SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol. Cell 15, 57–67 (2004). CAS PubMed Google Scholar Pasini, D., Bracken, A. P., Jensen, M
and class V-like SAM binding methyltransferase superfamily. SETD2 consists of several domains, including the associated with SET (AWS) domain; the SET domain; the post-SET domain; the locus control region (LCR); the WW domain, which binds to a proline-rich motif of a ...
Whereas the first MTase domain of METTL13 catalyzes lysine methylation of eEF1A, the second MTase domain (dark blue) is an eEF1A N-terminal MTase. 7BS, seven-β-strand; eEF1A, eukaryotic translation elongation factor 1α; KMT, lysine-specific MTase; METTL, methyltransferase-like; MTase, ...
and class V-like SAM binding methyltransferase superfamily. SETD2 consists of several domains, including the associated with SET (AWS) domain; the SET domain; the post-SET domain; the locus control region (LCR); the WW domain, which binds to a proline-rich motif of a ...
Here we show that mammalian VCP is trimethylated on Lys315 in a variety of cell lines and tissues, and that the previously uncharacterized protein METTL21D (denoted here as VCP lysine methyltransferase, VCP-KMT) is the responsible enzyme. VCP methylation was abolished in three human VCP- KMT ...
Here we show that the putative human Class I MTase METTL21D specifically catalyses the trimethylation of Lys315 in VCP in vitro, and the enzyme was thus named VCP-lysine methyltransferase (VCP-KMT). Moreover, this previously unknown VCP modification is present in mouse tissues and human cell ...