PXD043476 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | msqrob2PTM: differential abundance and differential usage analysis of MS-based proteomics data at the post-translational modification and peptidoform level |
Description | In the era of open-modification search engines, more post-translational modifications than ever can be detected by LC-MS/MS-based proteomics. This development can switch proteomics research into a higher gear, as PTMs are key in many cellular pathways important in cell proliferation, migration, metastasis and ageing. However, despite these advances in modification identification, statistical methods for PTM-level quantification and differential analysis have yet to catch up. This absence can partly be explained by the inherently low abundance of many PTMs and the confounding of PTM intensities with its parent protein abundance. Therefore, we have developed msqrob2PTM, a new workflow in the msqrob2 universe capable of differential abundance analysis at the PTM, and at the peptidoform level. The latter is important for validating significantly found PTMs. Indeed, as our method can deal with multiple PTMs per peptidoform, there is a possibility that significant PTMs stem from one significant peptidoform carrying another PTM, hinting that it might the other PTM driving the perceived differential abundance. Our workflows can flag both Differential Peptidoform (PTM) Abundance (DPA) and Differential Peptidoform (PTM) Usage (DPU). This enables a distinction between direct assessment of differential abundance of peptidoforms (DPA), and differences in the relative usage of peptidoforms corrected for corresponding protein abundances (DPU). For DPA, we directly model the log2-transformed peptidoform (PTM) intensities, while for DPU, we correct for parent protein abundance by an intermediate normalisation step which calculates the log2-ratio of the peptidoform (PTM) intensities to their summarized parent protein intensities. We demonstrated the utility and performance of msqrob2PTM by applying it on datasets with known ground truth, as well as on biological PTM-rich datasets. Our results show that msqrob2PTM is on par with, or surpassing the performance of, the current state-of-the-art method, MSstatsPTM. Moreover, msqrob2PTM is currently unique in providing output at the peptidoform level. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_06:45:58.940.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Marie GEBELIN |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | phosphorylated residue; acetylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive HF-X; Q Exactive Plus |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-07-03 02:40:52 | ID requested | |
1 | 2024-06-16 03:49:24 | announced | |
⏵ 2 | 2024-10-22 06:46:01 | announced | 2024-10-22: Updated project metadata. |
Publication List
Demeulemeester N, G, é, belin M, Caldi Gomes L, Lingor P, Carapito C, Martens L, Clement L, msqrob2PTM: Differential Abundance and Differential Usage Analysis of MS-Based Proteomics Data at the Posttranslational Modification and Peptidoform Level. Mol Cell Proteomics, 23(2):100708(2024) [pubmed] |
10.1016/j.mcpro.2023.100708; |
Keyword List
submitter keyword: msqrob2PTM, PTM, msqrob, peptidoform |
Contact List
Christine Carapito |
contact affiliation | Laboratoire de Spectrométrie de Masse BioOrganique, IPHC UMR 7178, CNRS, Université de Strasbourg |
contact email | ccarapito@unistra.fr |
lab head | |
Marie GEBELIN |
contact affiliation | Laboratoire de Spectometrie de Mass Bio-Organique, IPHC, CNRS |
contact email | marie.gebelin@etu.unistra.fr |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD043476
- Label: PRIDE project
- Name: msqrob2PTM: differential abundance and differential usage analysis of MS-based proteomics data at the post-translational modification and peptidoform level