Abstract
Phosphorylation of proteins on tyrosine is crucially involved in signal transduction and mitogenesis and is regulated by both kinases and phosphatases. Recently, a number of soluble and transmembrane receptor-linked protein tyrosine phosphatases (PTPase) have been characterized. Among these is a 48.4-kDa PTPase encoded by a cDNA isolated from a T-lymphocyte library by low-stringency screening with probes derived from placental PTPase 1B. A human T-cell PTPase (PTPT) cDNA and somatic cell hybrids were used to assign a PTPT gene to conserved syntentic groups on human chromosome 18 and on mouse chromosome 18. Two unlinked sequences, one on human chromosome 1, were also detected.
Original language | English (US) |
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Pages (from-to) | 151-154 |
Number of pages | 4 |
Journal | Genomics |
Volume | 12 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1992 |
ASJC Scopus subject areas
- Genetics