PARK7

Parkinson protein 7

PDB rendering based on 1j42 ^[1].

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1J42, 1P5F, 1PDV, 1PDW, 1PE0, 1Q2U, 1SOA, 1UCF, 2OR3, 2R1T, 2R1U, 2R1V, 2RK3, 2RK4, 2RK6, 3B36, 3B38, 3B3A, 3BWE, 3CY6, 3CYF, 3CZ9, 3CZA, 3EZG, 3F71, 3SF8, 4BTE, 4MNT, 4MTC, 4N0M, 4N12, 4OQ4, 4P2G, 4P34, 4P35, 4P36

Identifiers

Symbols

PARK7 ; DJ-1; DJ1; HEL-S-67p

External IDs

OMIM: 602533 MGI: 2135637 HomoloGene: 38295 GeneCards: PARK7 Gene

Gene ontology
Molecular function	• double-stranded DNA binding • single-stranded DNA binding • mRNA binding • peroxidase activity • receptor binding • protein binding • transcription factor binding • peptidase activity • superoxide dismutase copper chaperone activity • oxidoreductase activity, acting on peroxide as acceptor • enzyme binding • cytokine binding • identical protein binding • protein homodimerization activity • small protein activating enzyme binding • small protein conjugating enzyme binding • androgen receptor binding • peroxiredoxin activity • scaffold protein binding • cupric ion binding • cuprous ion binding • ubiquitin-specific protease binding
Cellular component	• nucleus • cytoplasm • mitochondrion • cytosol • plasma membrane • PML body • membrane raft • extracellular vesicular exosome
Biological process	• negative regulation of protein phosphorylation • negative regulation of protein kinase activity • proteolysis • autophagy • inflammatory response • mitochondrion organization • single fertilization • adult locomotory behavior • negative regulation of gene expression • negative regulation of protein binding • positive regulation of interleukin-8 production • cellular response to oxidative stress • hydrogen peroxide metabolic process • regulation of neuron apoptotic process • negative regulation of neuron apoptotic process • regulation of TRAIL receptor biosynthetic process • positive regulation of transcription from RNA polymerase II promoter • negative regulation of protein export from nucleus • regulation of inflammatory response • protein stabilization • dopamine uptake involved in synaptic transmission • regulation of mitochondrial membrane potential • membrane depolarization • oxidation-reduction process • membrane hyperpolarization • negative regulation of cell death • regulation of androgen receptor signaling pathway • cellular response to hydrogen peroxide • positive regulation of protein homodimerization activity • positive regulation of protein localization to nucleus • negative regulation of neuron death • negative regulation of hydrogen peroxide-mediated programmed cell death • positive regulation of superoxide dismutase activity • negative regulation of protein acetylation • negative regulation of death-inducing signaling complex assembly • negative regulation of protein K48-linked deubiquitination • negative regulation of TRAIL-activated apoptotic signaling pathway • negative regulation of ubiquitin-specific protease activity • positive regulation of oxidative phosphorylation uncoupler activity • positive regulation of androgen receptor activity • negative regulation of extrinsic apoptotic signaling pathway • negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
8.01 – 8.05 Mb

Chr 4:
150.9 – 150.91 Mb

PubMed search

Parkinson disease (autosomal recessive, early onset) 7, also known as PARK7, is a protein which in humans is encoded by the PARK7 gene.^[2] It is also known as DJ-1.

Function

PARK7 belongs to the peptidase C56 family of proteins. It acts as a positive regulator of androgen receptor-dependent transcription. It may also function as a redox-sensitive chaperone, as a sensor for oxidative stress, and it apparently protects neurons against oxidative stress and cell death.^[2]

Clinical significance

Defects in this gene are the cause of autosomal recessive early-onset Parkinson's disease 7.^[2]^[3]

Interactions

PARK7 has been shown to interact with:

References

↑ Lee, S. J.; Kim, S. J.; Kim, I. K.; Ko, J.; Jeong, C. S.; Kim, G. H.; Park, C.; Kang, S. O.; Suh, P. G. (2003). "Crystal Structures of Human DJ-1 and Escherichia coli Hsp31, Which Share an Evolutionarily Conserved Domain". Journal of Biological Chemistry 278 (45): 44552–44559. doi:10.1074/jbc.M304517200. PMID 12939276.
↑ 2.0 2.1 2.2 "Entrez Gene: PARK7".
↑ Bonifati V, Rizzu P, van Baren MJ, Schaap O, Breedveld GJ, Krieger E, Dekker MC, Squitieri F, Ibanez P, Joosse M, van Dongen JW, Vanacore N, van Swieten JC, Brice A, Meco G, van Duijn CM, Oostra BA, Heutink P (January 2003). "Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism". Science 299 (5604): 256–259. doi:10.1126/science.1077209. PMID 12446870.
↑ Mukherjee K, Slawson JB, Christmann BL, Griffith LC (2014). "Neuron-specific protein interactions of Drosophila CASK-β are revealed by mass spectrometry". Front Mol Neurosci 7: 58. doi:10.3389/fnmol.2014.00058. PMC 4075472. PMID 25071438.
↑ Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H (Feb 2003). "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex". Mol. Cancer Res. 1 (4): 247–61. PMID 12612053.
↑ Takahashi K, Taira T, Niki T, Seino C, Iguchi-Ariga SM, Ariga H (Oct 2001). "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor". J. Biol. Chem. 276 (40): 37556–63. doi:10.1074/jbc.M101730200. PMID 11477070.

Cookson MR (2003). "Pathways to Parkinsonism". Neuron 37 (1): 7–10. doi:10.1016/S0896-6273(02)01166-2. PMID 12526767.
Bonifati V, Oostra BA, Heutink P (2004). "Linking DJ-1 to neurodegeneration offers novel insights for understanding the pathogenesis of Parkinson's disease". J. Mol. Med. 82 (3): 163–74. doi:10.1007/s00109-003-0512-1. PMID 14712351.
Le W, Appel SH (2004). "Mutant genes responsible for Parkinson's disease". Current Opinion in Pharmacology 4 (1): 79–84. doi:10.1016/j.coph.2003.09.005. PMID 15018843.
Abou-Sleiman PM, Healy DG, Wood NW (2005). "Causes of Parkinson's disease: genetics of DJ-1". Cell Tissue Res. 318 (1): 185–8. doi:10.1007/s00441-004-0922-6. PMID 15503154.
Pankratz N, Foroud T (2005). "Genetics of Parkinson Disease". NeuroRx : the journal of the American Society for Experimental NeuroTherapeutics 1 (2): 235–42. doi:10.1602/neurorx.1.2.235. PMC 534935. PMID 15717024.
Heutink P (2006). "PINK-1 and DJ-1--new genes for autosomal recessive Parkinson's disease". J. Neural Transm. Suppl. Journal of Neural Transmission. Supplementa 70 (70): 215–9. doi:10.1007/978-3-211-45295-0_33. ISBN 978-3-211-28927-3. PMID 17017532.
Lev N, Roncevic D, Roncevich D, Ickowicz D, Melamed E, Offen D (2007). "Role of DJ-1 in Parkinson's disease". J. Mol. Neurosci. 29 (3): 215–25. doi:10.1385/JMN:29:3:215. PMID 17085780.
Nagakubo D, Taira T, Kitaura H, Ikeda M, Tamai K, Iguchi-Ariga SM, Ariga H (1997). "DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras". Biochem. Biophys. Res. Commun. 231 (2): 509–13. doi:10.1006/bbrc.1997.6132. PMID 9070310.
Taira T, Takahashi K, Kitagawa R, Iguchi-Ariga SM, Ariga H (2001). "Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter". Gene 263 (1–2): 285–92. doi:10.1016/S0378-1119(00)00590-4. PMID 11223268.
van Duijn CM, Dekker MC, Bonifati V, Galjaard RJ, Houwing-Duistermaat JJ, Snijders PJ, Testers L, Breedveld GJ, Horstink M, Sandkuijl LA, van Swieten JC, Oostra BA, Heutink P (2001). "PARK7, a Novel Locus for Autosomal Recessive Early-Onset Parkinsonism, on Chromosome 1p36". Am. J. Hum. Genet. 69 (3): 629–34. doi:10.1086/322996. PMC 1235491. PMID 11462174.
Takahashi K, Taira T, Niki T, Seino C, Iguchi-Ariga SM, Ariga H (2001). "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor". J. Biol. Chem. 276 (40): 37556–63. doi:10.1074/jbc.M101730200. PMID 11477070.
Bonifati V, Rizzu P, van Baren MJ, Schaap O, Breedveld GJ, Krieger E, Dekker MC, Squitieri F, Ibanez P, Joosse M, van Dongen JW, Vanacore N, van Swieten JC, Brice A, Meco G, van Duijn CM, Oostra BA, Heutink P (2003). "Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism". Science 299 (5604): 256–9. doi:10.1126/science.1077209. PMID 12446870.
Bonifati V, Dekker MC, Vanacore N, Fabbrini G, Squitieri F, Marconi R, Antonini A, Brustenghi P, Dalla Libera A, De Mari M, Stocchi F, Montagna P, Gallai V, Rizzu P, van Swieten JC, Oostra B, van Duijn CM, Meco G, Heutink P (2003). "Autosomal recessive early onset parkinsonism is linked to three loci: PARK2, PARK6, and PARK7". Neurol. Sci. 23 Suppl 2: S59–60. doi:10.1007/s100720200069. PMID 12548343.
Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H (2004). "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex". Mol. Cancer Res. 1 (4): 247–61. PMID 12612053.
Tao X, Tong L (2003). "Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease". J. Biol. Chem. 278 (33): 31372–9. doi:10.1074/jbc.M304221200. PMID 12761214.
Honbou K, Suzuki NN, Horiuchi M, Niki T, Taira T, Ariga H, Inagaki F (2003). "The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease". J. Biol. Chem. 278 (33): 31380–4. doi:10.1074/jbc.M305878200. PMID 12796482.
Dekker M, Bonifati V, van Swieten J, Leenders N, Galjaard RJ, Snijders P, Horstink M, Heutink P, Oostra B, van Duijn C (2004). "Clinical features and neuroimaging of PARK7-linked parkinsonism". Mov. Disord. 18 (7): 751–7. doi:10.1002/mds.10422. PMID 12815653.
Miller DW, Ahmad R, Hague S, Baptista MJ, Canet-Aviles R, McLendon C, Carter DM, Zhu PP, Stadler J, Chandran J, Klinefelter GR, Blackstone C, Cookson MR (2003). "L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system". J. Biol. Chem. 278 (38): 36588–95. doi:10.1074/jbc.M304272200. PMID 12851414.