Parkinson Protein 2, E3 Ubiquitin Protein Ligase (Parkin) Protéines (PARK2)

The precise function of PARK2 is unknown\; however, the encoded protein is a component of a multiprotein E3 ubiquitin ligase complex that mediates the targeting of substrate proteins for proteasomal degradation. De plus, nous expédions PARK2 Anticorps (200) et PARK2 Kits (21) et beaucoup plus de produits pour cette protéine.

afficher tous les protéines Gène GeneID UniProt
PARK2 5071 O60260
PARK2 56816 Q9JK66
PARK2 50873 Q9WVS6
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Showing 10 out of 13 products:

Catalogue No. Origin Source Conjugué Images Quantité Fournisseur Livraison Prix Détails
Cellules d'insectes Souris His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Connectez-vous pour afficher 60 Days
$9,626.73
Détails
Cellules d'insectes Humain His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Connectez-vous pour afficher 60 Days
$9,626.73
Détails
Escherichia coli (E. coli) Humain His tag 100 μg Connectez-vous pour afficher 13 to 16 Days
$400.00
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Wheat germ Humain GST tag 10 μg Connectez-vous pour afficher 11 to 12 Days
$414.29
Détails
Levure Rat His tag   1 mg Connectez-vous pour afficher 60 to 71 Days
$3,309.17
Détails
Escherichia coli (E. coli) Humain S tag,His tag 100 μg Connectez-vous pour afficher 15 to 18 Days
$624.00
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Escherichia coli (E. coli) Humain His tag   10 μg Connectez-vous pour afficher 15 to 16 Days
$225.00
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Escherichia coli (E. coli) Humain Inconjugué   5 applications Connectez-vous pour afficher 1 to 2 Days
$318.85
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Baculovirus infected Insect Cells Humain GST tag   50 μg Connectez-vous pour afficher 10 to 12 Days
$673.36
Détails
Baculovirus infected Insect Cells Humain GST tag   20 μg Connectez-vous pour afficher 1 to 2 Days
$309.10
Détails

PARK2 Protéines protéines par origine et source

Origin Exprimée danse Conjugué
Human , , , ,
, ,
Rat (Rattus)

Mouse (Murine)

Plus protéines pour Parkinson Protein 2, E3 Ubiquitin Protein Ligase (Parkin) (PARK2) partenaires d'interaction

Fruit Fly (Drosophila melanogaster) Parkinson Protein 2, E3 Ubiquitin Protein Ligase (Parkin) (PARK2) interaction partners

  1. Pink1 and parkin are not essential for bulk basal mitophagy in Drosophila

  2. Deficiency of parkin impairs age-dependent mitophagy in Drosophila.

  3. this study show that parkin deficient astrocytes have an exaggerated ER stress signature, increased JNK activation and blunting of neurotropic factor transcript induction following ER stress.

  4. The reduced expression of Parkin and HtrA2 interpret defective mitophagy leading to clustering of fragmented mitochondria and apoptotic inhibition in scrib knockdown tumors.

  5. Parkin null mutation is associated with climbing defects and defects and mitochondrial activity.

  6. Loss of parkin is associated with nuclear clustering and morphology defects in larval muscles and thus developing aortic aneurysms.

  7. This study found learning and memory abnormalities in Parkin mutant genotypes in Drosophila.

  8. parkin mutants have a longer lifespan when fed the 1:16 P:C compared to those fed the 1:2 P:C diet. Parkin mutants fed the 1:16 P:C diet have delayed climbing deficit, increased resistance to starvation. Mutant flies fed the 1:16 P:C diet also have improved mitochondrial functions as evidenced by increased respiratory control ratio

  9. Drosophila CHIP protects against mitochondrial dysfunction by acting downstream of Pink1 in parallel with Parkin

  10. Maintenance of tissue homeostasis upon reduction of Pink1 or Parkin appears to result from reduction of age- and stress-induced intestinal stem cell proliferation, in part, through induction of ISC senescence.

  11. activation of endoplasmic reticulum stress by defective mitochondria is neurotoxic in pink1 and parkin flies and that the reduction of this signalling is neuroprotective, independently of defective mitochondria.

  12. Pharmacological or genetic activation of heat shock protein 70 (Hsp70) protects against loss of parkin Function. Heat shock protein members may act as compensatory factors for parkin loss of function and that the exploitation of these factors may be of potential therapeutic value.

  13. autophosphorylation of PINK1 is essential for the mitochondrial translocation of Parkin and for subsequent phosphorylation and activation of Parkin.

  14. Our data indicate that PINK1 and Parkin play an important role in FUS-induced neurodegeneration. This study has uncovered a previously unknown link between FUS proteinopathy and PINK1/Parkin genes, providing new insights into the pathogenesis of FUS proteinopathy.

  15. Clu is upstream of and binds to VCP in vivo and promotes VCP-dependent Marf degradation in vitro Marf accumulates in whole muscle lysates of clu-deficient flies and is destabilized upon Clu overexpression. Thus, Clu is essential for mitochondrial homeostasis and functions in concert with Parkin and VCP for Marf degradation to promote damaged mitochondrial clearance.

  16. Buffy has a role enhancing the loss of parkin and suppressing the loss of Pink1 phenotypes in Drosophila

  17. Parkin-dependent mitophagy suppresses neural neurodegeneration by removing damaged mitochondria.

  18. We demonstrate here that vps35 genetically interacts with parkin

  19. Clu directly modulates mitochondrial function, and that Clu's function contributes to the PINK1-Park pathway of mitochondrial quality control.

  20. Human Mask homolog ANKHD1 may serve as a potential therapeutic target for treating Parkinson disease caused by pink1/parkin mutations.

Human Parkinson Protein 2, E3 Ubiquitin Protein Ligase (Parkin) (PARK2) interaction partners

  1. Mechanistically, parkin/PINK1 catalyze a rapid burst of Mfn2 phosphoubiquitination to trigger p97-dependent disassembly of Mfn2 complexes from the outer mitochondrial membrane, dissociating mitochondria from the endoplasmic reticulum.

  2. REVIEW: recent literature describing parkin-independent mitophagy and its role in various physiopathological conditions, therefore representing potential new targets to treat diseases affected by dysregulated mitophagy

  3. we use two distinct mitophagy reporter systems to reveal tonic suppression by USP30, of a PINK1-dependent component of basal mitophagy in cells lacking detectable Parkin.

  4. results support a role for PINK1- and parkin-mediated mitophagy in restraining innate immunity

  5. lowering parkin levels by extracellular ASN may significantly contribute to the propagation of neurodegeneration in Parkinson's disease pathology.

  6. Single nucleotide polymorphism in PARK2 gene is associated with schizophrenia.

  7. Parkin is an ubiquitin E3 ligase, and plays important roles in a variety of cellular processes implicated in tumorigenesis, including cell cycle, cell proliferation, apoptosis, metastasis, mitophagy and metabolic reprogramming [Review].

  8. The results show that novel compound heterozygous mutations were identified in a Chinese pedigree that might represent a cause of familial EOPD with autosomal dominant inheritance.

  9. MIDN promotes the expression of parkin E3 ubiquitin ligase, and that MIDN loss can trigger Parkinson's disease-related pathogenic mechanisms.

  10. Define the kinetics and site specificity of PARKIN-dependent target ubiquitylation, and mechanistically define the role of PARKIN UBL phosphorylation in pathway activation in induced neurons.

  11. The findings suggest that Parkin plays a novel role in innate immune signaling by targeting TRAF3 for degradation and maintaining the balance of innate antiviral immunity.

  12. data show how autoinhibition in parkin is resolved, and suggest a mechanism for how parkin ubiquitinates its substrates via an untethered RING2 domain; these findings open new avenues for the design of parkin activators for clinical use

  13. Five different PRKN structural variations were identified in families with early onset Parkinson disease. All identified PRKN SVs might originate through retrotransposition events.

  14. work provides a framework for the mechanisms of parkin's loss-of-function, indicating an interplay between ARJP-associated substitutions and phosphorylation of its Ubl domain.

  15. Data show that E3 ubiquitin-protein ligase parkin (Parkin) undergoes a conformational change upon phosphorylation.

  16. carnosic acid induces parkin by enhancing the ubiquitination of ARTS, leading to induction of XIAP.

  17. PARK2 promoter SNP's rs2276201 and rs9347683 are shown to be significantly associated with the risk of colorectal cancer development

  18. Increased levels of Parkin are detected in lens epithelial cells exposed to H2O2-oxidative stress. Parkin translocates to mitochondria of lens epithelial cells upon H2O2-oxidative stress exposure. Parkin ubiquitin ligase activity is required for clearance of damaged mitochondria in lens epithelial cells exposed to H2O2-oxidative stress.

  19. Examined the enzymatic activity of Parkin with M458L mutation. We show that the M458L mutant retains its autoubiquitination potential in vitro but not in cells. M458L mutant fails to protect the mitochondria against hydrogen peroxide, leading to cell death.

  20. The results demonstrate that Nix can serve as an alternative mediator of mitophagy to maintain mitochondrial turnover, identifying Nix as a promising target for neuroprotective treatment in PINK1/Parkin-related Parkinson's disease.

Zebrafish Parkinson Protein 2, E3 Ubiquitin Protein Ligase (Parkin) (PARK2) interaction partners

  1. Melatonin, added together with MPTP or added once MPTP was removed, prevented and recovered, respectively, the parkinsonian phenotype once it was established, restoring gene expression and normal function of the parkin/PINK1/DJ-1/MUL1 loop and also the normal motor activity of the embryos.

Pig (Porcine) Parkinson Protein 2, E3 Ubiquitin Protein Ligase (Parkin) (PARK2) interaction partners

  1. Single nucleotide polymorphism (SNP) analysis revealed seven SNPs in the porcine PARK2 gene, one missense and one silent mutation in exon 7 and five SNPs in intron 7

Mouse (Murine) Parkinson Protein 2, E3 Ubiquitin Protein Ligase (Parkin) (PARK2) interaction partners

  1. These results indicate that Parkin is a disease modifier in amyotrophic lateral sclerosis, because chronic Parkin-mediated mitochondria quality control activation depletes mitochondrial dynamics-related proteins, inhibits mitochondrial biogenesis, and worsens mitochondrial dysfunction.

  2. Faulty mitophagy in dystrophic hearts due to defects in the PINK1/PARKIN signaling pathway.

  3. results support a role for PINK1- and parkin-mediated mitophagy in restraining innate immunity

  4. Parkin gene defect did not increase the susceptibility of neonatal mice to adverse health effects associated with high-dose manganese exposure.

  5. Parkin gene silencing in primary cortical neurons selectively disrupts the vesicular sorting of the autophagy receptor ATG9A, a WASH-dependent retromer cargo. Parkin is not required for dopaminergic neurodegeneration induced by the expression of PD-linked D620N VPS35 in mice, consistent with VPS35 being located downstream of parkin function

  6. Phenotypically, Parkin (S65A/S65A) mice exhibit selective motor dysfunction in the absence of any overt neurodegeneration or alterations in nigrostriatal mitophagy.

  7. Low parkin expression is associated with Parkinson's disease.

  8. Parkin functions to blunt excessive CHOP to prevent maladaptive ER stress-induced cell death and adverse cardiac ventricular remodeling.

  9. data suggested that suppressed Sirt3-Foxo3A-Parkin signaling mediated downregulation of mitophagy may play a vital role in the development of diabetic cardiomyopathy.

  10. Overexpression of parkin resulted in a significant reduction of total-eNOS and p-eNOS in parallel with the downregulation of ERRalpha (a regulator of eNOS) protein and the enhancement of ERRalpha ubiquitination.

  11. Parkin mice carrying a deletion in exon 3 display impairments in the main pathway responsible for maintaining BH4 levels in the CNS, an essential cofactor for dopamine synthesis, under inflammatory conditions. Concomitant to this alteration, striatum cells do not upregulate BDNF to confer neuroprotection in LPS-exposed mice, displaying an increased number of mitochondria of smaller size with perinuclear clustering.

  12. the results indicate that PICK1 is a potent inhibitor of Parkin, and the reduction of PICK1 enhances the protective effect of Parkin.

  13. PINK1 and PARK2 suppress pancreatic tumorigenesis through control of mitochondrial iron-mediated immunometabolism

  14. When fed with iron-supplemented diet, DMT1-expressing mice exhibit rather selective accumulation of iron in the substantia nigra but otherwise seem normal. Parkin expression is also enhanced, likely as a neuroprotective response. When DMT1 is overexpressed against a Parkin null background, the double-mutant mice similarly resisted a disease phenotype when fed with iron or manganese, but greater susceptibility to 6-OHDA.

  15. Bnip3l knockout (bnip3l(-/-)) impaired mitophagy and aggravated cerebral I-R (ischemia-reperfusion) injury in mice, which can be rescued by BNIP3L overexpression. The rescuing effects of BNIP3L overexpression can be observed in park2(-/-) mice, which showed mitophagy deficiency after I-R.

  16. Parkin acts as a regulator of microtubule system during neuronal aging.

  17. The expression of PINK1 and Parkin were elevated in white adipose tissue in obese mice.

  18. crossed Parkin knockouts to the Twinkle-TG mouse in which mtDNA deletions are increased specifically in substantia nigra to determine the effect of increased deletion mutagenesis in the absence of mitochondrial quality control

  19. These findings reveal parkin-mediated cytoprotective mechanisms against misfolded SOD1 toxicity.

  20. Park2 deficiency exacerbates ethanol-induced dopaminergic neuron damage through p38 kinase dependent inhibition of autophagy and mitochondrial function.

Profil protéine PARK2

Profil protéine

The precise function of this gene is unknown\; however, the encoded protein is a component of a multiprotein E3 ubiquitin ligase complex that mediates the targeting of substrate proteins for proteasomal degradation. Mutations in this gene are known to cause Parkinson disease and autosomal recessive juvenile Parkinson disease. Alternative splicing of this gene produces multiple transcript variants encoding distinct isoforms. Additional splice variants of this gene have been described but currently lack transcript support.

Gene names and symbols associated with PARK2

  • parkin (park)
  • parkin RBR E3 ubiquitin protein ligase (PRKN)
  • parkin RBR E3 ubiquitin protein ligase (Prkn)
  • parkin RBR E3 ubiquitin protein ligase (prkn)
  • parkin (CpipJ_CPIJ014867)
  • Parkinson disease (autosomal recessive, juvenile) 2, parkin (Park2)
  • AR-JP Protéine
  • CG10523 Protéine
  • Dmel\\CG10523 Protéine
  • Dpark Protéine
  • dpk Protéine
  • LPRS2 Protéine
  • Park Protéine
  • PARK2 Protéine
  • PDJ Protéine
  • pdr-1 Protéine
  • Prkn Protéine
  • SD01679 Protéine
  • si:ch211-123f21.1 Protéine
  • zgc:112390 Protéine

Protein level used designations for PARK2

CG10523-PB , CG10523-PC , D-parkin , dparkin , park-PB , park-PC , E3 ubiquitin-protein ligase parkin , Parkinson disease (autosomal recessive, juvenile) 2, parkin , parkinson juvenile disease protein 2 , parkin variant SV5DEL , parkin , parkin protein , parkinson protein 2, E3 ubiquitin protein ligase (parkin)

GENE ID SPECIES
40336 Drosophila melanogaster
5071 Homo sapiens
56816 Rattus norvegicus
550328 Danio rerio
733673 Sus scrofa
741350 Pan troglodytes
6049109 Culex quinquefasciatus
50873 Mus musculus
612316 Canis lupus familiaris
100724550 Cavia porcellus
530858 Bos taurus
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