Abstract
Retinoic acid-induced protein 2 is a human protein of 530 residues encoded by the RAI2 gene (Q9Y5P3; RAI2_HUMAN). RAI2 is a novel tumor suppressor protein whose depletion in breast cancer cell lines results in the downregulation of several genes associated with differentiation along with increased invasiveness and aggressive tumor phenotype of the cells. The role of the protein is specified to be a transcriptional regulator that promotes chromosomal stability and hence controls the expression of several regulators of cancer and metastasis. Structurally, RAI2 remains an unknown entity and, hence, to obtain a detailed view on the structure function relationship we report the 1H, 13C, and 15N resonance assignments for the backbone and side chain nuclei of the C-terminal region (a.a. 303–451 of UniProt Q9Y5P3) of RAI2.
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The FLI is a member of the Leibniz Association (WGL) and is financially supported by the Federal Government of Germany and the State of Thuringia.
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Lang, A., Goradia, N., Wikman, H. et al. 1H, 13C, and 15N backbone assignments of the C-terminal region of the human retinoic acid-induced protein 2. Biomol NMR Assign 14, 271–275 (2020). https://doi.org/10.1007/s12104-020-09960-9
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DOI: https://doi.org/10.1007/s12104-020-09960-9