf1Infertility severity QTL 14.10.001seminal gland mass (VT:0010524)seminal vesicle wet weight (CMO:0001603)82266233067662330Rat
2303564Gluco43Glucose level QTL 433blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)82613018771130187Rat
2303572Insul13Insulin level QTL 132blood insulin amount (VT:0001560)blood insulin level (CMO:0000349)82613018771130187Rat
1359021Bp271Blood pressure QTL 2711.8arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)82664491246711092Rat
631648Stl5Serum triglyceride level QTL 540.0003blood triglyceride amount (VT:0002644)plasma triglyceride level (CMO:0000548)82720571554998217Rat
1358892Kidm26Kidney mass QTL 263.69kidney mass (VT:0002707)both kidneys wet weight to body weight ratio (CMO:0000340)82720571599103503Rat
1358896Bp262Blood pressure QTL 2622.89arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)82720571599103503Rat
1358907Cm40Cardiac mass QTL 401.89heart mass (VT:0007028)heart weight to body weight ratio (CMO:0000074)82720571599103503Rat
1331804Cm30Cardiac mass QTL 303.77443heart mass (VT:0007028)heart wet weight (CMO:0000069)82824291253961020Rat
1300146Rf17Renal function QTL 172.9renal blood flow trait (VT:2000006)absolute change in renal blood flow rate (CMO:0001168)82824291273242912Rat
8662823Vetf5Vascular elastic tissue fragility QTL 51.9artery integrity trait (VT:0010639)patent ductus arteriosus score (CMO:0002566)82824291299525068Rat
2302278Gluco36Glucose level QTL 364.2blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)82950266550095447Rat
724514Uae15Urinary albumin excretion QTL 152.9urine albumin amount (VT:0002871)urine albumin excretion rate (CMO:0000757)82950266570386295Rat
1549908Neudeg1Neurodegradation QTL 15.50nervous system integrity trait (VT:0010566)logarithm of the ratio of the lesioned side motor neuron count to contralateral side motor neuron count (CMO:0001986)83018886794457446Rat
61337Bp22Blood pressure QTL 225.1arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)83084815442692818Rat
1331744Bp217Blood pressure QTL 2173.398arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)83084815458482492Rat
61353Bp35Blood pressure QTL 350.001arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)83084815461290444Rat
61353Bp35Blood pressure QTL 350.001arterial blood pressure trait (VT:2000000)diastolic blood pressure (CMO:0000005)83084815461290444Rat
61353Bp35Blood pressure QTL 350.001arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)83084815461290444Rat
61353Bp35Blood pressure QTL 350.001arterial blood pressure trait (VT:2000000)diastolic blood pressure (CMO:0000005)83084815461290444Rat
11556286Cm81Cardiac mass QTL 810.01heart mass (VT:0007028)heart weight to body weight ratio (CMO:0000074)83084815461290444Rat
1359033Bp273Blood pressure QTL 273arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)83084815461290444Rat
2313046Bss78Bone structure and strength QTL 783.50.0001tibia strength trait (VT:1000284)tibia total energy absorbed before break (CMO:0001736)83084815482460899Rat
2313057Bss76Bone structure and strength QTL 7630.0001tibia size trait (VT:0100001)tibia midshaft cross-sectional area (CMO:0001717)83084815482460899Rat
2313067Bss77Bone structure and strength QTL 773.10.0001tibia size trait (VT:0100001)tibia midshaft endosteal cross-sectional area (CMO:0001716)83084815482460899Rat
2313088Bss75Bone structure and strength QTL 753.10.0001body length (VT:0001256)body length, nose to rump (CMO:0000079)83084815482460899Rat
1578755Pur5Proteinuria QTL 53.30.0001urine total protein amount (VT:0000032)urine total protein excretion rate (CMO:0000756)830848154101699754Rat
1578765Klgr1Kidney lesion grade QTL 13.30.0001kidney morphology trait (VT:0002135)organ lesion measurement (CMO:0000677)830848154101699754Rat
1578769Uae31Urinary albumin excretion QTL 313.30.001urine albumin amount (VT:0002871)urine albumin excretion rate (CMO:0000757)830848154101699754Rat
2316950Scl66Serum cholesterol level QTL 664.1blood cholesterol amount (VT:0000180)plasma total cholesterol level (CMO:0000585)830848259105647037Rat
1298065Scl16Serum cholesterol level QTL 163.8blood cholesterol amount (VT:0000180)plasma total cholesterol level (CMO:0000585)83085640475856404Rat
1582222Epfw2Epididymal fat weight QTL 23.20.0005epididymal fat pad mass (VT:0010421)epididymal fat pad weight to body weight ratio (CMO:0000658)83173772976737729Rat
61358Bp39Blood pressure QTL 392arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)83555193880551938Rat
61464Niddm11Non-insulin dependent diabetes mellitus QTL 113.10.001blood insulin amount (VT:0001560)plasma insulin level (CMO:0000342)83558203280582032Rat
1331838Niddm61Non-insulin dependent diabetes mellitus QTL 613.530.0004blood insulin amount (VT:0001560)plasma insulin level (CMO:0000342)83646953599083736Rat
737824Hcar10Hepatocarcinoma resistance QTL 102.9liver integrity trait (VT:0010547)liver tumorous lesion number (CMO:0001068)84071306682925667Rat
1358906Bp253Blood pressure QTL 25340.0004arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)84071306693965294Rat
1554321Bmd3Bone mineral density QTL 37.90.0001femur mineral mass (VT:0010011)volumetric bone mineral density (CMO:0001553)840952565123900184Rat


Expression


RNA-SEQ Expression
High: > 1000 TPM value   Medium: Between 11 and 1000 TPM
Low: Between 0.5 and 10 TPM   Below Cutoff: < 0.5 TPM

alimentary part of gastrointestinal system circulatory system endocrine system exocrine system hemolymphoid system hepatobiliary system integumental system musculoskeletal system nervous system renal system reproductive system respiratory system appendage
High 1 8 8 8 12 13 4 1
Medium 2 43 49 33 19 33 8 11 62 22 37 10 8
Low
Below cutoff

Sequence

Nucleotide Sequences
RefSeq Transcripts NM_024351 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
GenBank Nucleotide BC061547 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  BC098914 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  CH473975 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ212543 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ213866 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ216325 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ221758 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ226406 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ231618 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ231904 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ232261 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ232357 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ234652 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ235115 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  JACYVU010000198 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  M11942 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  Y00054 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles

Reference Sequences
RefSeq Acc Id: ENSRNOT00000044608   ⟹   ENSRNOP00000042159
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl841,183,264 - 41,187,259 (+)Ensembl
Rnor_6.0 Ensembl844,990,014 - 44,993,179 (+)Ensembl
RefSeq Acc Id: ENSRNOT00000098942   ⟹   ENSRNOP00000086914
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl841,183,264 - 41,187,259 (+)Ensembl
RefSeq Acc Id: ENSRNOT00000107246   ⟹   ENSRNOP00000088025
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl841,183,264 - 41,187,224 (+)Ensembl
RefSeq Acc Id: NM_024351   ⟹   NP_077327
RefSeq Status: VALIDATED
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2841,183,397 - 41,187,260 (+)NCBI
Rnor_6.0844,989,401 - 44,993,261 (+)NCBI
Rnor_5.0843,478,238 - 43,480,456 (+)NCBI
Rnor_5.0846,005,304 - 46,006,864 (-)NCBI
RGSC_v3.4843,784,035 - 43,787,760 (+)RGD
Celera840,782,916 - 40,786,778 (+)RGD
Sequence:
Reference Protein Sequences
RefSeq Acc Id: NP_077327   ⟸   NM_024351
- UniProtKB: Q4FZY7 (UniProtKB/Swiss-Prot),   Q62375 (UniProtKB/Swiss-Prot),   Q62374 (UniProtKB/Swiss-Prot),   Q62373 (UniProtKB/Swiss-Prot),   P12225 (UniProtKB/Swiss-Prot),   P08109 (UniProtKB/Swiss-Prot),   P63018 (UniProtKB/Swiss-Prot),   A6J3Q9 (UniProtKB/TrEMBL),   D4A4S3 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: ENSRNOP00000042159   ⟸   ENSRNOT00000044608
RefSeq Acc Id: ENSRNOP00000088025   ⟸   ENSRNOT00000107246
RefSeq Acc Id: ENSRNOP00000086914   ⟸   ENSRNOT00000098942

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-P63018-F1-model_v2 AlphaFold P63018 1-646 view protein structure

Transcriptome

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


Additional Information

Database Acc Id Source(s)
AGR Gene RGD:621725 AgrOrtholog
BioCyc Gene G2FUF-30834 BioCyc
Ensembl Genes ENSRNOG00000034066 Ensembl, ENTREZGENE, UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000044608 ENTREZGENE, UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  ENSRNOT00000098942.1 UniProtKB/TrEMBL
  ENSRNOT00000107246.1 UniProtKB/TrEMBL
Gene3D-CATH 1.20.1270.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.30.30.30 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.30.420.40 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
InterPro ATPase_NBD UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Heat_shock_70_CS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  HSP70_C_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  HSP70_peptide-bd_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Hsp_70_fam UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:24468 UniProtKB/Swiss-Prot
NCBI Gene 24468 ENTREZGENE
PANTHER HEAT SHOCK COGNATE 71 KDA PROTEIN UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PTHR19375 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam HSP70 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Hspa8 PhenoGen
PRINTS HEATSHOCK70 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PROSITE HSP70_1 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  HSP70_2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  HSP70_3 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000034066 RatGTEx
Superfamily-SCOP SSF100920 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF100934 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF53067 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
UniProt A0A8I6A278_RAT UniProtKB/TrEMBL
  A0A8I6A5N6_RAT UniProtKB/TrEMBL
  A6J3Q9 ENTREZGENE, UniProtKB/TrEMBL
  D4A4S3 ENTREZGENE, UniProtKB/TrEMBL
  HSP7C_RAT UniProtKB/Swiss-Prot
  P08109 ENTREZGENE
  P12225 ENTREZGENE
  P63018 ENTREZGENE
  Q4FZY7 ENTREZGENE
  Q62373 ENTREZGENE
  Q62374 ENTREZGENE
  Q62375 ENTREZGENE
UniProt Secondary P08109 UniProtKB/Swiss-Prot
  P12225 UniProtKB/Swiss-Prot
  Q4FZY7 UniProtKB/Swiss-Prot
  Q62373 UniProtKB/Swiss-Prot
  Q62374 UniProtKB/Swiss-Prot
  Q62375 UniProtKB/Swiss-Prot


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2015-11-25 Hspa8  heat shock protein family A (Hsp70) member 8  Hspa8  heat shock 70kDa protein 8  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2012-06-04 Hspa8  heat shock 70kDa protein 8  Hspa8  heat shock protein 8  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2011-04-29 Hspa8  heat shock protein 8  Hspa8  heat shock protein A8  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2009-10-06 Hspa8  heat shock protein A8  Hspa8  heat shock protein 8  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2003-04-09 Hspa8  heat shock protein 8      Symbol and Name updated 629477 APPROVED
2003-03-12 Hspa8  heat shock protein 8  Hsc70  Heat shock cognate protein 70  Data merged from RGD:2832 628472 PROVISIONAL
2003-03-12   heat shock protein 8  Hspa8  heat shock 70kD protein 8  Name updated to reflect Human and Mouse nomenclature 61478 PROVISIONAL
2002-11-06 Hspa8  heat shock 70kD protein 8      Symbol and Name updated 625702 APPROVED
2002-08-07 Hspa8        Symbol and Name status set to provisional 70820 PROVISIONAL
2002-06-10 Hsc70  Heat shock cognate protein 70      Symbol and Name status set to approved 70586 APPROVED