The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

SYVN1  -  synovial apoptosis inhibitor 1, synoviolin

Homo sapiens

Synonyms: DER3, E3 ubiquitin-protein ligase synoviolin, HRD1, KIAA1810, Synovial apoptosis inhibitor 1
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of SYVN1

  • The C-terminus of HIF3alpha contains a 36-amino acid sequence that shares 61% identity with the hypoxia responsive domain-1 (HRD1) of HIF1alpha [1].
 

High impact information on SYVN1

  • Conversely, synoviolin/hrd1(+/-) mice were resistant to collagen-induced arthritis by enhanced apoptosis of synovial cells [2].
  • We identify designated regions in the luminal domain of Hrd3p that interact with Yos9p and the ubiquitin ligase Hrd1p [3].
  • Synoviolin, also called HRD1, is an E3 ubiquitin ligase and is implicated in endoplasmic reticulum -associated degradation [4].
  • We confirmed that these conditions supported the ubiquitination of Hrd1p itself, and the transfer of ubiquitin to the prototype substrate Hmg2p-GFP, validating Hrd1p self-ubiquitination as a viable assay of ligase function [5].
  • A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin [6].
 

Anatomical context of SYVN1

  • Here, we show that HRD1, a component of the ERAD system, is upregulated in pancreatic islets of the Akita diabetes mouse model and enhances intracellular degradation of misfolded insulin [7].
  • Notably, another ER transmembrane E3, Hrd1 (also known as Der3), cannot localize efficiently to the inner nuclear membrane [8].
 

Other interactions of SYVN1

  • Furthermore, it was found that human HRD1 was up-regulated by ER stress via IRE1 and ATF6, which are ER stress transducers [9].

References

  1. Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha. Gu, Y.Z., Moran, S.M., Hogenesch, J.B., Wartman, L., Bradfield, C.A. Gene Expr. (1998) [Pubmed]
  2. Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy. 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. Genes Dev. (2003) [Pubmed]
  3. A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Gauss, R., Jarosch, E., Sommer, T., Hirsch, C. Nat. Cell Biol. (2006) [Pubmed]
  4. Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'. 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. EMBO J. (2007) [Pubmed]
  5. Determinants of RING-E2 Fidelity for Hrd1p, a Membrane-anchored Ubiquitin Ligase. Bazirgan, O.A., Garza, R.M., Hampton, R.Y. J. Biol. Chem. (2006) [Pubmed]
  6. A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin. 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. J. Neurochem. (2006) [Pubmed]
  7. High ER stress in beta-cells stimulates intracellular degradation of misfolded insulin. Allen, J.R., Nguyen, L.X., Sargent, K.E., Lipson, K.L., Hackett, A., Urano, F. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  8. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Deng, M., Hochstrasser, M. Nature (2006) [Pubmed]
  9. Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation. Kaneko, M., Ishiguro, M., Niinuma, Y., Uesugi, M., Nomura, Y. FEBS Lett. (2002) [Pubmed]
 
WikiGenes - Universities