ArticleScientific reports2014
Systematic analysis of the in situ crosstalk of tyrosine modifications reveals no additional natural selection on multiply modified residues.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- TPST2-mediated tyrosine sulfation orchestrates porcine preimplantation development.BMC biology · 2026Article
- Genetic variability in proteoglycan biosynthetic genes reveals new facets of heparan sulfate diversity.Essays in biochemistry · 2024Review
- Sulfoproteomics Workflow with Precursor Ion Accurate Mass Shift Analysis Reveals Novel Tyrosine Sulfoproteins in the Golgi.Journal of proteome research · 2024Article
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- "Glyco-sulfo barcodes" regulate chemokine receptor function.Cellular and molecular life sciences : CMLS · 2023Article
- Thirty years of molecular dynamics simulations on posttranslational modifications of proteins.Physical chemistry chemical physics : PCCP · 2022Review
- Engineering of HIV-1 neutralizing antibody CAP256V2LS for manufacturability and improved half life.Scientific reports · 2022Article
- Targeting the YXXΦ Motifs of the SARS Coronaviruses 1 and 2 ORF3a Peptides by In Silico Analysis to Predict Novel Virus-Host Interactions.Biomolecules · 2022Article
- PhosVarDeep: deep-learning based prediction of phospho-variants using sequence information.PeerJ · 2022Article
- Human transitional and IgMImmunology and cell biology · 2021Article
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- DeepPhos: prediction of protein phosphorylation sites with deep learning.Bioinformatics (Oxford, England) · 2019Article
- New insights into the heat responses of grape leaves via combined phosphoproteomic and acetylproteomic analyses.Horticulture research · 2019Article
- A novel chlorination-induced ribonuclease YabJ fromBioscience reports · 2018Article
- SVM-SulfoSite: A support vector machine based predictor for sulfenylation sites.Scientific reports · 2018Article
- A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- PTM-ssMP: A Web Server for Predicting Different Types of Post-translational Modification Sites Using Novel Site-specific Modification Profile.International journal of biological sciences · 2018Article
- Article
- Review
- Prediction of post-translational modification sites using multiple kernel support vector machine.PeerJ · 2017Article
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8 authors.
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Abstract
Recent studies have indicated that different post-translational modifications (PTMs) synergistically orchestrate specific biological processes by crosstalks. However, the preference of the crosstalk among different PTMs and the evolutionary constraint on the PTM crosstalk need further dissections. In this study, the in situ crosstalk at the same positions among three tyrosine PTMs including sulfation, nitration and phosphorylation were systematically analyzed. The experimentally identified sulfation, nitration and phosphorylation sites were collected and integrated with reliable predictions to perform large-scale analyses of in situ crosstalks. From the results, we observed that the in situ crosstalk between sulfation and nitration is significantly under-represented, whereas both sulfation and nitration prefer to co-occupy with phosphorylation at same tyrosines. Further analyses suggested that sulfation and nitration preferentially co-occur with phosphorylation at specific positions in proteins, and participate in distinct biological processes and functions. More interestingly, the long-term evolutionary analysis indicated that multi-PTM targeting tyrosines didn't show any higher conservation than singly modified ones. Also, the analysis of human genetic variations demonstrated that there is no additional functional constraint on inherited disease, cancer or rare mutations of multiply modified tyrosines. Taken together, our systematic analyses provided a better understanding of the in situ crosstalk among PTMs.
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