Assignment of tyrosine-specific T-cell phosphatase to conserved syntenic groups on human chromosome 18 and mouse chromosome 18.
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.
Sakaguchi
A Y
AY
Department of Cellular and Structural Biology, University of Texas Health Science Center, San Antonio 78284.
Sylvia
V L
VL
Martinez
L
L
Smith
E A
EA
Han
E S
ES
Lalley
P A
PA
Shows
T B
TB
Choudhury
G G
GG
D000818:Animals; D002874:Chromosome Mapping; D002887:Chromosomes, Human, Pair 18; D006801:Humans; D006822:Hybrid Cells; D051379:Mice; D009693:Nucleic Acid Hybridization; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases / Q000235:genetics*; D013601:T-Lymphocytes / Q000201:enzymology*
D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases