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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAHn_LAEbken_jPIbNb4TiQiFF1WhKEI5KzORpJVIiX0k#_10 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAHn_LAEbken_jPIbNb4TiQiFF1WhKEI5KzORpJVIiX0k#_10 http://www.w3.org/2000/01/rdf-schema#label Selventa http://www.tkuhn.ch/bel2nanopub/RAHn_LAEbken_jPIbNb4TiQiFF1WhKEI5KzORpJVIiX0k#_9 http://www.w3.org/ns/prov#value Stat5 proteins activated by IL-2. The phosphorylated tyrosines on IL-2Rbeta can then serve as docking sites for signaling molecules that otherwise cannot associate with IL-2Rbeta, including the adaptor protein Shc, Stat5a, and Stat5b (Figure 2). For example, only phosphorylated (but not non-phosphorylated) peptides spanning either Tyr-392 or Tyr-510 of IL-2Rbeta can efficiently compete with IL-2-induced Stat5 DNA binding to a GAS motif IL-2-mediated hetero-dimerization of its receptor triggers a rapid increase in the recruitment of Jak3 and activation of both Jak1 and Jak3 (Johnston et al., 1994; Witthuhn et al., 1994). These kinases phosphorylate the receptor as well as each other, and activate other signaling molecules associated with the receptor. 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