Other names published for NPL3: MTR13, MTS1, NOP3, NAB1, YDR432W
NPL3 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
NPL3 - Protein Sequence Features (23)
| Reference | Other Genes Addressed |
|---|---|
| Hart-Smith G, et al. (2012) Enhanced methylarginine characterization by post-translational modification-specific targeted data acquisition and electron-transfer dissociation mass spectrometry. J Am Soc Mass Spectrom 23(8):1376-89 | |
| Rajyaguru P, et al. (2012) Scd6 Targets eIF4G to Repress Translation: RGG Motif Proteins as a Class of eIF4G-Binding Proteins. Mol Cell 45(2):244-54 | |
| Kerr SC, et al. (2011) The ccr4-not complex interacts with the mRNA export machinery. PLoS One 6(3):e18302 | |
| Marino SM, et al. (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21 | |
| Estrella LA, et al. (2009) The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae. J Mol Biol 394(3):410-22 | |
| McBride AE, et al. (2009) Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function. Nucleic Acids Res 37(13):4322-30 | |
| Deka P, et al. (2008) Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals. J Mol Biol 375(1):136-50 | |
| Dermody JL, et al. (2008) Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation. PLoS ONE 3(9):e3273 | |
| Skrisovska L and Allain FH (2008) Improved segmental isotope labeling methods for the NMR study of multidomain or large proteins: application to the RRMs of Npl3p and hnRNP L. J Mol Biol 375(1):151-64 | |
| Lukasiewicz R, et al. (2007) The RGG domain of Npl3p recruits Sky1p through docking interactions. J Mol Biol 367(1):249-61 | |
| Kim Guisbert K, et al. (2005) Functional specificity of shuttling hnRNPs revealed by genome-wide analysis of their RNA binding profiles. RNA 11(4):383-93 | |
| McBride AE, et al. (2005) Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions. J Biol Chem 280(35):30888-98 | |
| Gilbert W, et al. (2001) Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation. RNA 7(2):302-13 | |
| Zahler AM (2001) Tale of a tail kinase. Nat Struct Biol 8(2):104-6 | |
| Yun CY and Fu XD (2000) Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae. J Cell Biol 150(4):707-18 | |
| Frankel A and Clarke S (1999) RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases. Biochem Biophys Res Commun 259(2):391-400 | |
| Liu Y, et al. (1999) A Crm1p-independent nuclear export path for the mRNA-associated protein, Npl3p/Mtr13p. Proc Natl Acad Sci U S A 96(12):6739-44 | |
| Senger B, et al. (1998) Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p. EMBO J 17(8):2196-207 | |
| Singleton DR, et al. (1995) A yeast protein that bidirectionally affects nucleocytoplasmic transport. J Cell Sci 108 ( Pt 1):265-72 | |
| Birney E, et al. (1993) Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res 21(25):5803-16 | |
| Ellis EM and Reid GA (1993) The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding protein involved in mitochondrial protein targeting. Gene 132(2):175-83 | |
| Bossie MA, et al. (1992) A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast. Mol Biol Cell 3(8):875-93 | |
| Russell ID and Tollervey D (1992) NOP3 is an essential yeast protein which is required for pre-rRNA processing. J Cell Biol 119(4):737-47 |



