|Other Names||Protein arginine N-methyltransferase 1, 211-, Histone-arginine N-methyltransferase PRMT1, Interferon receptor 1-bound protein 4, PRMT1, HMT2, HRMT1L2, IR1B4|
|Target/Specificity||The synthetic peptide sequence is selected from aa 23-40 of human PRMT1.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||HMT2, HRMT1L2, IR1B4|
|Function||Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed:25284789). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789).|
|Cellular Location||Nucleus. Nucleus, nucleoplasm. Cytoplasm, cytosol. Note=Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity).|
|Tissue Location||Widely expressed.|
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Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins, IL enhancer binding factor, nuclear factors, cell cycle proteins, signal transduction proteins, apoptosis proteins, and viral proteins. The mammalian PRMT family currently consists of 7 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all 7 PRMT members have been developed.
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