Prkn (parkin RBR E3 ubiquitin protein ligase) - Rat Genome Database

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Gene: Prkn (parkin RBR E3 ubiquitin protein ligase) Rattus norvegicus
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Symbol: Prkn
Name: parkin RBR E3 ubiquitin protein ligase
RGD ID: 61797
Description: Enables protein kinase binding activity. Involved in several processes, including cellular response to amino acid stimulus; modulation of chemical synaptic transmission; and regulation of apoptotic process. Located in several cellular components, including Golgi membrane; neuronal cell body; and synaptic vesicle. Is active in glutamatergic synapse; postsynapse; and synaptic vesicle membrane. Colocalizes with mitochondrion. Used to study Parkinson's disease. Biomarker of metabolic dysfunction-associated steatohepatitis and type 2 diabetes mellitus. Human ortholog(s) of this gene implicated in Parkinson's disease; Parkinson's disease 2; lung cancer; and ovarian cancer. Orthologous to human PRKN (parkin RBR E3 ubiquitin protein ligase); PARTICIPATES IN altered mitochondrial autophagy pathway; mitochondrial autophagy pathway; Parkinson's disease pathway; INTERACTS WITH 1,3-dichloropropan-2-ol; 3-chloropropane-1,2-diol; 3-methyladenine.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: E3 ubiquitin-protein ligase parkin; Park; Park2; parkin; parkin RBR E3 ubiquitin protein ligase 2; parkin variant SV5DEL; Parkinson disease (autosomal recessive, juvenile) 2, parkin; parkinson protein 2, E3 ubiquitin protein ligase
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Black Rat
Alliance Orthologs
More Info more info ...
Allele / Splice: Prknem1Sage
Genetic Models: LE-Prknem1Sage-/- ; LE-Prknem1Sage
Latest Assembly: GRCr8 - GRCr8 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr8151,236,410 - 52,430,242 (-)NCBIGRCr8GRCr8GRCr8
GRCr8 Ensembl151,210,330 - 52,430,304 (-)EnsemblGRCr8
mRatBN7.2148,688,651 - 49,882,520 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl148,690,556 - 49,882,555 (-)EnsemblmRatBN7.2
UTH_Rnor_SHR_Utx149,387,875 - 50,601,445 (-)NCBIUTH_Rnor_SHR_UtxUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0155,372,640 - 56,585,891 (-)NCBIUTH_Rnor_SHRSP_BbbUtx_1.0UTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0149,463,372 - 50,676,968 (-)NCBIUTH_Rnor_WKY_Bbb_1.0UTH_Rnor_WKY_Bbb_1.0
Rnor_6.0148,880,015 - 50,069,998 (-)NCBIRnor_6.0Rnor_6.0rn6Rnor6.0
Rnor_5.0149,684,308 - 50,875,397 (+)NCBIRnor_5.0Rnor_5.0rn5
RGSC_v3.4143,151,265 - 44,374,470 (-)NCBIRGSC_v3.4RGSC_v3.4rn4
Celera144,478,407 - 45,666,902 (-)NCBICelera
RGSC_v3.1143,154,209 - 44,377,415 (-)NCBI
Cytogenetic Map1q11NCBI
JBrowse:




Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(-)-selegiline  (ISO)
(1->4)-beta-D-glucan  (ISO)
(R)-lipoic acid  (ISO)
(S)-nicotine  (ISO)
1,2-dimethylhydrazine  (ISO)
1,3-dichloropropan-2-ol  (EXP)
1,4-benzoquinone  (ISO)
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine  (ISO)
17beta-estradiol  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (ISO)
3-BROMO-7-NITROINDAZOLE  (ISO)
3-chloropropane-1,2-diol  (EXP)
3-methyladenine  (EXP)
4,4'-sulfonyldiphenol  (ISO)
4,5,6,7-TETRABROMOBENZOTRIAZOLE  (ISO)
4-hydroxy-TEMPO  (EXP)
6-propyl-2-thiouracil  (EXP)
A-967079  (ISO)
acetaldehyde  (ISO)
acetamide  (EXP)
acetylcholine  (ISO)
aflatoxin B1  (ISO)
Aflatoxin B2 alpha  (ISO)
aldehydo-D-glucose  (EXP)
all-trans-retinoic acid  (ISO)
aluminium atom  (ISO)
aluminium(0)  (ISO)
ammonium chloride  (EXP)
amphetamine  (ISO)
androgen antagonist  (EXP)
antimycin A  (ISO)
antirheumatic drug  (ISO)
aristolochic acid A  (ISO)
Aroclor 1254  (EXP)
arsane  (ISO)
arsenic atom  (ISO)
arsenous acid  (EXP,ISO)
atrazine  (EXP)
azoxystrobin  (ISO)
Bardoxolone methyl  (EXP)
benzo[a]pyrene  (EXP,ISO)
benzo[e]pyrene  (ISO)
berberine  (EXP)
bis(2-ethylhexyl) phthalate  (EXP,ISO)
bisphenol A  (EXP,ISO)
bisphenol F  (ISO)
bupivacaine  (ISO)
Butylparaben  (EXP)
C60 fullerene  (EXP)
cadmium atom  (EXP,ISO)
cadmium dichloride  (EXP,ISO)
cannabidiol  (EXP)
cantharidin  (ISO)
carbon nanotube  (ISO)
carbonyl cyanide p-trifluoromethoxyphenylhydrazone  (ISO)
carnosic acid  (ISO)
CCCP  (EXP,ISO)
CGP 52608  (ISO)
chloroquine  (EXP,ISO)
chlorpyrifos  (ISO)
chromium(6+)  (ISO)
cinnarizine  (ISO)
cisplatin  (EXP)
clothianidin  (ISO)
coenzyme Q10  (ISO)
curcumin  (EXP,ISO)
cyclosporin A  (EXP,ISO)
D-glucose  (EXP)
DDE  (EXP)
diarsenic trioxide  (EXP,ISO)
diazinon  (EXP)
dibutyl phthalate  (EXP)
dieldrin  (ISO)
dioxygen  (EXP,ISO)
dopamine  (ISO)
dorsomorphin  (EXP)
doxorubicin  (EXP,ISO)
emtricitabine  (ISO)
enzacamene  (EXP)
epoxiconazole  (EXP)
epoxomicin  (EXP,ISO)
ethanol  (ISO)
fenpyroximate  (ISO)
folic acid  (ISO)
formaldehyde  (ISO)
fulvestrant  (ISO)
fumonisin B1  (ISO)
furan  (EXP)
furosemide  (EXP)
Genipin  (ISO)
ginsenoside Rb1  (EXP)
glucose  (EXP)
glutathione  (ISO)
hexadecanoic acid  (ISO)
Honokiol  (EXP)
hydrogen peroxide  (EXP,ISO)
indole-3-methanol  (EXP)
indometacin  (ISO)
inositol  (EXP)
iodixanol  (EXP)
ketoconazole  (EXP)
kynurenine  (ISO)
L-citrulline  (ISO)
Lasiocarpine  (ISO)
lead diacetate  (ISO)
lead(0)  (EXP,ISO)
linagliptin  (EXP)
linsidomine  (ISO)
linuron  (EXP)
lipoic acid  (ISO)
lipopolysaccharide  (EXP)
luteolin  (ISO)
lycopene  (ISO)
maneb  (ISO)
manganese atom  (EXP,ISO)
manganese(0)  (EXP,ISO)
manganese(II) chloride  (EXP,ISO)
melatonin  (EXP)
metformin  (ISO)
methamphetamine  (EXP,ISO)
methapyrilene  (ISO)
methoxychlor  (EXP)
methylmercury chloride  (ISO)
miconazole  (EXP)
minocycline  (ISO)
MitoTEMPO  (ISO)
mono(2-ethylhexyl) phthalate  (ISO)
N-acetyl-L-cysteine  (EXP,ISO)
N-benzyloxycarbonyl-L-leucyl-L-leucyl-L-leucinal  (EXP,ISO)
N-methyl-4-phenylpyridinium  (ISO)
N-Nitrosopyrrolidine  (ISO)
nickel atom  (ISO)
nickel dichloride  (ISO)
nicotine  (ISO)
O-acetyl-L-carnitine  (ISO)
O-methyleugenol  (ISO)
okadaic acid  (ISO)
oleic acid  (ISO)
oligomycin A  (ISO)
oxidopamine  (EXP,ISO)
ozone  (ISO)
paracetamol  (EXP,ISO)
paraquat  (ISO)
perfluorooctane-1-sulfonic acid  (EXP,ISO)
picoxystrobin  (ISO)
poly(guanylic acid)  (EXP)
poly(vinylpyrrolidone)  (ISO)
prochloraz  (EXP)
procymidone  (EXP)
pyrimidifen  (ISO)
quercetin 3-O-beta-D-glucofuranoside  (EXP)
quercetin 3-O-beta-D-glucopyranoside  (EXP)
reactive oxygen species  (ISO)
resveratrol  (EXP,ISO)
rimonabant  (EXP,ISO)
rotenone  (EXP,ISO)
rutin  (EXP)
S-nitrosoglutathione  (ISO)
silibinin  (ISO)
silicon dioxide  (EXP)
sirolimus  (EXP,ISO)
sirtinol  (ISO)
sodium arsenite  (EXP,ISO)
sodium fluoride  (ISO)
sorafenib  (ISO)
sunitinib  (ISO)
T-2 toxin  (EXP)
taurine  (EXP)
tebufenpyrad  (ISO)
tenofovir disoproxil fumarate  (ISO)
tetrachloromethane  (EXP,ISO)
thioacetamide  (EXP)
Tiron  (EXP,ISO)
titanium dioxide  (ISO)
trans-piceid  (ISO)
trifloxystrobin  (ISO)
trifluoperazine  (ISO)
trimellitic anhydride  (ISO)
tubocurarine  (ISO)
Urolithin A  (EXP,ISO)
valproic acid  (ISO)
vanillin  (ISO)
venlafaxine hydrochloride  (EXP)
vinclozolin  (EXP)

Gene Ontology Annotations     Click to see Annotation Detail View

Biological Process
adult locomotory behavior  (ISO,ISS)
aggresome assembly  (IEA,ISO,ISS)
autophagy  (IEA)
autophagy of mitochondrion  (IEA,ISO,ISS)
cellular response to hydrogen sulfide  (IDA)
cellular response to L-glutamate  (IDA)
cellular response to L-glutamine  (IEP)
cellular response to manganese ion  (IEP)
cellular response to oxidative stress  (IMP)
cellular response to toxic substance  (IEA,ISO,ISS)
DNA-templated transcription  (IEA)
dopamine metabolic process  (ISO)
dopamine uptake involved in synaptic transmission  (ISO)
free ubiquitin chain polymerization  (IEA,ISO)
host-mediated suppression of viral genome replication  (IEA,ISO)
learning  (ISO)
locomotory behavior  (ISO)
mitochondrial fission  (ISS)
mitochondrial fragmentation involved in apoptotic process  (IMP)
mitochondrion localization  (IDA)
mitochondrion organization  (ISS)
mitochondrion to lysosome vesicle-mediated transport  (IEA,ISO)
mitophagy  (IBA,IDA,IEA,ISO)
modulation of chemical synaptic transmission  (IBA,IEA,ISO)
negative regulation of actin filament bundle assembly  (IEA,ISO)
negative regulation of canonical Wnt signaling pathway  (IEA,ISO)
negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway  (IEA,ISO,ISS)
negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway  (IEA,ISO)
negative regulation of excitatory postsynaptic potential  (IMP)
negative regulation of exosomal secretion  (IEA,ISO)
negative regulation of gene expression  (IEA,ISO)
negative regulation of glucokinase activity  (ISO)
negative regulation of insulin secretion  (ISO,ISS)
negative regulation of intracellular signal transduction  (IEA)
negative regulation of intralumenal vesicle formation  (IEA,ISO)
negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator  (IEA,ISO)
negative regulation of JNK cascade  (ISS)
negative regulation of mitochondrial fission  (IMP)
negative regulation of mitochondrial fusion  (ISS)
negative regulation of neuron apoptotic process  (IEA,IGI,IMP,ISO,ISS)
negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway  (IEA,IGI,ISO,ISS)
negative regulation of reactive oxygen species biosynthetic process  (IMP)
negative regulation of reactive oxygen species metabolic process  (IEA,ISO,ISS)
negative regulation of release of cytochrome c from mitochondria  (IEA,ISO,ISS)
negative regulation of spontaneous neurotransmitter secretion  (IEA,ISO)
negative regulation of synaptic transmission, glutamatergic  (IMP)
negative regulation of transcription by RNA polymerase II  (IEA,ISO)
neuron cellular homeostasis  (ISS)
norepinephrine metabolic process  (ISO)
positive regulation of apoptotic process  (IMP)
positive regulation of ATP biosynthetic process  (IMP)
positive regulation of canonical NF-kappaB signal transduction  (IEA,ISO,ISS)
positive regulation of catabolic process  (IEA)
positive regulation of dendrite extension  (IEA,ISO)
positive regulation of gene expression  (IEA,ISO)
positive regulation of insulin secretion involved in cellular response to glucose stimulus  (IMP)
positive regulation of metabolic process  (IEA)
positive regulation of mitochondrial fission  (ISS)
positive regulation of mitochondrial fusion  (IEA,ISO,ISS)
positive regulation of mitochondrial membrane potential  (IMP)
positive regulation of mitophagy  (IEA,IMP,ISO)
positive regulation of neurotransmitter uptake  (IEA,ISO)
positive regulation of proteasomal protein catabolic process  (IEA,ISO)
positive regulation of proteasomal ubiquitin-dependent protein catabolic process  (IEA,ISO)
positive regulation of protein linear polyubiquitination  (IEA,ISO)
positive regulation of protein localization to membrane  (IEA,ISO)
positive regulation of transcription by RNA polymerase II  (IEA,ISO,ISS)
positive regulation of tumor necrosis factor-mediated signaling pathway  (IEA,ISO,ISS)
positive regulation of type 2 mitophagy  (IEA,ISO)
proteasomal protein catabolic process  (IEA,ISO)
proteasome-mediated ubiquitin-dependent protein catabolic process  (IEA,ISO,ISS)
protein autoubiquitination  (IEA,ISO,ISS)
protein catabolic process  (IEA,ISO)
protein destabilization  (IEA,ISO,ISS)
protein K11-linked ubiquitination  (IEA,ISO,ISS)
protein K27-linked ubiquitination  (IEA,ISO)
protein K48-linked ubiquitination  (IEA,ISO)
protein K6-linked ubiquitination  (IEA,ISO,ISS)
protein K63-linked ubiquitination  (IEA,ISO,ISS)
protein localization to mitochondrion  (IDA,IEA,ISO,ISS)
protein monoubiquitination  (IEA,ISO,ISS)
protein polyubiquitination  (IEA,ISO,ISS)
protein stabilization  (IEA,ISO)
protein ubiquitination  (IDA,IEA,ISO,ISS)
regulation of anatomical structure morphogenesis  (IEA)
regulation of autophagy  (IEA,ISO,ISS)
regulation of cellular response to oxidative stress  (IEA,ISO,ISS)
regulation of dopamine metabolic process  (IEA,ISO)
regulation of mitochondrial membrane potential  (IEA,ISO)
regulation of mitochondrion organization  (IEA,ISO,ISS)
regulation of neurotransmitter secretion  (ISO)
regulation of postsynaptic membrane neurotransmitter receptor levels  (IDA,IEP,IMP)
regulation of primary metabolic process  (IEA)
regulation of protein stability  (IEA,ISO)
regulation of protein ubiquitination  (IEA,ISO)
regulation of reactive oxygen species metabolic process  (IEA,ISO)
regulation of secretion by cell  (IEA)
regulation of synaptic vesicle endocytosis  (IEA,ISO)
regulation protein catabolic process at presynapse  (IEA,ISO)
response to corticosterone  (IEP)
response to curcumin  (IEP)
response to endoplasmic reticulum stress  (IEA,IEP,ISO)
response to muscle activity  (IEP)
response to oxidative stress  (ISS)
response to stress  (IEA)
response to unfolded protein  (IEP)
response to xenobiotic stimulus  (IEP)
startle response  (ISO)
synaptic transmission, dopaminergic  (ISO)
synaptic transmission, glutamatergic  (ISO)
type 2 mitophagy  (IEA,ISO)
ubiquitin-dependent protein catabolic process  (IBA,IEA,ISO,ISS)

Cellular Component

References

References - curated
# Reference Title Reference Citation
1. Genes associated with Parkinson's disease: regulation of autophagy and beyond. Beilina A and Cookson MR, J Neurochem. 2015 Jul 30. doi: 10.1111/jnc.13266.
2. Brain GLP-1/IGF-1 Signaling and Autophagy Mediate Exendin-4 Protection Against Apoptosis in Type 2 Diabetic Rats. Candeias E, etal., Mol Neurobiol. 2017 Jun 2. doi: 10.1007/s12035-017-0622-3.
3. Melatonin-mediated mitophagy protects against early brain injury after subarachnoid hemorrhage through inhibition of NLRP3 inflammasome activation. Cao S, etal., Sci Rep. 2017 May 25;7(1):2417. doi: 10.1038/s41598-017-02679-z.
4. BECN1 is involved in the initiation of mitophagy: it facilitates PARK2 translocation to mitochondria. Choubey V, etal., Autophagy. 2014 Jun;10(6):1105-19. doi: 10.4161/auto.28615.
5. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Ciechanover A and Brundin P, Neuron 2003 Oct 9;40(2):427-46.
6. Cloning and distribution of the rat parkin mRNA. D'Agata V, etal., Brain Res Mol Brain Res 2000 Feb 22;75(2):345-9.
7. Distribution of parkin in the adult rat brain. D'Agata V, etal., Prog Neuropsychopharmacol Biol Psychiatry 2002 Apr;26(3):519-27.
8. The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications. Durcan TM and Fon EA, Genes Dev. 2015 May 15;29(10):989-99. doi: 10.1101/gad.262758.115.
9. Thymoquinone exerts neuroprotective effect in animal model of Parkinson's disease. Ebrahimi SS, etal., Toxicol Lett. 2017 Jul 5;276:108-114. doi: 10.1016/j.toxlet.2017.05.018. Epub 2017 May 17.
10. Upregulation of miR-96-5p by bone marrow mesenchymal stem cells and their exosomes alleviate non-alcoholic steatohepatitis: Emphasis on caspase-2 signaling inhibition. El-Derany MO and AbdelHamid SG, Biochem Pharmacol. 2021 Aug;190:114624. doi: 10.1016/j.bcp.2021.114624. Epub 2021 May 27.
11. Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain. Fallon L, etal., J Biol Chem. 2002 Jan 4;277(1):486-91. Epub 2001 Oct 25.
12. Heterozygosity for a mutation in the parkin gene leads to later onset Parkinson disease. Foroud T, etal., Neurology 2003 Mar 11;60(5):796-801.
13. 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.
14. Rat ISS GO annotations from GOA human gene data--August 2006 GOA data from the GO Consortium
15. Cloning of rat parkin cDNA and distribution of parkin in rat brain. Gu WJ, etal., J Neurochem 2000 Apr;74(4):1773-6.
16. Parkin regulation of CHOP modulates susceptibility to cardiac endoplasmic reticulum stress. Han K, etal., Sci Rep. 2017 May 18;7(1):2093. doi: 10.1038/s41598-017-02339-2.
17. Pruning and loss of excitatory synapses by the parkin ubiquitin ligase. Helton TD, etal., Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19492-7. doi: 10.1073/pnas.0802280105. Epub 2008 Nov 25.
18. Parkin overexpression ameliorates hippocampal long-term potentiation and beta-amyloid load in an Alzheimer's disease mouse model. Hong X, etal., Hum Mol Genet. 2014 Feb 15;23(4):1056-72. doi: 10.1093/hmg/ddt501. Epub 2013 Oct 8.
19. Regulation of hippocampal parkin protein by corticosteroids. Horowitz JM, etal., Neuroreport. 2003 Dec 19;14(18):2327-30.
20. Parkin overexpression protects retinal ganglion cells against glutamate excitotoxicity. Hu X, etal., Mol Vis. 2017 Jul 19;23:447-456. eCollection 2017.
21. Parkin and synphilin-1 isoform expression changes in Lewy body diseases. Humbert J, etal., Neurobiol Dis. 2007 Jun;26(3):681-7. Epub 2007 Mar 27.
22. Impaired intracellular trafficking defines early Parkinson's disease. Hunn BH, etal., Trends Neurosci. 2015 Mar;38(3):178-88. doi: 10.1016/j.tins.2014.12.009. Epub 2015 Jan 29.
23. The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Huynh DP, etal., Hum Mol Genet. 2003 Oct 15;12(20):2587-97. Epub 2003 Aug 12.
24. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Imai Y, etal., Mol Cell. 2002 Jul;10(1):55-67.
25. The PARK2 gene is involved in the maintenance of pancreatic beta-cell functions related to insulin production and secretion. Jin HS, etal., Mol Cell Endocrinol. 2014 Jan 25;382(1):178-89. doi: 10.1016/j.mce.2013.09.031. Epub 2013 Oct 3.
26. Melatonin enhances mitophagy and mitochondrial biogenesis in rats with carbon tetrachloride-induced liver fibrosis. Kang JW, etal., J Pineal Res. 2016 May;60(4):383-93. doi: 10.1111/jpi.12319. Epub 2016 Mar 7.
27. KEGG: Kyoto Encyclopedia of Genes and Genomes KEGG
28. Parkin cleaves intracellular alpha-synuclein inclusions via the activation of calpain. Kim SJ, etal., J Biol Chem 2003 Oct 24;278(43):41890-9. Epub 2003 Aug 12.
29. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Kitada T, etal., Nature. 1998 Apr 9;392(6676):605-8.
30. Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function. Ko HS, etal., Proc Natl Acad Sci U S A. 2010 Sep 21;107(38):16691-6. doi: 10.1073/pnas.1006083107. Epub 2010 Sep 7.
31. Mitochondria and mitophagy: the yin and yang of cell death control. Kubli DA and Gustafsson AB, Circ Res. 2012 Oct 12;111(9):1208-21. doi: 10.1161/CIRCRESAHA.112.265819.
32. Parkin is associated with cellular vesicles. Kubo SI, etal., J Neurochem. 2001 Jul;78(1):42-54.
33. Astrocytic but not neuronal increased expression and redistribution of parkin during unfolded protein stress. Ledesma MD, etal., J Neurochem 2002 Dec;83(6):1431-40.
34. Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. Lee JY, etal., J Cell Biol. 2010 May 17;189(4):671-9. doi: 10.1083/jcb.201001039. Epub 2010 May 10.
35. Hydrogen Sulphide modulating mitochondrial morphology to promote mitophagy in endothelial cells under high-glucose and high-palmitate. Liu N, etal., J Cell Mol Med. 2017 Jun 13. doi: 10.1111/jcmm.13223.
36. Parkin regulates kainate receptors by interacting with the GluK2 subunit. Maraschi A, etal., Nat Commun. 2014 Oct 15;5:5182. doi: 10.1038/ncomms6182.
37. Physical exercise mitigates doxorubicin-induced brain cortex and cerebellum mitochondrial alterations and cellular quality control signaling. Marques-Aleixo I, etal., Mitochondrion. 2016 Jan;26:43-57. doi: 10.1016/j.mito.2015.12.002. Epub 2015 Dec 8.
38. Down-regulation of parkin protein in transient focal cerebral ischemia: A link between stroke and degenerative disease? Mengesdorf T, etal., Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):15042-7. Epub 2002 Nov 1.
39. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
40. Ultrastructural localization of parkin in the rat brainstem, thalamus and basal ganglia. Mouatt-Prigent A, etal., J Neural Transm. 2004 Oct;111(10-11):1209-18. Epub 2004 Apr 13.
41. Effect of the neurotoxic dose of methamphetamine on gene expression of parkin and Pael-receptors in rat striatum. Nakahara T, etal., Parkinsonism Relat Disord. 2003 Mar;9(4):213-9.
42. Genetic and epigenetic alterations affecting PARK-2 expression in cervical neoplasm among North Indian patients. Naseem A, etal., Tumour Biol. 2017 Jun;39(6):1010428317703635. doi: 10.1177/1010428317703635.
43. Motor alterations are reduced in mice lacking the PARK2 gene in the presence of a human FTDP-17 mutant form of four-repeat tau. Navarro P, etal., J Neurol Sci. 2008 Dec 15;275(1-2):139-44. doi: 10.1016/j.jns.2008.08.013. Epub 2008 Sep 24.
44. OMIM Disease Annotation Pipeline OMIM Disease Annotation Pipeline
45. Curcumin prevents cisplatin-induced renal alterations in mitochondrial bioenergetics and dynamic. Ortega-Domínguez B, etal., Food Chem Toxicol. 2017 Sep;107(Pt A):373-385. doi: 10.1016/j.fct.2017.07.018. Epub 2017 Jul 8.
46. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
47. Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. Ren Y, etal., J Neurosci. 2003 Apr 15;23(8):3316-24.
48. GOA pipeline RGD automated data pipeline
49. ClinVar Automated Import and Annotation Pipeline RGD automated import pipeline for ClinVar variants, variant-to-disease annotations and gene-to-disease annotations
50. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
51. Novel insights into the antioxidant role of tauroursodeoxycholic acid in experimental models of Parkinson's disease. Rosa AI, etal., Biochim Biophys Acta. 2017 Sep;1863(9):2171-2181. doi: 10.1016/j.bbadis.2017.06.004. Epub 2017 Jun 3.
52. Effects of partial suppression of parkin on huntingtin mutant R6/1 mice. Rubio I, etal., Brain Res. 2009 Jul 24;1281:91-100. doi: 10.1016/j.brainres.2009.05.039. Epub 2009 May 21.
53. Parkin and PINK1: much more than mitophagy. Scarffe LA, etal., Trends Neurosci. 2014 Jun;37(6):315-24. doi: 10.1016/j.tins.2014.03.004. Epub 2014 Apr 13.
54. Parkin localizes to the Lewy bodies of Parkinson disease and dementia with Lewy bodies. Schlossmacher MG, etal., Am J Pathol. 2002 May;160(5):1655-67.
55. Mitochondrial quality control in alveolar epithelial cells damaged by S. aureus pneumonia in mice. Suliman HB, etal., Am J Physiol Lung Cell Mol Physiol. 2017 Jun 29:ajplung.00197.2017. doi: 10.1152/ajplung.00197.2017.
56. ATF4 protects against neuronal death in cellular Parkinson's disease models by maintaining levels of parkin. Sun X, etal., J Neurosci. 2013 Feb 6;33(6):2398-407. doi: 10.1523/JNEUROSCI.2292-12.2013.
57. Parkin ubiquitinates and promotes the degradation of RanBP2. Um JW, etal., J Biol Chem. 2006 Feb 10;281(6):3595-603. Epub 2005 Dec 6.
58. Glutamate excitotoxicity in neurons triggers mitochondrial and endoplasmic reticulum accumulation of Parkin, and, in the presence of N-acetyl cysteine, mitophagy. Van Laar VS, etal., Neurobiol Dis. 2015 Feb;74:180-93. doi: 10.1016/j.nbd.2014.11.015. Epub 2014 Dec 3.
59. Parkin protects against neurotoxicity in the 6-hydroxydopamine rat model for Parkinson's disease. Vercammen L, etal., Mol Ther. 2006 Nov;14(5):716-23. Epub 2006 Aug 17.
60. Expression changes of dopaminergic system-related genes in PC12 cells induced by manganese, silver, or copper nanoparticles. Wang J, etal., Neurotoxicology. 2009 Nov;30(6):926-33. Epub 2009 Sep 23.
61. Developmental changes in the expression of parkin and UbcR7, a parkin-interacting and ubiquitin-conjugating enzyme, in rat brain. Wang M, etal., J Neurochem. 2001 Jun;77(6):1561-8.
62. Selective removal of mitochondria via mitophagy: distinct pathways for different mitochondrial stresses. Wei H, etal., Biochim Biophys Acta. 2015 Oct;1853(10 Pt B):2784-90. doi: 10.1016/j.bbamcr.2015.03.013. Epub 2015 Apr 1.
63. Parkinson's disease-associated parkin colocalizes with Alzheimer's disease and multiple sclerosis brain lesions. Witte ME, etal., Neurobiol Dis. 2009 Dec;36(3):445-52. doi: 10.1016/j.nbd.2009.08.009. Epub 2009 Aug 27.
64. High expression of Parkin predicts easier recurrence of patients with adjuvant transarterial chemoembolization. Zhang C, etal., Biomark Med. 2017 Sep 1. doi: 10.2217/bmm-2017-0129.
65. Sorafenib targets the mitochondrial electron transport chain complexes and ATP synthase to activate the PINK1-Parkin pathway and modulate cellular drug response. Zhang C, etal., J Biol Chem. 2017 Sep 8;292(36):15105-15120. doi: 10.1074/jbc.M117.783175. Epub 2017 Jul 3.
66. Transgenic Mice Overexpressing the Divalent Metal Transporter 1 Exhibit Iron Accumulation and Enhanced Parkin Expression in the Brain. Zhang CW, etal., Neuromolecular Med. 2017 Jul 10. doi: 10.1007/s12017-017-8451-0.
67. Calcium/calmodulin-dependent protein kinase regulates the PINK1/Parkin and DJ-1 pathways of mitophagy during sepsis. Zhang X, etal., FASEB J. 2017 Jun 14. pii: fj.201601096RRR. doi: 10.1096/fj.201601096RRR.
68. TDP-43 upregulation mediated by the NLRP3 inflammasome induces cognitive impairment in 2 2',4,4'-tetrabromodiphenyl ether (BDE-47)-treated mice. Zhuang J, etal., Brain Behav Immun. 2017 Oct;65:99-110. doi: 10.1016/j.bbi.2017.05.014. Epub 2017 May 19.
Additional References at PubMed
PMID:10973942   PMID:11078524   PMID:11439185   PMID:11675120   PMID:12628165   PMID:12915482   PMID:12930822   PMID:14530399   PMID:14645198   PMID:14985362   PMID:15249681   PMID:15252205  
PMID:15453267   PMID:15576511   PMID:15603737   PMID:15684050   PMID:15728840   PMID:15882845   PMID:15987638   PMID:16174552   PMID:16227987   PMID:16352719   PMID:16554120   PMID:16905117  
PMID:16955485   PMID:17097639   PMID:17116640   PMID:17314283   PMID:17327227   PMID:17512523   PMID:17553932   PMID:17873367   PMID:17883392   PMID:18190519   PMID:18195004   PMID:18346797  
PMID:18541373   PMID:19029340   PMID:19229105   PMID:19279012   PMID:19339245   PMID:19591802   PMID:19725078   PMID:19880420   PMID:20064468   PMID:20798600   PMID:20871098   PMID:20889974  
PMID:21113145   PMID:21376232   PMID:21466165   PMID:21508222   PMID:21532592   PMID:21613270   PMID:21694720   PMID:21753002   PMID:21890690   PMID:22314364   PMID:22511790   PMID:22792159  
PMID:23152496   PMID:23212910   PMID:23258539   PMID:23393160   PMID:23453807   PMID:23661642   PMID:23858059   PMID:23933751   PMID:23985028   PMID:24063750   PMID:24187134   PMID:24337465  
PMID:24446486   PMID:24660806   PMID:24784582   PMID:24896179   PMID:24898855   PMID:24949970   PMID:25101677   PMID:25244949   PMID:25583483   PMID:25621951   PMID:26224857   PMID:26260794  
PMID:26310625   PMID:26364802   PMID:26465230   PMID:26911690   PMID:26935412   PMID:27284007   PMID:27601173   PMID:27797717   PMID:27841025   PMID:27903732   PMID:28063983   PMID:28254618  
PMID:28724963   PMID:29311685   PMID:29367643   PMID:29367744   PMID:29475881   PMID:29538088   PMID:30250268   PMID:30387846   PMID:30796971   PMID:31406131   PMID:32173525   PMID:32392329  
PMID:32900550   PMID:33012239   PMID:33125104   PMID:33296434   PMID:34001858   PMID:34248837   PMID:34298012   PMID:35042405   PMID:35426609   PMID:35491809   PMID:36350063   PMID:36563856  
PMID:36647045   PMID:36766738   PMID:36805078   PMID:36941054   PMID:37715413   PMID:38393524   PMID:38788061   PMID:39097918   PMID:39267792  


Genomics

Comparative Map Data
Prkn
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr8151,236,410 - 52,430,242 (-)NCBIGRCr8GRCr8GRCr8
GRCr8 Ensembl151,210,330 - 52,430,304 (-)EnsemblGRCr8
mRatBN7.2148,688,651 - 49,882,520 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl148,690,556 - 49,882,555 (-)EnsemblmRatBN7.2
UTH_Rnor_SHR_Utx149,387,875 - 50,601,445 (-)NCBIUTH_Rnor_SHR_UtxUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0155,372,640 - 56,585,891 (-)NCBIUTH_Rnor_SHRSP_BbbUtx_1.0UTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0149,463,372 - 50,676,968 (-)NCBIUTH_Rnor_WKY_Bbb_1.0UTH_Rnor_WKY_Bbb_1.0
Rnor_6.0148,880,015 - 50,069,998 (-)NCBIRnor_6.0Rnor_6.0rn6Rnor6.0
Rnor_5.0149,684,308 - 50,875,397 (+)NCBIRnor_5.0Rnor_5.0rn5
RGSC_v3.4143,151,265 - 44,374,470 (-)NCBIRGSC_v3.4RGSC_v3.4rn4
Celera144,478,407 - 45,666,902 (-)NCBICelera
RGSC_v3.1143,154,209 - 44,377,415 (-)NCBI
Cytogenetic Map1q11NCBI
PRKN
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh386161,347,417 - 162,727,766 (-)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl6161,347,417 - 162,727,775 (-)Ensemblhg38GRCh38
GRCh376161,768,449 - 163,148,798 (-)NCBIGRCh37GRCh37hg19GRCh37
Build 366161,689,661 - 163,068,793 (-)NCBIBuild 36Build 36hg18NCBI36
Build 346161,740,081 - 163,119,211NCBI
Celera6162,497,923 - 163,878,436 (-)NCBICelera
Cytogenetic Map6q26NCBI
HuRef6159,224,034 - 160,600,983 (-)NCBIHuRef
CHM1_16162,031,091 - 163,411,071 (-)NCBICHM1_1
T2T-CHM13v2.06162,705,911 - 164,090,895 (-)NCBIT2T-CHM13v2.0
Prkn
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm391711,059,227 - 12,282,257 (+)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl1711,059,271 - 12,282,248 (+)EnsemblGRCm39 EnsemblGRCm39
GRCm381710,840,359 - 12,063,370 (+)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl1710,840,384 - 12,063,361 (+)Ensemblmm10GRCm38
MGSCv371711,033,250 - 12,256,227 (+)NCBIMGSCv37MGSCv37mm9NCBIm37
MGSCv361710,683,742 - 11,906,719 (+)NCBIMGSCv36mm8
Celera1710,880,667 - 12,092,859 (+)NCBICelera
Cytogenetic Map17A1NCBI
cM Map177.8NCBI
Prkn
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_00495543918,664,379 - 19,951,152 (+)Ensembl
ChiLan1.0NW_00495543918,664,230 - 19,953,358 (+)NCBIChiLan1.0ChiLan1.0
PRKN
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1-v25181,523,208 - 182,914,092 (-)NCBINHGRI_mPanPan1-v2
NHGRI_mPanPan16179,428,720 - 180,815,536 (-)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v06159,293,016 - 160,679,106 (-)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.16164,498,420 - 165,678,904 (-)NCBIPanPan1.1PanPan1.1panPan2
PanPan1.1 Ensembl6164,314,990 - 165,678,770 (-)EnsemblpanPan2panpan1.1
PRKN
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.1149,886,887 - 51,201,930 (-)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl149,889,005 - 51,201,764 (-)EnsemblcanFam3CanFam3.1
Dog10K_Boxer_Tasha150,729,328 - 52,042,064 (-)NCBIDog10K_Boxer_TashaDog10K_Boxer_Tasha
ROS_Cfam_1.0150,071,882 - 51,381,593 (-)NCBIROS_Cfam_1.0ROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl150,071,597 - 51,381,376 (-)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.1149,954,154 - 51,268,026 (-)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.0149,824,568 - 51,126,809 (-)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.0150,440,798 - 51,751,574 (-)NCBIUU_Cfam_GSD_1.0UU_Cfam_GSD_1.0
Prkn
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_024404946144,866,545 - 145,855,394 (-)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_00493648912,120,678 - 13,327,872 (-)EnsemblSpeTri2.0 Ensembl
SpeTri2.0NW_00493648912,118,538 - 12,913,664 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
PRKN
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl15,465,312 - 6,730,872 (+)EnsemblsusScr11Sscrofa11.1
Sscrofa11.115,698,508 - 6,731,132 (+)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.217,649,954 - 8,260,243 (+)NCBISscrofa10.2Sscrofa10.2susScr3
Sscrofa10.217,197,051 - 7,562,040 (+)NCBISscrofa10.2Sscrofa10.2susScr3
PRKN
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.11388,856,056 - 90,329,379 (-)NCBIChlSab1.1ChlSab1.1chlSab2
Vero_WHO_p1.0NW_02366604061,183,625 - 62,136,281 (-)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Prkn
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_004624855430,260 - 1,989,747 (+)EnsemblHetGla_female_1.0 EnsemblhetGla2HetGla_female_1.0 Ensembl
HetGla 1.0NW_004624855430,148 - 1,992,121 (+)NCBIHetGla 1.0HetGla 1.0hetGla2
Prkn
(Rattus rattus - black rat)
Black Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Rrattus_CSIRO_v12189,645,291 - 190,070,073 (+)NCBIRrattus_CSIRO_v1

Variants

.
Variants in Prkn
8104 total Variants

QTLs in Region (GRCr8)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
1331732Srn4Serum renin concentration QTL 44.467renin activity (VT:0005581)plasma renin activity level (CMO:0000116)14345783787558729Rat
631688Hcas2Hepatocarcinoma susceptibility QTL 230.0001liver integrity trait (VT:0010547)liver tumorous lesion number (CMO:0001068)1774611852746118Rat
1357397Bw41Body weight QTL 414.190.0001body mass (VT:0001259)body weight (CMO:0000012)12940927974409279Rat
1578649Bmd8Bone mineral density QTL 84.9femur mineral mass (VT:0010011)trabecular volumetric bone mineral density (CMO:0001729)151940904101229020Rat
1358359Sradr1Stress Responsive Adrenal Weight QTL 14.74adrenal gland mass (VT:0010420)both adrenal glands wet weight (CMO:0000164)139728272132889942Rat
4889929Bss87Bone structure and strength QTL 876.7tibia area (VT:1000281)tibia-fibula cortical bone endosteal cross-sectional area (CMO:0001722)14630261591302615Rat
634314Niddm44Non-insulin dependent diabetes mellitus QTL 44blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)151941022208479811Rat
1331792Rf29Renal function QTL 294.589urine potassium amount (VT:0010539)urine potassium level (CMO:0000128)14345783787558729Rat
2313062Bmd73Bone mineral density QTL 733.90.0001tibia mineral mass (VT:1000283)compact volumetric bone mineral density (CMO:0001730)14630261591302615Rat
8552900Pigfal1Plasma insulin-like growth factor 1 level QTL 17.4blood insulin-like growth factor amount (VT:0010479)plasma insulin-like growth factor 1 level (CMO:0001299)14350995288509952Rat
1578654Bss10Bone structure and strength QTL 104femur morphology trait (VT:0000559)femoral neck cortical cross-sectional area (CMO:0001702)151940904168768703Rat
1354643Foco2Food consumption QTL 27.170.0001eating behavior trait (VT:0001431)food intake rate (CMO:0000427)14212296887122968Rat
2313065Bss67Bone structure and strength QTL 673.10.0001tibia area (VT:1000281)tibia total energy absorbed before break (CMO:0001736)14630261591302615Rat
7421626Bp360Blood pressure QTL 3600.001arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)1694102251941022Rat
1357401Bw43Body weight QTL 433.75body mass (VT:0001259)body weight (CMO:0000012)1690935351909353Rat
2313069Bss68Bone structure and strength QTL 682.90.0001tibia size trait (VT:0100001)tibia total energy absorbed before break (CMO:0001736)14630261591302615Rat
631494Bp95Blood pressure QTL 95400.0001arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)11731537851816258Rat
5684998Bss101Bone structure and strength QTL 1013.6tibia strength trait (VT:1000284)tibia ultimate force (CMO:0001734)1690935351909353Rat
70225Bp58Blood pressure QTL 583.3arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)134184556172281316Rat
2313075Bss66Bone structure and strength QTL 663.40.0001tibia length (VT:0004357)tibia length (CMO:0000450)14630261591302615Rat
5684999Bss102Bone structure and strength QTL 1025.57e-07tibia strength trait (VT:1000284)tibia stiffness (CMO:0001735)1690935351909353Rat
10059597Bp377Blood pressure QTL 3773.420.025arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)134565911208798288Rat
1331778Rf28Renal function QTL 284.66urine potassium amount (VT:0010539)urine potassium excretion rate (CMO:0000761)14345783787558729Rat
2313077Bss69Bone structure and strength QTL 693.50.0001tibia strength trait (VT:1000284)bone polar moment of inertia (CMO:0001558)14630261591302615Rat
2313402Anxrr24Anxiety related response QTL 24aggression-related behavior trait (VT:0015014)tameness/aggressiveness composite score (CMO:0002136)151511344153680016Rat
1578756Iddm22Insulin dependent diabetes mellitus QTL 222.7blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)12050832665508326Rat
631508Sald1Serum aldosterone level QTL 13.7blood aldosterone amount (VT:0005346)serum aldosterone level (CMO:0000487)11168446456684464Rat
1331785Rf27Renal function QTL 274.643urine sodium amount (VT:0006274)urine sodium level (CMO:0000129)13070837587558729Rat
1300172Bp172Blood pressure QTL 1723.56arterial blood pressure trait (VT:2000000)diastolic blood pressure (CMO:0000005)13456572679565726Rat
4889962Bss94Bone structure and strength QTL 943.8tibia area (VT:1000281)tibia-fibula cortical bone endosteal cross-sectional area (CMO:0001722)15190920691302615Rat
4889451Eae29Experimental allergic encephalomyelitis QTL 295.51nervous system integrity trait (VT:0010566)experimental autoimmune encephalomyelitis severity score (CMO:0001419)1774612152746121Rat
1558642Prcr2Prostate cancer resistance QTL 24.3prostate integrity trait (VT:0010571)area of ventral prostate occupied by tumorous lesions to total ventral prostate area ratio (CMO:0000899)11037949255379492Rat
2313092Bmd72Bone mineral density QTL 722.50.0001tibia mineral mass (VT:1000283)total volumetric bone mineral density (CMO:0001728)14630261591302615Rat
2313097Bss70Bone structure and strength QTL 703.50.0001tibia strength trait (VT:1000284)tibia total energy absorbed before break (CMO:0001736)14630261591302615Rat
9589820Insglur3Insulin/glucose ratio QTL 310.750.001blood insulin amount (VT:0001560)calculated plasma insulin level (CMO:0002170)14350995288509952Rat
1354599Bw29Body weight QTL 293.460.001body mass (VT:0001259)body weight (CMO:0000012)14212296887122968Rat
2302038Pia31Pristane induced arthritis QTL 315.50.001blood autoantibody amount (VT:0003725)serum immunoglobulin M-type rheumatoid factor level relative to an arbitrary reference serum (CMO:0002111)11282049457820494Rat
4889919Bss86Bone structure and strength QTL 864.1tibia area (VT:1000281)tibia midshaft total cross-sectional area (CMO:0001715)14630261591302615Rat
8552948Pigfal11Plasma insulin-like growth factor 1 level QTL 114.7blood insulin-like growth factor amount (VT:0010479)plasma insulin-like growth factor 1 level (CMO:0001299)14350995288509952Rat
634353Rends2Renal damage susceptibility QTL 20.05kidney blood vessel morphology trait (VT:0000530)organ lesion measurement (CMO:0000677)12065642065656420Rat

Markers in Region
D1Mit9  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8151,909,206 - 51,909,353 (+)Marker Load Pipeline
mRatBN7.2149,361,465 - 49,361,612 (+)MAPPERmRatBN7.2
Rnor_6.0149,547,328 - 49,547,474NCBIRnor6.0
Rnor_5.0150,204,369 - 50,204,515UniSTSRnor5.0
RGSC_v3.4143,840,482 - 43,840,628UniSTSRGSC3.4
RGSC_v3.4143,840,481 - 43,840,628RGDRGSC3.4
Celera145,146,244 - 45,146,390UniSTS
RGSC_v3.1143,843,426 - 43,843,573RGD
RH 3.4 Map1575.1UniSTS
RH 3.4 Map1575.1RGD
RH 2.0 Map1291.4RGD
SHRSP x BN Map123.8RGD
Cytogenetic Map1q11UniSTS
D1Mgh4  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8151,511,344 - 51,511,557 (+)Marker Load Pipeline
mRatBN7.2148,963,584 - 48,963,799 (+)MAPPERmRatBN7.2
Rnor_6.0149,147,799 - 49,148,011NCBIRnor6.0
Rnor_5.0150,601,428 - 50,601,640UniSTSRnor5.0
RGSC_v3.4143,426,139 - 43,426,354RGDRGSC3.4
RGSC_v3.4143,426,140 - 43,426,354UniSTSRGSC3.4
RGSC_v3.1143,429,085 - 43,429,299RGD
RH 3.4 Map1574.4UniSTS
RH 3.4 Map1574.4RGD
RH 2.0 Map1287.8RGD
SHRSP x BN Map123.88RGD
Cytogenetic Map1q11UniSTS
D1Rat18  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8151,816,100 - 51,816,258 (+)Marker Load Pipeline
mRatBN7.2149,268,362 - 49,268,520 (+)MAPPERmRatBN7.2
Rnor_6.0149,454,221 - 49,454,378NCBIRnor6.0
Rnor_5.0150,297,465 - 50,297,622UniSTSRnor5.0
RGSC_v3.4143,747,374 - 43,747,532RGDRGSC3.4
RGSC_v3.4143,747,375 - 43,747,532UniSTSRGSC3.4
Celera145,054,420 - 45,054,577UniSTS
RGSC_v3.1143,750,320 - 43,750,477RGD
RH 3.4 Map1575.2UniSTS
RH 3.4 Map1575.2RGD
RH 2.0 Map1291.4RGD
SHRSP x BN Map123.88RGD
Cytogenetic Map1q11UniSTS
D1Rat19  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8151,940,904 - 51,941,022 (+)Marker Load Pipeline
mRatBN7.2149,393,172 - 49,393,289 (+)MAPPERmRatBN7.2
Rnor_6.0149,578,577 - 49,578,693NCBIRnor6.0
Rnor_5.0150,173,150 - 50,173,266UniSTSRnor5.0
RGSC_v3.4143,872,711 - 43,872,827UniSTSRGSC3.4
RGSC_v3.4143,872,710 - 43,872,827RGDRGSC3.4
Celera145,177,968 - 45,178,100UniSTS
RGSC_v3.1143,875,655 - 43,875,772RGD
RH 3.4 Map1573.5UniSTS
RH 3.4 Map1573.5RGD
SHRSP x BN Map123.8UniSTS
SHRSP x BN Map123.8RGD
Cytogenetic Map1q11UniSTS
D1Rat17  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8152,195,962 - 52,196,098 (+)Marker Load Pipeline
mRatBN7.2149,648,235 - 49,648,371 (+)MAPPERmRatBN7.2
Rnor_6.0149,835,153 - 49,835,288NCBIRnor6.0
Rnor_5.0149,918,738 - 49,918,873UniSTSRnor5.0
RGSC_v3.4144,136,888 - 44,137,155RGDRGSC3.4
RGSC_v3.4144,137,014 - 44,137,149UniSTSRGSC3.4
Celera145,432,877 - 45,433,012UniSTS
RGSC_v3.1144,139,959 - 44,140,094RGD
RH 3.4 Map1579.5UniSTS
RH 3.4 Map1579.5RGD
RH 2.0 Map1295.3RGD
SHRSP x BN Map123.8399RGD
Cytogenetic Map1q11UniSTS
D1Rat143  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8151,724,430 - 51,724,676 (+)Marker Load Pipeline
mRatBN7.2149,176,688 - 49,176,934 (+)MAPPERmRatBN7.2
Rnor_6.0149,361,976 - 49,362,221NCBIRnor6.0
Rnor_5.0150,389,523 - 50,389,768UniSTSRnor5.0
RGSC_v3.4143,655,631 - 43,655,876UniSTSRGSC3.4
RGSC_v3.4143,655,630 - 43,655,876RGDRGSC3.4
Celera144,962,761 - 44,963,008UniSTS
RGSC_v3.1143,658,576 - 43,658,821RGD
RH 3.4 Map21132.8UniSTS
RH 3.4 Map21132.8RGD
SHRSP x BN Map123.88RGD
SHRSP x BN Map123.88UniSTS
Cytogenetic Map1q11UniSTS
D1Rat191  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8151,511,344 - 51,511,569 (+)Marker Load Pipeline
mRatBN7.2148,963,584 - 48,963,811 (+)MAPPERmRatBN7.2
Rnor_6.0149,147,799 - 49,148,023NCBIRnor6.0
Rnor_5.0150,601,416 - 50,601,640UniSTSRnor5.0
RGSC_v3.4143,426,140 - 43,426,366UniSTSRGSC3.4
RGSC_v3.4143,426,139 - 43,426,366RGDRGSC3.4
RGSC_v3.1143,429,085 - 43,429,311RGD
RH 3.4 Map1574.3UniSTS
RH 3.4 Map1574.3RGD
SHRSP x BN Map124.95UniSTS
SHRSP x BN Map124.95RGD
Cytogenetic Map1q11UniSTS
D1Rat228  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8151,889,769 - 51,890,001 (+)Marker Load Pipeline
mRatBN7.2149,342,028 - 49,342,260 (+)MAPPERmRatBN7.2
Rnor_6.0149,527,891 - 49,528,122NCBIRnor6.0
Rnor_5.0150,223,721 - 50,223,952UniSTSRnor5.0
RGSC_v3.4143,820,945 - 43,821,344RGDRGSC3.4
RGSC_v3.4143,821,045 - 43,821,276UniSTSRGSC3.4
Celera145,126,810 - 45,127,041UniSTS
RGSC_v3.1143,823,990 - 43,824,221RGD
RH 3.4 Map1575.1UniSTS
RH 3.4 Map1575.1RGD
RH 2.0 Map1291.4RGD
SHRSP x BN Map124.95RGD
Cytogenetic Map1q11UniSTS
D1Got61  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2149,218,171 - 49,218,412 (+)MAPPERmRatBN7.2
Rnor_6.0149,403,457 - 49,403,697NCBIRnor6.0
Rnor_5.0150,348,047 - 50,348,287UniSTSRnor5.0
RGSC_v3.4143,697,167 - 43,697,408RGDRGSC3.4
RGSC_v3.4143,697,168 - 43,697,408UniSTSRGSC3.4
Celera145,004,275 - 45,004,503UniSTS
RGSC_v3.1143,700,113 - 43,700,353RGD
RH 3.4 Map1574.2UniSTS
RH 3.4 Map1574.2RGD
RH 2.0 Map1291.0RGD
Cytogenetic Map1q11UniSTS
RH134081  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2149,580,043 - 49,580,226 (+)MAPPERmRatBN7.2
Rnor_6.0149,765,013 - 49,765,195NCBIRnor6.0
Rnor_5.0149,987,414 - 49,987,596UniSTSRnor5.0
RGSC_v3.4144,068,411 - 44,068,593UniSTSRGSC3.4
Celera145,364,623 - 45,364,805UniSTS
RH 3.4 Map1574.9UniSTS
Cytogenetic Map1q11UniSTS
BE097220  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2148,961,574 - 48,961,782 (+)MAPPERmRatBN7.2
Rnor_6.0149,145,789 - 49,145,996NCBIRnor6.0
Rnor_5.0150,603,443 - 50,603,650UniSTSRnor5.0
RGSC_v3.4143,424,130 - 43,424,337UniSTSRGSC3.4
Celera144,748,614 - 44,748,821UniSTS
RH 3.4 Map1573.6UniSTS
Cytogenetic Map1q11UniSTS
BE107128  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2179,180,875 - 79,181,012 (-)MAPPERmRatBN7.2
mRatBN7.2179,180,875 - 79,181,012 (+)MAPPERmRatBN7.2
mRatBN7.2149,826,424 - 49,826,561 (-)MAPPERmRatBN7.2
mRatBN7.2149,826,424 - 49,826,561 (+)MAPPERmRatBN7.2
Rnor_6.0150,014,365 - 50,014,501NCBIRnor6.0
Rnor_6.0180,439,800 - 80,439,936NCBIRnor6.0
Rnor_5.0149,739,855 - 49,739,991UniSTSRnor5.0
Rnor_5.0181,705,821 - 81,705,957UniSTSRnor5.0
RGSC_v3.4178,884,493 - 78,884,629UniSTSRGSC3.4
RGSC_v3.4144,315,802 - 44,315,938UniSTSRGSC3.4
Celera145,610,880 - 45,611,016UniSTS
Celera173,640,456 - 73,640,592UniSTS
RH 3.4 Map1589.6UniSTS
Cytogenetic Map1q11UniSTS
Cytogenetic Map1q21UniSTS
BE120978  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2149,044,400 - 49,044,610 (+)MAPPERmRatBN7.2
Rnor_6.0149,227,529 - 49,227,738NCBIRnor6.0
Rnor_5.0150,522,152 - 50,522,361UniSTSRnor5.0
RGSC_v3.4143,507,299 - 43,507,508UniSTSRGSC3.4
Celera144,831,334 - 44,831,543UniSTS
RH 3.4 Map1572.3UniSTS
Cytogenetic Map1q11UniSTS
AI171223  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2148,889,265 - 48,889,408 (+)MAPPERmRatBN7.2
Rnor_6.0149,073,451 - 49,073,593NCBIRnor6.0
Rnor_5.0150,675,094 - 50,675,236UniSTSRnor5.0
RGSC_v3.4143,351,829 - 43,351,971UniSTSRGSC3.4
Celera144,676,562 - 44,676,704UniSTS
RH 3.4 Map1573.9UniSTS
Cytogenetic Map1q11UniSTS
AU048432  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2149,777,511 - 49,777,655 (+)MAPPERmRatBN7.2
Rnor_6.0149,965,368 - 49,965,511NCBIRnor6.0
Rnor_5.0149,788,592 - 49,788,735UniSTSRnor5.0
RGSC_v3.4144,267,128 - 44,267,271UniSTSRGSC3.4
Celera145,562,063 - 45,562,206UniSTS
Cytogenetic Map1q11UniSTS


Genetic Models
This gene Prkn is modified in the following models/strains:
LE-Prknem1Sage-/-     LE-Prknem1Sage    


Expression

RNA-SEQ Expression

alimentary part of gastrointestinal system
appendage
circulatory system
ectoderm
hemolymphoid system
mesenchyme
mesoderm
musculoskeletal system
nervous system
renal system
reproductive system
sensory system
visual system
4 3 27 91 57 180 103 21 99 73 35 38 38

Sequence

Nucleotide Sequences
RefSeq Transcripts NM_020093 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039088710 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039088713 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039088714 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039088717 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039088724 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272034 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272037 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272040 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272044 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272046 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272054 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272057 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272058 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_063272060 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
GenBank Nucleotide AB039878 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AC135026 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF168004 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF210434 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF257234 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF343574 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF343575 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF381277 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF381278 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF381279 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF381280 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF381281 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  AF381285 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  CH474059 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  GU322017 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  GU322019 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  GU322363 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  GU322364 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  GU345835 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  GU345836 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  JAXUCZ010000001 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  KC774169 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  KC774170 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  KC774172 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  KC774173 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  KC774174 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  KC774175 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  KC774176 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  KC774177 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  LC156097 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles

Ensembl Acc Id: ENSRNOT00000077423   ⟹   ENSRNOP00000074053
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl148,690,556 - 49,657,630 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000083884   ⟹   ENSRNOP00000072264
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl148,690,556 - 48,899,454 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000086127   ⟹   ENSRNOP00000075137
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl149,106,549 - 49,882,555 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000089439   ⟹   ENSRNOP00000070559
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl149,412,348 - 49,882,555 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000090521   ⟹   ENSRNOP00000071167
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl148,690,556 - 49,657,630 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000096213   ⟹   ENSRNOP00000077507
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl148,690,556 - 49,882,555 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000105555   ⟹   ENSRNOP00000091214
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl148,690,556 - 49,657,630 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000105567   ⟹   ENSRNOP00000086350
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl148,690,556 - 49,657,630 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000107769   ⟹   ENSRNOP00000088932
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl148,690,556 - 49,657,629 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000118849   ⟹   ENSRNOP00000079341
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl149,106,208 - 49,240,393 (-)Ensembl
RefSeq Acc Id: NM_020093   ⟹   NP_064478
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,238,230 - 52,430,166 (-)NCBI
mRatBN7.2148,690,481 - 49,882,447 (-)NCBI
Rnor_6.0148,880,015 - 50,069,998 (-)NCBI
Rnor_5.0149,684,308 - 50,875,397 (+)NCBI
RGSC_v3.4143,151,265 - 44,374,470 (-)RGD
Celera144,478,407 - 45,666,902 (-)RGD
Sequence:
RefSeq Acc Id: XM_039088710   ⟹   XP_038944638
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,430,241 (-)NCBI
mRatBN7.2148,688,651 - 49,882,511 (-)NCBI
RefSeq Acc Id: XM_039088713   ⟹   XP_038944641
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,271,596 (-)NCBI
mRatBN7.2148,688,651 - 49,723,571 (-)NCBI
RefSeq Acc Id: XM_039088714   ⟹   XP_038944642
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,215,729 (-)NCBI
mRatBN7.2148,688,651 - 49,882,508 (-)NCBI
RefSeq Acc Id: XM_039088717   ⟹   XP_038944645
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,215,730 (-)NCBI
mRatBN7.2148,688,651 - 49,882,508 (-)NCBI
RefSeq Acc Id: XM_039088724   ⟹   XP_038944652
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,429,860 (-)NCBI
mRatBN7.2148,688,651 - 49,882,347 (-)NCBI
RefSeq Acc Id: XM_063272034   ⟹   XP_063128104
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,215,731 (-)NCBI
RefSeq Acc Id: XM_063272037   ⟹   XP_063128107
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,215,732 (-)NCBI
RefSeq Acc Id: XM_063272040   ⟹   XP_063128110
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,430,242 (-)NCBI
RefSeq Acc Id: XM_063272044   ⟹   XP_063128114
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,215,730 (-)NCBI
RefSeq Acc Id: XM_063272046   ⟹   XP_063128116
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,430,241 (-)NCBI
RefSeq Acc Id: XM_063272054   ⟹   XP_063128124
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 52,327,816 (-)NCBI
RefSeq Acc Id: XM_063272057   ⟹   XP_063128127
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,236,410 - 51,948,920 (-)NCBI
RefSeq Acc Id: XM_063272058   ⟹   XP_063128128
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,990,511 - 52,215,744 (-)NCBI
RefSeq Acc Id: XM_063272060   ⟹   XP_063128130
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8151,959,561 - 52,215,741 (-)NCBI
Protein Sequences
Protein RefSeqs NP_064478 (Get FASTA)   NCBI Sequence Viewer  
  XP_038944638 (Get FASTA)   NCBI Sequence Viewer  
  XP_038944641 (Get FASTA)   NCBI Sequence Viewer  
  XP_038944642 (Get FASTA)   NCBI Sequence Viewer  
  XP_038944645 (Get FASTA)   NCBI Sequence Viewer  
  XP_038944652 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128104 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128107 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128110 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128114 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128116 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128124 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128127 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128128 (Get FASTA)   NCBI Sequence Viewer  
  XP_063128130 (Get FASTA)   NCBI Sequence Viewer  
GenBank Protein AAF34874 (Get FASTA)   NCBI Sequence Viewer  
  AAF68666 (Get FASTA)   NCBI Sequence Viewer  
  AAG37013 (Get FASTA)   NCBI Sequence Viewer  
  AAL73348 (Get FASTA)   NCBI Sequence Viewer  
  AAL73349 (Get FASTA)   NCBI Sequence Viewer  
  AAM21452 (Get FASTA)   NCBI Sequence Viewer  
  AAM21453 (Get FASTA)   NCBI Sequence Viewer  
  AAM21454 (Get FASTA)   NCBI Sequence Viewer  
  AAM21455 (Get FASTA)   NCBI Sequence Viewer  
  AAM21456 (Get FASTA)   NCBI Sequence Viewer  
  AAM21460 (Get FASTA)   NCBI Sequence Viewer  
  ADB77772 (Get FASTA)   NCBI Sequence Viewer  
  ADB77773 (Get FASTA)   NCBI Sequence Viewer  
  ADB90267 (Get FASTA)   NCBI Sequence Viewer  
  ADB90268 (Get FASTA)   NCBI Sequence Viewer  
  ADB96018 (Get FASTA)   NCBI Sequence Viewer  
  ADB96019 (Get FASTA)   NCBI Sequence Viewer  
  AGP25364 (Get FASTA)   NCBI Sequence Viewer  
  AGP25365 (Get FASTA)   NCBI Sequence Viewer  
  AGP25367 (Get FASTA)   NCBI Sequence Viewer  
  AGP25368 (Get FASTA)   NCBI Sequence Viewer  
  AGP25369 (Get FASTA)   NCBI Sequence Viewer  
  AGP25370 (Get FASTA)   NCBI Sequence Viewer  
  AGP25371 (Get FASTA)   NCBI Sequence Viewer  
  AGP25372 (Get FASTA)   NCBI Sequence Viewer  
  BAA92431 (Get FASTA)   NCBI Sequence Viewer  
  BAX00771 (Get FASTA)   NCBI Sequence Viewer  
  EDL83078 (Get FASTA)   NCBI Sequence Viewer  
  EDL83079 (Get FASTA)   NCBI Sequence Viewer  
  EDL83080 (Get FASTA)   NCBI Sequence Viewer  
  EDL83081 (Get FASTA)   NCBI Sequence Viewer  
  EDL83082 (Get FASTA)   NCBI Sequence Viewer  
  EDL83083 (Get FASTA)   NCBI Sequence Viewer  
  EDL83084 (Get FASTA)   NCBI Sequence Viewer  
  EDL83085 (Get FASTA)   NCBI Sequence Viewer  
Ensembl Protein ENSRNOP00000070559
  ENSRNOP00000071167
  ENSRNOP00000072264
  ENSRNOP00000075137
  ENSRNOP00000077507
  ENSRNOP00000077507.1
  ENSRNOP00000088932.1
  ENSRNOP00000091214
GenBank Protein Q9JK66 (Get FASTA)   NCBI Sequence Viewer  
RefSeq Acc Id: NP_064478   ⟸   NM_020093
- UniProtKB: A0A1S7IWU1 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: XP_038944638   ⟸   XM_039088710
- Peptide Label: isoform X3
- UniProtKB: A0A8I6A5N7 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_038944645   ⟸   XM_039088717
- Peptide Label: isoform X9
- UniProtKB: A0A8I6GIU4 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_038944642   ⟸   XM_039088714
- Peptide Label: isoform X6
- UniProtKB: Q9JM64 (UniProtKB/Swiss-Prot),   Q9JLL1 (UniProtKB/Swiss-Prot),   Q9JK66 (UniProtKB/Swiss-Prot),   Q8VHY6 (UniProtKB/Swiss-Prot),   Q8K5C6 (UniProtKB/Swiss-Prot),   Q8K5C5 (UniProtKB/Swiss-Prot),   Q8K5C4 (UniProtKB/Swiss-Prot),   Q8K5C3 (UniProtKB/Swiss-Prot),   A6KJZ1 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_038944652   ⟸   XM_039088724
- Peptide Label: isoform X10
- UniProtKB: S4X294 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_038944641   ⟸   XM_039088713
- Peptide Label: isoform X5
- UniProtKB: A0A8I6A5N7 (UniProtKB/TrEMBL)
Ensembl Acc Id: ENSRNOP00000074053   ⟸   ENSRNOT00000077423
Ensembl Acc Id: ENSRNOP00000070559   ⟸   ENSRNOT00000089439
Ensembl Acc Id: ENSRNOP00000091214   ⟸   ENSRNOT00000105555
Ensembl Acc Id: ENSRNOP00000072264   ⟸   ENSRNOT00000083884
Ensembl Acc Id: ENSRNOP00000079341   ⟸   ENSRNOT00000118849
Ensembl Acc Id: ENSRNOP00000075137   ⟸   ENSRNOT00000086127
Ensembl Acc Id: ENSRNOP00000077507   ⟸   ENSRNOT00000096213
Ensembl Acc Id: ENSRNOP00000088932   ⟸   ENSRNOT00000107769
Ensembl Acc Id: ENSRNOP00000086350   ⟸   ENSRNOT00000105567
Ensembl Acc Id: ENSRNOP00000071167   ⟸   ENSRNOT00000090521
RefSeq Acc Id: XP_063128110   ⟸   XM_063272040
- Peptide Label: isoform X4
- UniProtKB: A0A8I6A5N7 (UniProtKB/TrEMBL),   D3JVU6 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063128116   ⟸   XM_063272046
- Peptide Label: isoform X8
- UniProtKB: Q9JM64 (UniProtKB/Swiss-Prot),   Q9JLL1 (UniProtKB/Swiss-Prot),   Q9JK66 (UniProtKB/Swiss-Prot),   Q8VHY6 (UniProtKB/Swiss-Prot),   Q8K5C6 (UniProtKB/Swiss-Prot),   Q8K5C5 (UniProtKB/Swiss-Prot),   Q8K5C4 (UniProtKB/Swiss-Prot),   Q8K5C3 (UniProtKB/Swiss-Prot),   A0A1S7IWU1 (UniProtKB/TrEMBL),   A6KJZ1 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063128124   ⟸   XM_063272054
- Peptide Label: isoform X10
- UniProtKB: S4X294 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063128107   ⟸   XM_063272037
- Peptide Label: isoform X2
- UniProtKB: A0A8I6A5N7 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063128104   ⟸   XM_063272034
- Peptide Label: isoform X1
- UniProtKB: A0A8I6A5N7 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063128114   ⟸   XM_063272044
- Peptide Label: isoform X7
- UniProtKB: Q9JM64 (UniProtKB/Swiss-Prot),   Q9JLL1 (UniProtKB/Swiss-Prot),   Q9JK66 (UniProtKB/Swiss-Prot),   Q8VHY6 (UniProtKB/Swiss-Prot),   Q8K5C6 (UniProtKB/Swiss-Prot),   Q8K5C5 (UniProtKB/Swiss-Prot),   Q8K5C4 (UniProtKB/Swiss-Prot),   Q8K5C3 (UniProtKB/Swiss-Prot),   A0A1S7IWU1 (UniProtKB/TrEMBL),   A6KJZ1 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063128127   ⟸   XM_063272057
- Peptide Label: isoform X11
- UniProtKB: S4X294 (UniProtKB/TrEMBL),   A6KJZ3 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063128130   ⟸   XM_063272060
- Peptide Label: isoform X13
- UniProtKB: A0A0G2JY87 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_063128128   ⟸   XM_063272058
- Peptide Label: isoform X12
Protein Domains
RING-type   Ubiquitin-like

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-A0A0G2K9U8-F1-model_v2 AlphaFold A0A0G2K9U8 1-289 view protein structure
AF-Q9JK66-F1-model_v2 AlphaFold Q9JK66 1-465 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:61797 AgrOrtholog
BioCyc Gene G2FUF-61554 BioCyc
Ensembl Genes ENSRNOG00000055547 Ensembl, ENTREZGENE, UniProtKB/Swiss-Prot
Ensembl Transcript ENSRNOT00000083884 ENTREZGENE
  ENSRNOT00000086127 ENTREZGENE
  ENSRNOT00000089439 ENTREZGENE
  ENSRNOT00000090521 ENTREZGENE
  ENSRNOT00000096213 ENTREZGENE
  ENSRNOT00000096213.1 UniProtKB/Swiss-Prot
  ENSRNOT00000105555 ENTREZGENE
  ENSRNOT00000107769.1 UniProtKB/Swiss-Prot
Gene3D-CATH 1.20.120.1750 UniProtKB/Swiss-Prot
  2.20.25.20 UniProtKB/Swiss-Prot
  Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1 UniProtKB/Swiss-Prot
InterPro BRcat_RBR_parkin UniProtKB/Swiss-Prot
  IBR_dom UniProtKB/Swiss-Prot
  Parkin UniProtKB/Swiss-Prot
  Parkin-like_IBR UniProtKB/Swiss-Prot
  Parkin_Znf-RING UniProtKB/Swiss-Prot
  Rcat_RBR_parkin UniProtKB/Swiss-Prot
  RING-HC_RBR_parkin UniProtKB/Swiss-Prot
  TRIAD_supradom UniProtKB/Swiss-Prot
  Ubiquilin UniProtKB/Swiss-Prot
  Ubiquitin-like_domsf UniProtKB/Swiss-Prot
  Ubiquitin_dom UniProtKB/Swiss-Prot
  Znf-RING_14 UniProtKB/Swiss-Prot
KEGG Report rno:56816 UniProtKB/Swiss-Prot
NCBI Gene 56816 ENTREZGENE
PANTHER UBIQUILIN UniProtKB/Swiss-Prot
  UBIQUITIN-LIKE DOMAIN-CONTAINING PROTEIN UniProtKB/Swiss-Prot
Pfam IBR_2 UniProtKB/Swiss-Prot
  ubiquitin UniProtKB/Swiss-Prot
  zf-RING_12 UniProtKB/Swiss-Prot
  zf-RING_14 UniProtKB/Swiss-Prot
PhenoGen Prkn PhenoGen
PIRSF Parkin UniProtKB/Swiss-Prot
PRINTS PARKIN UniProtKB/Swiss-Prot
PROSITE TRIAD UniProtKB/Swiss-Prot
  UBIQUITIN_2 UniProtKB/Swiss-Prot
RatGTEx ENSRNOG00000055547 RatGTEx
SMART IBR UniProtKB/Swiss-Prot
  UBQ UniProtKB/Swiss-Prot
Superfamily-SCOP RING/U-box UniProtKB/Swiss-Prot
  SSF54236 UniProtKB/Swiss-Prot
UniProt A0A0G2JY87 ENTREZGENE, UniProtKB/TrEMBL
  A0A0G2JZS8_RAT UniProtKB/TrEMBL
  A0A0G2K2J2_RAT UniProtKB/TrEMBL
  A0A0G2K740_RAT UniProtKB/TrEMBL
  A0A1S7IWU1 ENTREZGENE, UniProtKB/TrEMBL
  A0A8I6A5N7 ENTREZGENE, UniProtKB/TrEMBL
  A0A8I6GIU4 ENTREZGENE, UniProtKB/TrEMBL
  A0ABZ3NNQ4_RAT UniProtKB/TrEMBL
  A6KJZ1 ENTREZGENE, UniProtKB/TrEMBL
  A6KJZ3 ENTREZGENE, UniProtKB/TrEMBL
  D3JVU6 ENTREZGENE, UniProtKB/TrEMBL
  PRKN_RAT UniProtKB/Swiss-Prot
  Q8K5C3 ENTREZGENE
  Q8K5C4 ENTREZGENE
  Q8K5C5 ENTREZGENE
  Q8K5C6 ENTREZGENE
  Q8VHY6 ENTREZGENE
  Q9JK66 ENTREZGENE
  Q9JLL1 ENTREZGENE
  Q9JM64 ENTREZGENE
  S4X294 ENTREZGENE, UniProtKB/TrEMBL
UniProt Secondary Q8K5C3 UniProtKB/Swiss-Prot
  Q8K5C4 UniProtKB/Swiss-Prot
  Q8K5C5 UniProtKB/Swiss-Prot
  Q8K5C6 UniProtKB/Swiss-Prot
  Q8VHY6 UniProtKB/Swiss-Prot
  Q9JLL1 UniProtKB/Swiss-Prot
  Q9JM64 UniProtKB/Swiss-Prot


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2011-08-02 Park2  parkinson protein 2, E3 ubiquitin protein ligase  Park2  Parkinson disease (autosomal recessive, juvenile) 2, parkin  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2008-10-30 Park2  Parkinson disease (autosomal recessive, juvenile) 2, parkin  Park2  parkin   Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2002-06-10 Park2  parkin       Name updated 70584 APPROVED

RGD Curation Notes
Note Type Note Reference
gene_cellular_localization primarily associated with ER in hippocampal neurons; localized to Golgi membranes, nuclei and light vesicles of astrocytes 628414
gene_disease human homolog may be involved in early onset parkinsonism 633597
gene_disease involved in dopamine neuron degeneration in common autosomal recessive form of Parkinsons Disease 628414
gene_function possesses ubiquitin ligase activity leading to target protein degradation 628414
gene_pathway part of the ubiquitin -proteasomal enzyme pathway 628414
gene_process selective in conferring specificity to protein ubiquitination; recognizes specific cellular protein substrates and ubitquitin conjugates; capable of degrading imporperly folded proteins such as cytoplasmic inclusions, Lewy bodies and Lewy neurites 628414
gene_process ubiquitin ligase facilitating proteasomal protein degradation in cytosol, membranes and ER secretory pathway 628414
gene_protein N-terminal homology to ubiquitin; RING domains of ubiquitin ligase family proteins found in C-terminal 628414
gene_regulation unfolded protein responses (UPR) in cells cause increased levels and redistribution in astrocytes 628414