Data on peptides identified by mass spectrometry analysis of in vitro DYRK1A-mediated phosphorylation sites on GLI1

Publication date: Available online 2 October 2017
Source:Data in Brief
Author(s): Ben K. Ehe, David R. Lamson, Michael Tarpley, Rob U. Onyenwoke, Lee M. Graves, Kevin P. Williams
The data presented in this article supports the accompanying research article "Identification of a DYRK1A-mediated phosphorylation site within the nuclear localization sequence of the hedgehog transcription factor GLI1" (Ehe et al., 2017) [1]. Although it has been demonstrated that DYRK1A (dual-specificity tyrosine-regulated kinase 1A) can phosphorylate the hedgehog pathway transcription factor GLI1 (GLIoma-associated oncogene homolog 1) the exact DYRK1A-mediated sites of phosphorylation on GLI1 were unknown. This article details the mass spectrometry methods and resulting dataset for the peptides identified from GLI1 when incubated with DYRK1A under varying conditions. The data includes details of sequence coverage and all phospho-peptides identified.



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