Histone-lysine N-methyltransferase MECOM (MECOM)

Histone-lysine N-methyltransferase MECOM (MDS1 and EVI1 complex locus, MECOM) is a nuclear protein functioning as both a transcriptional regulator and a histone modification enzyme, specifically capable of methylating lysine 9 on histone H3 (H3K9)[1][9]. It contains multiple zinc finger domains and is involved in development, hematopoiesis, cell proliferation, differentiation, and apoptosis, playing key roles in both normal and malignant states. Alterations of MECOM, particularly gene rearrangements or overexpression (EVI1 isoform), are strongly associated with myeloid leukemias, where its upregulation acts as an oncogenic driver and a marker for poor prognosis. As a histone methyltransferase, it modulates chromatin state and gene expression, with its dysregulation contributing to altered transcriptional programs in cancer and congenital diseases. Currently, while no approved therapies directly target MECOM, it is a therapeutic focus for research targeting epigenetic abnormalities in hematologic malignancies[1][2][9][10].

Other names

MDS1 and EVI1 complex locusEVI1MDS1MDS1-EVI1PRDM3KMT8EEcotropic virus integration site 1 protein homologMyelodysplasia syndrome-associated protein 1PR domain 3AML1-EVI-1EVI-1AML1-EVI1 fusion proteinMDS1 and EVI1 complex locus proteinZinc finger protein Evi1Histone-lysine N-methyltransferase MECOM

Inhibition of transcriptional activity or methyltransferase function (hypothetical, as no direct inhibitors are clinically established) - Modulation of chromatin state and gene expression via epigenetic mechanisms