Evidence map›Paper›PMID 24782567›Full record

ArticleScience signaling2014

Proteome-wide identification of SUMO2 modification sites.

Triin Tammsalu, Ivan Matic, Ellis G Jaffray, Adel F M Ibrahim, Michael H Tatham, Ronald T Hay

Abstract read
In one paragraph

Article in Science signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed
14.0field-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

136 citing papers in PubMed, 205 citations in OpenAlex.

  1. Assays to Study SUMOylation of RNA Helicase DHX9.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Article
  3. Article
  4. A Landscape Analysis of Human SUMOylation.Molecular & cellular proteomics : MCP · 2026
    Article
  5. Article
  6. Induced opening of conformational switch I in GTP-bound Ran GTPase.Protein science : a publication of the Protein Society · 2026
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

76 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

6 authors at 2 institutions in 1 country.

Triin Tammsalu *Centre for Gene Regulation and Expression, University of Dundee, Sir James Black Centre, Dow Street, Dundee DD1 5EH. UK.
Ivan Matic *Centre for Gene Regulation and Expression, University of Dundee, Sir James Black Centre, Dow Street, Dundee DD1 5EH. UK.
Ellis G JaffrayCentre for Gene Regulation and Expression, University of Dundee, Sir James Black Centre, Dow Street, Dundee DD1 5EH. UK.
Adel F M IbrahimMRC Protein Phosphorylation and Ubiquitination Unit, College of Life Sciences, University of Dundee, Sir James Black Centre, Dow Street, Dundee DD1 5EH. UK.
Michael H TathamCentre for Gene Regulation and Expression, University of Dundee, Sir James Black Centre, Dow Street, Dundee DD1 5EH. UK.
Ronald T HayCentre for Gene Regulation and Expression, University of Dundee, Sir James Black Centre, Dow Street, Dundee DD1 5EH. UK.
University of Dundee · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Cancer Research UK 13067Cancer Research UK A13067Wellcome Trust 088957Wellcome Trust 097945Wellcome Trust 098391
6 · The paper itself

Abstract

Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMO-specific enzymes conjugate SUMOs to lysine residues in target proteins. Although proteomic studies have identified hundreds of sumoylated substrates, methods to identify the modified lysines on a proteomic scale are lacking. We developed a method that enabled proteome-wide identification of sumoylated lysines that involves the expression of polyhistidine (6His)-tagged SUMO2 with Thr(90) mutated to Lys. Endoproteinase cleavage with Lys-C of 6His-SUMO2(T90K)-modified proteins from human cell lysates produced a diGly remnant on SUMO2(T90K)-conjugated lysines, enabling immunoprecipitation of SUMO2(T90K)-modified peptides and producing a unique mass-to-charge signature. Mass spectrometry analysis of SUMO-enriched peptides revealed more than 1000 sumoylated lysines in 539 proteins, including many functionally related proteins involved in cell cycle, transcription, and DNA repair. Not only can this strategy be used to study the dynamics of sumoylation and other potentially similar posttranslational modifications, but also, these data provide an unprecedented resource for future research on the role of sumoylation in cellular physiology and disease.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceBlotting, WesternHEK293 CellsHistidineHumansLysineMass SpectrometryMolecular Sequence DataMutationPeptidesProteomeProteomicsSequence Homology, Amino AcidSignal TransductionSmall Ubiquitin-Related Modifier ProteinsHistidineLysinePeptidespolyhistidineProteomeSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanThreonine

Identifiers

PMID24782567
PMCPMC4051997
OpenAlexW2156475142

What OpenQuestion holds

Textmetadata
LicenceTDM
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.