Results
Your Query
▶
▶
| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/2569467 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2569467 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2569467 | http://www.w3.org/2000/01/rdf-schema#comment | "Elongation Factor 1 alpha (EF-1 alpha), an important eukaryotic translation factor, transports charged aminoacyl-tRNA from the cytosol to the ribosomes during poly-peptide synthesis. Metabolic radiolabeling with [3H] ethanolamine shows that, in all cells examined, EF-1 alpha is the major radiolabeled protein. Radiolabeled EF-1 alpha has an apparent Mr = 53,000 and a basic isoelectric point. It is cytosolic and does not contain N-linked oligosaccharides. Trypsin digestion of murine EF-1 alpha generated two major [3H]ethanolamine-labeled peptides. Three peptides were sequenced and were identical to two distinct regions of the human EF-1 alpha protein. Blank sequencing cycles coinciding with glutamic acid in the human cDNA-derived sequence were also found to release [3H]ethanolamine, and compositional analysis of these peptides confirmed the presence of glutamic acid. Dansylation analysis demonstrates that the amine group of the ethanolamine is blocked. These results indicate that EF-1 alpha is posttranslationally modified by the covalent attachment of ethanolamine via an amide bond to at least two specific glutamic acid residues (Glu-301 and Glu-374). The hydroxyl group of the attached ethanolamine was shown by mass spectrometry and compositional analysis, to be further modified by the addition of a phosphoglycerol unit. This novel posttranslational modification may represent an important alteration of EF-1 alpha, comparable to the regulatory effects of posttranslational methylation of EF-1 alpha lysine residues."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)71682-7"xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)71682-7"xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Hart G.W."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Hart G.W."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Cotter R.J."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Cotter R.J."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Shenbagarmurthi P."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Shenbagarmurthi P."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Whiteheart S.W."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/author | "Whiteheart S.W."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/date | "1989"xsd:gYear |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/date | "1989"xsd:gYear |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/pages | "14334-14341"xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/pages | "14334-14341"xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/title | "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/title | "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha."xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/volume | "264"xsd:string |
| http://purl.uniprot.org/citations/2569467 | http://purl.uniprot.org/core/volume | "264"xsd:string |