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http://purl.uniprot.org/citations/17925405http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17925405http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17925405http://www.w3.org/2000/01/rdf-schema#comment"Human protein arginine methyltransferase PRMT8 has been recently described as a type I enzyme in brain that is localized to the plasma membrane by N-terminal myristoylation. The amino acid sequence of human PRMT8 is almost 80% identical to human PRMT1, the major protein arginine methyltransferase activity in mammalian cells. However, the activity of a recombinant PRMT8 GST fusion protein toward methyl-accepting substrates is much lower than that of a GST fusion of PRMT1. We show here that both His-tagged and GST fusion species lacking the initial 60 amino acid residues of PRMT8 have enhanced enzymatic activity, suggesting that the N-terminal domain may regulate PRMT8 activity. This conclusion is supported by limited proteolysis experiments showing an increase in the activity of the digested full-length protein, consistent with the loss of the N-terminal domain. In contrast, the activity of the N-terminal truncated protein was slightly diminished by limited proteolysis. Significantly, we detect automethylation at two sites in the N-terminal domain, as well as binding sites for SH3 domain-containing proteins. We suggest that the N-terminal domain may function as an autoregulator that may be displaced by interaction with one or more physiological inducers."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m704650200"xsd:string
http://purl.uniprot.org/citations/17925405http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m704650200"xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Bedford M.T."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Bedford M.T."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Webb K."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Webb K."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Cheng D."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Cheng D."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Clarke S.G."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Clarke S.G."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Sayegh J."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/author"Sayegh J."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/pages"36444-36453"xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/pages"36444-36453"xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/title"Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/title"Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain."xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17925405http://purl.uniprot.org/core/volume"282"xsd:string