Evidence map›Paper›PMID 23749301›Full record

ArticleNature methods2013

Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.

Danielle L Swaney, Pedro Beltrao, Lea Starita, Ailan Guo, John Rush, Stanley Fields, Nevan J Krogan, Judit Villén

Open access · greenAbstract read
In one paragraph

Article in Nature methods, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 357 papers.

0numbers the graph read from it
0cells of the map it votes in
357citing papers in PubMed
17.0field-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

357 citing papers in PubMed, 620 citations in OpenAlex.

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  7. Mutational analyses of an instability domain reveal its conserved role in the regulation of class-B ARF levels inProceedings of the National Academy of Sciences of the United States of America · 2026
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  13. Aberrant cohesin function inbioRxiv : the preprint server for biology · 2025
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297 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 5 institutions in 2 countries.

Danielle L SwaneyDepartment of Genome Sciences, University of Washington, Seattle, Washington, USA.
Pedro Beltrao
Lea Starita
Ailan Guo
John Rush
Stanley Fields
Nevan J Krogan
Judit Villén
University of Washington · USCell Signaling Technology (United States) · USEuropean Bioinformatics Institute · GBHoward Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRANKEL, ALAN D · 2007 to 2018
$48.8M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Molecular Virology and Systems Biology Screening CoreP01AI090935 · NIAID · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI YOUNG, JOHN A T · 2010 to 2014
$20.4M
Rewiring Therapeutic Cells: User-Controlled T Cells and Stem CellsP50GM081879 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIM, WENDELL A · 2010 to 2017
$19.0M
Unbiased Functional Characterization of Enterovirus-Host InteractionsP01AI091575 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ANDINO, RAUL · 2011 to 2015
$10.5M
Proteome-wide study of signaling networks in cancer by mass spectrometryR00CA140789 · NCI · UNIVERSITY OF WASHINGTON · PI VILLEN, JUDIT · 2010 to 2012
$732k
Howard Hughes Medical InstituteNCI NIH HHS R00 CA140789NCI NIH HHS R00CA140789NIAID NIH HHS P01 AI090935NIAID NIH HHS P01 AI091575NIGMS NIH HHS P41 GM103533NIGMS NIH HHS P50 GM081879NIGMS NIH HHS P50 GM082250
6 · The paper itself

Abstract

Cross-talk between different types of post-translational modifications on the same protein molecule adds specificity and combinatorial logic to signal processing, but it has not been characterized on a large-scale basis. We developed two methods to identify protein isoforms that are both phosphorylated and ubiquitylated in the yeast Saccharomyces cerevisiae, identifying 466 proteins with 2,100 phosphorylation sites co-occurring with 2,189 ubiquitylation sites. We applied these methods quantitatively to identify phosphorylation sites that regulate protein degradation via the ubiquitin-proteasome system. Our results demonstrate that distinct phosphorylation sites are often used in conjunction with ubiquitylation and that these sites are more highly conserved than the entire set of phosphorylation sites. Finally, we investigated how the phosphorylation machinery can be regulated by ubiquitylation. We found evidence for novel regulatory mechanisms of kinases and 14-3-3 scaffold proteins via proteasome-independent ubiquitylation.

Indexed as

Binding SitesFungal ProteinsPhosphorylationProtein BindingProtein Interaction MappingSaccharomyces cerevisiaeUbiquitinated ProteinsUbiquitinationFungal ProteinsUbiquitinated Proteins

Identifiers

PMID23749301
PMCPMC3868471
OpenAlexW2150091336

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.