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Fig. 1 | Cellular & Molecular Biology Letters

Fig. 1

From: The low-complexity domains of the KMT2D protein regulate histone monomethylation transcription to facilitate pancreatic cancer progression

Fig. 1

Structural and functional insights into the KMT2D protein. a Schematic representation of the domain structure for KMT2D protein. KMT2D contains two clusters of plant homeotic domains (PHDs) in the amino-terminal region. The second cluster can recognize unmethylated histone H4 tails. On the C terminus, FY-rich N-terminal (FYRN) and FYR C-terminal (FYRC) and an enzymatically active SET domain are closely connected to generate a functional and stable protein. A high mobility group I (HMG-I) binding motif (frequently found in transcription factors and cofactors) and a PHD domain are present in the protein sequences. The two domains of interest are indicated as LCD1 and LCD2. b–d Analyses of KMT2D, KMT2D LCD1, and KMT2D LCD2 using the PONDR database. KMT2D protein has two intrinsically disordered regions with multi-phosphorylation sites and a high proportion of proline and glutamine. e Analyses of KMT2D expression in pancreatic cancer (Tumor, n = 179) and normal tissue (Not-tumor, n = 171) based on previously published gene expression array data listed in The Cancer Genome Atlas (TCGA) database. In contrast to normal tissues, significant overexpression of KMT2D was found in pancreatic cancer tissues (p < 0.01)

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