Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein ArginineN-Methyltransferase 1
- 1 January 2003
- journal article
- Published by American Society for Cell Biology (ASCB) in Molecular Biology of the Cell
- Vol. 14 (1) , 274-287
- https://doi.org/10.1091/mbc.e02-08-0484
Abstract
RNA binding proteins often contain multiple arginine glycine repeats, a sequence that is frequently methylated by protein arginine methyltransferases. The role of this posttranslational modificatio...Keywords
This publication has 57 references indexed in Scilit:
- Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone ReceptorScience, 2001
- Identification of Sam68 Arginine Glycine-rich Sequences Capable of Conferring Nonspecific RNA Binding to the GSG DomainPublished by Elsevier ,2001
- State of the ArgCell, 2001
- Role of protein methylation in chromatin remodeling and transcriptional regulationOncogene, 2001
- The C-terminal RG Dipeptide Repeats of the Spliceosomal Sm Proteins D1 and D3 Contain Symmetrical Dimethylarginines, Which Form a Major B-cell Epitope for Anti-Sm AutoantibodiesJournal of Biological Chemistry, 2000
- Arginine Methylation Inhibits the Binding of Proline-rich Ligands to Src Homology 3, but Not WW, DomainsJournal of Biological Chemistry, 2000
- Regulation of Transcription by a Protein MethyltransferaseScience, 1999
- RNase Treatment of Yeast and Mammalian Cell Extracts Affects in Vitro Substrate Methylation by Type I Protein Arginine N-MethyltransferasesBiochemical and Biophysical Research Communications, 1999
- The Mammalian Immediate-early TIS21 Protein and the Leukemia-associated BTG1 Protein Interact with a Protein-arginine -MethyltransferaseJournal of Biological Chemistry, 1996
- An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosisNature, 1994