ArticleNature communications2015
Extreme multifunctional proteins identified from a human protein interaction network.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 121 citations in OpenAlex.
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- Structural variability of multifunctional proteins indicates frequent stochastic evolution of protein oligomers.Communications biology · 2025Article
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- Role of RNA in genome folding: It's all about affinity.Current opinion in structural biology · 2025Review
- Selecting genes for analysis using historically contingent progress: from RNA changes to protein-protein interactions.Nucleic acids research · 2025Article
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- How Multifunctioning Joints Produce Highly Agile Limbs in Animals with Lessons for Robotics.Biomimetics (Basel, Switzerland) · 2024Review
- Rhes, a striatal enriched protein, regulates post-translational small-ubiquitin-like-modifier (SUMO) modification of nuclear proteins and alters gene expression.Cellular and molecular life sciences : CMLS · 2024Article
- MultifacetedProtDB: a database of human proteins with multiple functions.Nucleic acids research · 2024Article
- HPC-Atlas: Computationally Constructing A Comprehensive Atlas of Human Protein Complexes.Genomics, proteomics & bioinformatics · 2023Article
- Moonlighting enzymes: when cellular context defines specificity.Cellular and molecular life sciences : CMLS · 2023Review
- Predictive modeling of moonlighting DNA-binding proteins.NAR genomics and bioinformatics · 2022Article
- Biological interacting units identified in human protein networks reveal tissue-functional diversification and its impact on disease.Computational and structural biotechnology journal · 2022Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Moonlighting proteins are a subclass of multifunctional proteins whose functions are unrelated. Although they may play important roles in cells, there has been no large-scale method to identify them, nor any effort to characterize them as a group. Here, we propose the first method for the identification of 'extreme multifunctional' proteins from an interactome as a first step to characterize moonlighting proteins. By combining network topological information with protein annotations, we identify 430 extreme multifunctional proteins (3% of the human interactome). We show that the candidates form a distinct sub-group of proteins, characterized by specific features, which form a signature of extreme multifunctionality. Overall, extreme multifunctional proteins are enriched in linear motifs and less intrinsically disordered than network hubs. We also provide MoonDB, a database containing information on all the candidates identified in the analysis and a set of manually curated human moonlighting proteins.
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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 OpenQuestion graph.