Evidence map›Paper›PMID 31433507›Full record

ArticleThe EMBO journal2019

Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation.

Gemma Hardman, Simon Perkins, Philip J Brownridge, Christopher J Clarke, Dominic P Byrne, Amy E Campbell, Anton Kalyuzhnyy, Ashleigh Myall, Patrick A Eyers, Andrew R Jones and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
13.2field-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

76 citing papers in PubMed, 169 citations in OpenAlex.

  1. Review
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  13. Novel compound heterozygousExperimental and therapeutic medicine · 2025
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  15. Review
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  18. Pyro(phospho)mania.Nature chemical biology · 2024
    Article
  19. Article
  20. Article

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

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

11 authors at 1 institution in 1 country.

Gemma HardmanCentre for Proteome Research, Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Simon PerkinsDepartment of Comparative and Functional Genomics, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Philip J BrownridgeCentre for Proteome Research, Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Christopher J ClarkeCentre for Proteome Research, Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Dominic P ByrneDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Amy E CampbellCentre for Proteome Research, Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Anton KalyuzhnyyDepartment of Comparative and Functional Genomics, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Ashleigh MyallDepartment of Comparative and Functional Genomics, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Patrick A EyersDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.ORCID 0000-0002-9220-2966
Andrew R JonesDepartment of Comparative and Functional Genomics, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.
Claire E EyersCentre for Proteome Research, Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool, UK.ORCID 0000-0002-3223-5926
University of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H007113/1Biotechnology and Biological Sciences Research Council BB/N021703/1North West Cancer Research Fund (NWCR) CR1037North West Cancer Research Fund (NWCR) CR1088North West Cancer Research Fund (NWCR) CR1157UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC) BB/H007113/1UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC) BB/L005239/1UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC) BB/M012557/1UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC) BB/M023818/1UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC) BB/M025705/1UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC) BB/R02216X/1
6 · The paper itself

Abstract

Phosphorylation is a key regulator of protein function under (patho)physiological conditions, and defining site-specific phosphorylation is essential to understand basic and disease biology. In vertebrates, the investigative focus has primarily been on serine, threonine and tyrosine phosphorylation, but mounting evidence suggests that phosphorylation of other "non-canonical" amino acids also regulates critical aspects of cell biology. However, standard methods of phosphoprotein characterisation are largely unsuitable for the analysis of non-canonical phosphorylation due to their relative instability under acidic conditions and/or elevated temperature. Consequently, the complete landscape of phosphorylation remains unexplored. Here, we report an unbiased phosphopeptide enrichment strategy based on strong anion exchange (SAX) chromatography (UPAX), which permits identification of histidine (His), arginine (Arg), lysine (Lys), aspartate (Asp), glutamate (Glu) and cysteine (Cys) phosphorylation sites on human proteins by mass spectrometry-based phosphoproteomics. Remarkably, under basal conditions, and having accounted for false site localisation probabilities, the number of unique non-canonical phosphosites is approximately one-third of the number of observed canonical phosphosites. Our resource reveals the previously unappreciated diversity of protein phosphorylation in human cells, and opens up avenues for high-throughput exploration of non-canonical phosphorylation in all organisms.

Indexed as

AnionsChromatography, Ion ExchangeComputational BiologyHeLa CellsHumansMass SpectrometryPhosphopeptidesPhosphoproteinsPhosphorylationProteomeAnionsPhosphopeptidesPhosphoproteinsProteomemass spectrometrynon-canonical phosphorylationphosphohistidinephosphoproteomicsstrong anion exchange chromatography

Identifiers

PMID31433507
PMCPMC6826212
OpenAlexW2969694788

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.