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http://purl.uniprot.org/citations/1736296http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1736296http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1736296http://www.w3.org/2000/01/rdf-schema#comment"Tyrosine phosphorylation is controlled by the opposing actions of tyrosine kinases and phosphotyrosine phosphatases (PTPs). src homology 2 domains (SH2) are found in several types of signaling proteins, including some tyrosine kinases. These domains bind phosphotyrosyl proteins and thus help promote signal transduction. Using mixed oligonucleotide-directed polymerase chain reactions, two previously undescribed rat PTP cDNA fragments were generated. Through subsequent screening of rat megakaryocyte and human erythroleukemia libraries, we obtained a full-length coding sequence for one of these fragments. This cDNA, SH-PTP1, encodes a tyrosine phosphatase containing two highly conserved SH2 domains. SH-PTP1, with a 2.4-kilobase mRNA, a predicted open reading frame of 595 amino acids, and a structure suggesting a nontransmembrane protein, is expressed primarily in hematopoietic and epithelial cells. When expressed in Escherichia coli, SH-PTP1 possesses PTP activity. The structure of SH-PTP1 establishes an additional branch of the tyrosine phosphatase family and suggests mechanisms through which tyrosine phosphatases might participate in signal transduction pathways."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.org/dc/terms/identifier"doi:10.1073/pnas.89.3.1123"xsd:string
http://purl.uniprot.org/citations/1736296http://purl.org/dc/terms/identifier"doi:10.1073/pnas.89.3.1123"xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/author"Rosenberg R.D."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/author"Rosenberg R.D."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/author"Neel B.G."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/author"Neel B.G."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/author"Plutzky J."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/author"Plutzky J."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/pages"1123-1127"xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/pages"1123-1127"xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/title"Isolation of a src homology 2-containing tyrosine phosphatase."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/title"Isolation of a src homology 2-containing tyrosine phosphatase."xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/volume"89"xsd:string
http://purl.uniprot.org/citations/1736296http://purl.uniprot.org/core/volume"89"xsd:string
http://purl.uniprot.org/citations/1736296http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1736296
http://purl.uniprot.org/citations/1736296http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1736296
http://purl.uniprot.org/citations/1736296http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1736296
http://purl.uniprot.org/citations/1736296http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1736296