Histone-lysine N-methyltransferase PRDM16 (PRDM16)

Histone-lysine N-methyltransferase PRDM16 (PRDM16) is an epigenetic and transcriptional regulator that belongs to the PRDM family and contains a PR (PRDI-BF1 and RIZ1 homology) domain with intrinsic histone methyltransferase activity, specifically catalyzing mono- and di-methylation of lysine 4 on histone H3 (H3K4)[1][2]. It is a master regulator of cell fate and differentiation, crucial for development of brown/beige adipose tissue, maintenance of hematopoietic and neural stem cells, and suppression of MLL-rearranged leukemia through repression of the HOXA gene cluster via activation of GFI1b[1][2][3]. PRDM16 acts as both transcriptional coactivator and corepressor, interacting with various transcription factors and chromatin modification complexes, influencing multiple developmental, metabolic, and disease processes across tissues[1][2][3]. Its dysregulation is implicated in cancer (notably as a tumor suppressor in acute myeloid leukemia), cardiovascular disease, metabolic syndrome, and disorders of stem cell maintenance.

Other names

PR/SET domain 16KIAA1675MEL1PFM13MDS1/EVI1-like gene 1MGC166915KMT8FPR domain zinc finger protein 16PR domain-containing protein 16Transcription factor MEL1CMD1LLLVNC8

Epigenetic regulation via H3K4 methylation, altering chromatin structure and gene expression. Coactivation with transcription factors (e.g., PPAR-γ, PGC-1α, MED1) and repression through other protein interactions.