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. 2020 Sep 30;58(2):631–646. doi: 10.1007/s12035-020-02137-4

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — RNA binding domains in hnRNPs. RNA-binding domains in hnRNP include RRM (RNA Recognition Motif), KH (K-Homology), and RGG (Arginine-Glycine-Glycine). hnRNPA1 UP1, which spans the first 196 aa at the N-terminus, contains two RRM one in each subdomain of UP1. a RRM contains two α-helices (RRM1: cyan, RRM2: pink), four β-sheets (RRM1: blue, RRM2: purple), and five loops (RRM1: green, RRM2: orange) that order as βαββαβ. b The C-terminal of hnRNPA1 contains another RNA-binding motif known as RGG. The name reflects the abundance of Arg-Gly-Gly tripeptide repeats in the motif. c The KH domain of hnRNPK consists of three α-helices (cyan), three β-sheets (green), and five loops (purple) that fold in the order of βααββα [7–11]