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{{Infobox_gene}}
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'''E3 ubiquitin-protein ligase synoviolin''' is an [[enzyme]] that in humans is encoded by the ''SYVN1'' [[gene]].<ref name="pmid12975321">{{cite journal | vauthors = 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 | title = Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy | journal = Genes Dev | volume = 17 | issue = 19 | pages = 2436–49 |date=Oct 2003 | pmid = 12975321 | pmc = 218080 | doi = 10.1101/gad.1096603 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SYVN1 synovial apoptosis inhibitor 1, synoviolin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84447| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = Synovial apoptosis inhibitor 1, synoviolin
| HGNCid = 20738
| Symbol = SYVN1
| AltSymbols =; HRD1; KIAA1810; MGC40372
| OMIM = 608046
| ECnumber = 
| Homologene = 32700
| MGIid = 1921376
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 84447
    | Hs_Ensembl = ENSG00000162298
    | Hs_RefseqProtein = NP_115807
    | Hs_RefseqmRNA = NM_032431
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 64651329
    | Hs_GenLoc_end = 64658580
    | Hs_Uniprot =
    | Mm_EntrezGene = 74126
    | Mm_Ensembl = ENSMUSG00000024807
    | Mm_RefseqmRNA = NM_028769
    | Mm_RefseqProtein = NP_083045
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 6046662
    | Mm_GenLoc_end = 6053709
    | Mm_Uniprot = 
  }}
}}
'''Synovial apoptosis inhibitor 1, synoviolin''', also known as '''SYVN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SYVN1 synovial apoptosis inhibitor 1, synoviolin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84447| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: SYVN1 synovial apoptosis inhibitor 1, synoviolin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84447| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal   |vauthors=Simpson JC, Wellenreuther R, Poustka A, etal |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 | pmc=1083732 }}
*{{cite journal | author=Nagase T, Nakayama M, Nakajima D, ''et al.'' |title=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. |journal=DNA Res. |volume=8 |issue= 2 |pages= 85-95 |year= 2001 |pmid= 11347906 |doi= }}
*{{cite journal   |vauthors=Nagase T, Nakayama M, Nakajima D, etal |title=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 |journal=DNA Res. |volume=8 |issue= 2 |pages= 85–95 |year= 2001 |pmid= 11347906 |doi=10.1093/dnares/8.2.85  }}
*{{cite journal | author=Kaneko M, Ishiguro M, Niinuma Y, ''et al.'' |title=Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation. |journal=FEBS Lett. |volume=532 |issue= 1-2 |pages= 147-52 |year= 2003 |pmid= 12459480 |doi= }}
*{{cite journal   |vauthors=Kaneko M, Ishiguro M, Niinuma Y, etal |title=Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation |journal=FEBS Lett. |volume=532 |issue= 1–2 |pages= 147–52 |year= 2003 |pmid= 12459480 |doi=10.1016/S0014-5793(02)03660-8  }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Nadav E, Shmueli A, Barr H, ''et al.'' |title=A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1. |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 1 |pages= 91-7 |year= 2003 |pmid= 12646171 |doi=  }}
*{{cite journal   |vauthors=Nadav E, Shmueli A, Barr H, etal |title=A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1 |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 1 |pages= 91–7 |year= 2003 |pmid= 12646171 |doi=10.1016/S0006-291X(03)00279-1 }}
*{{cite journal | author=Amano T, Yamasaki S, Yagishita N, ''et al.'' |title=Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy. |journal=Genes Dev. |volume=17 |issue= 19 |pages= 2436-49 |year= 2003 |pmid= 12975321 |doi= 10.1101/gad.1096603 }}
*{{cite journal   |vauthors=Kikkert M, Doolman R, Dai M, etal |title=Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum |journal=J. Biol. Chem. |volume=279 |issue= 5 |pages= 3525–34 |year= 2004 |pmid= 14593114 |doi= 10.1074/jbc.M307453200 }}
*{{cite journal | author=Kikkert M, Doolman R, Dai M, ''et al.'' |title=Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=279 |issue= 5 |pages= 3525-34 |year= 2004 |pmid= 14593114 |doi= 10.1074/jbc.M307453200 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Lilley BN, Ploegh HL |title=Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 40 |pages= 14296–301 |year= 2006 |pmid= 16186509 |doi= 10.1073/pnas.0505014102  | pmc=1242303 }}
*{{cite journal | author=Lilley BN, Ploegh HL |title=Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 40 |pages= 14296-301 |year= 2006 |pmid= 16186509 |doi= 10.1073/pnas.0505014102 }}
*{{cite journal   |vauthors=Ye Y, Shibata Y, Kikkert M, etal |title=Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 40 |pages= 14132–8 |year= 2006 |pmid= 16186510 |doi= 10.1073/pnas.0505006102  | pmc=1242302 }}
*{{cite journal | author=Ye Y, Shibata Y, Kikkert M, ''et al.'' |title=Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 40 |pages= 14132-8 |year= 2006 |pmid= 16186510 |doi= 10.1073/pnas.0505006102 }}
*{{cite journal   |vauthors=Schulze A, Standera S, Buerger E, etal |title=The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway |journal=J. Mol. Biol. |volume=354 |issue= 5 |pages= 1021–7 |year= 2006 |pmid= 16289116 |doi= 10.1016/j.jmb.2005.10.020 }}
*{{cite journal | author=Schulze A, Standera S, Buerger E, ''et al.'' |title=The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. |journal=J. Mol. Biol. |volume=354 |issue= 5 |pages= 1021-7 |year= 2006 |pmid= 16289116 |doi= 10.1016/j.jmb.2005.10.020 }}
*{{cite journal   |vauthors=Lim J, Hao T, Shaw C, etal |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration |journal=Cell |volume=125 |issue= 4 |pages= 801–14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal | author=Lim J, Hao T, Shaw C, ''et al.'' |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801-14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal   |vauthors=Yamasaki S, Yagishita N, Tsuchimochi K, etal |title=Resistance to endoplasmic reticulum stress is an acquired cellular characteristic of rheumatoid synovial cells |journal=Int. J. Mol. Med. |volume=18 |issue= 1 |pages= 113–7 |year= 2006 |pmid= 16786162 |doi= 10.3892/ijmm.18.1.113}}
*{{cite journal | author=Yamasaki S, Yagishita N, Tsuchimochi K, ''et al.'' |title=Resistance to endoplasmic reticulum stress is an acquired cellular characteristic of rheumatoid synovial cells. |journal=Int. J. Mol. Med. |volume=18 |issue= 1 |pages= 113-7 |year= 2006 |pmid= 16786162 |doi= }}
*{{cite journal   |vauthors=Toh ML, Marotte H, Blond JL, etal |title=Overexpression of synoviolin in peripheral blood and synoviocytes from rheumatoid arthritis patients and continued elevation in nonresponders to infliximab treatment |journal=Arthritis Rheum. |volume=54 |issue= 7 |pages= 2109–18 |year= 2006 |pmid= 16802346 |doi= 10.1002/art.21926 }}
*{{cite journal | author=Toh ML, Marotte H, Blond JL, ''et al.'' |title=Overexpression of synoviolin in peripheral blood and synoviocytes from rheumatoid arthritis patients and continued elevation in nonresponders to infliximab treatment. |journal=Arthritis Rheum. |volume=54 |issue= 7 |pages= 2109-18 |year= 2006 |pmid= 16802346 |doi= 10.1002/art.21926 }}
*{{cite journal   |vauthors=Arteaga MF, Wang L, Ravid T, etal |title=An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 30 |pages= 11178–83 |year= 2006 |pmid= 16847254 |doi= 10.1073/pnas.0604816103  | pmc=1544061 }}
*{{cite journal | author=Arteaga MF, Wang L, Ravid T, ''et al.'' |title=An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 30 |pages= 11178-83 |year= 2006 |pmid= 16847254 |doi= 10.1073/pnas.0604816103 }}
*{{cite journal   |vauthors=Omura T, Kaneko M, Okuma Y, etal |title=A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin |journal=J. Neurochem. |volume=99 |issue= 6 |pages= 1456–69 |year= 2007 |pmid= 17059562 |doi= 10.1111/j.1471-4159.2006.04155.x }}
*{{cite journal | author=Omura T, Kaneko M, Okuma Y, ''et al.'' |title=A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin. |journal=J. Neurochem. |volume=99 |issue= 6 |pages= 1456-69 |year= 2007 |pmid= 17059562 |doi= 10.1111/j.1471-4159.2006.04155.x }}
*{{cite journal   |vauthors=Yang H, Zhong X, Ballar P, etal |title=Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin |journal=Exp. Cell Res. |volume=313 |issue= 3 |pages= 538–50 |year= 2007 |pmid= 17141218 |doi= 10.1016/j.yexcr.2006.10.031 }}
*{{cite journal | author=Yang H, Zhong X, Ballar P, ''et al.'' |title=Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin. |journal=Exp. Cell Res. |volume=313 |issue= 3 |pages= 538-50 |year= 2007 |pmid= 17141218 |doi= 10.1016/j.yexcr.2006.10.031 }}
*{{cite journal   |vauthors=Yamasaki S, Yagishita N, Sasaki T, etal |title=Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin' |journal=EMBO J. |volume=26 |issue= 1 |pages= 113–22 |year= 2007 |pmid= 17170702 |doi= 10.1038/sj.emboj.7601490 | pmc=1782373 }}
*{{cite journal | author=Yamasaki S, Yagishita N, Sasaki T, ''et al.'' |title=Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'. |journal=EMBO J. |volume=26 |issue= 1 |pages= 113-22 |year= 2007 |pmid= 17170702 |doi= 10.1038/sj.emboj.7601490 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 07:24, 11 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: SYVN1 synovial apoptosis inhibitor 1, synoviolin".

Further reading



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