ArticleProtein science : a publication of the Protein Society2016
Large-scale analysis of intrinsic disorder flavors and associated functions in the protein sequence universe.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 60 citations in OpenAlex.
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- Shoebill: an interpretable AlphaFold2-informed predictor of protein crystallization propensity using XGBoost.Briefings in bioinformatics · 2026Article
- Modern resources for intrinsic disorder predictions: protein language models, deep learning, meta-servers, and databases.Cellular and molecular life sciences : CMLS · 2026Review
- Prediction of Intrinsically Disordered Regions That Bind RNA with DisoRDPbind.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Noncovalent Lasso Entanglements are Common in Experimentally Derived Intrinsically Disordered Protein Ensembles and Strongly Influenced by Protein Length and Charge.The journal of physical chemistry. B · 2025Article
- Taxonomy-specific assessment of intrinsic disorder predictions at residue and region levels in higher eukaryotes, protists, archaea, bacteria and viruses.Computational and structural biotechnology journal · 2024Article
- Phase separation of SPIN1 through its IDR facilitates histone methylation readout and tumorigenesis.Journal of molecular cell biology · 2024Article
- DisProt in 2024: improving function annotation of intrinsically disordered proteins.Nucleic acids research · 2024Article
- Protein intrinsically disordered regions have a non-random, modular architecture.Bioinformatics (Oxford, England) · 2023Article
- CAID prediction portal: a comprehensive service for predicting intrinsic disorder and binding regions in proteins.Nucleic acids research · 2023Article
- Antimicrobial Peptide Arsenal Predicted from the Venom Gland Transcriptome of the Tropical Trap-Jaw AntToxins · 2023Article
- Mapping the Constrained Coding Regions in the Human Genome to Their Corresponding Proteins.Journal of molecular biology · 2023Article
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions.Biomolecules · 2022Article
- Discovering molecular features of intrinsically disordered regions by using evolution for contrastive learning.PLoS computational biology · 2022Article
- Characterization of intrinsically disordered regions in proteins informed by human genetic diversity.PLoS computational biology · 2022Article
- Databases for intrinsically disordered proteins.Acta crystallographica. Section D, Structural biology · 2022Review
- Deep learning in prediction of intrinsic disorder in proteins.Computational and structural biotechnology journal · 2022Review
- Assembly-Line Catalysis in Bifunctional Terpene Synthases.Accounts of chemical research · 2021Review
- flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions.Nature communications · 2021Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsic disorder (ID) in proteins has been extensively described for the last decade; a large-scale classification of ID in proteins is mostly missing. Here, we provide an extensive analysis of ID in the protein universe on the UniProt database derived from sequence-based predictions in MobiDB. Almost half the sequences contain an ID region of at least five residues. About 9% of proteins have a long ID region of over 20 residues which are more abundant in Eukaryotic organisms and most frequently cover less than 20% of the sequence. A small subset of about 67,000 (out of over 80 million) proteins is fully disordered and mostly found in Viruses. Most proteins have only one ID, with short ID evenly distributed along the sequence and long ID overrepresented in the center. The charged residue composition of Das and Pappu was used to classify ID proteins by structural propensities and corresponding functional enrichment. Swollen Coils seem to be used mainly as structural components and in biosynthesis in both Prokaryotes and Eukaryotes. In Bacteria, they are confined in the nucleoid and in Viruses provide DNA binding function. Coils & Hairpins seem to be specialized in ribosome binding and methylation activities. Globules & Tadpoles bind antigens in Eukaryotes but are involved in killing other organisms and cytolysis in Bacteria. The Undefined class is used by Bacteria to bind toxic substances and mediate transport and movement between and within organisms in Viruses. Fully disordered proteins behave similarly, but are enriched for glycine residues and extracellular structures.
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