| http://purl.uniprot.org/citations/9858543 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9858543 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9858543 | http://www.w3.org/2000/01/rdf-schema#comment | "The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. The underlying ubiquitin-dependent proteolytic system, called the N-end rule pathway, is organized hierarchically: N-terminal aspartate and glutamate (and also cysteine in metazoans) are secondary destabilizing residues, in that they function through their conjugation, by arginyl-tRNA-protein transferase (R-transferase), to arginine, a primary destabilizing residue. We isolated cDNA encoding the 516-residue mouse R-transferase, ATE1p, and found two species, termed Ate1-1 and Ate1-2. The Ate1 mRNAs are produced through a most unusual alternative splicing that retains one or the other of the two homologous 129-bp exons, which are adjacent in the mouse Ate1 gene. Human ATE1 also contains the alternative 129-bp exons, whereas the plant (Arabidopsis thaliana) and fly (Drosophila melanogaster) Ate1 genes encode a single form of ATE1p. A fusion of ATE1-1p with green fluorescent protein (GFP) is present in both the nucleus and the cytosol, whereas ATE1-2p-GFP is exclusively cytosolic. Mouse ATE1-1p and ATE1-2p were examined by expressing them in ate1Delta Saccharomyces cerevisiae in the presence of test substrates that included Asp-betagal (beta-galactosidase) and Cys-betagal. Both forms of the mouse R-transferase conferred instability on Asp-betagal (but not on Cys-betagal) through the arginylation of its N-terminal Asp, the ATE1-1p enzyme being more active than ATE1-2p. The ratio of Ate1-1 to Ate1-2 mRNA varies greatly among the mouse tissues; it is approximately 0.1 in the skeletal muscle, approximately 0.25 in the spleen, approximately 3.3 in the liver and brain, and approximately 10 in the testis, suggesting that the two R-transferases are functionally distinct."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.19.1.182"xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.19.1.182"xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/author | "Varshavsky A."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/author | "Varshavsky A."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/author | "Kashina A.S."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/author | "Kashina A.S."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/author | "Kwon Y.T."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/author | "Kwon Y.T."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/pages | "182-193"xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/pages | "182-193"xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/title | "Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/title | "Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway."xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/volume | "19"xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://purl.uniprot.org/core/volume | "19"xsd:string |
| http://purl.uniprot.org/citations/9858543 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9858543 |
| http://purl.uniprot.org/citations/9858543 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9858543 |
| http://purl.uniprot.org/citations/9858543 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9858543 |
| http://purl.uniprot.org/citations/9858543 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9858543 |