PRMT8 S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer. Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily. Brain-specific. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 2.1.1.-; Methyltransferase; Methyltransferase, protein arginine
Chromosomal Location of human Ortholog: 12p13.32
Cellular Component:  cytoplasmic side of plasma membrane; nucleus; plasma membrane
Molecular Function:  enzyme binding; histone arginine N-methyltransferase activity; identical protein binding; protein binding; protein homodimerization activity; protein-arginine omega-N asymmetric methyltransferase activity; protein-arginine omega-N monomethyltransferase activity; S-adenosyl-L-methionine binding; S-adenosylmethionine-dependent methyltransferase activity
Biological Process:  histone methylation; peptidyl-arginine methylation; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; protein homooligomerization; protein methylation; regulation of protein binding
Reference #:  Q9NR22 (UniProtKB)
Alt. Names/Synonyms: ANM8; arginine methyltransferase 8; Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4; HMT1 hnRNP methyltransferase-like 3; HMT1 hnRNP methyltransferase-like 4; HRMT1L3; HRMT1L4; PRMT8; protein arginine methyltransferase 8; protein arginine N-methyltransferase 4; Protein arginine N-methyltransferase 8
Gene Symbols: PRMT8
Molecular weight: 45,291 Da
Basal Isoelectric point: 6.47  Predict pI for various phosphorylation states
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Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene