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

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 Lett

journal_title

FEBS letters

authors

Adachi M,Sekiya M,Miyachi T,Matsuno K,Hinoda Y,Imai K,Yachi A

doi

10.1016/0014-5793(92)81500-l

keywords:

subject

Has Abstract

pub_date

1992-12-21 00:00:00

pages

335-9

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)81500-L

journal_volume

314

pub_type

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