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

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.