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http://purl.uniprot.org/citations/11724789http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11724789http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11724789http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11724789http://www.w3.org/2000/01/rdf-schema#comment"Protein arginine methylation is a prevalent posttranslational modification in eukaryotic cells that has been implicated in signal transduction, the metabolism of nascent pre-RNA, and the transcriptional activation processes. In searching the human genome for protein arginine N-methyltransferase (PRMT) family members, a novel gene has been found on chromosome 1 that encodes for an apparent methyltransferase, PRMT6. The polypeptide chain of PRMT6 is 41.9 kDa consisting of a catalytic core sequence common to other PRMT enzymes. Expressed as a glutathione S-transferase fusion protein, PRMT6 demonstrates type I PRMT activity, capable of forming both omega-N(G)-monomethylarginine and asymmetric omega-N(G),N(G)-dimethylarginine derivatives on the recombinant glycine- and arginine-rich substrate in a processive manner with a specific activity of 144 pmol methyl groups transferred min(-1) mg(-1) enzyme. A comparison of substrate specificity reveals that PRMT6 is functionally distinct from two previously characterized type I enzymes, PRMT1 and PRMT4. In addition, PRMT6 displays automethylation activity; it is the first PRMT to do so. This novel human PRMT, which resides solely in the nucleus when fused to the green fluorescent protein, joins a family of enzymes with diverse functions within cells."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m108786200"xsd:string
http://purl.uniprot.org/citations/11724789http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m108786200"xsd:string
http://purl.uniprot.org/citations/11724789http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m108786200"xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Bedford M.T."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Bedford M.T."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Lee J."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Lee J."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Clarke S."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Clarke S."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Frankel A."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Frankel A."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Branscombe T.L."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Branscombe T.L."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Yadav N."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/author"Yadav N."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/pages"3537-3543"xsd:string
http://purl.uniprot.org/citations/11724789http://purl.uniprot.org/core/pages"3537-3543"xsd:string