| URL: | https://biodataai.uth.edu/ASpdb |
| Full name: | Alternative Splicing database |
| Description: | ASpdb is a comprehensive database integrating experimentally determined structures and AlphaFold 2-predicted models for human protein isoforms. ASpdb includes over 3400 canonical isoforms, each represented by both experimentally resolved and predicted structures, and >7200 alternative isoforms with AlphaFold 2 predictions. In addition to detailed splicing events, 3D structures, sequence variations and functional annotations, ASpdb uniquely offers comparative analyses and visualization of structural alterations among isoforms. |
| Year founded: | 2024 |
| Last update: | 2025-01-06 |
| Version: | v1.0 |
| Accessibility: |
Accessible
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| Country/Region: | United States |
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| University/Institution: | The University of Texas Health Science Center at Houston |
| Address: | |
| City: | Houston |
| Province/State: | Texas |
| Country/Region: | United States |
| Contact name (PI/Team): | W Jim Zheng |
| Contact email (PI/Helpdesk): | Wenjin.J.Zheng@uth.tmc.edu |
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ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures. [PMID: 39530217]
Alternative splicing is a crucial cellular process in eukaryotes, enabling the generation of multiple protein isoforms with diverse functions from a single gene. To better understand the impact of alternative splicing on protein structures, protein-protein interaction and human diseases, we developed ASpdb (https://biodataai.uth.edu/ASpdb/), a comprehensive database integrating experimentally determined structures and AlphaFold 2-predicted models for human protein isoforms. ASpdb includes over 3400 canonical isoforms, each represented by both experimentally resolved and predicted structures, and >7200 alternative isoforms with AlphaFold 2 predictions. In addition to detailed splicing events, 3D structures, sequence variations and functional annotations, ASpdb uniquely offers comparative analyses and visualization of structural alterations among isoforms. This resource is invaluable for advancing research in alternative splicing, structural biology and disease mechanisms. |