PXD058797-1
PXD058797 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Affinity peptide ligands: New tools for chasing non-canonical N-phosphoproteome |
Description | Protein N-phosphorylation enrichment is faced with great difficulties due to the intrinsic instability of the N-P bond, which has seriously hindered its biological function unraveling. Current methods for N-phosphopeptides enrichment are challenging to fulfil high selectivity for all types of N-phosphorylation with minimum contamination. To address this, we reported the first affinity peptide functionalized magnetic beads for N-phosphopeptides enrichment under neutral aqueous solution. The affinity peptide, capable of binding the N-PO3 group specifically, was identified using phage display technology based on a delicate target. We demonstrated robust enrichment capacity of the peptide-modified magnetic beads across diverse biological samples, from prokaryotes to eukaryotes, as well as various organelles and tissues. Accordingly, 262 and 2307 N-phosphorylation sites were identified from E.coli and HeLa cells, which demonstrated the enhanced enrichment capability and greatly expanded the scale of N-phosphoproteome databases. Furthermore, we found that N-phosphorylation was highly enriched in the nucleus and played a vital role in regulating processes like DNA repair. Given the high efficiency and quantitative reproducibility of the method, it was found that N-phosphorylation level for kinases and proteins involved in regulation of metabolism and microtubules varied during the progression of Alzheimer's disease. Our work expands the tools library for N-phosphorylated proteome, and provides critical insights into the roles of N-phosphorylated proteins in physiology and pathology processes. |
HostingRepository | iProX |
AnnounceDate | 2024-12-12 |
AnnouncementXML | Submission_2024-12-11_20:35:23.936.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | He Wang |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Homo sapiens; NCBI TaxID: 9606; scientific name: Mus musculus; NCBI TaxID: 10090; |
ModificationList | No PTMs are included in the dataset |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2024-12-11 20:34:40 | ID requested | |
⏵ 1 | 2024-12-11 20:35:24 | announced |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Phage Display Technology, Affinity Peptide, N-phosphopeptides Enrichment , Neutral Aqueous Solution (or organelle) ,Quantitation Analysis |
Contact List
Lihua Zhang | |
---|---|
contact affiliation | Dalian Institute of Chemical Physics, Chinese Academy of Sciences |
contact email | lihuazhang@dicp.ac.cn |
lab head | |
He Wang | |
contact affiliation | Dalian Institute of Chemical Physics, Chinese Academy of Sciences |
contact email | crane_wanghe@dicp.ac.cn |
dataset submitter |
Full Dataset Link List
iProX dataset URI |