ArticleProtein science : a publication of the Protein Society2014
The structural and functional signatures of proteins that undergo multiple events of post-translational modification.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 176 papers, 3 of them syntheses that pooled it.
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Who cites it
176 citing papers in PubMed, 3 syntheses or guidelines pooled it.
- Current computational tools for protein lysine acylation site prediction.Briefings in bioinformatics · 2024Pooled it
- Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)Autophagy · 2021Guideline
- Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).Autophagy · 2016Guideline
- No Time to Fold: Intrinsically Disordered Microproteins in Action.Biochemistry · 2026Review
- A comprehensive in silico investigation into the deleterious nonsynonymous single nucleotide polymorphisms of the human transcription factor EB (TFEB) gene and their predicted association with cancer.Journal, genetic engineering & biotechnology · 2026Article
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Amyloid-β, Tau Protein, α-Synuclein, TDP-43, and FUS in Mixed Pathology: And Intrinsic Disorder to Rule Them All.International journal of molecular sciences · 2026Review
- Generative design of intrinsically disordered protein regions with IDiom.bioRxiv : the preprint server for biology · 2026Article
- A New Detailed Mass Offset Search in MSFragger for Improved Interpretation of Complex PTMs.Journal of proteome research · 2026Article
- Metabolic and post-translational modifications in sepsis-associated immune dysfunction: a conceptual framework.Frontiers in immunology · 2026Review
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.bioRxiv : the preprint server for biology · 2025Article
- DeepMVP: deep learning models trained on high-quality data accurately predict PTM sites and variant-induced alterations.Nature methods · 2025Article
- Hallmarks of cellular senescence: biology, mechanisms, regulations.Experimental & molecular medicine · 2025Review
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Intrinsic Disorder and Phase Separation Coordinate Exocytosis, Motility, and Chromatin Remodeling in the Human Acrosomal Proteome.Proteomes · 2025Article
- Binding mode-guided development of high-performance antibodies targeting site-specific posttranslational modifications.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Flexible iron: disorder in the ironome brings order to protein structure and function.Frontiers in molecular biosciences · 2025Article
- Improved prediction of post-translational modification crosstalk within proteins using DeepPCT.Bioinformatics (Oxford, England) · 2024Article
- On the Roles of Protein Intrinsic Disorder in the Origin of Life and Evolution.Life (Basel, Switzerland) · 2024Review
116 more citing papers are in PubMed but not listed here.
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6 authors.
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Abstract
unlabelledThe structural, functional, and mechanistic characterization of several types of post-translational modifications (PTMs) is well-documented. PTMs, however, may interact or interfere with one another when regulating protein function. Yet, characterization of the structural and functional signatures of their crosstalk has been hindered by the scarcity of data. To this end, we developed a unified sequence-based predictor of 23 types of PTM sites that, we believe, is a useful tool in guiding biological experiments and data interpretation. We then used experimentally determined and predicted PTM sites to investigate two particular cases of potential PTM crosstalk in eukaryotes. First, we identified proteins statistically enriched in multiple types of PTM sites and found that they show preferences toward intrinsically disordered regions as well as functional roles in transcriptional, posttranscriptional, and developmental processes. Second, we observed that target sites modified by more than one type of PTM, referred to as shared PTM sites, show even stronger preferences toward disordered regions than their single-PTM counterparts; we explain this by the need for these regions to accommodate multiple partners. Finally, we investigated the influence of single and shared PTMs on differential regulation of protein-protein interactions. We provide evidence that molecular recognition features (MoRFs) show significant preferences for PTM sites, particularly shared PTM sites, implicating PTMs in the modulation of this specific type of macromolecular recognition. We conclude that intrinsic disorder is a strong structural prerequisite for complex PTM-based regulation, particularly in context-dependent protein-protein interactions related to transcriptional and developmental processes. AVAILABILITY: www.modpred.org.
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