HRD1
SYVN1
Protein-coding gene in the species Homo sapiens
E3 ubiquitin-protein ligase synoviolin is an enzyme that in humans is encoded by the SYVN1 gene.[5][6]
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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.[6]
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- 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 (October 2003). "Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy". Genes & Development. 17 (19): 2436–49. doi:10.1101/gad.1096603. PMC 218080. PMID 12975321.
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- Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O (April 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 Research. 8 (2): 85–95. doi:10.1093/dnares/8.2.85. PMID 11347906.
- Kaneko M, Ishiguro M, Niinuma Y, Uesugi M, Nomura Y (December 2002). "Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation". FEBS Letters. 532 (1–2): 147–52. doi:10.1016/S0014-5793(02)03660-8. PMID 12459480. S2CID 44570384.
- Nadav E, Shmueli A, Barr H, Gonen H, Ciechanover A, Reiss Y (March 2003). "A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1". Biochemical and Biophysical Research Communications. 303 (1): 91–7. doi:10.1016/S0006-291X(03)00279-1. PMID 12646171.
- Kikkert M, Doolman R, Dai M, Avner R, Hassink G, van Voorden S, Thanedar S, Roitelman J, Chau V, Wiertz E (January 2004). "Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum". The Journal of Biological Chemistry. 279 (5): 3525–34. doi:10.1074/jbc.M307453200. PMID 14593114.
- Lilley BN, Ploegh HL (October 2005). "Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane". Proceedings of the National Academy of Sciences of the United States of America. 102 (40): 14296–301. Bibcode:2005PNAS..10214296L. doi:10.1073/pnas.0505014102. PMC 1242303. PMID 16186509.
- Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E, Rapoport TA (October 2005). "Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane". Proceedings of the National Academy of Sciences of the United States of America. 102 (40): 14132–8. Bibcode:2005PNAS..10214132Y. doi:10.1073/pnas.0505006102. PMC 1242302. PMID 16186510.
- Schulze A, Standera S, Buerger E, Kikkert M, van Voorden S, Wiertz E, Koning F, Kloetzel PM, Seeger M (December 2005). "The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway". Journal of Molecular Biology. 354 (5): 1021–7. doi:10.1016/j.jmb.2005.10.020. PMID 16289116.
- Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 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. S2CID 13709685.
- Yamasaki S, Yagishita N, Tsuchimochi K, Kato Y, Sasaki T, Amano T, Beppu M, Aoki H, Nakamura H, Nishioka K, Nakajima T (July 2006). "Resistance to endoplasmic reticulum stress is an acquired cellular characteristic of rheumatoid synovial cells". International Journal of Molecular Medicine. 18 (1): 113–7. doi:10.3892/ijmm.18.1.113. PMID 16786162.
- Toh ML, Marotte H, Blond JL, Jhumka U, Eljaafari A, Mougin B, Miossec P (July 2006). "Overexpression of synoviolin in peripheral blood and synoviocytes from rheumatoid arthritis patients and continued elevation in nonresponders to infliximab treatment". Arthritis and Rheumatism. 54 (7): 2109–18. doi:10.1002/art.21926. PMID 16802346.
- Arteaga MF, Wang L, Ravid T, Hochstrasser M, Canessa CM (July 2006). "An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery". Proceedings of the National Academy of Sciences of the United States of America. 103 (30): 11178–83. Bibcode:2006PNAS..10311178A. doi:10.1073/pnas.0604816103. PMC 1544061. PMID 16847254.
- Omura T, Kaneko M, Okuma Y, Orba Y, Nagashima K, Takahashi R, Fujitani N, Matsumura S, Hata A, Kubota K, Murahashi K, Uehara T, Nomura Y (December 2006). "A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin". Journal of Neurochemistry. 99 (6): 1456–69. doi:10.1111/j.1471-4159.2006.04155.x. hdl:2115/17141. PMID 17059562. S2CID 6256027.
- Yang H, Zhong X, Ballar P, Luo S, Shen Y, Rubinsztein DC, Monteiro MJ, Fang S (February 2007). "Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin". Experimental Cell Research. 313 (3): 538–50. doi:10.1016/j.yexcr.2006.10.031. PMID 17141218.
- Yamasaki S, Yagishita N, Sasaki T, Nakazawa M, Kato Y, Yamadera T, Bae E, Toriyama S, Ikeda R, Zhang L, Fujitani K, Yoo E, Tsuchimochi K, Ohta T, Araya N, Fujita H, Aratani S, Eguchi K, Komiya S, Maruyama I, Higashi N, Sato M, Senoo H, Ochi T, Yokoyama S, Amano T, Kim J, Gay S, Fukamizu A, Nishioka K, Tanaka K, Nakajima T (January 2007). "Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'". The EMBO Journal. 26 (1): 113–22. doi:10.1038/sj.emboj.7601490. PMC 1782373. PMID 17170702.
