关于白细胞介素（IL）-2和IL-15依赖的IL-2受体（IL-2R）及IL-2Rγ复合物变化的数据。
Data on interleukin (IL)-2- and IL-15-dependent changes in IL-2R and IL-2Rγ complexes.
作者信息
Osinalde Nerea, Sánchez-Quiles Virginia, Blagoev Blagoy, Kratchmarova Irina
机构信息
Department of Biochemistry and Molecular Biology, University of the Basque Country UPV/EHU, 01006 Vitoria-Gasteiz, Spain.
Molecular Oncology Group, UMR 144 CNRS, Curie Institute, 26, rue d'Ulm, 75248 Paris, France.
出版信息
Data Brief. 2017 Mar 2;11:499-506. doi: 10.1016/j.dib.2017.02.030. eCollection 2017 Apr.
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.
我们提供了详细的数据集，这些数据集来自于我们对在用白细胞介素-2（IL-2）或白细胞介素-15（IL-15）刺激的T细胞中与IL-2Rβ和IL-2Rγ相关的蛋白质的分析，与静息T细胞相比，这些蛋白质是通过基于稳定同位素标记氨基酸的细胞培养（SILAC）的定量蛋白质组学鉴定出来的。我们还包括了关于在IL-2Rβ和IL-2Rγ中观察到的位点特异性磷酸化事件的定量数据。此外，我们提供的结果表明了其中四个位点特异性磷酸化的特定蛋白质招募能力。本文中描述的蛋白质组学和磷酸蛋白质组学数据与一篇题为“白细胞介素（IL）-2和IL-15激活的T淋巴细胞中受体相关蛋白复合物组装的表征”的研究文章相关（奥西纳德等人，2016 [1]）。质谱数据已存入蛋白质组交换联盟，标识符为PXD002386。
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