RNF19A

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Ring finger protein 19
Identifiers
Symbol(s) RNF19; DKFZp566B1346; DORFIN
External IDs OMIM: 607119 MGI1353623 HomoloGene8501
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 25897 30945
Ensembl ENSG00000034677 ENSMUSG00000022280
Uniprot Q9NV58 Q3TM18
Refseq NM_015435 (mRNA)
NP_056250 (protein)
NM_013923 (mRNA)
NP_038951 (protein)
Location Chr 8: 101.34 - 101.39 Mb Chr 15: 36.18 - 36.21 Mb
Pubmed search [1] [2]

Ring finger protein 19, also known as RNF19, is a human gene.[1]

The protein encoded this gene contains two RING-finger motifs and an IBR (in between RING fingers) motif. This protein is an E3 ubiquintin ligase that is localized in Lewy bodies (LBs), a characteristic neuronal inclusion in Parkinson's disease (PD) brains. This protein interacts with UBE2L3/UBCH7 and UBE2E2/UBCH8, but not other ubiquitin-conjugating enzymes. This protein is found to bind and ubiquitylate synphilin 1 (SNCAIP), which is an interacting protein of alpha synuclein in neurons, and a major component of LB. Alternatively spliced transcript variants encoding the same protein have been reported.[1]

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[edit] Further reading

  • Gunther M, Laithier M, Brison O (2000). "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening.". Mol. Cell. Biochem. 210 (1-2): 131-42. PMID 10976766. 
  • Niwa J, Ishigaki S, Doyu M, et al. (2001). "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity.". Biochem. Biophys. Res. Commun. 281 (3): 706-13. doi:10.1006/bbrc.2001.4414. PMID 11237715. 
  • Niwa J, Ishigaki S, Hishikawa N, et al. (2002). "Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity.". J. Biol. Chem. 277 (39): 36793-8. doi:10.1074/jbc. M206559200. PMID 12145308. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Ito T, Niwa J, Hishikawa N, et al. (2003). "Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1.". J. Biol. Chem. 278 (31): 29106-14. doi:10.1074/jbc. M302763200. PMID 12750386. 
  • Hishikawa N, Niwa J, Doyu M, et al. (2003). "Dorfin localizes to the ubiquitylated inclusions in Parkinson's disease, dementia with Lewy bodies, multiple system atrophy, and amyotrophic lateral sclerosis.". Am. J. Pathol. 163 (2): 609-19. PMID 12875980. 
  • Paces-Fessy M, Boucher D, Petit E, et al. (2004). "The negative regulator of Gli, Suppressor of fused (Sufu), interacts with SAP18, Galectin3 and other nuclear proteins.". Biochem. J. 378 (Pt 2): 353-62. doi:10.1042/BJ20030786. PMID 14611647. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. 
  • Takeuchi H, Niwa J, Hishikawa N, et al. (2004). "Dorfin prevents cell death by reducing mitochondrial localizing mutant superoxide dismutase 1 in a neuronal cell model of familial amyotrophic lateral sclerosis.". J. Neurochem. 89 (1): 64-72. doi:10.1046/j.1471-4159.2003.02289.x. PMID 15030390. 
  • Ishigaki S, Hishikawa N, Niwa J, et al. (2005). "Physical and functional interaction between Dorfin and Valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders.". J. Biol. Chem. 279 (49): 51376-85. doi:10.1074/jbc. M406683200. PMID 15456787. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Huang Y, Niwa J, Sobue G, Breitwieser GE (2006). "Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin.". J. Biol. Chem. 281 (17): 11610-7. doi:10.1074/jbc. M513552200. PMID 16513638. 
  • Ishigaki S, Niwa J, Yamada S, et al. (2007). "Dorfin-CHIP chimeric proteins potently ubiquitylate and degrade familial ALS-related mutant SOD1 proteins and reduce their cellular toxicity.". Neurobiol. Dis. 25 (2): 331-41. doi:10.1016/j.nbd.2006.09.017. PMID 17157513. 

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