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Data Brief. 2017 Mar 02;11:499-506. doi: 10.1016/j.dib.2017.02.030. eCollection 2017 Apr.

Data on interleukin (IL)-2- and IL-15-dependent changes in IL-2R.

Data in brief

Nerea Osinalde, Virginia Sánchez-Quiles, Blagoy Blagoev, Irina Kratchmarova

Affiliations

  1. Department of Biochemistry and Molecular Biology, University of the Basque Country UPV/EHU, 01006 Vitoria-Gasteiz, Spain.
  2. Molecular Oncology Group, UMR 144 CNRS, Curie Institute, 26, rue d'Ulm, 75248 Paris, France.
  3. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark.

PMID: 28331895 PMCID: PMC5345956 DOI: 10.1016/j.dib.2017.02.030

Abstract

We provide detailed datasets from our analysis of the proteins that associate with IL-2Rβ and IL-2Rγ in T-cells stimulated with IL-2 or IL-15 compared with resting T-cells, as identified by SILAC-based quantitative proteomics. We also include quantitative data regarding site-specific phosphorylation events observed both in IL-2Rβ and IL-2Rγ. Moreover, we provide results demonstrating the specific protein recruitment capacity of four of those site-specific phosphorylations. The proteomics and phosphoproteomics data described in this article is associated with a research article entitled "Characterization of receptor-associated protein complex assembly in Interleukin (IL)-2- and IL-15-activated T-lymphocytes" (Osinalde et al., 2016 [1]). The mass spectrometry data have been deposited to the ProteomeEXchange Constorium with the identifier PXD002386.

Keywords: Cell signaling; Interactome; Interleukin; Phosphotyrosine; SILAC; T-lymphocytes

References

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