Proteomics

Dataset Information

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Systematic characterization of 21 post-translational modification using synthetic peptides

ABSTRACT: The data presented in this study in the - context of the ProteoemTools project - is based on the synthesis of about 5000 synthetic peptides carrying 21 different post-translational modifications to systematically characterize their chromatographic and mass spectrometric properties using multimodal LC-MS/MS.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Daniel Zolg  

LAB HEAD: Bernhard Kuster

PROVIDER: PXD009449 | Pride | 2018-06-04

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
02330a_BA4_4087_1_PTM_TrainKit_Ymod_Phospho_200fmol_2xIT_2xHCD_R1.raw Raw
02330a_BA4_4087_1_PTM_TrainKit_Ymod_Phospho_200fmol_3xHCD_R1.raw Raw
02330a_BA4_4087_1_PTM_TrainKit_Ymod_Phospho_200fmol_ETD_R1.raw Raw
02330a_BA4_4087_1_PTM_TrainKit_Ymod_Phospho_200fmol_survey_R1.raw Raw
02330a_GA1_3990_01_PTM_TrainKit_Rmod_Unmod_200fmol_2xIT_2xHCD_R1.raw Raw
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Publications

ProteomeTools: Systematic Characterization of 21 Post-translational Protein Modifications by Liquid Chromatography Tandem Mass Spectrometry (LC-MS/MS) Using Synthetic Peptides.

Zolg Daniel Paul DP   Wilhelm Mathias M   Schmidt Tobias T   Médard Guillaume G   Zerweck Johannes J   Knaute Tobias T   Wenschuh Holger H   Reimer Ulf U   Schnatbaum Karsten K   Kuster Bernhard B  

Molecular & cellular proteomics : MCP 20180529 9

The analysis of the post-translational modification (PTM) state of proteins using mass spectrometry-based bottom-up proteomic workflows has evolved into a powerful tool for the study of cellular regulatory events that are not directly encoded at the genome level. Besides frequently detected modifications such as phosphorylation, acetylation and ubiquitination, many low abundant or less frequently detected PTMs are known or postulated to serve important regulatory functions. To more broadly under  ...[more]

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