Journal
DATA IN BRIEF
Volume 4, Issue -, Pages 379-383Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.dib.2015.06.010
Keywords
Protein modification; Myristoylation; Tagging by substrate; Modification site
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Funding
- Deutsche Forschungsgemeinschaft [Br 4387/1-1]
- European Union [PIEF-GA-2011-299740, PIEF-GA-2010-273868]
- Imperial College London Institute of Chemical Biology EPSRC Centre for Doctoral Training studentship [EP/F500416/1]
- Biotechnology and Biological Sciences Research Council [978583] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/J021199/1] Funding Source: researchfish
- EPSRC [EP/J021199/1] Funding Source: UKRI
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Human cells (HEK 293, HeLa, MCF-7) and zebrafish embryos were metabolically ragged with an alkynyl myrisric acid probe, lysed with an SDS buffer and Lagged proreornes ligarecl ro multifunctional capture reagents via copper-caralyzed alkyne azide cycloadclirion (CuAAC). This allowed for affinity enrichment and high-confidence identification, by delivering direct MS/MS evidence for the modification site, of 87 and 61 co-translationally myristoylated proteins in human cells and zebrafish, respectively. The data have been deposited to ProteomeXchange Consortium (Vizcarno et al., 2014 Nat. Biotechnol., 32, 223-6) (PXD001863 and PXD001876) and are described in detail in Multifunctional reagents for quantitative proteome-wide analysis of protein mortification in human cells and dynamic protein lipiclation during vertebrate development by Broncel et al., Angew. Chern. Int. Ed. (C) 2015 The Authors. Published by Elsevier Inc.
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