n-methyltransferase

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. tRNA (guanine-N(7)-)-methyltransferase Protein, Brugia malayi, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 36.3 kDa and the accession number is A8NFF0.

METTL4 Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 61.5 kDa and the accession number is Q8N3J2.

METTL11A Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 25.5 kDa and the accession number is A0A024R8E4.

N6AMT1 (N-6 Adenine-Specific DNA Methyltransferase 1) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. This gene encodes an N(6)-adenine-specific DNA methyltransferase. It belongs to the eukaryotic archaeal PrmC-related family. The encoded enzyme may be involved in the methylation of release factor I during translation termination. N6AMT1 has a significant role in determining susceptibility to arsenic toxicity and carcinogenicity because of its specific activity in methylating MMAIII to DMA and other unknown mechanisms. N6AMT1 methylates the toxic inorganic arsenic (iAs) metabolite, monomethylarsonous acid (MMA), to the less toxic dimethylarsinic acid (DMA). N6AMT1 polymorphisms were associated with arsenic methylation in Andean women, independent of AS3MT.

Glycine N-Methyltransferase (GNMT) is a tetrameric cytosolic protein. GNMT catalyzes the synthesis of N-methylglycine from glycine using S-adenosylmethionine (AdoMet) as the methyl donor. It can affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine, playing an important role in maintaining normal AdoMet levels. GNMT is highly expressed in liver. As a major folate-binding protein, GNMT takes part in the detoxification pathway. Defects in GNMT are the cause of hypermethioninemia. the patients with this deficiency are mild hepatomegaly and chronic elevation of serum transaminases.

Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine. HNMT Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 41.1 kDa and the accession number is Q91VF2.

N-methyltransferase that catalyzes the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).

Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'. EEF2KMT Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 41.0 kDa and the accession number is Q96G04.

Associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Chromatin interaction is mediated via the binding to tri-methylated histone H3 at 'Lys-4' (H3K4me3). Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation. Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages including G1 S transition, S phase progression and mitotic entry. Recruited to E2F1 responsive promoters by HCFC1 where it stimulates tri-methylation of histone H3 at 'Lys-4' and transcriptional activation and thereby facilitates G1 to S phase transition. During myoblast differentiation, required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells.; Cellular ligand for NCR2 NKp44, may play a role as a danger signal in cytotoxicity and NK-cell-mediated innate immunity.

Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds. Catalyzes the N-methylation of tryptamine and structurally related compounds.

The guanine-N7 methyltransferase domain of vaccinia virus mRNA capping enzyme is a heterodimer composed of a catalytic subunit and a stimulatory subunit. Cap (guanine-N7) methylation is an essential step in eukaryal mRNA synthesis and a potential target for antiviral, antifungal, and antiprotozoal drug discovery.

GAMT is a methyltransferase which belongs to the class I-like SAM-binding methyltransferase superfamily. It contains one RMT2 (arginine N-methyltransferase 2-like) domain and is expressed in liver. GAMT converts guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects in GAMT are the cause of guanidinoacetate methyltransferase deficiency, which is an autosomal recessive disorder characterized by developmental delay regression, mental retardation, severe disturbance of expressive and cognitive speech, intractable seizures and movement disturbances, severe depletion of creatine phosphocreatine in the brain, and accumulation of guanidinoacetic acid in brain and body fluids.

METTL11A Protein, Human, Recombinant (GST) is expressed in E. coli expression system with GST tag. The predicted molecular weight is 52.2 kDa and the accession number is A0A024R8E4.

SMYD3 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.

HNMT (Histamine N-methyltransferase) is a Protein Coding gene. This gene encodes the first enzyme which is found in the cytosol and uses S-adenosyl-L-methionine as the methyl donor. HNMT, the major enzyme for the metabolism of histamine in the rat brain, is potently inhibited by 9-amino-1,2,3,4-tetrahydroacridine (tacrine). Methylation is an important pathway in the biotransformation of many drugs, neurotransmitters, and xenobiotic compounds. Histamine N-methyltransferase (HNMT) catalyzes the N tau-methylation of histamine and structurally related compounds. Histamine N-methyltransferase (HNMT) is believed to be the sole pathway for termination of the neurotransmitter action of histamine in the mammalian brain. That highlights the importance of the inclusion of HNMT for genetic testing of individuals presenting with intellectual disability.

SET and MYND domain-containing protein 3, also known as Zinc finger MYND domain-containing protein 1, SMYD3, and ZMYND, is a member of the histone-lysine methyltransferase family. SMYD3 contains one MYND-type zinc finger and one SET domain. SMYD3 is a histone H3 lysine-4-specific methyltransferase. It is expressed in skeletal muscles and testis. It is overexpressed in a majority of colorectal carcinoma (CRC) and hepatocellular carcinoma (HCC). SMYD3 plays an important role in transcriptional regulation in human carcinogenesis. It activates the transcription of a set of downstream genes. Of these downstream genes, there are several oncogenes and genes associated with cell adhesion (including those of N-Myc, CrkL, Wnt1b, L-selectin, CD31 and galectin-4), which have been shown to have effects on cell viability, adhesion, migration and metastasis. Increased SMYD3 expression is essential for the proliferation of breast cancer cells. SMYD3 may be a promising new target of therapeutic intervention for the treatment of cancers or other pathological processes associated with cell adhesion and migration.

Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure. ERG Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 56.6 kDa and the accession number is P11308.

Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-318'. EEF1AKMT2 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 32.9 kDa and the accession number is Q9D853.

Protein arginine N-methyltransferase 6, also known as Histone-arginine N-methyltransferase PRMT6, PRMT6, and HRMT1L6, is a member of the protein arginine N-methyltransferase family and PRMT6 subfamily. PRMT6 is highly expressed in kidney and testes. PRMT6 is known to catalyze the generation of asymmetric dimethylarginine in polypeptides. It has been implicated in human immunodeficiency virus pathogenesis, DNA repair, and transcriptional regulation. PRMT6 is known to methylate histone H3 Arg-2 (H3R2), and this negatively regulates the lysine methylation of H3K4 resulting in gene repression. PRMT6 plays a key role in coupling process by functioning as a transcriptional coactivator that can regulate alternative splicing. PRMT6 coactivates the progesterone, glucocorticoid and oestrogen receptors in luciferase reporter assays in a hormone-dependent manner. Small interfering RNA (siRNA) oligonucleotide duplex knockdown of PRMT6 disrupts oestrogen-stimulated transcription of endogenous GREB1 and progesterone receptor in MCF-7 breast cancer cells. Neutralizing the activity of PRMT6 could inhibit tumor progression and may be of cancer therapeutic significance.

Histone-lysine N-methyltransferase SUV42H2, also known as Suppressor of variegation 4-2 homolog 2, Su(var)4-2 homolog 2, Lysine N-methyltransferase 5C, SUV42H2 and KMT5C, is nucleus protein that belongs to the histone-lysine methyltransferase family and Suvar4-2 subfamily. SUV42H2 is a histone methyltransferase that specifically trimethylates 'Lys-2' of histone H4. H4 'Lys-2' trimethylation represents a specific tag for epigenetic transcriptional repression. SUV42H2 mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV42H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2). FRAP experiments reveal that SUV42H2 is strongly associated with pericentric heterochromatin. The fraction of SUV42H2 captured and characterized by TAP MS is a soluble fraction which may be in a stable association with HP1. SUV42H2 may be recruited to heterochromatin in association with HP1, and stably maintained at its heterochromatin sites in an HP1-independent fashion.

tRNA (guanine-N(7)-)-methyltransferase, also known as Methyltransferase-like protein 1, tRNA (m7G46)-methyltransferase and METTL1, is a nucleus protein that belongs to the methyltransferase superfamily and TrmB family. METTL1 gene has been identified by its sequence similarity to the yeast ORF YDL21w. The human cDNA and the genomic structure of METTL1 have been analyzed. The transcript contains 1292 nucleotides and codes for a protein of 276 amino acids. The METTL1 gene product shows high sequence similarities to putative proteins from mouse, Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, and yeast (39.8% identity between all six species). Computer analyses of the deduced protein sequence reveal two highly conserved amino acid motifs, one of which is typical for methyltransferases. Both motifs are also present in hypothetical proteins from eubacteria. Disruption of the homologous yeast ORF YDL21w shows that the gene is at least not essential for vegetative growth in Saccharomyces cerevisiae.

Histone-lysine N-methyltransferase SETD7, also known as SET domain containing (lysine methyltransferase) 7, SET7 9, Histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, and SETD7, is a member of the histone-lysine methyltransferase family and SET7 subfamily. SETD7 is widely expressed and expressed in pancreatic islets. SETD7 contains three MORN repeats and one SET domain. SETD7 plays a central role in the transcriptional activation of genes such as collagenase or insulin. As a protein lysine methyltransferase (PKMT), SETD7 also has methyltransferase activity toward non-histone proteins such as p53 TP53, TAF1, and possibly TAF7 by recognizing and binding in substrate proteins. The mono-methyltransferase activity of SETD7 is achieved by disrupting the formation at near-attack conformations for the dimethylation reaction. SETD7 is also a novel coactivator of NF-kappaB and plays a role in inflammation and diabetes.

Histone-lysine N-methyltransferase, H3 lysine-79 specific, also known as Histone H3-K79 methyltransferase, DOT1-like protein, Lysine N-methyltransferase 4 and DOT1L, is a nucleus protein which belongs to theDOT1 family. In contrast to other lysine histone methyltransferase, DOT1L does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones. DOT1L is an histone methyltransferase. It methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. DOT1L binds to DNA. Methylation of lysine 79 on histone H3 (H3K79) is mediated by DOT1L. It is involved in the regulation of telomeric silencing, development, cell cycle checkpoint and transcription. Mass spectrometry of the DOT1L-containing complex revealed that AF9, ENL and NPM1 were shown to be major DOT1L-interacting proteins. DOT1L might control AF9- and ENL-mediated transcription, regulate RNA processing, and function as a histone chaperone in a NPM1-dependent manner.

Protein arginine methyltransferase 3, also known as PRMT3, is one of four type I protein arginine methyltransferases (PRMT) that in humans is encoded by the PRMT3 gene. Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of PRMTs. The modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. In human cells, the PRMT family consists of eight canonical members. PRMTs have been classified into two groups based on the end product. Certain PRMTs display different subcellular localization in different cell types, implicating cell- and tissue-specific mechanisms for regulating PRMT functions. PRMT3 is unique in that its N-terminus harbours a C2H2 zinc-finger domain that is proposed to confer substrate specificity. Besides, PRMT3 is the only type I enzyme that is restricted to the cytoplasm. A large proportion of this cystosolic PRMT3 is found associated with ribosomes. It is tethered to the ribosomes through its interaction with rpS2, which is also its substrate.