E3 ubiquitin-protein ligase synoviolin is an enzyme that in humans is encoded by the SYVN1 gene.[1][2]
This gene encodes a protein involved in endoplasmic reticulum (ER)-associated degradation. The encoded protein removes unfolded proteins, accumulated during ER stress, by retrograde transport to the cytosol from the ER. This protein also uses the ubiquitin-proteasome system for additional degradation of unfolded proteins. This gene and the mitochondrial ribosomal protein L49 gene use in their respective 3' UTRs some of the same genomic sequence. Sequence analysis identified two transcript variants that encode different isoforms.[2]
References [link]
- ^ Amano T, Yamasaki S, Yagishita N, Tsuchimochi K, Shin H, Kawahara K, Aratani S, Fujita H, Zhang L, Ikeda R, Fujii R, Miura N, Komiya S, Nishioka K, Maruyama I, Fukamizu A, Nakajima T (Oct 2003). "Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy". Genes Dev 17 (19): 2436–49. DOI:10.1101/gad.1096603. PMC 218080. PMID 12975321. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=218080.
- ^ a b "Entrez Gene: SYVN1 synovial apoptosis inhibitor 1, synoviolin". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84447.
Further reading [link]
- Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. DOI:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1083732.
- Nagase T, Nakayama M, Nakajima D, et al. (2001). "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 8 (2): 85–95. DOI:10.1093/dnares/8.2.85. PMID 11347906.
- Kaneko M, Ishiguro M, Niinuma Y, et al. (2003). "Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation". FEBS Lett. 532 (1–2): 147–52. DOI:10.1016/S0014-5793(02)03660-8. PMID 12459480.
- 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. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Nadav E, Shmueli A, Barr H, et al. (2003). "A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1". Biochem. Biophys. Res. Commun. 303 (1): 91–7. DOI:10.1016/S0006-291X(03)00279-1. PMID 12646171.
- Kikkert M, Doolman R, Dai M, et al. (2004). "Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum". J. Biol. Chem. 279 (5): 3525–34. DOI:10.1074/jbc.M307453200. PMID 14593114.
- 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Lilley BN, Ploegh HL (2006). "Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14296–301. DOI:10.1073/pnas.0505014102. PMC 1242303. PMID 16186509. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1242303.
- Ye Y, Shibata Y, Kikkert M, et al. (2006). "Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14132–8. DOI:10.1073/pnas.0505006102. PMC 1242302. PMID 16186510. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1242302.
- Schulze A, Standera S, Buerger E, et al. (2006). "The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway". J. Mol. Biol. 354 (5): 1021–7. DOI:10.1016/j.jmb.2005.10.020. PMID 16289116.
- Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. DOI:10.1016/j.cell.2006.03.032. PMID 16713569.
- Yamasaki S, Yagishita N, Tsuchimochi K, et al. (2006). "Resistance to endoplasmic reticulum stress is an acquired cellular characteristic of rheumatoid synovial cells". Int. J. Mol. Med. 18 (1): 113–7. PMID 16786162.
- Toh ML, Marotte H, Blond JL, et al. (2006). "Overexpression of synoviolin in peripheral blood and synoviocytes from rheumatoid arthritis patients and continued elevation in nonresponders to infliximab treatment". Arthritis Rheum. 54 (7): 2109–18. DOI:10.1002/art.21926. PMID 16802346.
- Arteaga MF, Wang L, Ravid T, et al. (2006). "An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery". Proc. Natl. Acad. Sci. U.S.A. 103 (30): 11178–83. DOI:10.1073/pnas.0604816103. PMC 1544061. PMID 16847254. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1544061.
- Omura T, Kaneko M, Okuma Y, et al. (2007). "A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin". J. Neurochem. 99 (6): 1456–69. DOI:10.1111/j.1471-4159.2006.04155.x. PMID 17059562.
- Yang H, Zhong X, Ballar P, et al. (2007). "Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin". Exp. Cell Res. 313 (3): 538–50. DOI:10.1016/j.yexcr.2006.10.031. PMID 17141218.
- Yamasaki S, Yagishita N, Sasaki T, et al. (2007). "Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'". EMBO J. 26 (1): 113–22. DOI:10.1038/sj.emboj.7601490. PMC 1782373. PMID 17170702. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1782373.
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