title: Data detailing the platelet acetyl-lysine proteome.
abstract: Here we detail proteomics data that describe the acetyl-lysine proteome of blood platelets (Aslan et al., 2015 [1]). An affinity purification - mass spectrometry (AP-MS) approach was used to identify proteins modified by Nε-lysine acetylation in quiescent, washed human platelets. The data provide insights into potential regulatory mechanisms of platelet function mediated by protein lysine acetylation. Additionally, as platelets are anucleate and lack histone proteins, they offer a unique and valuable system to study the regulation of cytosolic proteins by lysine acetylation. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (Vizcaino et al., 2014 [2]) via with PRIDE partner repository with the dataset identifier PXD002332.
authors.affiliation: Departments of Biomedical Engineering, Portland, OR 97239, USA; Cell and Developmental Biology, Portland, OR 97239, USA; Knight Cardiovascular Institute, Portland, OR 97239, USA.
authors.forename: Joseph E
authors.initials: JE
authors.lastname: Aslan
authors.affiliation: Proteomics Shared Resource, Oregon Health & Science University, Portland, OR 97239, USA.
authors.forename: Larry L
authors.initials: LL
authors.lastname: David
authors.affiliation: Departments of Biomedical Engineering, Portland, OR 97239, USA; Cell and Developmental Biology, Portland, OR 97239, USA; Division of Hematology & Medical Oncology School of Medicine, Portland, OR 97239, USA.
authors.forename: Owen J T
authors.initials: OJ
authors.lastname: McCarty
keywords: Acetylation; Hemostasis; Platelets; Proteomics