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Background SMYD3 (SET and MYND domain containing protein 3) is a member of the SMYD lysine methylase family and plays an important role in lysine methylation of various histone and non-histone proteins such as H2A.Z.1-K101, VEDFR1-K831, MAP3K2-K260, HER2-K175 or AKT1-K14. SMYD3 is overexpressed in numerous human tumors and is a potential therapeutic target and prognostic Read More …
Background PRMT8 is type I protein arginine methyltransferase expressed mainly in the brain, which mono- and asymmetrically dimethylates histone and nonhistone proteins (Fig.1). It shares over 80% of amino acid sequence homology with PRMT1. At the N-terminus, it harbors a glycine that can be myristoylated which results in its plasma membrane localization (PIMID: 16051612). Fig.1. Read More …
Background PRDM9 (PR domain-containing protein 9) contains a subclass of the SET (PR/SET) domain that trimethylates histone 3 on lysine 4 and 36 (PIMID:24095733). It is expressed mainly in germ cells playing an important role in meiotic recombination (PIMID:27362481). Its aberrant expression has also been associated with genomic instability in cancer (PIMID:30341163). Assay Validation Consistent Read More …
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 …
Background PRMT5 in complex with the WD-repeat protein MEP50 is the major type II protein arginine methyltransferase responsible for mono- and symmetric dimethylation of arginine in a great variety of proteins (Fig.1). It plays a critical role in diverse cellular processes such as genome organization, transcription, translation, differentiation, cell cycle, DNA repair, RNA processing, and Read More …
Background The mammalian MYST1 is a member of the MYST family of histone acetyltransferases and is the primary enzyme that catalyzes the acetylation of histone H4 on lysine 16 (H4K16). Acetylation of K16 is a prevalent mark associated with chromatin decondensation. MYST1 has been shown to play an essential role in embryonic formation and development, Read More …
