A unified nomenclature and amino acid numbering for human PTEN
Pulido, R.; Baker, S. J.; Barata, J. T.; Carracedo Álvarez, Ángel; Cid, V. J.; Chin-Sang, I. D.; Davé, V.; den Hertog, J.; Devreotes, P.; Eickholt, B. J.; Eng, C.; Furnari, F. B.; Georgescu, M. M.; Gericke, A.; Hopkins, B.; Jiang, X.; Lee, S. R.; Lösche, M.; Malaney, P.; Matias-Guiu, X.; Molina, M.; Pandolfi, P. P.; Parsons, R.; Pinton, P.; Rivas ?, Carmen; Rocha, R. M.; Rodríguez, M. S.; Ross, A. H.; Serrano, M.; Stambolic, V.; Stiles, B.; Suzuki, A.; Tan, S. S.; Tonks, N. K.; Trotman, L. C.; Wolff, N.; Woscholski, R.; Wu, H.; Leslie, N. R.
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Identificadores
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Data de publicación
2014Título da revista
Science Signaling
Tipo de contido
Artigo
MeSH
Amino Acid Sequence | Amino Acids | Codon, Initiator | Databases, Protein | Humans | PTEN Phosphohydrolase | Terminology as TopicResumo
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.