⮝ Full datasets listing
PXD052682
PXD052682 is an original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Proteome-wide quantification of inositol pyrophosphate-protein interactions |
| Description | Inositol polyphosphates (InsPs) and inositol pyrophosphates (PP-InsPs) constitute a group of highly phosphorylated molecules that are involved in many cellular signaling processes. To characterize discrete signaling events of these structurally closely related molecules, a mass spectrometry approach was developed to derive apparent binding constants for these ligands on a proteome-wide scale. The method employed a series of chemically synthesized, biotinylated affinity reagents for inositol hexakisphosphate (InsP6), and the inositol pyrophosphates 1PP-InsP5, 5PP-InsP5 and 1,5(PP)2-InsP4 (also termed InsP8). Application of these affinity reagents at different concentrations, in combination with tandem mass tag (TMT) labeling, provided binding data for thousands of proteins from a mammalian cell lysate. Investigation of different enrichment conditions, where Mg2+ ions were either available or not, showcased a strong influence of Mg2+ on the protein binding capacities of PP-InsPs. Gene ontology analysis closely linked PP-InsPs-interacting proteins to transcriptional processes in the nucleus. Subsequent data analysis enabled a targeted search for protein pyrophosphorylation among PP-InsP interactors, and identified four new targets . The data presented here constitute a valuable resource for the community, and application of the method reported here to other biological contexts will enable the exploration of PP-InsP dependent signaling pathways across species. |
| HostingRepository | jPOST |
| AnnounceDate | 2026-04-27 |
| AnnouncementXML | Submission_2026-04-27_07:10:12.385.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Non peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Max Ruwolt |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
| ModificationList | S-carboxamidomethyl-L-cysteine; L-methionine sulfoxide; TMT6plex reporter+balance reagent N-acylated residue; TMT6plex reporter+balance reagent acylated N-terminal; alpha-amino acetylated residue; O-phospho-L-serine; O-phospho-L-threonine; O4'-phospho-L-tyrosine; pyrophospho; pyrophospho |
| Instrument | Orbitrap Fusion Lumos; Orbitrap Fusion ETD |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|---|---|---|
| 0 | 2024-05-29 12:32:29 | ID requested | |
| ⏵ 1 | 2026-04-27 07:10:12 | announced |
Publication List
| Dataset with its publication pending |
Keyword List
| submitter keyword: pyrophosphorylation, InsP, TMT, streptavidin pulldown |
Contact List
| Dorothea Fiedler | |
|---|---|
| lab head | |
| Max Ruwolt | |
| contact affiliation | Leibniz FMP |
| dataset submitter | |
Full Dataset Link List
| jPOST dataset URI |
| Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.jpostdb.org/JPST003145/ |




