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Updated: Oct 23, 2025

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
Published on: August 9, 2019
POSTAR3: an updated platform for exploring post-transcriptional regulation coordinated by RNA-binding proteins
Weihao Zhao1, Shang Zhang1, Yumin Zhu1,2
1MOE Key Laboratory of Bioinformatics, Center for Synthetic and Systems Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
POSTAR3 is a comprehensive database mapping RNA-binding protein (RBP) sites across species. It enhances understanding of gene regulation by integrating diverse functional genomic data and disease-associated variants.
Area of Science:
- Genomics
- Molecular Biology
- Bioinformatics
Background:
- RNA-binding proteins (RBPs) are crucial for post-transcriptional gene regulation.
- Identifying RBP binding sites across various species and conditions is essential for understanding gene expression control in health and disease.
Purpose of the Study:
- To present POSTAR3, an updated database for annotating RBP binding sites and post-transcriptional regulation.
- To provide a comprehensive resource for studying RBP functions in diverse biological contexts.
Main Methods:
- Integrated large-scale CLIP-seq and Ribo-seq datasets covering expanded biological conditions, technologies, and species.
- Incorporated RNA secondary structure profiling, miRNA-mediated degradation events (validated by degradome-seq), and RBP binding sites at circRNA junctions.
- Expanded annotation with updated genomic variants and disease-associated mutations.
Main Results:
- POSTAR3 offers a significantly updated and expanded map of RBP binding sites.
- The database includes novel annotations for RNA secondary structures, miRNA interactions, and circRNA binding.
- Enhanced integration of disease-related genomic variants provides insights into pathological mechanisms.
Conclusions:
- POSTAR3 serves as a valuable, freely accessible resource for researchers studying RBP-mediated gene regulation.
- The updated database facilitates deeper investigation into the roles of RBPs in physiological and pathological processes across multiple species.
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