Methyltransferase 22, Kin17 lysine (METTL22)

Methyltransferase 22, Kin17 lysine (METTL22) is a non-histone protein methyltransferase that specifically trimethylates the lysine-135 residue of the DNA/RNA-binding protein Kin17 (KIN, also known as KIN or KIN17) in vitro. Kin17 is involved in crucial cellular processes such as DNA replication, DNA repair, and RNA metabolism; methylation of Kin17 by METTL22 is thought to modulate its subcellular localization and functional activity, which may impact genome maintenance and cellular stress responses. METTL22 is part of the evolutionarily conserved methyltransferase-like (METTL) protein family, classified structurally by a characteristic seven-beta-strand domain supporting S-adenosylmethionine (SAM)-dependent methyltransferase activity. The physiological and disease-related functions of METTL22 are still emerging, and while methyltransferases targeting similar substrates have been implicated in cancer and other conditions, the direct role of METTL22 is not fully established. METTL22 is broadly expressed and is active primarily in the nucleus.

Other names

Methyltransferase-like protein 22METTL22C16orf68LP8272FLJ12433MGC2654methyltransferase like 22