Hsp90ab1 (heat shock protein 90 alpha family class B member 1) - Rat Genome Database

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Gene: Hsp90ab1 (heat shock protein 90 alpha family class B member 1) Rattus norvegicus
Analyze
Symbol: Hsp90ab1
Name: heat shock protein 90 alpha family class B member 1
RGD ID: 1303075
Description: Enables nucleotide binding activity; sulfonylurea receptor binding activity; and transmembrane transporter binding activity. Involved in several processes, including negative regulation of complement-dependent cytotoxicity; positive regulation of cell size; and positive regulation of protein import into nucleus. Located in several cellular components, including basolateral plasma membrane; brush border membrane; and ooplasm. Biomarker of muscular atrophy; pancreatitis; and pulmonary fibrosis. Human ortholog(s) of this gene implicated in multiple sclerosis. Orthologous to several human genes including HSP90AB1 (heat shock protein 90 alpha family class B member 1); PARTICIPATES IN aldosterone signaling pathway; androgen signaling pathway; cortisol signaling pathway; INTERACTS WITH (R)-adrenaline; 1,1,1-Trichloro-2-(o-chlorophenyl)-2-(p-chlorophenyl)ethane; 1-naphthyl isothiocyanate.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: heat shock 84 kDa; heat shock 90kDa protein 1, beta; heat shock protein 90 alpha (cytosolic), class B member 1; heat shock protein 90kDa alpha (cytosolic), class B member 1; heat shock protein 90kDa alpha family class B member 1; heat shock protein HSP 90-beta; HSP 84; HSP84; HSP90-BETA; HSP90B; HSPC2; Hspcb; MGC94263
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Alliance Genes
More Info more info ...
Related Pseudogenes: Hsp90ab1-ps13   Hsp90ab1-ps17  
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.2915,432,986 - 15,438,358 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl915,433,691 - 15,438,488 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx924,019,488 - 24,024,885 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0929,082,165 - 29,087,562 (+)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0927,382,927 - 27,388,324 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0917,817,791 - 17,823,163 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl917,817,721 - 17,823,243 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0916,706,512 - 16,711,884 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4911,033,496 - 11,038,868 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1911,030,786 - 11,036,319 (+)NCBI
Celera913,176,225 - 13,181,597 (+)NCBICelera
Cytogenetic Map9q12NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(1->4)-beta-D-glucan  (ISO)
(R)-adrenaline  (EXP)
(Z)-3-butylidenephthalide  (ISO)
1,1,1-Trichloro-2-(o-chlorophenyl)-2-(p-chlorophenyl)ethane  (EXP)
1,2-dimethylhydrazine  (ISO)
1-naphthyl isothiocyanate  (EXP)
17alpha-ethynylestradiol  (EXP,ISO)
17beta-estradiol  (EXP,ISO)
17beta-hydroxy-5alpha-androstan-3-one  (ISO)
1H-pyrazole  (ISO)
2,2',4,4'-Tetrabromodiphenyl ether  (ISO)
2,2',5,5'-tetrachlorobiphenyl  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,4-diaminotoluene  (ISO)
2,4-dinitrotoluene  (EXP)
2-amino-4,6-dinitrotoluene  (EXP)
3,3',4,4',5-pentachlorobiphenyl  (ISO)
3,4-dihydrocoumarin  (ISO)
3-chloropropane-1,2-diol  (EXP)
3-isobutyl-1-methyl-7H-xanthine  (ISO)
3H-1,2-dithiole-3-thione  (EXP,ISO)
4,4'-diaminodiphenylmethane  (ISO)
4,4'-sulfonyldiphenol  (ISO)
4-amino-2,6-dinitrotoluene  (EXP)
4-hydroxynon-2-enal  (EXP)
4-vinylcyclohexene dioxide  (ISO)
6-anilino-5,8-quinolinedione  (EXP)
7,12-dimethyltetraphene  (EXP)
7H-xanthine  (EXP)
9H-xanthine  (EXP)
acrylamide  (EXP,ISO)
afimoxifene  (ISO)
aflatoxin B1  (EXP,ISO)
albendazole  (ISO)
all-trans-retinoic acid  (ISO)
ammonium chloride  (EXP)
amphibole asbestos  (ISO)
aniline  (ISO)
antimycin A  (ISO)
arachidonic acid  (ISO)
Aroclor 1254  (ISO)
arsenous acid  (ISO)
astemizole  (EXP)
atrazine  (ISO)
BAPTA  (ISO)
benzo[a]pyrene  (EXP,ISO)
benzo[a]pyrene diol epoxide I  (ISO)
beta-naphthoflavone  (ISO)
bis(2-ethylhexyl) phthalate  (EXP)
bisphenol A  (EXP,ISO)
Bisphenol B  (ISO)
bisphenol F  (ISO)
bortezomib  (ISO)
butanal  (ISO)
cadmium atom  (ISO)
cadmium dichloride  (ISO)
cadmium sulfate  (ISO)
caffeine  (ISO)
calcidiol  (EXP)
cannabidiol  (ISO)
carbon nanotube  (ISO)
celastrol  (EXP)
chloropicrin  (ISO)
chloroprene  (ISO)
chlorpyrifos  (ISO)
choline  (ISO)
chromium(6+)  (ISO)
Cinobufagin  (ISO)
clofibrate  (EXP,ISO)
clofibric acid  (EXP)
cobalt dichloride  (ISO)
cocaine  (EXP)
copper atom  (ISO)
copper(0)  (ISO)
copper(II) sulfate  (ISO)
coumarin  (ISO)
coumestrol  (EXP)
Cuprizon  (EXP)
curcumin  (EXP)
cyclophosphamide  (EXP)
cyclosporin A  (ISO)
DDT  (EXP)
deguelin  (ISO)
deoxynivalenol  (ISO)
dexamethasone  (ISO)
dextran sulfate  (EXP)
diarsenic trioxide  (ISO)
dibutyl phthalate  (EXP)
diethylstilbestrol  (EXP)
disodium selenite  (ISO)
disulfiram  (ISO)
dopamine  (ISO)
doxorubicin  (ISO)
elemental selenium  (ISO)
enzyme inhibitor  (ISO)
ethanol  (EXP,ISO)
fenofibrate  (ISO)
finasteride  (EXP)
flutamide  (EXP)
folic acid  (ISO)
fulvestrant  (ISO)
gamendazole  (EXP)
geldanamycin  (EXP,ISO)
genistein  (EXP)
gentamycin  (EXP)
gold atom  (ISO)
gold(0)  (ISO)
hexachlorobenzene  (EXP)
indometacin  (ISO)
isoflavones  (EXP)
ivermectin  (ISO)
kojic acid  (EXP)
L-ascorbic acid  (ISO)
lead nitrate  (ISO)
leflunomide  (EXP)
limonene  (EXP)
lipopolysaccharide  (ISO)
lovastatin  (ISO)
methyl methanesulfonate  (ISO)
Methylazoxymethanol acetate  (EXP)
methylisothiazolinone  (ISO)
miconazole  (ISO)
morphine  (EXP)
motexafin gadolinium  (ISO)
N-ethyl-N-nitrosourea  (EXP)
N-methyl-4-phenylpyridinium  (ISO)
N-methyl-N'-nitro-N-nitrosoguanidine  (ISO)
N-nitrosodiethylamine  (EXP)
N-nitrosomorpholine  (EXP)
nefazodone  (EXP)
nickel dichloride  (ISO)
nimesulide  (EXP)
nonanoic acid  (ISO)
ochratoxin A  (EXP)
oxidopamine  (EXP)
ozone  (EXP,ISO)
p-menthan-3-ol  (ISO)
paracetamol  (EXP,ISO)
paraoxon  (ISO)
PCB138  (EXP,ISO)
perfluorooctane-1-sulfonic acid  (ISO)
perfluorooctanoic acid  (EXP)
phenobarbital  (EXP,ISO)
PhIP  (EXP)
phlorizin  (ISO)
pinosylvin  (ISO)
pirinixic acid  (EXP,ISO)
potassium dichromate  (ISO)
prostaglandin A1  (ISO)
quercetin  (EXP,ISO)
raloxifene  (ISO)
resveratrol  (EXP)
rotenone  (EXP,ISO)
S-butyl-DL-homocysteine (S,R)-sulfoximine  (ISO)
selenium atom  (ISO)
silicon dioxide  (ISO)
sodium arsenite  (EXP,ISO)
sodium dichromate  (EXP,ISO)
sodium fluoride  (ISO)
sulfasalazine  (ISO)
T-2 toxin  (EXP)
tamibarotene  (ISO)
tamoxifen  (ISO)
tanespimycin  (ISO)
tetrachloromethane  (ISO)
thimerosal  (ISO)
thioacetamide  (EXP)
thiostrepton  (ISO)
toluene 2,4-diisocyanate  (ISO)
trans-pinosylvin  (ISO)
Tributyltin oxide  (ISO)
trichloroethene  (ISO)
trimellitic anhydride  (ISO)
triphenylstannane  (ISO)
troglitazone  (ISO)
tunicamycin  (ISO)
uranium atom  (ISO)
usnic acid  (ISO)
valdecoxib  (EXP)
valproic acid  (EXP)
vinclozolin  (EXP)
vitamin E  (ISO)
vorinostat  (ISO)
warfarin  (ISO)
zearalenone  (ISO)
zinc acetate  (ISO)
zinc pyrithione  (ISO)

Gene Ontology Annotations     Click to see Annotation Detail View

Biological Process
cellular response to heat  (IBA,IEA,ISO)
cellular response to interleukin-4  (IEA,ISO)
cellular response to organic cyclic compound  (IEP)
chaperone-mediated autophagy  (NAS)
chaperone-mediated protein complex assembly  (IEA,ISO)
negative regulation of apoptotic process  (IEA,ISO)
negative regulation of complement-dependent cytotoxicity  (IMP)
negative regulation of neuron apoptotic process  (IMP)
negative regulation of proteasomal protein catabolic process  (IMP,ISO)
negative regulation of proteasomal ubiquitin-dependent protein catabolic process  (IEA,ISO,ISS)
negative regulation of protein metabolic process  (IMP)
negative regulation of transforming growth factor beta activation  (IEA,ISO,ISS)
placenta development  (IEA,ISO)
positive regulation of cell differentiation  (IEA,ISO)
positive regulation of cell size  (IMP)
positive regulation of protein binding  (IMP)
positive regulation of protein import into nucleus  (IMP)
positive regulation of protein localization to cell surface  (IEA,ISO)
positive regulation of protein serine/threonine kinase activity  (IMP)
positive regulation of transforming growth factor beta receptor signaling pathway  (IEA,ISO,ISS)
protein folding  (IBA,IEA,ISO,TAS)
protein stabilization  (IBA)
regulation of cell cycle  (IEA,ISO,ISS)
regulation of protein complex stability  (NAS)
regulation of protein localization  (ISO)
regulation of protein ubiquitination  (IEA,ISO)
response to cocaine  (IEP)
response to organic substance  (ISO)
response to salt stress  (IEP)
response to unfolded protein  (TAS)
response to xenobiotic stimulus  (IEP)
supramolecular fiber organization  (IEA,ISO)
telomerase holoenzyme complex assembly  (IEA,ISO)
telomere maintenance via telomerase  (IEA,ISO)
virion attachment to host cell  (IEA,ISO)

References

References - curated
# Reference Title Reference Citation
1. 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.
2. Antitumor activity of the combination of an HSP90 inhibitor and a PI3K/mTOR dual inhibitor against cholangiocarcinoma. Chen MH, etal., Oncotarget. 2014 May 15;5(9):2372-89. doi: 10.18632/oncotarget.1706.
3. Protection of oligodendrocyte precursor cells by low doses of HSP90 inhibitors in cell culture. Cid C and Alcazar A, Exp Neurol. 2010 Sep;225(1):29-33. Epub 2009 Dec 4.
4. Antibodies reactive to heat shock protein 90 induce oligodendrocyte precursor cell death in culture. Implications for demyelination in multiple sclerosis. Cid C, etal., FASEB J. 2004 Feb;18(2):409-11. Epub 2003 Dec 19.
5. Anti-heat shock protein 90beta antibodies decrease pre-oligodendrocyte population in perinatal and adult cell cultures. Implications for remyelination in multiple sclerosis. Cid C, etal., J Neurochem. 2005 Oct;95(2):349-60. Epub 2005 Aug 31.
6. Canonical and kinase activity-independent mechanisms for extracellular signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation of Hsp90 from the ERK5-Cdc37 complex. Erazo T, etal., Mol Cell Biol. 2013 Apr;33(8):1671-86. doi: 10.1128/MCB.01246-12. Epub 2013 Feb 19.
7. Mass spectrometry analysis of complexes formed by myotonic dystrophy protein kinase (DMPK). Forner F, etal., Biochim Biophys Acta. 2010 Jun;1804(6):1334-41. Epub 2010 Feb 25.
8. HSP90 interacting with IRS-2 is involved in cAMP-dependent potentiation of IGF-I signals in FRTL-5 cells. Fukushima T, etal., Mol Cell Endocrinol. 2011 Sep 15;344(1-2):81-9. Epub 2011 Jul 1.
9. Cocaine withdrawal causes delayed dysregulation of stress genes in the hippocampus. Garcia-Fuster MJ, etal., PLoS One. 2012;7(7):e42092. doi: 10.1371/journal.pone.0042092. Epub 2012 Jul 30.
10. 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.
11. Apg-2 has a chaperone-like activity similar to Hsp110 and is overexpressed in hepatocellular carcinomas. Gotoh K, etal., FEBS Lett 2004 Feb 27;560(1-3):19-24.
12. Down-regulation of heat shock protein HSP90ab1 in radiation-damaged lung cells other than mast cells. Haase MG, etal., J Histochem Cytochem. 2014 May;62(5):355-68. doi: 10.1369/0022155414529133. Epub 2014 Mar 26.
13. Protein kinase C-delta mediates neuronal apoptosis in the retinas of diabetic rats via the Akt signaling pathway. Kim YH, etal., Diabetes. 2008 Aug;57(8):2181-90. Epub 2008 Apr 28.
14. Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein Hsp90. Krzemień-Ojak Ł, etal., J Cell Biochem. 2017 Feb;118(2):420-429. doi: 10.1002/jcb.25669. Epub 2016 Oct 17.
15. Heat shock protein 90 regulates IkappaB kinase complex and NF-kappaB activation in angiotensin II-induced cardiac cell hypertrophy. Lee KH, etal., Exp Mol Med. 2010 Oct 31;42(10):703-11.
16. 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.
17. Purification and identification of secreted oxidative stress-induced factors from vascular smooth muscle cells. Liao DF, etal., J Biol Chem 2000 Jan 7;275(1):189-96.
18. Protective effect of L-Arginine administration on proteins of unloaded m. soleus. Lomonosova YN, etal., Biochemistry (Mosc). 2011 May;76(5):571-80. doi: 10.1134/S0006297911050075.
19. Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. Luo W, etal., Proc Natl Acad Sci U S A. 2007 May 29;104(22):9511-6. doi: 10.1073/pnas.0701055104. Epub 2007 May 21.
20. Paternal exposure to testis cancer chemotherapeutics alters sperm fertilizing capacity and affects gene expression in the eight-cell stage rat embryo. Maselli J, etal., Andrology. 2014 Mar;2(2):259-66. doi: 10.1111/j.2047-2927.2014.00185.x. Epub 2014 Jan 29.
21. Cloning and regulation by glucocorticoid receptor ligands of a rat hsp90. McGuire JA, etal., J Steroid Biochem Mol Biol 1992 Sep;42(8):813-22.
22. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
23. Acute pancreatitis: hypertonic saline increases heat shock proteins 70 and 90 and reduces neutrophil infiltration in lung injury. Moretti AI, etal., Pancreas. 2009 Jul;38(5):507-14.
24. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
25. PID Annotation Import Pipeline Pipeline to import Pathway Interaction Database annotations from NCI into RGD
26. A block in the road to fertility: autoantibodies to heat-shock protein 90-beta in human ovarian autoimmunity. Pires ES and Khole VV, Fertil Steril. 2009 Oct;92(4):1395-409. doi: 10.1016/j.fertnstert.2008.08.068. Epub 2008 Nov 19.
27. Chaperoning of glucocorticoid receptors. Pratt WB, etal., Handb Exp Pharmacol. 2006;(172):111-38.
28. Molecular chaperones throughout the life cycle of the androgen receptor. Prescott J and Coetzee GA, Cancer Lett. 2006 Jan 8;231(1):12-9.
29. Upregulation and intrarenal redistribution of heat shock proteins 90alpha and 90beta by low-sodium diet in the rat. Ramirez V, etal., Cell Stress Chaperones. 2004 Summer;9(2):198-206.
30. GOA pipeline RGD automated data pipeline
31. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
32. Identification of HSP90 as a new GABARAPL1 (GEC1)-interacting protein. Seguin-Py S, etal., Biochimie. 2011 Nov 20.
33. Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions. Smith DF and Toft DO, Mol Endocrinol. 2008 Oct;22(10):2229-40. Epub 2008 May 1.
34. Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site. Soti C, etal., Eur J Biochem 2003 Jun;270(11):2421-8.
35. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Strausberg RL, etal., Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.
36. Gamendazole, an orally active indazole carboxylic acid male contraceptive agent, targets HSP90AB1 (HSP90BETA) and EEF1A1 (eEF1A), and stimulates Il1a transcription in rat Sertoli cells. Tash JS, etal., Biol Reprod. 2008 Jun;78(6):1139-52. doi: 10.1095/biolreprod.107.062679. Epub 2008 Jan 23.
37. Pseudovacuoles--immobilized by high-pressure freezing--are associated with blebbing in walker carcinosarcoma cells. Vanhecke D, etal., J Microsc. 2008 May;230(Pt 2):253-62.
38. Role of Hsp90 in biogenesis of the beta-cell ATP-sensitive potassium channel complex. Yan FF, etal., Mol Biol Cell. 2010 Jun 15;21(12):1945-54. Epub 2010 Apr 28.
39. Interactions of the mineralocorticoid receptor--within and without. Yang J and Fuller PJ, Mol Cell Endocrinol. 2012 Mar 24;350(2):196-205. doi: 10.1016/j.mce.2011.07.001. Epub 2011 Jul 18.
40. The potential role of heat shock proteins in acute spinal cord injury. Zhou Y, etal., Eur Spine J. 2014 Jul;23(7):1480-90. doi: 10.1007/s00586-014-3214-1. Epub 2014 Feb 6.
Additional References at PubMed
PMID:3189818   PMID:7588731   PMID:8663025   PMID:9122205   PMID:9798653   PMID:10197982   PMID:10543959   PMID:10654595   PMID:10791971   PMID:10811660   PMID:11732320   PMID:11785981  
PMID:14651853   PMID:15489334   PMID:15581363   PMID:15713458   PMID:15808839   PMID:16166581   PMID:16207813   PMID:16280321   PMID:16396499   PMID:16580629   PMID:16641100   PMID:16809764  
PMID:16854843   PMID:17475835   PMID:17562399   PMID:17908927   PMID:18239673   PMID:18320580   PMID:18845059   PMID:18850735   PMID:19292454   PMID:19751963   PMID:19946888   PMID:20353823  
PMID:20458337   PMID:20599762   PMID:20833797   PMID:21063103   PMID:21183720   PMID:21266579   PMID:21855797   PMID:22082260   PMID:22658674   PMID:22681889   PMID:22843495   PMID:22871113  
PMID:22939624   PMID:23106098   PMID:23349634   PMID:23431407   PMID:23484111   PMID:23533145   PMID:23904609   PMID:24098578   PMID:24286867   PMID:24466266   PMID:24613385   PMID:24625528  
PMID:24880080   PMID:25468996   PMID:26316108   PMID:26593036   PMID:27686098   PMID:29476059   PMID:30382094   PMID:31686426   PMID:32357304  


Genomics

Comparative Map Data
Hsp90ab1
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.2915,432,986 - 15,438,358 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl915,433,691 - 15,438,488 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx924,019,488 - 24,024,885 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0929,082,165 - 29,087,562 (+)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0927,382,927 - 27,388,324 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0917,817,791 - 17,823,163 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl917,817,721 - 17,823,243 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0916,706,512 - 16,711,884 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4911,033,496 - 11,038,868 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1911,030,786 - 11,036,319 (+)NCBI
Celera913,176,225 - 13,181,597 (+)NCBICelera
Cytogenetic Map9q12NCBI
HSP90AB1
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh38644,246,194 - 44,253,883 (+)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl644,246,166 - 44,253,888 (+)EnsemblGRCh38hg38GRCh38
GRCh37644,213,931 - 44,221,620 (+)NCBIGRCh37GRCh37hg19GRCh37
Build 36644,322,827 - 44,329,592 (+)NCBINCBI36Build 36hg18NCBI36
Build 34644,322,826 - 44,329,592NCBI
Celera645,767,994 - 45,774,759 (+)NCBICelera
Cytogenetic Map6p21.1NCBI
HuRef643,935,917 - 43,943,640 (+)NCBIHuRef
CHM1_1644,217,626 - 44,225,330 (+)NCBICHM1_1
T2T-CHM13v2.0644,080,360 - 44,088,031 (+)NCBIT2T-CHM13v2.0
Hsp90ab1
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm391745,878,704 - 45,884,187 (-)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl1745,878,701 - 45,884,197 (-)EnsemblGRCm39 Ensembl
GRCm381745,567,778 - 45,573,261 (-)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl1745,567,775 - 45,573,271 (-)EnsemblGRCm38mm10GRCm38
MGSCv371745,704,727 - 45,710,210 (-)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv361745,031,359 - 45,036,842 (-)NCBIMGSCv36mm8
Celera1749,000,428 - 49,005,921 (-)NCBICelera
Cytogenetic Map17B3NCBI
cM Map1722.59NCBI
Hsp90ab1
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_0049554379,873,908 - 9,878,459 (+)EnsemblChiLan1.0
ChiLan1.0NW_0049554379,872,649 - 9,878,459 (+)NCBIChiLan1.0ChiLan1.0
HSP90AB1
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1654,620,583 - 54,627,983 (+)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v0643,842,796 - 43,849,637 (+)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.1645,126,060 - 45,132,972 (+)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl645,125,773 - 45,133,872 (+)Ensemblpanpan1.1panPan2
HSP90AB1
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.11212,658,415 - 12,664,945 (+)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl1212,660,008 - 12,664,940 (+)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha1212,682,075 - 12,689,685 (+)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.01213,139,324 - 13,147,144 (+)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl1213,140,459 - 13,147,650 (+)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.11212,665,005 - 12,672,579 (+)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.01212,752,685 - 12,760,264 (+)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.01212,846,448 - 12,854,258 (+)NCBIUU_Cfam_GSD_1.0
Hsp90ab1
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_02440494648,123,181 - 48,129,743 (+)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_00493647615,830,459 - 15,835,535 (-)EnsemblSpeTri2.0
SpeTri2.0NW_00493647615,830,459 - 15,836,994 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
HSP90AB1
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl739,244,458 - 39,250,481 (+)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.1739,237,299 - 39,250,479 (+)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.2745,106,779 - 45,119,936 (+)NCBISscrofa10.2Sscrofa10.2susScr3
HSP90AB1
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.11727,914,261 - 27,921,666 (-)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl1727,911,013 - 27,921,251 (-)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_02366604444,300,580 - 44,307,963 (+)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Hsp90ab1
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_00462475415,609,920 - 15,614,263 (-)EnsemblHetGla_female_1.0HetGla_female_1.0 EnsemblhetGla2
HetGla 1.0NW_00462475415,609,932 - 15,615,580 (-)NCBIHetGla_female_1.0HetGla 1.0hetGla2

Variants

.
Variants in Hsp90ab1
42 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:292
Count of miRNA genes:191
Interacting mature miRNAs:214
Transcripts:ENSRNOT00000026920
Prediction methods:Microtar, 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
70226Eae4Experimental allergic encephalomyelitis QTL 4nervous system integrity trait (VT:0010566)experimental autoimmune encephalomyelitis incidence/prevalence measurement (CMO:0001046)9125661317Rat
9589055Scfw5Subcutaneous fat weight QTL 55.550.001subcutaneous adipose mass (VT:1000472)abdominal subcutaneous fat pad weight (CMO:0002069)9137999212Rat
7411592Foco8Food consumption QTL 87.40.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)9137999212Rat
9589158Gluco65Glucose level QTL 656.820.001blood glucose amount (VT:0000188)plasma glucose level (CMO:0000042)9137999212Rat
1300124Cm4Cardiac mass QTL 43.55heart mass (VT:0007028)heart weight to body weight ratio (CMO:0000074)9140594091Rat
1298088Edpm11Estrogen-dependent pituitary mass QTL 112.5pituitary gland mass (VT:0010496)pituitary gland wet weight (CMO:0000853)9143718459Rat
1641911Alcrsp13Alcohol response QTL 13response to alcohol trait (VT:0010489)brain neurotensin receptor 1 density (CMO:0002068)9143718459Rat
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
1354650Despr5Despair related QTL 54.010.0017locomotor behavior trait (VT:0001392)amount of time spent in voluntary immobility (CMO:0001043)9125408446254084Rat
2303559Gluco54Glucose level QTL 542blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)9125408446254084Rat
61425Cia15Collagen induced arthritis QTL 154.6joint integrity trait (VT:0010548)joint inflammation composite score (CMO:0000919)9510982642921101Rat
631211Bw4Body weight QTL45.31retroperitoneal fat pad mass (VT:0010430)retroperitoneal fat pad weight to body weight ratio (CMO:0000635)9510982650109826Rat
11353947Bp392Blood pressure QTL 392arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)9728325252283252Rat
61450Ciaa3CIA Autoantibody QTL 36.5blood autoantibody amount (VT:0003725)calculated serum anti-type 2 collagen antibody titer (CMO:0001279)9795472022071169Rat
9589133Insul26Insulin level QTL 2617.960.001blood insulin amount (VT:0001560)plasma insulin level (CMO:0000342)9895256053952560Rat
7411609Foco16Food consumption QTL 1625.60.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)9895256053952560Rat
1600365Mcs20Mammary carcinoma susceptibility QTL 203mammary gland integrity trait (VT:0010552)mammary tumor growth rate (CMO:0000344)91353377042791750Rat

Markers in Region
RH127542  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2915,438,717 - 15,438,913 (+)MAPPERmRatBN7.2
Rnor_6.0917,823,523 - 17,823,718NCBIRnor6.0
Rnor_5.0916,712,244 - 16,712,439UniSTSRnor5.0
RGSC_v3.4911,039,228 - 11,039,424UniSTSRGSC3.4
Celera913,181,957 - 13,182,152UniSTS
RH 3.4 Map978.5UniSTS
Cytogenetic Map9q12UniSTS
RH129394  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2915,438,604 - 15,438,786 (+)MAPPERmRatBN7.2
Rnor_6.0917,823,410 - 17,823,591NCBIRnor6.0
Rnor_5.0916,712,131 - 16,712,312UniSTSRnor5.0
RGSC_v3.4911,039,115 - 11,039,296UniSTSRGSC3.4
Celera913,181,844 - 13,182,025UniSTS
RH 3.4 Map21089.99UniSTS
Cytogenetic Map9q12UniSTS
RH140045  
Rat AssemblyChrPosition (strand)SourceJBrowse
Rnor_5.02196,981,799 - 196,982,006NCBIRnor5.0
Rnor_5.02249,154,349 - 249,154,557NCBIRnor5.0
RGSC_v3.42223,131,022 - 223,131,229UniSTSRGSC3.4
RGSC_v3.42170,299,880 - 170,300,086UniSTSRGSC3.4
Celera2206,759,298 - 206,759,505UniSTS
Celera2158,132,772 - 158,132,978UniSTS
RH 3.4 Map979.0UniSTS
Cytogenetic Map9q12UniSTS
Cytogenetic Map2q42UniSTS


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 2 22 12 12 2 12 64 18 29 2
Medium 1 21 45 29 17 29 8 11 10 17 12 9 8
Low
Below cutoff

Sequence

Nucleotide Sequences
RefSeq Transcripts NM_001004082 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
GenBank Nucleotide AC096454 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AY695392 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AY695393 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AY724481 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  BC082009 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  DQ022068 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ214469 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ215307 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ223952 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ225238 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ225402 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ227008 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ231832 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ233455 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ233497 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ233518 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  JACYVU010000213 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  S45392 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles

Reference Sequences
RefSeq Acc Id: ENSRNOT00000026920   ⟹   ENSRNOP00000026920
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl915,433,691 - 15,438,361 (+)Ensembl
Rnor_6.0 Ensembl917,817,791 - 17,823,163 (+)Ensembl
RefSeq Acc Id: ENSRNOT00000086986   ⟹   ENSRNOP00000074112
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl915,434,254 - 15,438,488 (+)Ensembl
Rnor_6.0 Ensembl917,817,721 - 17,823,243 (+)Ensembl
RefSeq Acc Id: ENSRNOT00000113617   ⟹   ENSRNOP00000093861
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl915,434,254 - 15,438,488 (+)Ensembl
RefSeq Acc Id: NM_001004082   ⟹   NP_001004082
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2915,432,986 - 15,438,358 (+)NCBI
Rnor_6.0917,817,791 - 17,823,163 (+)NCBI
Rnor_5.0916,706,512 - 16,711,884 (+)NCBI
RGSC_v3.4911,033,496 - 11,038,868 (+)RGD
Celera913,176,225 - 13,181,597 (+)RGD
Sequence:
Reference Protein Sequences
RefSeq Acc Id: NP_001004082   ⟸   NM_001004082
- UniProtKB: Q68GV5 (UniProtKB/Swiss-Prot),   Q66H55 (UniProtKB/Swiss-Prot),   Q1PSW2 (UniProtKB/Swiss-Prot),   Q9QWC6 (UniProtKB/Swiss-Prot),   P34058 (UniProtKB/Swiss-Prot),   A0A8L2QEA3 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: ENSRNOP00000026920   ⟸   ENSRNOT00000026920
RefSeq Acc Id: ENSRNOP00000074112   ⟸   ENSRNOT00000086986
RefSeq Acc Id: ENSRNOP00000093861   ⟸   ENSRNOT00000113617
Protein Domains
Histidine kinase/HSP90-like ATPase

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-P34058-F1-model_v2 AlphaFold P34058 1-724 view protein structure

Transcriptome

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

Promoters
RGD ID:13696546
Promoter ID:EPDNEW_R7065
Type:multiple initiation site
Name:Hsp90ab1_1
Description:heat shock protein 90 alpha family class B 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_6.0917,817,739 - 17,817,799EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:1303075 AgrOrtholog
BioCyc Gene G2FUF-28175 BioCyc
Ensembl Genes ENSRNOG00000019834 Ensembl, ENTREZGENE, UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000026920.7 UniProtKB/TrEMBL
  ENSRNOT00000086986 ENTREZGENE, UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  ENSRNOT00000113617.1 UniProtKB/TrEMBL
Gene3D-CATH 1.20.120.790 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.30.230.80 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.30.565.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.40.50.11260 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
IMAGE_CLONE IMAGE:7131767 IMAGE-MGC_LOAD
InterPro HATPase_C UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  HATPase_C_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Heat_shock_protein_90_CS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  HSP90_C UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Hsp90_fam UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Hsp90_N UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Ribosomal_S5_D2-typ_fold UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:301252 UniProtKB/Swiss-Prot
MGC_CLONE MGC:94263 IMAGE-MGC_LOAD
NCBI Gene 301252 ENTREZGENE
PANTHER HEAT SHOCK PROTEIN HSP 90-BETA UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PTHR11528 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam HATPase_c UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  HSP90 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Hsp90ab1 PhenoGen
PIRSF Hsp90 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PRINTS HEATSHOCK90 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PROSITE HSP90 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000019834 RatGTEx
SMART HATPase_c UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Superfamily-SCOP SSF110942 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF54211 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF55874 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
UniProt A0A0G2K793_RAT UniProtKB/TrEMBL
  A0A8I6AKS6_RAT UniProtKB/TrEMBL
  A0A8L2QEA3 ENTREZGENE, UniProtKB/TrEMBL
  HS90B_RAT UniProtKB/Swiss-Prot, ENTREZGENE
  Q1PSW2 ENTREZGENE
  Q66H55 ENTREZGENE
  Q68GV5 ENTREZGENE
  Q9QWC6 ENTREZGENE
UniProt Secondary Q1PSW2 UniProtKB/Swiss-Prot
  Q66H55 UniProtKB/Swiss-Prot
  Q68GV5 UniProtKB/Swiss-Prot
  Q9QWC6 UniProtKB/Swiss-Prot


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2016-06-29 Hsp90ab1  heat shock protein 90 alpha family class B member 1  Hsp90ab1  heat shock protein 90kDa alpha family class B member 1  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2016-02-25 Hsp90ab1  heat shock protein 90kDa alpha family class B member 1  Hsp90ab1  heat shock protein 90 alpha (cytosolic), class B member 1  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2011-04-27 Hsp90ab1  heat shock protein 90 alpha (cytosolic), class B member 1  Hsp90ab1  heat shock protein 90kDa alpha (cytosolic), class B member 1  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2008-01-09 Hsp90ab1  heat shock protein 90kDa alpha (cytosolic), class B member 1  Hspcb  heat shock 90kDa protein 1, beta  Symbol and Name updated to reflect Human and Mouse nomenclature 1299863 APPROVED
2006-03-30 Hspcb  heat shock 90kDa protein 1, beta      Symbol and Name status set to approved 1299863 APPROVED
2005-02-14 Hspcb  heat shock 90kDa protein 1, beta      Symbol and Name status set to provisional 70820 PROVISIONAL