Methyltransferase-like protein 13 (METTL13)

Methyltransferase-like protein 13 (METTL13) is a unique dual-function methyltransferase enzyme that specifically catalyzes the methylation of both the N terminus and lysine 55 of eukaryotic translation elongation factor 1 alpha (eEF1A)[1][2][3][4]. It consists of two structurally distinct methyltransferase domains, with one targeting the eEF1A N terminus and the other lysine 55, leading to two different methylations critical for modulating translation[1][2][4]. METTL13-mediated methylation of eEF1A alters the rate of protein synthesis globally and modulates codon-specific translation efficiency[1][3][4]. Although expressed at faint levels in most normal tissues, METTL13 is frequently overexpressed in several cancers, associating it with potential oncogenic roles[2][3]. Its aberrant expression has been documented in tumorigenesis, while mutations in the locus are linked to deafness phenotypes[5]. METTL13's enzyme specificity and regulatory impact on translation make it a protein of interest for cancer biology and therapeutic targeting, but detailed therapeutic exploitation and drug interaction profiles have not yet been documented[2][3].\n\n**Notes:** \n- No known direct small-molecule drugs or inhibitors for METTL13 are currently documented in the literature as of September 2025[2][3].\n- Current knowledge is based on structural biology, cancer biology, and disease-modifier research; further drug discovery and biomarker validation is ongoing[1][2][3].

Other names

eEF1A lysine and N-terminal methyltransferaseeEF1A-KNMTFEATCGI-01EEF1AKNMTfaint expression in normal tissues aberrant overexpression in tumors5630401D24RikDFNB26DFNB26MDFNM1KIAA0859antiapoptotic protein FEAT