ArticleProtein science : a publication of the Protein Society2020
Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Molecular dynamics simulations of intrinsically disordered protein regions enable biophysical interpretation of variant-effect predictors.HGG advances · 2026Article
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast.Nucleic acids research · 2023Article
- Poly(ADP-ribose)-binding protein RCD1 is a plant PARylation reader regulated by Photoregulatory Protein Kinases.Communications biology · 2023Article
- Prediction of chaperonin GroE substrates using small structural patterns of proteins.FEBS open bio · 2023Article
- Computational Methods to Predict Intrinsically Disordered Regions and Functional Regions in Them.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Conservation of land plant-specific receptor-like cytoplasmic kinase subfamily XI possessing a unique kinase insert domain.Frontiers in plant science · 2023Article
- Article
- Evolutionary crossroads of cell signaling: PP1 and PP2A substrate sites in intrinsically disordered regions.Biochemical Society transactions · 2021Review
- Optical chemosensors for the detection of proximally phosphorylated peptides and proteins.RSC chemical biology · 2021Review
- Functional and Predictive Structural Characterization of WRINKLED2, A Unique Oil Biosynthesis Regulator in Avocado.Frontiers in plant science · 2021Article
- Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2020Article
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4 authors.
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Abstract
Phosphorylation is a major post-translational modification that plays a central role in signaling pathways. Protein kinases phosphorylate substrates (phosphoproteins) by adding phosphate at Ser/Thr or Tyr residues (phosphosites). A large amount of data identifying and describing phosphosites in phosphoproteins has been reported but the specificity of phosphorylation is not fully resolved. In this report, data of kinase-substrate pairs identified by the Kinase-Interacting Substrate Screening (KISS) method were used to analyze phosphosites in intrinsically disordered regions (IDRs) of intrinsically disordered proteins. We compared phosphorylated and nonphosphorylated IDRs and found that the phosphorylated IDRs were significantly longer than nonphosphorylated IDRs. The phosphorylated IDR is often the longest IDR (71%) in a phosphoprotein when only a single phosphosite exists in the IDR, and when the phosphoprotein has multiple phosphosites in an IDR(s), the phosphosites are primarily localized in a single IDR (78%) and this IDR is usually the longest one (81%). We constructed a stochastic model of phosphorylation to estimate the effect of IDR length. The model that accounted for IDR length produced more realistic results when compared with a model that excluded the IDR length. We propose that the IDR length is a significant determinant for locating kinase phosphorylation sites in phosphoproteins.
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