ArticleCellular and molecular life sciences : CMLS2021
IDPology of the living cell: intrinsic disorder in the subcellular compartments of the human cell.
Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Modern resources for intrinsic disorder predictions: protein language models, deep learning, meta-servers, and databases.Cellular and molecular life sciences : CMLS · 2026Review
- Hyperactive 20Science advances · 2025Article
- Accurate and Fast Prediction of Intrinsic Disorder Using flDPnn.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Evaluation of predictions of disordered binding regions in the CAID2 experiment.Computational and structural biotechnology journal · 2025Review
- Macromolecular Crowding in Mitochondria.Sub-cellular biochemistry · 2025Review
- Prediction of Intrinsic Disorder Functions with DEPICTER2.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Systematic identification of 20S proteasome substrates.Molecular systems biology · 2024Article
- Tutorial: a guide for the selection of fast and accurate computational tools for the prediction of intrinsic disorder in proteins.Nature protocols · 2023Review
- Chaotic aging: intrinsically disordered proteins in aging-related processes.Cellular and molecular life sciences : CMLS · 2023Article
- DEPICTER2: a comprehensive webserver for intrinsic disorder and disorder function prediction.Nucleic acids research · 2023Article
- HybridRNAbind: prediction of RNA interacting residues across structure-annotated and disorder-annotated proteins.Nucleic acids research · 2023Article
- Comparative evaluation of AlphaFold2 and disorder predictors for prediction of intrinsic disorder, disorder content and fully disordered proteins.Computational and structural biotechnology journal · 2023Article
- Enrichment patterns of intrinsic disorder in proteins.Biophysical reviews · 2022Review
- iFeatureOmega: an integrative platform for engineering, visualization and analysis of features from molecular sequences, structural and ligand data sets.Nucleic acids research · 2022Article
- Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions.Biomolecules · 2022Article
- Intrinsically Disordered Proteins: Critical Components of the Wetware.Chemical reviews · 2022Review
- Complementarity of the residue-level protein function and structure predictions in human proteins.Computational and structural biotechnology journal · 2022Article
- Deep learning in prediction of intrinsic disorder in proteins.Computational and structural biotechnology journal · 2022Review
- flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions.Nature communications · 2021Article
- QUARTERplus: Accurate disorder predictions integrated with interpretable residue-level quality assessment scores.Computational and structural biotechnology journal · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Intrinsic disorder can be found in all proteomes of all kingdoms of life and in viruses, being particularly prevalent in the eukaryotes. We conduct a comprehensive analysis of the intrinsic disorder in the human proteins while mapping them into 24 compartments of the human cell. In agreement with previous studies, we show that human proteins are significantly enriched in disorder relative to a generic protein set that represents the protein universe. In fact, the fraction of proteins with long disordered regions and the average protein-level disorder content in the human proteome are about 3 times higher than in the protein universe. Furthermore, levels of intrinsic disorder in the majority of human subcellular compartments significantly exceed the average disorder content in the protein universe. Relative to the overall amount of disorder in the human proteome, proteins localized in the nucleus and cytoskeleton have significantly increased amounts of disorder, measured by both high disorder content and presence of multiple long intrinsically disordered regions. We empirically demonstrate that, on average, human proteins are assigned to 2.3 subcellular compartments, with proteins localized to few subcellular compartments being more disordered than the proteins that are localized to many compartments. Functionally, the disordered proteins localized in the most disorder-enriched subcellular compartments are primarily responsible for interactions with nucleic acids and protein partners. This is the first-time disorder is comprehensively mapped into the human cell. Our observations add a missing piece to the puzzle of functional disorder and its organization inside the cell.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.