Evidence map›Paper›PMID 22817900›Full record

ArticleCell2012

Systematic functional prioritization of protein posttranslational modifications.

Pedro Beltrao, Véronique Albanèse, Lillian R Kenner, Danielle L Swaney, Alma Burlingame, Judit Villén, Wendell A Lim, James S Fraser, Judith Frydman, Nevan J Krogan

Abstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 254 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
254citing papers in PubMed, 1 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

254 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. CLASPP: A unified model for predicting post-translational modifications.bioRxiv : the preprint server for biology · 2026
    Article
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  7. Review
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  11. Article
  12. Article
  13. Review
  14. Article
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194 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Pedro BeltraoDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94107, USA. pedro.beltrao@ucsf.edu
Véronique Albanèse
Lillian R Kenner
Danielle L Swaney
Alma Burlingame
Judit Villén
Wendell A Lim
James S Fraser
Judith Frydman
Nevan J Krogan

Funding

Virology CoreP30AI027763 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STEVEN Grant DEEKS · 1988 to 2026
$93.6M
X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRANKEL, ALAN D · 2007 to 2018
$48.8M
YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ORTIZ DE MONTELLANO, PAUL R · 1985 to 2011
$24.1M
Molecular Virology and Systems Biology Screening CoreP01AI090935 · NIAID · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI HOFFMANN, ALEXANDER · 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
Cellular Control:Synthetic Signaling/Motility (RMI)PN2EY016546 · NEI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIM, WENDELL A · 2005 to 2014
$16.0M
PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLR01GM056433 · NIGMS · STANFORD UNIVERSITY · PI Judith Frydman · 1997 to 2026
$5.0M
Protein Folding in the Eukaryotic CytosolR37GM056433 · NIGMS · STANFORD UNIVERSITY · PI FRYDMAN, JUDITH · 2013 to 2022
$4.6M
Comparative Analysis of Genetic Interaction NetworksR01GM084279 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI IDEKER, TREY, KROGAN, NEVAN J · 2008 to 2017
$3.9M
PROTEIN RECOGNITION IN SIGNAL TRANSDUCTIONR01GM055040 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIM, WENDELL A · 1997 to 2015
$3.5M
Genetic Analysis of the Nucleosome and RNA Polymerase II: A Systems ApproachR01GM084448 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KROGAN, NEVAN J · 2008 to 2012
$2.3M
PROTEIN INTERACTIONS REGULATING CELL MOTILITYR01GM062583 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIM, WENDELL A · 2001 to 2009
$2.2M
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR001614NCRR NIH HHS RR01614NEI NIH HHS PN2 EY016546NIAID NIH HHS AI090935NIAID NIH HHS P01 AI090935NIAID NIH HHS P30 AI027763NIGMS NIH HHS GM062583NIGMS NIH HHS GM081879NIGMS NIH HHS GM082250NIGMS NIH HHS GM084279NIGMS NIH HHS GM084448NIGMS NIH HHS GM55040NIGMS NIH HHS GM56433NIGMS NIH HHS P50 GM081879NIGMS NIH HHS P50 GM082250NIGMS NIH HHS R01 GM055040NIGMS NIH HHS R01 GM056433NIGMS NIH HHS R01 GM062583NIGMS NIH HHS R01 GM084279NIGMS NIH HHS R01 GM084448NIGMS NIH HHS R37 GM056433NIH HHS DP5 OD009180
6 · The paper itself

Abstract

Protein function is often regulated by posttranslational modifications (PTMs), and recent advances in mass spectrometry have resulted in an exponential increase in PTM identification. However, the functional significance of the vast majority of these modifications remains unknown. To address this problem, we compiled nearly 200,000 phosphorylation, acetylation, and ubiquitination sites from 11 eukaryotic species, including 2,500 newly identified ubiquitylation sites for Saccharomyces cerevisiae. We developed methods to prioritize the functional relevance of these PTMs by predicting those that likely participate in cross-regulatory events, regulate domain activity, or mediate protein-protein interactions. PTM conservation within domain families identifies regulatory "hot spots" that overlap with functionally important regions, a concept that we experimentally validated on the HSP70 domain family. Finally, our analysis of the evolution of PTM regulation highlights potential routes for neutral drift in regulatory interactions and suggests that only a fraction of modification sites are likely to have a significant biological role.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceAnimalsEukaryotaHSP70 Heat-Shock ProteinsHumansModels, MolecularMolecular Sequence DataPhosphorylationProtein Interaction Domains and MotifsProtein Structure, TertiarySaccharomyces cerevisiaeSequence AlignmentUbiquitinationHSP70 Heat-Shock Proteins

Identifiers

PMID22817900
PMCPMC3404735

What OpenQuestion holds

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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.