Evidence map›Paper›PMID 26572964›Full record

ArticleMolecular & cellular proteomics : MCP2016

Uncovering Phosphorylation-Based Specificities through Functional Interaction Networks.

Omar Wagih, Naoyuki Sugiyama, Yasushi Ishihama, Pedro Beltrao

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 3 pooled it
–field-weighted citation impact
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

49 citing papers in PubMed, 3 syntheses or guidelines pooled it.

  1. An AI-Ready Phosphorylation Meta-Analysis forJournal of proteome research · 2026
    Pooled it
  2. Phosphorylation in theJournal of proteome research · 2024
    Pooled it
  3. Pooled it
  4. Mapping the proteome landscape inPlant signaling & behavior · 2026
    Article
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  7. A Landscape Analysis of Human SUMOylation.Molecular & cellular proteomics : MCP · 2026
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  12. Article
  13. Searching for Sulfotyrosines (sY) in a HA(pY)STACK.Journal of proteome research · 2025
    Article
  14. Article
  15. Article
  16. Nphos: Database and Predictor of Protein N-phosphorylation.Genomics, proteomics & bioinformatics · 2024
    Article
  17. Article
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Omar WagihFrom the ‡European Bioinformatics Institute, European Molecular Biology Laboratory, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SD;
Naoyuki Sugiyama§Graduate School of Pharmaceutical Sciences, Kyoto University, 46-29 Yoshidashimoadachi-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Yasushi Ishihama§Graduate School of Pharmaceutical Sciences, Kyoto University, 46-29 Yoshidashimoadachi-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Pedro BeltraoFrom the ‡European Bioinformatics Institute, European Molecular Biology Laboratory, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SD; pbeltrao@ebi.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinases are an important class of enzymes involved in the phosphorylation of their targets, which regulate key cellular processes and are typically mediated by a specificity for certain residues around the target phospho-acceptor residue. While efforts have been made to identify such specificities, only ∼30% of human kinases have a significant number of known binding sites. We describe a computational method that utilizes functional interaction data and phosphorylation data to predict specificities of kinases. We applied this method to human kinases to predict substrate preferences for 57% of all known kinases and show that we are able to reconstruct well-known specificities. We used an in vitro mass spectrometry approach to validate four understudied kinases and show that predicted models closely resemble true specificities. We show that this method can be applied to different organisms and can be extended to other phospho-recognition domains. Applying this approach to different types of posttranslational modifications (PTMs) and binding domains could uncover specificities of understudied PTM recognition domains and provide significant insight into the mechanisms of signaling networks.

Indexed as

Protein Interaction MapsAmino Acid SequenceAnimalsBinding SitesComputational BiologyHeLa CellsHumansMicePhosphorylationProtein KinasesProtein Processing, Post-TranslationalProteomeProteomicsReproducibility of ResultsSignal TransductionSubstrate SpecificityProtein KinasesProteome

Identifiers

PMID26572964
PMCPMC4762521

What OpenQuestion holds

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Registered trials

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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.