E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme

Sun Joo Lee, Ju Youn Choi, Yong Mo Sung, Hyewon Park, Hyangshuk Rhim, Seongman Kang

Research output: Contribution to journalArticle

32 Citations (Scopus)


To identify proteins that interact with Huntingtin-interacting protein-2 (Hip-2), a ubiquitin-conjugating enzyme, a yeast two-hybrid screen system was used to isolate five positive clones. Sequence analyses showed that, with one exception, all Hip-2-interacting proteins contained the RING finger motifs. The interaction of Hip-2 with RNF2, one of the clones, was further confirmed through in vitro and in vivo experiments. Mutations in the RING domain of RNF2 prevented the clone from binding to Hip-2, an indication that the RING domain is the binding determinant. RNF2 showed a ubiquitin ligase (E3) activity in the presence of Hip-2, suggesting that a subset of RING finger proteins may have roles as E3s.

Original languageEnglish
Pages (from-to)61-64
Number of pages4
JournalFEBS Letters
Issue number1
Publication statusPublished - 2001 Aug 10



  • Huntingtin-interacting protein-2
  • RING motif
  • Ubiquitin ligase
  • Ubiquitin-conjugating enzyme
  • Yeast two-hybrid

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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