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Molecular cloning of a novel protein‐tyrosine phosphatase SH‐PTP3 with sequence similarity to the src ‐homology region 2
Author(s) -
Adachi Masaaki,
Sekiya Masuo,
Miyachi Toshiki,
Matsuno Keiki,
Hinoda Yuji,
Imai Kohzoh,
Yachi Akira
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81500-l
Subject(s) - homology (biology) , protein tyrosine phosphatase , proto oncogene tyrosine protein kinase src , sequence homology , cloning (programming) , molecular cloning , nucleic acid sequence , peptide sequence , microbiology and biotechnology , biology , sequence (biology) , genetics , tyrosine , computational biology , biochemistry , amino acid , dna , gene , phosphorylation , computer science , programming language
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 ∼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 tarpets' enzyme activity.