HeLa cell nuclear extracts contain a protein reactive with antibodies against PRP8, a polypeptide essential for pre-mRNA splicing in yeast and a specific component of the yeast U5 small nuclear ribonucleoprotein (snRNP) [Lossky, M., Anderson, G. J., Jackson, S. P. & Beggs, J. (1987) Cell 51, 1019-1026]. The mammalian protein appears as a doublet at approximately 200 kDa, smaller than the 260-kDa yeast protein, and possesses an Sm epitope as determined by immunoblotting. Its association with a snRNP of the Sm class other than U1 or U2 is indicated by its immunoprecipitation by anti-Sm and anti-trimethylguanosine antibodies but not by anti-(U1) or anti-(U2) RNP sera. Gradient fractionation of splicing extracts demonstrates that the 200-kDa protein is a component of the U4/5/6 snRNP complex and of U5 snRNPs. It is also present in affinity-purified spliceosomes.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Annotation Extension||Reference|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Assay||Construct||Conditions||Strain Background||Reference|