PRMT4 Antibody – Rabbit Polyclonal

This gene belongs to the protein arginine methyltransferase (PRMT) family. The encoded enzyme catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. The enzyme acts specifically on histones and other chromatin-associated proteins and is involved in regulation of gene expression. The enzyme may act in association with other proteins or within multi-protein complexes and may play a role in cell type-specific functions and cell lineage specification. A related pseudogene is located on chromosome 9. [provided by RefSeq, Aug 2013]

CARM1: a protein arginine methyltransferase that methylates histones and other proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginine residues. A key epigenetic regulator of hematopoiesis affecting multiple lineages. Recruited to promoters upon gene activation together with histone acetyltransferases from P300 and p160 families, methylates histone H3 at R17 (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2 activation, acts synergically with P300 and either one of the p160 histone acetyltransferases SRC1, NCoA2 and SRC-3 or CTNNB1 to activate transcription. During myogenic transcriptional activation, acts together with SRC-3 as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53 transcriptional activation. Methylates P300, both at R 2142, which may loosen its interaction with NCoA2, and at R580 and R604 in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Methylates RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA- stabilizing properties and the half-life of their target mRNAs. Interacts with the C-terminus of NCoA2, SRC-3 and SRC1. Part of a complex consisting of CARM1, P300 and NCoA2. Interacts with FLII, TP53, myogenic factor MEF2, P300, TRIM24, CREBBP and CTNNB1. Identified in a complex containing CARM1, TRIM24 and NCoA2. Interacts with SRC3. Interacts with SNRPC. Interacts with NR1H4. Interacts with RELA. Interacts with HTLV-1 Tax-1. Overexpressed in prostate adenocarcinomas and high-grade prostatic intraepithelial neoplasia. Methylation of H3R17 (H3R17me) by CARM1 is stimulated by preacetylation of H3 K18 (H3K18ac) H3 K23 (H3K23ac) by EP300 and blocked by citrullination of H3 R17 (H3R17ci) by PADI4. Belongs to the protein arginine N-methyltransferase family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 2.1.1.125; Methyltransferase, protein arginine; Methyltransferase; Nuclear receptor co-regulator

Chromosomal Location of Human Ortholog: 19p13.2

Cellular Component: nucleoplasm; cytoplasm; nucleus; cytosol

Molecular Function: histone methyltransferase activity; protein-arginine omega-N asymmetric methyltransferase activity; protein binding; protein-arginine N-methyltransferase activity; protein homodimerization activity; ligand-dependent nuclear receptor transcription coactivator activity; transcription coactivator activity; histone-arginine N-methyltransferase activity; beta-catenin binding; protein methyltransferase activity

Biological Process: regulation of estrogen receptor signaling pathway; establishment and/or maintenance of chromatin architecture; response to cAMP; estrogen receptor signaling pathway; transcription, DNA-dependent; viral reproduction; pathogenesis; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; cellular lipid metabolic process; histone methylation; regulation of transcription, DNA-dependent; positive regulation of cell proliferation; positive regulation of fat cell differentiation; negative regulation of protein binding