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4g56
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g56 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g56 RCSB], [http://www.ebi.ac.uk/pdbsum/4g56 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g56 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g56 RCSB], [http://www.ebi.ac.uk/pdbsum/4g56 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ANM5_XENLA ANM5_XENLA]] 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; such methylation being required for the assembly and biogenesis of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates the arginine in the motif G-R-G-X-G in its substrates histone H2A, H2AFX and H4, producing both monomethylated and symmetrically dimethylated 'Arg-3'. Methylates nucleoplasmin at 'Arg-192', producing both monomethylated and symmetrically dimethylated 'Arg-192'. Involved in the DNA replication checkpoint. Promotes entry into mitosis by promoting the proteasomal degradation of wee2-a. [[http://www.uniprot.org/uniprot/MEP50_XENLA MEP50_XENLA]] Non-catalytic component of the 20S prmt5-containing methyltransferase complex, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. Required for normal prmt5 methyltransferase activity. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 11:19, 25 December 2014
Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis
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