Evidence map›Paper›PMID 35576205›Full record

ArticlePLoS biology2022

The structural context of posttranslational modifications at a proteome-wide scale.

Isabell Bludau, Sander Willems, Wen-Feng Zeng, Maximilian T Strauss, Fynn M Hansen, Maria C Tanzer, Ozge Karayel, Brenda A Schulman, Matthias Mann

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
9.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

77 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
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  8. Article
  9. Review
  10. Article
  11. Review
  12. Post-Translational Modifications in Animal Circadian Clocks.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. TheJournal of proteome research · 2026
    Article
  18. Review
  19. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  20. Review

17 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Isabell BludauDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Sander WillemsDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Wen-Feng ZengDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Maximilian T StraussProteomics Program, NNF Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.
Fynn M HansenDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Maria C TanzerDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Ozge KarayelDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Max Planck Institute of Biochemistry · DEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recent revolution in computational protein structure prediction provides folding models for entire proteomes, which can now be integrated with large-scale experimental data. Mass spectrometry (MS)-based proteomics has identified and quantified tens of thousands of posttranslational modifications (PTMs), most of them of uncertain functional relevance. In this study, we determine the structural context of these PTMs and investigate how this information can be leveraged to pinpoint potential regulatory sites. Our analysis uncovers global patterns of PTM occurrence across folded and intrinsically disordered regions. We found that this information can help to distinguish regulatory PTMs from those marking improperly folded proteins. Interestingly, the human proteome contains thousands of proteins that have large folded domains linked by short, disordered regions that are strongly enriched in regulatory phosphosites. These include well-known kinase activation loops that induce protein conformational changes upon phosphorylation. This regulatory mechanism appears to be widespread in kinases but also occurs in other protein families such as solute carriers. It is not limited to phosphorylation but includes ubiquitination and acetylation sites as well. Furthermore, we performed three-dimensional proximity analysis, which revealed examples of spatial coregulation of different PTM types and potential PTM crosstalk. To enable the community to build upon these first analyses, we provide tools for 3D visualization of proteomics data and PTMs as well as python libraries for data accession and processing.

Indexed as

Protein Processing, Post-TranslationalProteomeHumansMass SpectrometryPhosphorylationProteomicsProteome

Identifiers

PMID35576205
PMCPMC9135334
OpenAlexW4280512557

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.