Calmodulin-lysine N-methyltransferase (CAMKMT)

Calmodulin-lysine N-methyltransferase (CAMKMT) is a class I protein methyltransferase that specifically catalyzes the trimethylation of lysine 115 on calmodulin, a key mediator of calcium-dependent cell signaling[1][3][4][6]. CAMKMT contains an S-adenosyl-methionine (AdoMet) binding motif and is highly conserved, playing a pivotal regulatory role by modulating post-translational conformation and interaction properties of calmodulin[1][3]. Through methylation, CAMKMT may influence diverse downstream cellular processes such as enzyme regulation, cytoskeletal organization, and transcriptional control, integrating calcium signaling with cell stress responses and developmental regulation[1][3][4]. The gene is known to be deleted in certain congenital syndromes, including hypotonia-cystinuria syndrome (as part of 2p21 deletion syndrome) in humans; disruption can contribute to complex disease phenotypes[3][4]. No drugs specifically targeting CAMKMT are currently known, and no unique safety or toxicity challenges have been reported regarding this enzyme as a therapeutic target[1][4][6].

Other names

CAMKMTC2orf34CLNMTCaM KMTKMT

Methylation of lysine residue (specifically Lys-115) on calmodulin, affecting post-translational modification status and thereby altering functional properties of calmodulin