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Gene Review

ATE1  -  arginyltransferase 1

Homo sapiens

Synonyms: Arginine-tRNA--protein transferase 1, Arginyl-tRNA--protein transferase 1, Arginyltransferase 1, R-transferase 1
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High impact information on ATE1

  • In eukaryotes, ATE1-encoded arginyl-transferases (R(D,E,C*)-transferases) conjugate Arg (R), an Nd(p) residue, to Nd(s) residues Asp (D), Glu (E), or oxidized Cys residue (C*) [1].
  • Human glutathione transferases (GSTs; RX:glutathione R-transferase, EC of classes Alpha, Mu, and Pi were shown to promote the conjugation of glutathione with base propenals and related alkenes [2].
  • We have identified a region in the 5' flanking sequence of the glutathione S-transferase (RX:glutathione R-transferase, EC Ya subunit gene that contains a unique xenobiotic-responsive element (XRE) [3].
  • 0. The intracellular level of the Yc subunit is elevated greater than 40-fold in the drug-resistant cell line, which could account for the increase in glutathione S-transferase (RX:glutathione R-transferase; EC activity toward both 1-chloro-2,4-dinitrobenzene and cumene hydroperoxide [4].
  • 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 [5].

Biological context of ATE1

  • 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 [5].

Anatomical context of ATE1


Associations of ATE1 with chemical compounds

  • We examined tetracycline-resistant isolates of the animal commensal and opportunistic pathogen Arcanobacterium pyogenes, all of which carried tet(W), and identified three genetic elements designated ATE-1, ATE-2, and ATE-3 [7].


  1. Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen. Graciet, E., Hu, R.G., Piatkov, K., Rhee, J.H., Schwarz, E.M., Varshavsky, A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Berhane, K., Widersten, M., Engström, A., Kozarich, J.W., Mannervik, B. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  3. Regulation of glutathione S-transferase Ya subunit gene expression: identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds. Rushmore, T.H., King, R.G., Paulson, K.E., Pickett, C.B. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  4. Amplification and increased expression of alpha class glutathione S-transferase-encoding genes associated with resistance to nitrogen mustards. Lewis, A.D., Hickson, I.D., Robson, C.N., Harris, A.L., Hayes, J.D., Griffiths, S.A., Manson, M.M., Hall, A.E., Moss, J.E., Wolf, C.R. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  5. 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. Kwon, Y.T., Kashina, A.S., Varshavsky, A. Mol. Cell. Biol. (1999) [Pubmed]
  6. Post-translational arginylation and intracellular proteolysis. Bohley, P., Kopitz, J., Adam, G., Rist, B., von Appen, F., Urban, S. Biomed. Biochim. Acta (1991) [Pubmed]
  7. Multiple Genetic Elements Carry the Tetracycline Resistance Gene tet(W) in the Animal Pathogen Arcanobacterium pyogenes. Billington, S.J., Jost, B.H. Antimicrob. Agents Chemother. (2006) [Pubmed]
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