ArticleProtein science : a publication of the Protein Society2024
Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Update of the Methyltransferase Gene Family: Classification, Evolution and Biological Functions.Human genomics · 2026Review
- E2F1 K117 methylation by SETD6 disrupts BRD4-E2F1 binding and modulates E2F1 chromatin binding and gene regulation in prostate cancer cells.Nucleic acids research · 2026Article
- HemK class methyltransferase, a protein translation regulator: role in growth, development and phenotypic diversity.Molecular biology reports · 2025Review
- Mechanisms of Substrate Recognition by the Multispecific Protein Lysine Methyltransferase SETD6.Life (Basel, Switzerland) · 2025Article
- Orchestrating epigenetics: a comprehensive review of the methyltransferase SETD6.Experimental & molecular medicine · 2025Review
- CytosolicProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The HEMK2 protein methyltransferase has been described as glutamine methyltransferase catalyzing ERF1-Q185me1 and lysine methyltransferase catalyzing H4K12me1. Methylation of two distinct target residues is unique for this class of enzymes. To understand the specific catalytic adaptations of HEMK2 allowing it to master this chemically challenging task, we conducted a detailed investigation of the substrate sequence specificities of HEMK2 for Q- and K-methylation. Our data show that HEMK2 prefers methylation of Q over K at peptide and protein level. Moreover, the ERF1 sequence is strongly preferred as substrate over the H4K12 sequence. With peptide SPOT array methylation experiments, we show that Q-methylation preferentially occurs in a G-Q-X
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Registered trials
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