ATE1 BASIC INFORMATION
| Standard Name | ATE1 |
|---|---|
| Systematic Name | YGL017W |
| Feature Type | ORF, Verified |
| Description | Arginyl-tRNA-protein transferase, catalyzes post-translational conjugation of arginine to the amino termini of acceptor proteins which are then subject to degradation via the N-end rule pathway (1 and see Summary Paragraph)
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| Name Description | Arginyl-tRNA-protein transfErase 2 |
| Gene Product Alias | arginyl-tRNA-protein transferase 1 |
| GO Annotations | All ATE1 GO evidence and references |
|---|---|
| View Computational GO annotations for ATE1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Mutant Phenotype | All ATE1 Phenotype details and references |
|---|---|
| Classical genetics | |
| overexpression | |
| Large-scale survey | |
| null | |
| overexpression |
| Interactions | ATE1 All interactions details and references |
|---|---|
| View additional details at BioGRID | |
| 11 total interaction(s) for 10 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Post-translational Modifications | PhosphoGRID | PhosphoPep Database |
|---|
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
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| Primary SGDID | S000002985 |
|---|
ADDITIONAL INFORMATION for ATE1
SUMMARY PARAGRAPH for ATE1
ATE1 encodes a cytoplasmic arginyl transferase, responsible for transferring an L-arginyl residue from a tRNA to the N-terminus of a protein (1). Proteins with aspartate or glutamate as their N-terminal residues can act as acceptors for this posttranslational protein modification (3). The transferred arginine acts as a destabilizing residue, subjecting the acceptor protein to the ubiquitin-dependent proteolysis of the N-end rule pathway (1, 3). Cells that lack Ate1p are viable, but are unable to degrade those substrates of the N-end rule pathway that are usually processed by the arginyl transferase (1). Homologs of the yeast arginyl transferase exist in mouse, human, Arabidopsis, and Drosophila (3).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for ATE1]
| 1) | Balzi E, et al. (1990) Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae. J Biol Chem 265(13):7464-71 |
| 2) | Savage M, et al. (1983) A mutant of Saccharomyces cerevisiae defective in arginyl-tRNA-protein transferase Curr Genet 7():285-288 |
| 3) | Kwon YT, et al. (1999) 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. Mol Cell Biol 19(1):182-93 |




