Hspd1 (heat shock protein family D (Hsp60) member 1) - Rat Genome Database

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Pathways
Gene: Hspd1 (heat shock protein family D (Hsp60) member 1) Rattus norvegicus
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Symbol: Hspd1
Name: heat shock protein family D (Hsp60) member 1
RGD ID: 621314
Description: Enables modification-dependent protein binding activity. Involved in several processes, including negative regulation of apoptotic process; positive regulation of cytokine production; and response to ischemia. Located in several cellular components, including mitochondrial crista; peroxisomal matrix; and zymogen granule. Used to study Alzheimer's disease and low tension glaucoma. Biomarker of several diseases, including artery disease (multiple); hydrocephalus; hyperglycemia; pulmonary fibrosis; and varicocele. Human ortholog(s) of this gene implicated in artery disease (multiple); autistic disorder; glucose intolerance; hereditary spastic paraplegia (multiple); and hypomyelinating leukodystrophy 4. Orthologous to human HSPD1 (heat shock protein family D (Hsp60) member 1); PARTICIPATES IN RNA degradation pathway; tuberculosis pathway; type 1 diabetes mellitus pathway; INTERACTS WITH 1,1,1-Trichloro-2-(o-chlorophenyl)-2-(p-chlorophenyl)ethane; 1,1-dichloroethene; 1-bromopropane.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: 60 kDa chaperonin; 60 kDa heat shock protein, mitochondrial; chaperonin 60; CPN60; heat shock 60kD protein 1 (chaperonin); heat shock 60kDa protein 1; heat shock protein 1 (chaperonin); heat shock protein 60 (liver); heat shock protein family D member 1; HSP-60; HSP-65; Hsp60; Hspd1-30p; mitochondrial matrix protein P1
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Alliance Genes
More Info more info ...
Related Pseudogenes: Hspd1-ps1   Hspd1-ps10   Hspd1-ps11   Hspd1-ps12   Hspd1-ps13   Hspd1-ps14   Hspd1-ps15   Hspd1-ps16   Hspd1-ps17   Hspd1-ps18   Hspd1-ps19   Hspd1-ps2   Hspd1-ps20   Hspd1-ps21   Hspd1-ps22   Hspd1-ps23   Hspd1-ps25   Hspd1-ps26   Hspd1-ps27   Hspd1-ps28   Hspd1-ps29   Hspd1-ps3   Hspd1-ps31   Hspd1-ps32   Hspd1-ps4   Hspd1-ps5   Hspd1-ps6   Hspd1-ps7   Hspd1-ps8   Hspd1-ps9  
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.2956,579,195 - 56,590,011 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl956,579,201 - 56,589,662 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx965,088,118 - 65,098,576 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0970,204,015 - 70,214,473 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0968,503,767 - 68,514,191 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0961,680,529 - 61,691,202 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl961,680,530 - 61,690,956 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0961,361,745 - 61,372,414 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4953,884,193 - 53,895,043 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1953,885,606 - 53,895,580 (-)NCBI
Celera954,060,669 - 54,071,096 (-)NCBICelera
Cytogenetic Map9q31NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Disease Annotations     Click to see Annotation Detail View

Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(+)-catechin  (ISO)
(1->4)-beta-D-glucan  (ISO)
1,1,1-Trichloro-2-(o-chlorophenyl)-2-(p-chlorophenyl)ethane  (EXP,ISO)
1,1-dichloroethene  (EXP)
1,2-dimethylhydrazine  (ISO)
1-bromopropane  (EXP)
1-chloro-2,4-dinitrobenzene  (ISO)
1-naphthyl isothiocyanate  (EXP)
17alpha-ethynylestradiol  (EXP,ISO)
17beta-estradiol  (ISO)
2,2',4,4'-Tetrabromodiphenyl ether  (EXP,ISO)
2,2,2-tetramine  (EXP)
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)
2,6-dinitrotoluene  (EXP)
2-methylcholine  (ISO)
3'-amino-3'-deoxy-N(6),N(6)-dimethyladenosine  (EXP)
3,3',5,5'-tetrabromobisphenol A  (ISO)
3-\{1-[3-(dimethylamino)propyl]-1H-indol-3-yl\}-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dione  (EXP)
3-chloropropane-1,2-diol  (EXP)
3-isobutyl-1-methyl-7H-xanthine  (ISO)
3H-1,2-dithiole-3-thione  (EXP)
4,4'-diaminodiphenylmethane  (ISO)
4-amino-2,6-dinitrotoluene  (EXP)
4-hydroxynon-2-enal  (ISO)
5-methyl-4-oxido-2-pyrazin-4-iumcarboxylic acid  (ISO)
6-propyl-2-thiouracil  (EXP)
7,12-dimethyltetraphene  (EXP,ISO)
7H-xanthine  (EXP)
9H-xanthine  (EXP)
acrylamide  (ISO)
afimoxifene  (ISO)
aflatoxin B1  (ISO)
albendazole  (ISO)
aldehydo-D-glucose  (ISO)
all-trans-retinoic acid  (ISO)
amiodarone  (EXP)
amitrole  (EXP)
amlodipine  (EXP)
ammonium chloride  (EXP)
amphibole asbestos  (ISO)
antimycin A  (ISO)
aristolochic acid A  (ISO)
Aroclor 1254  (ISO)
arsane  (ISO)
arsenic atom  (ISO)
arsenite(3-)  (EXP,ISO)
arsenous acid  (ISO)
ATP  (EXP)
atrazine  (ISO)
azoxystrobin  (ISO)
benzo[a]pyrene  (ISO)
bis(2-ethylhexyl) phthalate  (EXP,ISO)
bisphenol A  (EXP,ISO)
Bisphenol B  (ISO)
bisphenol F  (ISO)
Brodifacoum  (EXP)
butyric acid  (EXP)
cadmium atom  (ISO)
cadmium dichloride  (EXP,ISO)
caffeine  (ISO)
calcitriol  (ISO)
captan  (ISO)
carbon nanotube  (ISO)
CCCP  (ISO)
chelerythrine  (EXP)
chloroacetic acid  (EXP)
chloropicrin  (ISO)
chromium trinitrate  (ISO)
chromium(6+)  (ISO)
cisplatin  (EXP)
clofibrate  (EXP,ISO)
clonidine  (EXP)
clonidine (amino form)  (EXP)
clonidine (imino form)  (EXP)
cocaine  (ISO)
colforsin daropate hydrochloride  (ISO)
copper atom  (ISO)
copper(0)  (ISO)
copper(II) sulfate  (ISO)
curcumin  (EXP,ISO)
cyclophosphamide  (EXP)
cyclosporin A  (ISO)
cylindrospermopsin  (ISO)
cypermethrin  (EXP)
D-glucose  (ISO)
deguelin  (ISO)
desferrioxamine B  (ISO)
dexamethasone  (ISO)
dexmedetomidine  (EXP)
diallyl trisulfide  (ISO)
diarsenic trioxide  (ISO)
dibutyl phthalate  (EXP)
dichlorine  (EXP,ISO)
dicrotophos  (ISO)
dihydroxyacetone  (ISO)
dimethylarsinic acid  (EXP)
dioxygen  (ISO)
disodium selenite  (ISO)
dorsomorphin  (ISO)
doxorubicin  (EXP,ISO)
drospirenone  (ISO)
enzyme inhibitor  (ISO)
ethyl methanesulfonate  (ISO)
fenbuconazole  (ISO)
ferric ammonium citrate  (ISO)
ferric oxide  (ISO)
finasteride  (EXP)
flavone  (ISO)
flavonoids  (ISO)
flutamide  (EXP)
folic acid  (ISO)
folpet  (ISO)
formaldehyde  (ISO)
fructose  (EXP)
fulvestrant  (ISO)
Fusaric acid  (ISO)
geldanamycin  (ISO)
genistein  (EXP)
gentamycin  (EXP)
ginsenoside Re  (ISO)
glucose  (ISO)
gold atom  (ISO)
gold(0)  (ISO)
graphite  (ISO)
Honokiol  (EXP)
hyaluronic acid  (EXP)
hydrogen peroxide  (EXP)
Indeno[1,2,3-cd]pyrene  (ISO)
indirubin  (ISO)
indometacin  (ISO)
inulin  (ISO)
isotretinoin  (ISO)
ivermectin  (ISO)
ketoconazole  (EXP)
kojic acid  (EXP)
lead diacetate  (ISO)
lead(II) chloride  (ISO)
limonene  (EXP)
lipopolysaccharide  (ISO)
liquiritigenin  (EXP,ISO)
liquiritin  (EXP,ISO)
lovastatin  (ISO)
mercury atom  (EXP)
mercury(0)  (EXP)
methamphetamine  (EXP)
methanol  (EXP)
methapyrilene  (EXP)
methimazole  (EXP)
methotrexate  (ISO)
methyl methanesulfonate  (ISO)
methylisothiazolinone  (ISO)
methylmercury chloride  (ISO)
methylparaben  (ISO)
mevinphos  (EXP)
miconazole  (EXP)
minocycline  (EXP)
Mitotane  (EXP)
monocrotaline  (EXP,ISO)
motexafin gadolinium  (ISO)
N-acetyl-L-cysteine  (ISO)
N-methyl-4-phenylpyridinium  (ISO)
N-methyl-N'-nitro-N-nitrosoguanidine  (ISO)
N-methylformamide  (ISO)
N-nitrosodiethylamine  (EXP,ISO)
N-nitrosomorpholine  (EXP)
nefazodone  (EXP)
neomycin  (EXP)
nickel atom  (ISO)
nimesulide  (EXP)
nitroprusside  (ISO)
ochratoxin A  (EXP)
ouabain  (ISO)
ozone  (EXP,ISO)
p-chloromercuribenzoic acid  (ISO)
p-menthan-3-ol  (ISO)
paracetamol  (EXP,ISO)
paraquat  (EXP,ISO)
perfluorododecanoic acid  (EXP)
perfluorooctane-1-sulfonic acid  (ISO)
perfluorooctanoic acid  (EXP,ISO)
phenobarbital  (EXP)
phenytoin  (ISO)
PhIP  (EXP)
phlorizin  (ISO)
picolinic acid  (EXP)
picoxystrobin  (ISO)
pirinixic acid  (EXP,ISO)
poly(propylene imine) macromolecule  (ISO)
potassium chromate  (ISO)
potassium dichromate  (EXP,ISO)
pregnenolone 16alpha-carbonitrile  (EXP)
Propiverine  (EXP)
quartz  (ISO)
quercetin  (ISO)
raloxifene  (EXP,ISO)
reactive oxygen species  (ISO)
Rebamipide  (EXP)
resveratrol  (EXP,ISO)
rifampicin  (ISO)
rotenone  (EXP,ISO)
sarin  (EXP)
SB 431542  (ISO)
sevoflurane  (EXP)
silicon dioxide  (ISO)
sodium arsenite  (ISO)
sodium chromate  (ISO)
sodium dichromate  (EXP,ISO)
sodium fluoride  (EXP,ISO)
stavudine  (ISO)
streptozocin  (EXP)
sulfadimethoxine  (EXP)
sulforaphane  (ISO)
sunitinib  (ISO)
T-2 toxin  (EXP)
tamoxifen  (EXP,ISO)
tanespimycin  (ISO)
tebufenpyrad  (ISO)
tenofovir disoproxil fumarate  (ISO)
tert-butyl hydroperoxide  (ISO)
tetrachloromethane  (EXP,ISO)
tetracycline  (EXP)
tetraphene  (ISO)
thapsigargin  (EXP,ISO)
thioacetamide  (EXP)
thiostrepton  (ISO)
trichloroethene  (EXP)
trimellitic anhydride  (ISO)
Triptolide  (EXP)
troglitazone  (ISO)
tunicamycin  (ISO)
valproic acid  (EXP,ISO)
vinclozolin  (EXP)
vincristine  (ISO)
vorinostat  (ISO)
warfarin  (ISO)
zidovudine  (ISO)
zinc acetate  (ISO)
zinc atom  (ISO)
zinc dichloride  (EXP)
zinc pyrithione  (ISO)
zinc(0)  (ISO)

Gene Ontology Annotations     Click to see Annotation Detail View

Biological Process
'de novo' protein folding  (IC)
adhesion of symbiont to host  (ISO)
apoptotic mitochondrial changes  (IBA,IMP)
B cell activation  (ISO)
B cell proliferation  (ISO)
cellular response to heat  (IEP)
cellular response to interleukin-7  (ISO)
isotype switching to IgG isotypes  (ISO)
mitochondrial unfolded protein response  (IBA)
MyD88-dependent toll-like receptor signaling pathway  (ISO)
negative regulation of apoptotic process  (IMP,ISO)
negative regulation of apoptotic process in bone marrow cell  (IMP)
negative regulation of neuron apoptotic process  (IMP)
negative regulation of reactive oxygen species biosynthetic process  (IMP)
positive regulation of apoptotic process  (ISO)
positive regulation of interferon-alpha production  (IBA,ISO)
positive regulation of interleukin-10 production  (ISO)
positive regulation of interleukin-12 production  (ISO)
positive regulation of interleukin-6 production  (IBA,IMP,ISO)
positive regulation of macrophage activation  (ISO)
positive regulation of T cell activation  (IBA,ISO)
positive regulation of T cell mediated immune response to tumor cell  (ISO)
positive regulation of tumor necrosis factor production  (IMP)
positive regulation of type II interferon production  (IBA,ISO)
protein folding  (IBA)
protein import into mitochondrial intermembrane space  (IBA)
protein refolding  (ISO)
protein stabilization  (ISO)
response to activity  (IEP)
response to ATP  (IEP)
response to cocaine  (IEP)
response to cold  (ISS)
response to estrogen  (IEP)
response to glucocorticoid  (IEP)
response to hydrogen peroxide  (IEP)
response to hypoxia  (IEP)
response to ischemia  (IEP)
response to lipopolysaccharide  (IEP)
response to organic cyclic compound  (IEP)
response to organic substance  (IEP)
response to unfolded protein  (ISO)
response to xenobiotic stimulus  (IEP)
T cell activation  (IBA,ISO)

Molecular Pathway Annotations     Click to see Annotation Detail View
References

References - curated
# Reference Title Reference Citation
1. Colocalization of chaperone Cpn60, proinsulin and convertase PC1 within immature secretory granules of insulin-secreting cells suggests a role for Cpn60 in insulin processing. Arias AE, etal., J Cell Sci. 2000 Jun;113 ( Pt 11):2075-83.
2. Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid beta-peptide (1-42) into rat brain: implications for Alzheimer's disease. Boyd-Kimball D, etal., Neuroscience. 2005;132(2):313-24.
3. Deficiency of chaperonin 60 in Down's syndrome. Bozner P, etal., J Alzheimers Dis. 2002 Dec;4(6):479-86.
4. Mitochondrial stress protein recognition of inactivated dehydrogenases during mammalian cell death. Bruschi SA, etal., Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13413-8.
5. Temporal variations of Hsp60 and HSF-1 in primary rat myocardial cells in vitro under heat stress. Buriro R, etal., Genet Mol Res. 2013 Aug 20;12(3):3003-16. doi: 10.4238/2013.August.20.2.
6. Heat shock protein 60 or 70 activates nitric-oxide synthase (NOS) I- and inhibits NOS II-associated signaling and depresses the mitochondrial apoptotic cascade during brain stem death. Chan JY, etal., J Biol Chem. 2007 Feb 16;282(7):4585-600. Epub 2006 Dec 5.
7. Heat shock protein 60 in rostral ventrolateral medulla reduces cardiovascular fatality during endotoxaemia in the rat. Chang AY, etal., J Physiol. 2006 Jul 15;574(Pt 2):547-64. Epub 2006 May 4.
8. Elucidation of ATP-stimulated stress protein expression of RBA-2 type-2 astrocytes: ATP potentiate HSP60 and Cu/Zn SOD expression and stimulates pI shift of peroxiredoxin II. Chen HB, etal., J Cell Biochem. 2006 Feb 1;97(2):314-26.
9. Myocardial heat shock protein 60 expression in insulin-resistant and diabetic rats. Chen HS, etal., J Endocrinol. 2009 Feb;200(2):151-7. doi: 10.1677/JOE-08-0387. Epub 2008 Oct 23.
10. 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.
11. Inactivation of the hereditary spastic paraplegia-associated Hspd1 gene encoding the Hsp60 chaperone results in early embryonic lethality in mice. Christensen JH, etal., Cell Stress Chaperones. 2010 Nov;15(6):851-63. doi: 10.1007/s12192-010-0194-x.
12. Antibodies to human HSP60 in patients with juvenile chronic arthritis, diabetes mellitus, and cystic fibrosis. de Graeff-Meeder ER, etal., Pediatr Res. 1993 Oct;34(4):424-8.
13. HSP 60 expression in recurrent oral ulcerations of Beh├žet's disease. Deniz E, etal., Oral Surg Oral Med Oral Pathol Oral Radiol Endod. 2010 Aug;110(2):196-200. doi: 10.1016/j.tripleo.2010.03.020. Epub 2010 Jun 26.
14. Proteomic analysis of altered protein expression in skeletal muscle of rats in a hypermetabolic state induced by burn sepsis. Duan X, etal., Biochem J. 2006 Jul 1;397(1):149-58.
15. The expression and release of Hsp60 in 6-OHDA induced in vivo and in vitro models of Parkinson's disease. Feng Mj, etal., Neurochem Res. 2013 Oct;38(10):2180-9. doi: 10.1007/s11064-013-1127-8. Epub 2013 Aug 14.
16. Identification of immunodominant autoantigens in rat autoimmune orchitis. Fijak M, etal., J Pathol. 2005 Oct;207(2):127-38.
17. 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.
18. Rat ISS GO annotations from GOA human gene data--August 2006 GOA data from the GO Consortium
19. Different heat shock protein 60 species share pro-inflammatory activity but not binding sites on macrophages. Habich C, etal., FEBS Lett. 2003 Jan 2;533(1-3):105-9.
20. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Hansen JJ, etal., Am J Hum Genet. 2002 May;70(5):1328-32. Epub 2002 Mar 15.
21. Similar effects of cocaine and immobilization stress on the levels of heat-shock proteins and stress-activated protein kinases in the rat hippocampus, and on swimming behaviors: the contribution of dopamine and benzodiazepine receptors. Hayase T, etal., Behav Pharmacol. 2003 Nov;14(7):551-62.
22. Contribution of extrathymic gamma delta T cells to the expression of heat-shock protein and to protective immunity in mice infected with Toxoplasma gondii. Hisaeda H, etal., Immunology. 1996 Aug;88(4):551-7.
23. Attenuation of mitochondrial unfolded protein response is associated with hepatic dysfunction in septic rats. Huang LJ, etal., Shock. 2012 Dec;38(6):642-8. doi: 10.1097/SHK.0b013e3182734ff9.
24. Differential protein expression in pancreatic islets after treatment with an imidazoline compound. Jagerbrink T, etal., Cell Mol Life Sci. 2007 Apr 27;.
25. Autoantibodies to pancreatic hsp60 precede the development of glucose intolerance in patients with cystic fibrosis. Jensen P, etal., J Autoimmun. 2001 Sep;17(2):165-72.
26. Enhanced characterization of serum autoantibody reactivity following HSP 60 immunization in a rat model of experimental autoimmune glaucoma. Joachim SC, etal., Curr Eye Res. 2010 Oct;35(10):900-8. doi: 10.3109/02713683.2010.495829.
27. Role of heat shock protein 60 (HSP60) on paraquat intoxication. Kaetsu A, etal., J Appl Toxicol. 2001 Sep-Oct;21(5):425-30.
28. Antibodies to human heat shock protein 60, hypertension and dyslipidemia. A study of joint effects on coronary risk. Kervinen H, etal., Atherosclerosis. 2003 Aug;169(2):339-44.
29. Heat shock protein 60 modified with O-linked N-acetylglucosamine is involved in pancreatic beta-cell death under hyperglycemic conditions. Kim HS, etal., FEBS Lett. 2006 Apr 17;580(9):2311-6. Epub 2006 Mar 24.
30. Cytosolic heat shock protein 60, apoptosis, and myocardial injury. Kirchhoff SR, etal., Circulation. 2002 Jun 18;105(24):2899-904.
31. T-cell reactivity against HSP60 relates to early but not advanced atherosclerosis. Knoflach M, etal., Atherosclerosis. 2006 Oct 26;.
32. High expression of heat shock protein 60 in follicular cells of Hashimoto's thyroiditis. Kotani T, etal., Autoimmunity. 1996;25(1):1-8.
33. Exercise training and experimental diabetes modulate heat shock protein response in brain. Lappalainen Z, etal., Scand J Med Sci Sports. 2010 Feb;20(1):83-9. doi: 10.1111/j.1600-0838.2008.00872.x.
34. Possible association of chaperonin 60 with secretory proteins in pancreatic acinar cells. Le Gall IM and Bendayan M, J Histochem Cytochem. 1996 Jul;44(7):743-9.
35. HSP90 inhibition by 17-DMAG attenuates oxidative stress in experimental atherosclerosis. Madrigal-Matute J, etal., Cardiovasc Res. 2012 Jul 1;95(1):116-23. doi: 10.1093/cvr/cvs158. Epub 2012 Apr 30.
36. Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy. Magen D, etal., Am J Hum Genet. 2008 Jul;83(1):30-42. doi: 10.1016/j.ajhg.2008.05.016. Epub 2008 Jun 19.
37. Late onset motoneuron disorder caused by mitochondrial Hsp60 chaperone deficiency in mice. Magnoni R, etal., Neurobiol Dis. 2013 Jun;54:12-23. doi: 10.1016/j.nbd.2013.02.012. Epub 2013 Mar 4.
38. Neoangiogenesis, T-lymphocyte infiltration, and heat shock protein-60 are biological hallmarks of an immunomediated inflammatory process in end-stage calcified aortic valve stenosis. Mazzone A, etal., J Am Coll Cardiol. 2004 May 5;43(9):1670-6.
39. Expression of mitochondrial heat shock protein 60 in distinct cell types and defined stages of rat seminiferous epithelium. Meinhardt A, etal., Biol Reprod. 1995 Apr;52(4):798-807.
40. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
41. Clonidine-Induced Heat-Shock Protein Expression in Rat Aorta. Moen RJ, etal., J Cardiovasc Pharmacol Ther. 1998 Apr;3(2):171-184.
42. Differential expression of stress response genes in the H-Tx rat model of congenital hydrocephalus. Morgan FW, etal., Brain Res Mol Brain Res. 2005 Aug 18;138(2):273-90.
43. Induction of heat shock proteins by hyperglycemic cerebral ischemia. Muranyi M, etal., Brain Res Mol Brain Res. 2005 Sep 13;139(1):80-7.
44. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
45. Alpha-lipoic Acid modulates heat shock factor-1 expression in streptozotocin-induced diabetic rat kidney. Oksala NK, etal., Antioxid Redox Signal. 2007 Apr;9(4):497-506.
46. OMIM Disease Annotation Pipeline OMIM Disease Annotation Pipeline
47. A self-hsp60 peptide acts as a partial agonist inducing expression of B7-2 on mycobacterial hsp60-specific T cells: a possible mechanism for inhibitory T cell regulation of adjuvant arthritis? Paul AG, etal., Int Immunol. 2000 Jul;12(7):1041-50.
48. cDNA and deduced amino acid sequence of rat liver prehsp60 (chaperonin-60). Peralta D, etal., Nucleic Acids Res 1990 Dec 11;18(23):7162.
49. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
50. Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein: immune cross-regulation with the 60-kd heat-shock protein. Quintana FJ, etal., Arthritis Rheum. 2004 Nov;50(11):3712-20.
51. GOA pipeline RGD automated data pipeline
52. ClinVar Automated Import and Annotation Pipeline RGD automated import pipeline for ClinVar variants, variant-to-disease annotations and gene-to-disease annotations
53. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
54. The genes encoding mammalian chaperonin 60 and chaperonin 10 are linked head-to-head and share a bidirectional promoter. Ryan MT, etal., Gene 1997 Sep 1;196(1-2):9-17.
55. Proteomic analysis of rat heart in ischemia and ischemia-reperfusion using fluorescence two-dimensional difference gel electrophoresis. Sakai J, etal., Proteomics. 2003 Jul;3(7):1318-24.
56. Heat shock proteins expression in brain stem after subarachnoid hemorrhage in rats. Satoh M, etal., Acta Neurochir Suppl. 2003;86:477-82.
57. Heat shock protein gene expression profile may differentiate between rheumatoid arthritis, osteoarthritis, and healthy controls. Sedlackova L, etal., Scand J Rheumatol. 2011;40(5):354-7. doi: 10.3109/03009742.2011.552522. Epub 2011 Mar 21.
58. Coexpression of heat-shock protein 60 and intercellular-adhesion molecule-1 is related to increased adhesion of monocytes and T cells to aortic endothelium of rats in response to endotoxin. Seitz CS, etal., Lab Invest. 1996 Jan;74(1):241-52.
59. Extracellular HSP60 induces inflammation through activating and up-regulating TLRs in cardiomyocytes. Tian J, etal., Cardiovasc Res. 2013 Jun 1;98(3):391-401. doi: 10.1093/cvr/cvt047. Epub 2013 Feb 27.
60. Changes in Hsp60 level of the failing heart following acute myocardial infarction and the effect of long-term treatment with trandolapril. Toga W, etal., Biol Pharm Bull. 2007 Jan;30(1):105-10.
61. Subcellular stress response after traumatic brain injury. Truettner JS, etal., J Neurotrauma. 2007 Apr;24(4):599-612.
62. Presence of Chromatium vinosum chaperonins 10 and 60 in mitochondria and peroxisomes of rat hepatocytes. Velez-Granell CS, etal., Biol Cell. 1995;85(1):67-75.
63. Nucleotide sequence of rat hsp60 (chaperonin, GroEL homolog) cDNA. Venner TJ and Gupta RS, Nucleic Acids Res 1990 Sep 11;18(17):5309.
64. Complement activating antibodies against the human 60 kDa heat shock protein as a new independent family risk factor of coronary heart disease. Veres A, etal., Eur J Clin Invest. 2002 Jun;32(6):405-10.
65. Heat shock protein and gliadin peptide promote development of peptidase antibodies in children with autism and patients with autoimmune disease. Vojdani A, etal., Clin Diagn Lab Immunol. 2004 May;11(3):515-24.
66. Swedish Alzheimer mutation induces mitochondrial dysfunction mediated by HSP60 mislocalization of amyloid precursor protein (APP) and beta-amyloid. Walls KC, etal., J Biol Chem. 2012 Aug 31;287(36):30317-27. doi: 10.1074/jbc.M112.365890. Epub 2012 Jun 29.
67. Heat shock protein 60 protects skeletal tissue against glucocorticoid-induced bone mass loss by regulating osteoblast survival. Wang FS, etal., Bone. 2011 Nov;49(5):1080-9. doi: 10.1016/j.bone.2011.08.006. Epub 2011 Aug 11.
68. Cell stress response in rat chronic small bowel allograft rejection. Wang J, etal., Transplant Proc. 2013 Jul-Aug;45(6):2539-42. doi: 10.1016/j.transproceed.2013.02.120.
69. Surface staining and cytotoxic activity of heat-shock protein 60 antibody in stressed aortic endothelial cells. Xu Q, etal., Circ Res. 1994 Dec;75(6):1078-85.
70. Mechanism of cardioprotection following trauma-hemorrhagic shock by a selective estrogen receptor-beta agonist: up-regulation of cardiac heat shock factor-1 and heat shock proteins. Yu HP, etal., J Mol Cell Cardiol. 2006 Jan;40(1):185-94. Epub 2005 Nov 8.
71. Decreased testicular expression of cAMP response element modulator (CREM) in rat with varicocele. Yu JJ and Xu YM, Arch Androl. 2005 Mar-Apr;51(2):93-7.
72. Angiotensin II AT1 receptor blockade abolishes brain microvascular inflammation and heat shock protein responses in hypertensive rats. Zhou J, etal., J Cereb Blood Flow Metab. 2005 Jul;25(7):878-86.
73. Antibodies to human heat-shock protein 60 are associated with the presence and severity of coronary artery disease: evidence for an autoimmune component of atherogenesis. Zhu J, etal., Circulation. 2001 Feb 27;103(8):1071-5.
Additional References at PubMed
PMID:1348860   PMID:1516759   PMID:7904573   PMID:8101099   PMID:8824711   PMID:9243807   PMID:9867803   PMID:10205158   PMID:10663613   PMID:11027668   PMID:11050098   PMID:11445587  
PMID:11807771   PMID:12477932   PMID:12865426   PMID:12931191   PMID:12967636   PMID:12970367   PMID:14651853   PMID:15136728   PMID:15252132   PMID:15316393   PMID:15371451   PMID:15489334  
PMID:15616026   PMID:16148103   PMID:16708399   PMID:16854843   PMID:16959573   PMID:17164250   PMID:17307989   PMID:17634366   PMID:17675567   PMID:17823127   PMID:17923681   PMID:18086682  
PMID:18229457   PMID:18614015   PMID:18766470   PMID:19056867   PMID:19107191   PMID:19393246   PMID:19527807   PMID:19725078   PMID:19875724   PMID:19945465   PMID:19946888   PMID:20080761  
PMID:20193073   PMID:20458337   PMID:20507888   PMID:20633027   PMID:21245038   PMID:21266579   PMID:21276792   PMID:21328542   PMID:21391123   PMID:21753002   PMID:21874024   PMID:22658674  
PMID:23106098   PMID:23349634   PMID:23976951   PMID:23979707   PMID:24625528   PMID:24746669   PMID:25501148   PMID:25801186   PMID:25870185   PMID:26316108   PMID:26477505   PMID:26767982  
PMID:27056903   PMID:27818197   PMID:29476059   PMID:29581031   PMID:30196524   PMID:30896796   PMID:31686426   PMID:31802366   PMID:31904090   PMID:32357304   PMID:32892424   PMID:33219889  


Genomics

Comparative Map Data
Hspd1
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.2956,579,195 - 56,590,011 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl956,579,201 - 56,589,662 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx965,088,118 - 65,098,576 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0970,204,015 - 70,214,473 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0968,503,767 - 68,514,191 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0961,680,529 - 61,691,202 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl961,680,530 - 61,690,956 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0961,361,745 - 61,372,414 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4953,884,193 - 53,895,043 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1953,885,606 - 53,895,580 (-)NCBI
Celera954,060,669 - 54,071,096 (-)NCBICelera
Cytogenetic Map9q31NCBI
HSPD1
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh382197,486,584 - 197,500,274 (-)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl2197,486,584 - 197,516,737 (-)EnsemblGRCh38hg38GRCh38
GRCh372198,351,308 - 198,364,998 (-)NCBIGRCh37GRCh37hg19GRCh37
Build 362198,059,553 - 198,073,243 (-)NCBINCBI36Build 36hg18NCBI36
Build 342198,176,815 - 198,190,504NCBI
Celera2192,107,181 - 192,120,871 (-)NCBICelera
Cytogenetic Map2q33.1NCBI
HuRef2190,203,711 - 190,217,402 (-)NCBIHuRef
CHM1_12198,357,144 - 198,370,838 (-)NCBICHM1_1
T2T-CHM13v2.02197,970,209 - 197,983,875 (-)NCBIT2T-CHM13v2.0
Hspd1
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm39155,116,992 - 55,127,402 (-)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl155,116,994 - 55,127,402 (-)EnsemblGRCm39 Ensembl
GRCm38155,077,833 - 55,088,243 (-)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl155,077,835 - 55,088,243 (-)EnsemblGRCm38mm10GRCm38
MGSCv37155,134,678 - 55,144,776 (-)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv36155,022,380 - 55,032,390 (-)NCBIMGSCv36mm8
Celera155,597,904 - 55,608,002 (-)NCBICelera
Cytogenetic Map1C1.2NCBI
cM Map128.01NCBI
Hspd1
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_0049554033,063,133 - 3,073,419 (+)EnsemblChiLan1.0
ChiLan1.0NW_0049554033,062,724 - 3,073,419 (+)NCBIChiLan1.0ChiLan1.0
HSPD1
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan12B100,115,490 - 100,129,121 (-)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v02B84,729,615 - 84,743,352 (-)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.12B202,623,497 - 202,637,045 (-)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl2B202,623,497 - 202,636,959 (-)Ensemblpanpan1.1panPan2
HSPD1
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.1377,010,421 - 7,025,912 (-)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha377,956,566 - 7,967,852 (-)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.0376,900,931 - 6,911,990 (-)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl376,900,933 - 6,911,980 (-)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.1376,899,765 - 6,910,835 (-)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.0376,866,679 - 6,877,757 (-)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.0376,889,830 - 6,900,900 (-)NCBIUU_Cfam_GSD_1.0
Hspd1
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_024405303155,150,440 - 155,160,005 (-)NCBIHiC_Itri_2
SpeTri2.0NW_0049365061,678,069 - 1,687,632 (+)NCBISpeTri2.0SpeTri2.0SpeTri2.0
HSPD1
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl15101,360,094 - 101,373,526 (-)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.115101,360,355 - 101,373,498 (-)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.215112,534,459 - 112,547,603 (-)NCBISscrofa10.2Sscrofa10.2susScr3
HSPD1
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.11083,003,266 - 83,017,397 (-)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl1083,003,717 - 83,017,363 (-)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_023666040116,426,692 - 116,441,017 (+)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Hspd1
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla 1.0NW_0046248892,736,727 - 2,746,333 (+)NCBIHetGla_female_1.0HetGla 1.0hetGla2

Variants

.
Variants in Hspd1
32 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:55
Count of miRNA genes:50
Interacting mature miRNAs:54
Transcripts:ENSRNOT00000066589
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 (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
10054125Srcrt7Stress Responsive Cort QTL 73.330.0011blood corticosterone amount (VT:0005345)plasma corticosterone level (CMO:0001173)9187073594Rat
1331757Cdexp1CD45RC expression in CD8 T cells QTL 14.3CD8-positive T cell quantity (VT:0008077)blood CD45RC(high) CD8 T cell count to CD45RC(low) CD8 T cell count ratio (CMO:0001990)9102453767509080Rat
631680Cm11Cardiac mass QTL 113.10.00089heart left ventricle mass (VT:0007031)heart left ventricle weight to body weight ratio (CMO:0000530)92043051965430519Rat
70186Niddm26Non-insulin dependent diabetes mellitus QTL 263.87blood glucose amount (VT:0000188)blood glucose level area under curve (AUC) (CMO:0000350)92207116986369743Rat
631643Bp120Blood pressure QTL 12030.004arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)92207120067071200Rat
7207805Bmd88Bone mineral density QTL 884femur mineral mass (VT:0010011)total volumetric bone mineral density (CMO:0001728)92375402458157242Rat
1300180Bw14Body weight QTL 143.776body mass (VT:0001259)body weight (CMO:0000012)92375402461381613Rat
7207814Bmd91Bone mineral density QTL 913.5femur size trait (VT:1000369)femoral neck cross-sectional area (CMO:0001697)92375414483851531Rat
70218Cm28Cardiac mass QTL 288.30.0001heart mass (VT:0007028)heart wet weight (CMO:0000069)92526804479271759Rat
724544Uae9Urinary albumin excretion QTL 94.5urine albumin amount (VT:0002871)urine albumin level (CMO:0000130)925268044114175309Rat
731164Uae25Urinary albumin excretion QTL 253.50.0001urine albumin amount (VT:0002871)urine albumin excretion rate (CMO:0000757)925661188100929786Rat
1641894Alcrsp12Alcohol response QTL 12response to alcohol trait (VT:0010489)brain neurotensin receptor 1 density (CMO:0002068)92746863972468639Rat
7411656Foco26Food consumption QTL 269.80.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)93253550577535505Rat
7411571Bw138Body weight QTL 13814.30.001body mass (VT:0001259)body weight gain (CMO:0000420)93253550577535505Rat
1598834Memor11Memory QTL 112.5exploratory behavior trait (VT:0010471)average horizontal distance between subject and target during voluntary locomotion in an experimental apparatus (CMO:0002674)93696235977814038Rat
8662828Vetf6Vascular elastic tissue fragility QTL 63.9artery integrity trait (VT:0010639)patent ductus arteriosus score (CMO:0002566)93696235992058970Rat
2290450Scl57Serum cholesterol level QTL 574.15blood cholesterol amount (VT:0000180)plasma total cholesterol level (CMO:0000585)93696235995410867Rat
6903941Pur31Proteinuria QTL 310.036urine total protein amount (VT:0000032)urine protein excretion rate (CMO:0000759)94019418885194188Rat
11353949Bp393Blood pressure QTL 393arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)94019418885194188Rat
61352Bp34Blood pressure QTL 345arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)94249534379271511Rat
10058949Gmadr5Adrenal mass QTL 520.014adrenal gland mass (VT:0010420)both adrenal glands wet weight to body weight ratio (CMO:0002411)94279151387976209Rat
11353951Bp394Blood pressure QTL 394arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)94464992189649921Rat
12879506Pur33Proteinuria QTL 33urine total protein amount (VT:0000032)urine total protein excretion rate (CMO:0000756)94464992189649921Rat
11353957Bmd92Bone mineral density QTL 920.01tibia mineral mass (VT:1000283)volumetric bone mineral density (CMO:0001553)94611419991114199Rat
631656Bp108Blood pressure QTL 1085.970.0001arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)94859825193598251Rat
1598849Memor17Memory QTL 172.2exploratory behavior trait (VT:0010471)difference between time of physical contact/close proximity of test subject and social stimulus during sample phase and test phase (CMO:0002678)94996854671098346Rat
2303170Bp332Blood pressure QTL 3323.730.027arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)95584784177026453Rat


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 4 14 6 6 2 4
Medium 3 39 43 35 19 35 8 11 72 35 37 11 8
Low
Below cutoff

Sequence


RefSeq Acc Id: ENSRNOT00000066589   ⟹   ENSRNOP00000063666
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl956,579,201 - 56,589,662 (-)Ensembl
Rnor_6.0 Ensembl961,680,530 - 61,690,956 (-)Ensembl
RefSeq Acc Id: NM_022229   ⟹   NP_071565
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2956,579,196 - 56,589,622 (-)NCBI
Rnor_6.0961,680,530 - 61,690,956 (-)NCBI
Rnor_5.0961,361,745 - 61,372,414 (-)NCBI
RGSC_v3.4953,884,193 - 53,895,043 (-)RGD
Celera954,060,669 - 54,071,096 (-)RGD
Sequence:
RefSeq Acc Id: XM_006244932   ⟹   XP_006244994
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2956,579,195 - 56,590,011 (-)NCBI
Rnor_6.0961,680,529 - 61,691,202 (-)NCBI
Rnor_5.0961,361,745 - 61,372,414 (-)NCBI
Sequence:
RefSeq Acc Id: NP_071565   ⟸   NM_022229
- UniProtKB: P63039 (UniProtKB/Swiss-Prot),   A0A482IDN3 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: XP_006244994   ⟸   XM_006244932
- Peptide Label: isoform X1
- UniProtKB: P63039 (UniProtKB/Swiss-Prot),   A0A482IDN3 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: ENSRNOP00000063666   ⟸   ENSRNOT00000066589

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-P63039-F1-model_v2 AlphaFold P63039 1-573 view protein structure

Transcriptome

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

Promoters
RGD ID:13696671
Promoter ID:EPDNEW_R7195
Type:initiation region
Name:Hspd1_1
Description:heat shock protein family D member 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_6.0961,690,958 - 61,691,018EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:621314 AgrOrtholog
BioCyc Gene G2FUF-27534 BioCyc
Ensembl Genes ENSRNOG00000014525 Ensembl, ENTREZGENE, UniProtKB/Swiss-Prot
Ensembl Transcript ENSRNOT00000066589 ENTREZGENE, UniProtKB/Swiss-Prot
Gene3D-CATH 1.10.560.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.30.260.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.50.7.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
IMAGE_CLONE IMAGE:7103955 IMAGE-MGC_LOAD
InterPro Chaperonin_Cpn60_CS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Chaprnin_Cpn60 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Cpn60/TCP-1 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  GroEL-like_apical_dom_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  GROEL-like_equatorial_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  TCP-1-like_intermed_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:63868 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
MGC_CLONE MGC:91701 IMAGE-MGC_LOAD
NCBI Gene 63868 ENTREZGENE
PANTHER 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL UniProtKB/Swiss-Prot
  60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL UniProtKB/Swiss-Prot
  60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL UniProtKB/TrEMBL
  60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL UniProtKB/TrEMBL
Pfam Cpn60_TCP1 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Hspd1 PhenoGen
PRINTS CHAPERONIN60 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PROSITE CHAPERONINS_CPN60 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000014525 RatGTEx
Superfamily-SCOP SSF48592 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF52029 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF54849 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
UniProt A0A482IDN3 ENTREZGENE, UniProtKB/TrEMBL
  CH60_RAT UniProtKB/Swiss-Prot, ENTREZGENE
UniProt Secondary P19226 UniProtKB/Swiss-Prot
  P19227 UniProtKB/Swiss-Prot
  P97602 UniProtKB/Swiss-Prot


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2019-04-10 Hspd1  heat shock protein family D (Hsp60) member 1  Hspd1  heat shock protein family D member 1  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2016-02-25 Hspd1  heat shock protein family D member 1  Hspd1  heat shock protein 1 (chaperonin)  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2010-09-03 Hspd1  heat shock protein 1 (chaperonin)  Hspd1  heat shock 60kDa protein 1  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2010-08-12 Hspd1  heat shock 60kDa protein 1  Hspd1  heat shock protein 1 (chaperonin)  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2005-01-20 Hspd1  heat shock protein 1 (chaperonin)  Hsp60  heat shock protein 60 (liver)  Symbol and Name updated 1299863 APPROVED
2002-08-07 Hsp60  heat shock protein 60 (liver)      Symbol and Name status set to provisional 70820 PROVISIONAL

RGD Curation Notes
Note Type Note Reference
gene_physical_interaction linked to Hspe1 by a region of 280 bp 633052