| http://purl.uniprot.org/citations/10602027 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10602027 | http://www.w3.org/2000/01/rdf-schema#comment | "Upon IL-2 stimulation of T lymphocytes, the IL-2 receptor (IL-2R) becomes phosphorylated on specific tyrosine residues which serve as docking sites for proteins containing SH2 or phosphotyrosine binding domains. To study the interaction of the IL-2Rbeta chain with Shc and STAT proteins, subdomains of the IL-2Rbeta chain were expressed as tyrosine-phosphorylated glutathione S-transferase fusion proteins and used to pull-down interacting proteins from Kit 225 cell lysates. These experiments provide direct biochemical evidence that binding to the IL-2R of the adaptor protein Shc requires phosphorylation of Tyr-338 in the IL-2Rbeta acidic subdomain. In addition, we report that STAT proteins that are activated by IL-2, i.e. STAT1, STAT3 and STAT5, indeed associate with the IL-2Rbeta chain. Both the A and B isoforms of STAT5 were found to associate with Tyr-510 of the IL-2Rbeta C-terminal region, depending on its phosphorylation. In contrast, STAT1 and STAT3 associated with the IL-2Rbeta chain through its acidic subdomain. These results indicate that the interaction between IL-2Rbeta and STAT1 or 3 does not require either phosphorylation of the receptor or even the presence of tyrosine residues of IL-2Rbeta. Thus, the IL-2R recruits STAT proteins through different modes of interaction."xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://purl.org/dc/terms/identifier | "doi:10.1002/1521-4141(200001)30:1<59::aid-immu59>3.0.co;2-1"xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://purl.uniprot.org/core/author | "Bertoglio J."xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://purl.uniprot.org/core/author | "Bouvier G."xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://purl.uniprot.org/core/author | "Delespine-Carmagnat M."xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10602027 | http://purl.uniprot.org/core/name | "Eur J Immunol"xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://purl.uniprot.org/core/pages | "59-68"xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://purl.uniprot.org/core/title | "Association of STAT1, STAT3 and STAT5 proteins with the IL-2 receptor involves different subdomains of the IL-2 receptor beta chain."xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://purl.uniprot.org/core/volume | "30"xsd:string |
| http://purl.uniprot.org/citations/10602027 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10602027 |
| http://purl.uniprot.org/citations/10602027 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10602027 |
| http://purl.uniprot.org/uniprot/#_P14784-mappedCitation-10602027 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10602027 |
| http://purl.uniprot.org/uniprot/#_P51692-mappedCitation-10602027 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10602027 |
| http://purl.uniprot.org/uniprot/#_P42229-mappedCitation-10602027 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10602027 |
| http://purl.uniprot.org/uniprot/P42229 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10602027 |
| http://purl.uniprot.org/uniprot/P14784 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10602027 |
| http://purl.uniprot.org/uniprot/P51692 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10602027 |