// Workers AI · dad joke modeWhat did SYVN1 say to its friend? "You sync with me.

SYVN1
Identifiers
Aliases	SYVN1, DER3, HRD1, synoviolin 1
External IDs	OMIM: 608046; MGI: 1921376; HomoloGene: 32700; GeneCards: SYVN1; OMA:SYVN1 - orthologs
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 2.3.2.27 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 11 (human) Band 11q13.1 Start 65,121,780 bp End 65,134,532 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 A Start 6,096,606 bp End 6,103,742 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of ileum body of pancreas right lobe of liver bone marrow cell appendix stromal cell of endometrium islet of Langerhans right lobe of thyroid gland lymph node left lobe of thyroid gland Top expressed in mesenteric lymph nodes lacrimal gland salivary gland decidua left lobe of liver islet of Langerhans molar spleen seminal vesicula renal corpuscle More reference expression data BioGPS n/a
Gene ontology Molecular function chaperone binding unfolded protein binding ATPase binding metal ion binding protein binding ubiquitin-specific protease binding ubiquitin protein ligase activity transferase activity Cellular component integral component of membrane endoplasmic reticulum membrane nucleoplasm smooth endoplasmic reticulum integral component of endoplasmic reticulum membrane endoplasmic reticulum quality control compartment Derlin-1 retrotranslocation complex Hrd1p ubiquitin ligase complex Hrd1p ubiquitin ligase ERAD-L complex membrane endoplasmic reticulum Biological process protein stabilization protein K48-linked ubiquitination retrograde protein transport, ER to cytosol IRE1-mediated unfolded protein response negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway protein N-linked glycosylation via asparagine endoplasmic reticulum mannose trimming ERAD pathway endoplasmic reticulum unfolded protein response ubiquitin-dependent ERAD pathway protein ubiquitination ubiquitin-dependent protein catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 84447 74126 Ensembl ENSG00000162298 ENSMUSG00000024807 UniProt Q86TM6 Q9DBY1 RefSeq (mRNA) NM_032431 NM_172230 NM_001164709 NM_028769 RefSeq (protein) NP_115807 NP_757385 NP_001158181 NP_083045 Location (UCSC) Chr 11: 65.12 – 65.13 Mb Chr 19: 6.1 – 6.1 Mb PubMed search
Wikidata
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E3 ubiquitin-protein ligase synoviolin is an enzyme that in humans is encoded by the SYVN1 gene.

Function

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.

Further reading

• Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (September 2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
• 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.

External links

• Overview of all the structural information available in the PDB for UniProt: Q86TM6 (E3 ubiquitin-protein ligase synoviolin) at the PDBe-KB.