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)
 

Editor

Share

Personal info

View

Links

  • Homologues
  • NCBI Gene
  • NCBI SNP
  • iHOP resource
  • OMIM
  • SNPedia
  • UniProt
  • Ensembl
  • HGNC

Table of contents

About

Terms

 

Gene Review: 

UBE3C  -  ubiquitin protein ligase E3C

Homo sapiens

Synonyms: HectH2, KIAA0010, KIAA10, Ubiquitin-protein ligase E3C
 
 
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.
 

High impact information on UBE3C

  • Here, we used a combination of mutagenesis, biochemistry, and mass spectrometry to map determinants of linkage choice in chain assembly catalyzed by KIAA10, an HECT (Homologous to E6AP C-Terminus) domain E3 that synthesizes K29- and K48-linked chains [1].
  • We show that E6AP builds up a K48-linked chain on its HECT cysteine residue, while KIAA10 builds up K48- and K29-linked chains as free entities [2].
  • We report that the N-domain of KIAA10 also mediates an association with TIP120B (TATA-binding protein-interacting protein 120B), a putative transcriptional regulator [3].
  • Biochemical and co-transfection studies revealed that TIP120B, but not the closely related protein TIP120A, is a specific substrate of KIAA10 in vitro and within C2C12 myoblasts but not in Cos-1 cells [3].
  • The KIAA10 protein is a member of the HECT (homologous to E6-AP carboxyl terminus) domain family of E3s [4].

References

  1. Molecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase. Wang, M., Cheng, D., Peng, J., Pickart, C.M. EMBO J. (2006) [Pubmed]
  2. Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis. Wang, M., Pickart, C.M. EMBO J. (2005) [Pubmed]
  3. Proteolytic targeting of transcriptional regulator TIP120B by a HECT domain E3 ligase. You, J., Wang, M., Aoki, T., Tamura, T.A., Pickart, C.M. J. Biol. Chem. (2003) [Pubmed]
  4. A HECT domain E3 enzyme assembles novel polyubiquitin chains. You, J., Pickart, C.M. J. Biol. Chem. (2001) [Pubmed]
Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities