ArticleNature communications2019
Conserved phosphorylation hotspots in eukaryotic protein domain families.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Mapping protein states and interactions across the tree of life with co-fractionation mass spectrometry.Nature communications · 2023Pooled it
- An AI-enabled structural atlas decodes kinase specificity across the human proteome.Nature biotechnology · 2026Article
- Illuminating the Co-Phosphoregulatory Network of the Dark Kinase STK10 by Omics Approaches.BioMed research international · 2026Article
- Phosphoproteomics of aged insulin-resistant bone identifies P70S6K phosphorylation of AFF4 as a gene-specific transcriptional regulator.Nature communications · 2025Article
- Global comparative structural analysis of responses to protein phosphorylation.Nature communications · 2025Article
- The functional landscape of the human ubiquitinome.bioRxiv : the preprint server for biology · 2025Article
- Autophosphorylation of conserved yeast and human casein kinase 1 isozymes regulates Elongator-dependent tRNA modifications.Nucleic acids research · 2025Article
- Applying a Conservation-Based Approach for Predicting Novel Phosphorylation Sites in Eukaryotes and Evaluating Their Functional Relevance.Journal of proteome research · 2025Article
- DivergentLife science alliance · 2025Article
- High resolution profiling of cell cycle-dependent protein and phosphorylation abundance changes in non-transformed cells.Nature communications · 2025Article
- PTMoreR-enabled cross-species PTM mapping and comparative phosphoproteomics across mammals.Cell reports methods · 2024Article
- Genetic constraint at single amino acid resolution in protein domains improves missense variant prioritisation and gene discovery.Genome medicine · 2024Article
- Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail.Nature communications · 2024Article
- Article
- Protein kinase CK2 modulates the activity of Maf-family bZIP transcription factor NRL in rod photoreceptors of mammalian retina.Human molecular genetics · 2023Article
- Evolutionary Divergence of Phosphorylation to Regulate Interactive Protein Networks in Lower and Higher Species.International journal of molecular sciences · 2022Article
- Article
- Molecular insights into the heat shock proteins of the human parasitic blood fluke Schistosoma mansoni.Parasites & vectors · 2022Article
- Trafficking regulator of GLUT4-1 (TRARG1) is a GSK3 substrate.The Biochemical journal · 2022Article
- Phosphorylation of guanosine monophosphate reductase triggers a GTP-dependent switch from pro- to anti-oncogenic function of EPHA4.Cell chemical biology · 2022Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Protein phosphorylation is the best characterized post-translational modification that regulates almost all cellular processes through diverse mechanisms such as changing protein conformations, interactions, and localization. While the inventory for phosphorylation sites across different species has rapidly expanded, their functional role remains poorly investigated. Here, we combine 537,321 phosphosites from 40 eukaryotic species to identify highly conserved phosphorylation hotspot regions within domain families. Mapping these regions onto structural data reveals that they are often found at interfaces, near catalytic residues and tend to harbor functionally important phosphosites. Notably, functional studies of a phospho-deficient mutant in the C-terminal hotspot region within the ribosomal S11 domain in the yeast ribosomal protein uS11 shows impaired growth and defective cytoplasmic 20S pre-rRNA processing at 16 °C and 20 °C. Altogether, our study identifies phosphorylation hotspots for 162 protein domains suggestive of an ancient role for the control of diverse eukaryotic domain families.
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