Data on peptides identified by mass spectrometry analysis of in vitro DYRK1A-mediated phosphorylation sites on GLI1
Ben K. Ehe,
David R. Lamson,
Michael Tarpley,
Rob U. Onyenwoke,
Lee M. Graves,
Kevin P. Williams
Affiliations
Ben K. Ehe
Biomanufacturing Research Institute and Technology Enterprise, North Carolina Central University, Durham, NC 27707, USA
David R. Lamson
Biomanufacturing Research Institute and Technology Enterprise, North Carolina Central University, Durham, NC 27707, USA
Michael Tarpley
Biomanufacturing Research Institute and Technology Enterprise, North Carolina Central University, Durham, NC 27707, USA
Rob U. Onyenwoke
Biomanufacturing Research Institute and Technology Enterprise, North Carolina Central University, Durham, NC 27707, USA; Department of Pharmaceutical Sciences, North Carolina Central University, Durham, NC 27707, USA
Lee M. Graves
Department of Pharmacology, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA
Kevin P. Williams
Biomanufacturing Research Institute and Technology Enterprise, North Carolina Central University, Durham, NC 27707, USA; Department of Pharmaceutical Sciences, North Carolina Central University, Durham, NC 27707, USA; Corresponding author.
The data presented in this article support the accompanying research article âIdentification of a DYRK1A-mediated phosphorylation site within the nuclear localization sequence of the hedgehog transcription factor GLI1â (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) and promote its nuclear localization, the DYRK1A-mediated sites of phosphorylation on GLI1 involved were not fully known. 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 include details of sequence coverage and all phospho-peptides identified.
