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http://purl.uniprot.org/citations/9038134http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9038134http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9038134http://www.w3.org/2000/01/rdf-schema#comment"Activation of resting T lymphocytes is initiated by rapid but transient tyrosine phosphorylation of a number of cellular proteins. Several protein tyrosine kinases and protein tyrosine phosphatases are known to be important for this response. Here we report that normal T lymphocytes express the B isoform of low molecular weight protein tyrosine phosphatase B (LMPTP-B). The cDNA was cloned from Jurkat T cells, and an antiserum was raised against it. LMPTP immunoprecipitated from resting Jurkat T cells was found to be tyrosine phosphorylated. On stimulation of the cells through their T cell antigen receptor, the phosphotyrosine content of LMPTP-B declined rapidly. In co-transfected COS cells, Lck and Fyn caused phosphorylation of LMPTP, whereas Csk, Zap, and Jak2 did not. Most of the phosphate was located at Tyr-131, and some was also located at Tyr-132. Incubation of wild-type LMPTP with Lck and adenosine 5'-O-(thiotriphosphate) caused a 2-fold increase in the activity of LMPTP. Site-directed mutagenesis showed that Tyr-131 is important for the catalytic activity of LMPTP, and that thiophosphorylation of Tyr-131, and to a lesser degree Tyr-132, is responsible for the activation."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.9.5371"xsd:string
http://purl.uniprot.org/citations/9038134http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.9.5371"xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Williams S."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Williams S."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Mustelin T."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Mustelin T."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Couture C."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Couture C."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Tailor P."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Tailor P."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Gilman J."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/author"Gilman J."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/pages"5371-5374"xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/pages"5371-5374"xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/title"Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/title"Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132."xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9038134http://purl.uniprot.org/core/volume"272"xsd:string