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Data for positive selection test and co-evolutionary analysis on mammalian cereblon. | LitMetric

Data for positive selection test and co-evolutionary analysis on mammalian cereblon.

Data Brief

Faculty of Science and Engineering, Waseda University, TWIns, 2-2 Wakamatsu, Shinjuku, Tokyo, 162-8480, Japan.

Published: October 2019

AI Article Synopsis

  • Cereblon (CRBN) is a key protein in the CRL4 E3 ubiquitin ligase complex that regulates protein degradation, energy metabolism, and stress response in cells by binding to specific substrates.
  • The study presents two datasets showing that CRBN underwent positive selection, as indicated by dN/dS calculations from multiple sequence alignments.
  • It also includes co-evolutionary analysis demonstrating evolutionary similarities between CRBN and related proteins, with a focus on its modified functions and efficiency in binding to AMPK.

Article Abstract

Cereblon (CRBN) is a substrate recognition subunit of the CRL4 E3 ubiquitin ligase complex, directly binding to specific substrates for poly-ubiquitination followed by proteasome-dependent degradation of proteins. Cellular CRBN is responsible for energy metabolism, ion-channel activation, and cellular stress response through binding to proteins related to the respective pathways. As CRBN binds to various proteins, the selective pressure at the interacting surface is expected to result in functional divergence. Here, we present two mammalian CRBN datasets of molecular evolutionary analyses. (1) The multiple sequence alignment data shows that positive selection occurred, determined with a dN/dS calculation. (2) Data on co-evolutionary analysis between vertebrate CRBN and related proteins are represented by calculating the correlation coefficient based on the comparison of phylogenetic trees. Co-evolutionary analysis shows the similarity of evolutionary traits of two proteins. Further molecular, functional interpretation of these analyses is explained in 'Positive selection of Cereblon modified function including its E3 Ubiquitin Ligase activity and binding efficiency with AMPK' (W. Onodera, T. Asahi, N. Sawamura, Positive selection of cereblon modified function including its E3 ubiquitin ligase activity and binding efficiency with AMPK. Mol Phylogenet Evol. (2019) 135:78-85. [1]).

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6811870PMC
http://dx.doi.org/10.1016/j.dib.2019.104499DOI Listing

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