Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Adachi M,Sekiya M,Miyachi T,Matsuno K,Hinoda Y,Imai K,Yachi Adoi
10.1016/0014-5793(92)81500-lkeywords:
subject
Has Abstractpub_date
1992-12-21 00:00:00pages
335-9issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(92)81500-Ljournal_volume
314pub_type
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