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Background SMYD2 is protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53. It monomethylates K370 of p53 leading to decreased DNA-binding and consequently the lower transcriptional regulation activity of p53 (PIMID:17108971). Assay validation Based on the findings (PIMID:17108971), we developed SMYD2 cellular assay in which exogenous FLAG-tagged p53 is methylated by exogenous V5-tagged Read More …
Background GID4 is the substrate-recognition subunit of the CTLH E3 ubiquitin-protein ligase complex which has been shown to possess E3-ligase enzymatic activity (PIMID:31885576). GID4 was shown to bind proteins and peptides with a Pro/N-degron consisting of an unmodified N-terminal Pro and has the highest affinity for the peptide Pro-Gly-Leu-Trp (PIMID:29632410). In yeast Gid4 specifically targets Read More …
Background PRMT3 is type I protein arginine methyltransferase which mono- and asymmetrically dimethylates proteins, mainly in glycine and arginine-rich motifs (Fig.1, PIMID: 15175657). Fig.1. Mammalian PRMTs. There are 9 members and 3 types of the PRMT family. Type I, II and III PRMTs catalyze the formation of monomethyl arginines (Rme1). Type I PRMTs catalyze asymmetric arginine Read More …
Background PRMT6 is type I protein arginine methyltransferase which mono- and asymmetrically dimethylates histone and nonhistone proteins, mainly in glycine and arginine rich motifs (Fig.1). PRMT6 shows predominant nuclear localization and is implicated in the regulation of nuclear processes such as DNA repair and gene expression (PIMID: 11724789, 18079182). Fig.1. Mammalian PRMTs. There are 9 Read More …
Background PRMT4 (CARM1) is type I protein arginine methyltransferase which mono- or asymmetrically dimethylates proteins (Fig.1) within proline-methionine rich motives, that are involved in transcription, splicing and RNA processing such as H3R17, EP300, PABP1, CA150, BAF155, MED12 (PIMID:19150423). Fig.1. Mammalian PRMTs. There are 9 members and 3 types of the PRMT family. Type I, II Read More …
