Chair of Experimental Bioinformatics, TUM School of Life Sciences Weihenstephan, Technical University of Munich, 85354 Freising, Germany.
Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz Centre for Infection Research (HZI), 66123 Saarbrücken, Germany.
Nucleic Acids Res. 2021 Jan 8;49(D1):D309-D318. doi: 10.1093/nar/gkaa768.
Alternative splicing plays a major role in regulating the functional repertoire of the proteome. However, isoform-specific effects to protein-protein interactions (PPIs) are usually overlooked, making it impossible to judge the functional role of individual exons on a systems biology level. We overcome this barrier by integrating protein-protein interactions, domain-domain interactions and residue-level interactions information to lift exon expression analysis to a network level. Our user-friendly database DIGGER is available at https://exbio.wzw.tum.de/digger and allows users to seamlessly switch between isoform and exon-centric views of the interactome and to extract sub-networks of relevant isoforms, making it an essential resource for studying mechanistic consequences of alternative splicing.
可变剪接在调节蛋白质组的功能库方面起着重要作用。然而，通常会忽略对蛋白质-蛋白质相互作用 (PPI) 的异构体特异性影响，这使得无法在系统生物学水平上判断各个外显子的功能作用。我们通过整合蛋白质-蛋白质相互作用、结构域-结构域相互作用和残基水平相互作用信息，将外显子表达分析提升到网络水平，从而克服了这一障碍。我们易于使用的数据库 DIGGER 可在 https://exbio.wzw.tum.de/digger 上获取，允许用户在互作体的异构体和外显子中心视图之间无缝切换，并提取相关异构体的子网络，使其成为研究可变剪接的机制后果的重要资源。
