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Gene Review

UBE3C  -  ubiquitin protein ligase E3C

Homo sapiens

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


  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]
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