ID:ANM5_HUMAN DESCRIPTION: RecName: Full=Protein arginine N-methyltransferase 5; EC=2.1.1.-; AltName: Full=72 kDa ICln-binding protein; AltName: Full=Histone-arginine N-methyltransferase PRMT5; EC=2.1.1.125; AltName: Full=Jak-binding protein 1; AltName: Full=Shk1 kinase-binding protein 1 homolog; Short=SKB1 homolog; Short=SKB1Hs; Contains: RecName: Full=Protein arginine N-methyltransferase 5, N-terminally processed; FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation. CATALYTIC ACTIVITY: S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. ENZYME REGULATION: Activity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment. SUBUNIT: Forms, at least, homodimers and homotetramers. Interacts with PRDM1 (By similarity). Component of the methylosome, a 20S complex containing at least pICLn, PRMT1/SKB1 and MEP50. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Also interacts with Sm proteins, JAK2, SSTR1 and SUPT5H. Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPR5/C17orf79; promoting its recruitment on histone H4. Interacts with RPS10. Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation. Interacts with BRAF and with active RAF1. Interacts with HOXA9. Interacts with SRGAP2. INTERACTION: P62805:HIST2H4B; NbExp=3; IntAct=EBI-351098, EBI-302023; O75044:SRGAP2; NbExp=4; IntAct=EBI-351098, EBI-1051034; SUBCELLULAR LOCATION: Cytoplasm. Nucleus. TISSUE SPECIFICITY: Ubiquitous. PTM: Disulfide bonds and non-covalent association mediate homooligomers formation. SIMILARITY: Belongs to the protein arginine N-methyltransferase family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on O14744
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
