RNF13: an emerging RING finger ubiquitin ligase important in cell proliferation

FEBS J. 2011 Jan;278(1):78-84. doi: 10.1111/j.1742-4658.2010.07925.x. Epub 2010 Nov 16.


Protein ubiquitination mediated by ubiquitin ligases plays a very important role in a wide spectrum of biological processes including development and disease pathogenesis. RING finger protein 13 (RNF13) is a recently identified ubiquitin ligase which contains an N-terminal protease-associated domain and a C-terminal RING finger domain separated by a transmembrane region. RNF13 is an evolutionarily conserved protein. Most interestingly, RNF13 expression is developmentally regulated during myogenesis and is upregulated in various human tumors. These data suggest that RNF13, acting as an ubiquitin ligase, might have profound biological functions during development and disease. This minireview summarizes recent work on RNF13 functions related to cell proliferation, differentiation and cancer development.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Cell Proliferation
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Molecular Sequence Data
  • RING Finger Domains
  • Sequence Alignment
  • Ubiquitin-Protein Ligases / metabolism*


  • RNF13 protein, human
  • Ubiquitin-Protein Ligases