Molecular cloning of a novel protein‐tyrosine phosphatase SH‐PTP3 with sequence similarity to the src‐homology region 2

作者：Masaaki Adachi, Masuo Sekiya, Toshiki Miyachi, Keiki Matsuno, Yuji Hinoda, Kohzoh Imai, Akira Yachi · 发表于：FEBS Letters · 年份：1992 · DOI：10.1016/0014-5793(92)81500-l · 被引用次数：94 · 研究领域：Protein Tyrosine Phosphatases、RNA modifications and cancer、ATP Synthase and ATPases Research

Protein-tyrosine phosphorylation and dephosphorylation are directly associated with cellular growth, signal transduction, and neoplastic transformation. Here we report the isolation of a complementary DNA (cDNA) clone encoding a novel protein-tyrosine phosphatase (PTP) from a human T cell PEER cDNA library. The predicted open reading frame encodes a approximately 68-kDa protein composed of 593 amino acids which contains two src-homology region 2's (SH2 domains) at the N terminus; this PTP is designated as SH-PTP3. Northern blot analysis revealed that SH-PTP3 mRNA was expressed throughout many tissues and the transcriptional size was consistent at about 6.0 kb. As with other SH2 domains in src-family kinases, the SH2 domains of SH-PTP3 may play a crucial role in interactions with tyrosine phosphorylated signaling proteins, including itself and protein tyrosine kinases (PTKs), to regulate targets' enzyme activity.