ArticleProtein science : a publication of the Protein Society2020
IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions-Insights from transcription factors.
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 16 papers.
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Who cites it
16 citing papers in PubMed.
- Autoinhibition of untimely DNA binding by structural disorder in the full-length peroxisome proliferator-activated receptors (PPARs).Nature communications · 2026Article
- Hierarchy in regulator interactions with distant transcriptional activation domains empowers rheostatic regulation.Protein science : a publication of the Protein Society · 2025Article
- Importance of an N-terminal structural switch in the distinction between small RNA-bound and free ARGONAUTE.Nature structural & molecular biology · 2025Article
- Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation.Nucleic acids research · 2025Article
- Deep mutational scanning of the Trypanosoma brucei developmental regulator RBP6 reveals an essential disordered region influenced by positive residues.Nature communications · 2025Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Protein intrinsically disordered regions have a non-random, modular architecture.Bioinformatics (Oxford, England) · 2023Article
- SHEPHARD: a modular and extensible software architecture for analyzing and annotating large protein datasets.Bioinformatics (Oxford, England) · 2023Article
- Low Complexity Regions in Proteins and DNA are Poorly Correlated.Molecular biology and evolution · 2023Article
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- Structure, dynamics, and stability of the globular domain of human linker histone H1.0 and the role of positive charges.Protein science : a publication of the Protein Society · 2022Article
- Evolution of A bHLH Interaction Motif.International journal of molecular sciences · 2021Article
- Orchestration of signaling by structural disorder in class 1 cytokine receptors.Cell communication and signaling : CCS · 2020Article
- Production of Intrinsically Disordered Proteins for Biophysical Studies: Tips and Tricks.Methods in molecular biology (Clifton, N.J.) · 2020Article
- IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions-Insights from transcription factors.Protein science : a publication of the Protein Society · 2020Article
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6 authors.
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Abstract
Protein domains constitute regions of distinct structural properties and molecular functions that are retained when removed from the rest of the protein. However, due to the lack of tertiary structure, the identification of domains has been largely neglected for long (>50 residues) intrinsically disordered regions. Here we present a sequence-based approach to assess and visualize domain organization in long intrinsically disordered regions based on compositional sequence biases. An online tool to find putative intrinsically disordered domains (IDDomainSpotter) in any protein sequence or sequence alignment using any particular sequence trait is available at http://www.bio.ku.dk/sbinlab/IDDomainSpotter. Using this tool, we have identified a putative domain enriched in hydrophilic and disorder-promoting residues (Pro, Ser, and Thr) and depleted in positive charges (Arg and Lys) bordering the folded DNA-binding domains of several transcription factors (p53, GCR, NAC46, MYB28, and MYB29). This domain, from two different MYB transcription factors, was characterized biophysically to determine its properties. Our analyses show the domain to be extended, dynamic and highly disordered. It connects the DNA-binding domain to other disordered domains and is present and conserved in several transcription factors from different families and domains of life. This example illustrates the potential of IDDomainSpotter to predict, from sequence alone, putative domains of functional interest in otherwise uncharacterized disordered proteins.
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