A unified nomenclature and amino acid numbering for human PTEN

Rafael Pulido*, Suzanne J. Baker, Joao T. Barata, Arkaitz Carracedo, Victor J. Cid, Ian D. Chin-Sang, Vrushank Davé, Jeroen Den Hertog, Peter Devreotes, Britta J. Eickholt, Charis Eng, Frank B. Furnari, Maria Magdalena Georgescu, Arne Gericke, Benjamin Hopkins, Xeujun Jiang, Seung Rock Lee, Mathias Lösche, Prerna Malaney, Xavier Matias-GuiuMaría Molina, Pier Paolo Pandolfi, Ramon Parsons, Paolo Pinton, Carmen Rivas, Rafael M. Rocha, Manuel S. Rodríguez, Alonzo H. Ross, Manuel Serrano, Vuk Stambolic, Bangyan Stiles, Akira Suzuki, Seong Seng Tan, Nicholas K. Tonks, Lloyd C. Trotman, Nicolas Wolff, Rudiger Woscholski, Hong Wu, Nicholas R. Leslie

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)
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The tumor suppressor PTEN is a major brake for cell transformation, mainly due to its phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] phosphatase activity that directly counteracts the oncogenicity of phosphoinositide 3-kinase (PI3K). PTEN mutations are frequent in tumors and in the germ line of patients with tumor predisposition or with neurological or cognitive disorders, which makes the PTEN gene and protein a major focus of interest in current biomedical research. After almost two decades of intense investigation on the 403-residue-long PTEN protein, a previously uncharacterized form of PTEN has been discovered that contains 173 amino-terminal extra amino acids, as a result of an alternate translation initiation site. To facilitate research in the field and to avoid ambiguities in the naming and identification of PTEN amino acids from publications and databases, we propose here a unifying nomenclature and amino acid numbering for this longer form of PTEN.

Original languageEnglish
Article numberpe15
JournalScience Signaling
Issue number332
Publication statusPublished - 1 Jul 2014

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology


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