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RNF19A
Identifiers
Aliases	RNF19A, RNF19, ring finger protein 19A, RBR E3 ubiquitin protein ligase
External IDs	OMIM: 607119; MGI: 1353623; HomoloGene: 8501; GeneCards: RNF19A; OMA:RNF19A - orthologs
Gene location (Human) Chr. Chromosome 8 (human) Band 8q22.2 Start 100,257,060 bp End 100,336,218 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15|15 B3.1 Start 36,240,079 bp End 36,283,293 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon sperm epithelium of colon right lung canal of the cervix gallbladder epithelium of nasopharynx left uterine tube tonsil mucosa of paranasal sinus Top expressed in spermatid spermatocyte seminiferous tubule renal corpuscle granulocyte lumbar spinal ganglion medullary collecting duct fetal liver hematopoietic progenitor cell zygote secondary oocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transcription factor binding ubiquitin conjugating enzyme binding ubiquitin protein ligase activity metal ion binding ubiquitin-protein transferase activity transferase activity Cellular component cytoplasm integral component of membrane microtubule organizing center centrosome cytoskeleton membrane ubiquitin ligase complex cytosol hippocampal mossy fiber to CA3 synapse postsynapse glutamatergic synapse Biological process microtubule cytoskeleton organization positive regulation of proteasomal ubiquitin-dependent protein catabolic process protein ubiquitination protein polyubiquitination regulation of protein catabolic process at postsynapse, modulating synaptic transmission ubiquitin-dependent protein catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 25897 30945 Ensembl ENSG00000034677 ENSMUSG00000022280 UniProt Q9NV58 P50636 RefSeq (mRNA) NM_001280539 NM_015435 NM_183419 NM_001353837 NM_001353838 NM_013923 NM_001357631 RefSeq (protein) NP_001267468 NP_056250 NP_904355 NP_001340766 NP_001340767 NP_038951 NP_001344560 Location (UCSC) Chr 8: 100.26 – 100.34 Mb Chr 15: 36.24 – 36.28 Mb PubMed search
Wikidata
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E3 ubiquitin-protein ligase RNF19A is an enzyme that in humans is encoded by the RNF19A gene.

The protein encoded by this gene contains two RING-finger motifs and an IBR (in between RING fingers) motif. This protein is an E3 ubiquitin ligase that is localized in Lewy bodies (LBs), neuronal inclusions characteristic of Parkinson's disease (PD). 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.

See also

• RING finger domain

References

1. ^ GRCh38: Ensembl release 89: ENSG00000034677 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000022280 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Niwa J, Ishigaki S, Doyu M, Suzuki T, Tanaka K, Sobue G (Mar 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.
6. Gunther M, Laithier M, Brison O (Dec 2000). "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening". Mol Cell Biochem. 210 (1–2): 131–42. doi:10.1023/A:1007177623283. PMID 10976766. S2CID 1339642.
7. ^ "Entrez Gene: RNF19 ring finger protein 19".

Further reading

• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. doi:10.1016/S0002-9440(10)63688-7. PMC 1868225. 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. PMC 1223961. 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. S2CID 19295830.
• 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. PMC 528928. 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. S2CID 311022.

External links

• RNF19A+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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