POSTAR: a platform for exploring post-transcriptional regulation coordinated by RNA-binding proteins

B Hu, YCT Yang, Y Huang, Y Zhu… - Nucleic acids research, 2017 - academic.oup.com
B Hu, YCT Yang, Y Huang, Y Zhu, ZJ Lu
Nucleic acids research, 2017academic.oup.com
Abstract We present POSTAR (http://POSTAR. ncrnalab. org), a resource of POST-tr A
nscriptional R egulation coordinated by RNA-binding proteins (RBPs). Precise
characterization of post-transcriptional regulatory maps has accelerated dramatically in the
past few years. Based on new studies and resources, POSTAR supplies the largest
collection of experimentally probed (∼ 23 million) and computationally predicted
(approximately 117 million) RBP binding sites in the human and mouse transcriptomes …
Abstract
We present POSTAR (http://POSTAR.ncrnalab.org), a resource of POST-trAnscriptional Regulation coordinated by RNA-binding proteins (RBPs). Precise characterization of post-transcriptional regulatory maps has accelerated dramatically in the past few years. Based on new studies and resources, POSTAR supplies the largest collection of experimentally probed (∼23 million) and computationally predicted (approximately 117 million) RBP binding sites in the human and mouse transcriptomes. POSTAR annotates every transcript and its RBP binding sites using extensive information regarding various molecular regulatory events (e.g., splicing, editing, and modification), RNA secondary structures, disease-associated variants, and gene expression and function. Moreover, POSTAR provides a friendly, multi-mode, integrated search interface, which helps users to connect multiple RBP binding sites with post-transcriptional regulatory events, phenotypes, and diseases. Based on our platform, we were able to obtain novel insights into post-transcriptional regulation, such as the putative association between CPSF6 binding, RNA structural domains, and Li-Fraumeni syndrome SNPs. In summary, POSTAR represents an early effort to systematically annotate post-transcriptional regulatory maps and explore the putative roles of RBPs in human diseases.
Oxford University Press