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Biochem Biophys Res Commun ; 278(3): 671-8, 2000 Nov 30.
Article in English | MEDLINE | ID: mdl-11095967

ABSTRACT

A human cDNA encoding a novel protein tyrosine phosphatase has been isolated. The phosphatase has unique features in its domain structure: a "Zn-hand" domain containing several SH3-binding motifs, a tyrosine phosphatase domain, a C-terminal PEST motif, and an N-terminal domain similar to yeast BRO1, an apoptosis-related mammalian AIP1 and to a RHO-binding protein, Rhophilin. The gene is located at chromosome 3p21.3, an area frequently deleted in many types of cancer, especially within the functionally defined narrow region. The gene may be a human homolog of the rat PTP-TD14 gene reported by others, which can suppress H-ras-mediated transformation. We identified a hemizygous missense mutation in a lung cancer cell line. Thus, the phosphatase gene may be a candidate for one of the tumor suppressor genes located on 3p21.3.


Subject(s)
Chromosomes, Human, Pair 3 , Loss of Heterozygosity , Protein Tyrosine Phosphatases/genetics , Amino Acid Sequence , Animals , Chromosome Mapping , Chromosomes, Artificial, Yeast , DNA, Complementary , Genetic Markers , Humans , Models, Molecular , Molecular Sequence Data , Polymerase Chain Reaction , Polymorphism, Single-Stranded Conformational , Protein Structure, Secondary , Protein Tyrosine Phosphatases/chemistry , Protein Tyrosine Phosphatases, Non-Receptor , Rats , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , Transfection , Tumor Cells, Cultured
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