| http://purl.uniprot.org/citations/10441131 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10441131 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10441131 | http://www.w3.org/2000/01/rdf-schema#comment | "The cellular location and substrate specificity of the catalytic subunit (C) of protein phosphatase 2A (PP2A) depend on its interaction with A and B subunits. The distribution of epitope-tagged wild-type or mutated C subunits was studied by transient expression in COS-7 cells. Wild-type tagged C expressed at low levels formed ABC trimer and AC dimer like the endogenous C. Single mutations of C at the site of phosphorylation (Y307F) or carboxymethylation (L309Q) resulted in recovery of only AC dimer. Double mutation of both residues resulted in association of C with alpha 4 protein (alpha 4), a novel subunit of PP2A, instead of with A and B subunits. Thus, the distribution of C between ABC trimer, AC dimer, and alpha 4C complexes can be affected by modifications of the C-terminal residues. The alpha 4 protein is a homologue of the yeast Tap42 protein that functions downstream of the TOR protein to regulate protein synthesis. Transient overexpression of FLAG-alpha 4 resulted in increased dephosphorylation of elongation factor 2, but had no effect on phosphorylation of either p70S6 kinase or PHAS-I (eIF4E-BP). Signals that affect phosphorylation or methylation of the C subunit of PP2A may promote subunit exchange and direct phosphatase activity to specific intracellular substrates."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi990902g"xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi990902g"xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/author | "Murata K."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/author | "Murata K."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/author | "Nairn A.C."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/author | "Nairn A.C."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/author | "Brautigan D.L."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/author | "Brautigan D.L."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/author | "Chung H."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/author | "Chung H."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/pages | "10371-10376"xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/pages | "10371-10376"xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/title | "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/title | "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2."xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/volume | "38"xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://purl.uniprot.org/core/volume | "38"xsd:string |
| http://purl.uniprot.org/citations/10441131 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10441131 |
| http://purl.uniprot.org/citations/10441131 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10441131 |