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Data for identification of GPI-anchored peptides and ?-sites in cancer cell lines.

ABSTRACT: We present data obtained using a focused proteomics approach to identify the glycosylphosphatidylinositol (GPI)-anchored peptides in 19 human cancer cell lines. GPI-anchored proteins (GPI-APs), which localize to the outer leaflet of the membrane microdomains commonly referred to as lipid rafts play important roles in diverse biological processes. Due to the complex structure of the GPI-anchor moiety, it has been difficult to identify GPI-anchored peptide sequences on the proteomic scale by database searches using tools such as MASCOT. Here we provide data from 73 ?-sites derived from 49 GPI-APs in 19 human cancer cell lines. This article contains data related to the research article entitled "Identification of glycosylphosphatidylinositol-anchored proteins and ?-sites using TiO2-based affinity purification followed by hydrogen fluoride treatment" (Masuishi et al., 2016) [1].

SUBMITTER: Masuishi Y

PROVIDER: S-EPMC4838930 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines.

Masuishi Yusuke Y Kimura Yayoi Y Arakawa Noriaki N Hirano Hisashi H

Data in brief 20160408

We present data obtained using a focused proteomics approach to identify the glycosylphosphatidylinositol (GPI)-anchored peptides in 19 human cancer cell lines. GPI-anchored proteins (GPI-APs), which localize to the outer leaflet of the membrane microdomains commonly referred to as lipid rafts play important roles in diverse biological processes. Due to the complex structure of the GPI-anchor moiety, it has been difficult to identify GPI-anchored peptide sequences on the proteomic scale by datab ...[more]

PMID: 27141528

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