SYVN1 - synovial apoptosis inhibitor 1, synoviolin
Entrez Gene Name: synovial apoptosis inhibitor 1, synoviolin
Entrez GeneID: Human(84447)
, Mouse(74126), Rat(361712)
, Mouse(74126), Rat(361712) Synonyms: 1200010c09RIK, AW211966, C85322, D530017H19Rik, HRD1, KIAA1810, MGC40372, RGD1310488, SYVN1
Gene Summary
- Human (84447): 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. [provided by RefSeq]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras
Cell Regulation
Biological Process
anti-apoptosis, ER-associated protein catabolic process, in utero embryonic development, modification-dependent protein catabolic process, multicellular organismal development, response to stress, response to unfolded protein
Cellular Components
endoplasmic reticulum, endoplasmic reticulum membrane, integral to membrane, membrane, nucleolus, nucleus, ubiquitin ligase complex
Literature References
- 12975321Amano 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. Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy.Genes Dev 2003 Oct 01;17(19):2436-49
- 17141218Yang H, Zhong X, Ballar P, Luo S, Shen Y, Rubinsztein DC, Monteiro MJ, Fang S. Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin.Exp Cell Res 2007 02 1;313(3):538-50
- 16186510Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E, Rapoport TA. Inaugural Article: 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 2005 Oct 04;102(40):14132-8 View 151 categorized literature findings and their references in IPA
Molecular Functions
acid-amino acid ligase activity, ligase activity, metal ion binding, protein binding, ubiquitin-protein ligase activity, zinc ion binding
Protein Domains
Acid-D-amino acid ligase, RING domain, RING-H2 domain, transporter, Ubiquitin-protein ligase
Subcellular Locations
cytoplasm, endoplasmic reticulum, endoplasmic reticulum membrane, smooth endoplasmatic reticulum
