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RNA-seq and label-free quantitative proteomics data from: KDM4A serves as an α-tubulin demethylase regulating microtubule polymerization and cell mitosis

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Sep 19, 2025 version files 37.38 GB

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Abstract

Tri-methylation on lysine 40 of α-tubulin is involved in cell division and neuronal development. We report that KDM4A, a member of the histone demethylase family, demethylates α-tubulin. Degradation of KDM4A for 12 h leads to an increase in methylation of α-tubulin and histone, as well as mitotic defects in KDM4A-FKBP12F36V-2×HA-T2A-Puro knock-in HEK293T cells (termed as KDM4A-dTAG cells). We performed RNA-seq and label-free quantitative proteomics to evaluate the consequence of genetic alteration resulting from an increase in histone methylation in KDM4A-dTAG cells upon 12 h of dTAG-13 treatment. Notably, we identified 23 genes that showed more than 1.5-fold expression change after 12 h of dTAG-13 treatment, with 13 up-regulated and 10 down-regulated genes, and 16 proteins showed more than 1.5-fold expression alteration except KDM4A, including 10 up-regulated and 6 down-regulated proteins. This dataset contains all raw data of RNA-seq and label-free quantitative proteomics described in this study.