FEBS Letters
Volume 579, Issue 16 , Pages 3369-3375, 20 June 2005

A genome-wide analysis of sumoylation-related biological processes and functions in human nucleus

Edited by Takashi Gojobori

  • Fengfeng Zhou

      Affiliations

    • National High-Performance Computing Center at Hefei, University of Science and Technology of China, Hefei 230027, China
    • The authors contributed equally to this work.
  • ,
  • Yu Xue

      Affiliations

    • Laboratory of Cell Dynamics, University of Science and Technology of China, Hefei 230027, China
    • The authors contributed equally to this work.
  • ,
  • Hualei Lu

      Affiliations

    • Laboratory of Cell Dynamics, University of Science and Technology of China, Hefei 230027, China
  • ,
  • Guoliang Chen

      Affiliations

    • National High-Performance Computing Center at Hefei, University of Science and Technology of China, Hefei 230027, China
  • ,
  • Xuebiao Yao

      Affiliations

    • Laboratory of Cell Dynamics, University of Science and Technology of China, Hefei 230027, China
    • Department of Physiology, Morehouse School of Medicine, Atlanta, GA 30310, USA
    • Corresponding Author InformationCorresponding author. Fax: +86 551 3607141

Received 30 March 2005; accepted 26 April 2005. published online 23 May 2005.

Abstract 

Protein sumoylation is an important reversible post-translational modification of proteins in the nucleus, and it orchestrates a variety of the cellular processes. Genome-wide analysis of functional abundance and distribution of Small Ubiquitin-related MOdifier (SUMO) substrates may shed a light on how sumoylation is involved in nuclear biological processes and functions. Two interesting questions about sumoylation have emerged: (1) how many SUMO substrates exist in mammalian proteomes, such as human and mouse, (2) and what are their functions and how are they involved in a variety of biological processes? To address these two questions,we present an in silico genome-scale analysis for SUMO substrates in human. Based on the pattern recognition and phylogenetic conservation, we retrieved a list of 2683 potential SUMO substrates conserved in both human and mouse. Then, by functional enrichment analysis, we surveyed the over-represented GO terms and functional domains of them against the whole human proteome. Besides the consistence between our analyses and in vivo or in vitro work, the in silico predicted candidates also point to several potential roles of sumoylation, e.g., perception of sound. These potential SUMO substrates in human are of great value for further in vivo or in vitro experimental analysis.

Keywords: SUMO, Sumoylation, Transcription factor, Signal transduction, Perception of sound

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PII: S0014-5793(05)00566-1

doi:10.1016/j.febslet.2005.04.076

FEBS Letters
Volume 579, Issue 16 , Pages 3369-3375, 20 June 2005