| http://purl.uniprot.org/citations/12270932 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12270932 | http://www.w3.org/2000/01/rdf-schema#comment | "Signal transducer and activator of transcription (STAT) proteins are both tyrosine- and serine-phosphorylated, mediating signal transduction and gene regulation. Following gene regulation, STAT activity in the nucleus is then terminated by a nuclear protein phosphatase(s), which remains unidentified. Using novel antibody arrays to screen the Stat1-specific protein phosphatase(s), we identified a SHP-2-Stat1 interaction in the A431 cell nucleus. SHP-2 and Stat1 nuclear localization and their association in response to either epidermal growth factor or interferon-gamma (IFNgamma) were confirmed by immunofluorescent staining and affinity precipitation assays. The SHP-2 C-terminal region containing protein-tyrosine phosphatase activity interacted with the C-terminal SH2 transcriptional activation domain of Stat1. In SHP-2-/-mouse fibroblast cells, Stat1 phosphorylation at both the tyrosine residue Tyr(701) and the serine residue Ser(727) by IFNgamma was enhanced and prolonged. Consistently, purified GST-SHP-2 dephosphorylated Stat1 at both tyrosine and serine residues when immunoprecipitated phospho-Stat1 or a peptide corresponding to the sequence surrounding Tyr(P)(701) or Ser(P)(727) of Stat1 was used as the substrate. Overexpression of SHP-2 in 293T cells inhibited IFNgamma-dependent Stat1 phosphorylation and suppressed Stat1-dependent induction of luciferase activity. Our findings demonstrate that SHP-2 is a dual-specificity protein phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues and plays an important role in modulating STAT function in gene regulation."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m207536200"xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Campbell A.G."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Wang X.D."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Chin Y.E."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Chung A.S."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Hong Y.K."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Feng G.S."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Dragoi A.M."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Han Z.Y."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Ling M.Y."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/author | "Wu T.R."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/pages | "47572-47580"xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/title | "SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei."xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/12270932 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12270932 |
| http://purl.uniprot.org/citations/12270932 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12270932 |
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