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. 2018 Feb 8;8:2683. doi: 10.1038/s41598-018-21040-6

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© The Author(s) 2018

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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The protein interaction network of B55α. (A) The top 30 most abundant proteins identified as B55α-associated proteins. Recombinant B55α was purified, and incubated in interphase Xenopus egg extracts for 30 min. B55α-associated protein complexes were then purified and analyzed by mass spectrometry, as described in Materials and Methods. The identified proteins and numbers of peptides are shown. The proteins previously known to bind B55α are shown in red. (B) B55α-associated proteins were classified into various functional groups. (C) Representative B55α-associated proteins involved in distinct cellular pathways are shown.