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Literature summary extracted from

  • Wang, J.; Pejaver, V.R.; Dann, G.P.; Wolf, M.Y.; Kellis, M.; Huang, Y.; Garcia, B.A.; Radivojac, P.; Kashina, A.
    Target site specificity and in vivo complexity of the mammalian arginylome (2018), Sci. Rep., 8, 16177 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + protein Mus musculus
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 tRNAArg + L-arginyl-[protein]
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.8 Mus musculus Q9Z2A5
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + protein
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 Mus musculus tRNAArg + L-arginyl-[protein]
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 ?
2.3.2.8 additional information the four mouse ATE1 isoforms have different, partially overlapping substrate specificity toward their N-terminal target sites, detailed overview. The four mouse ATE1 isoforms show prominent and consistent differences in target site specificity, both at the N-terminus and the side chain sites. At the N-terminal sites, only three of the four ATE1 isoforms (ATE1-1, 2, and 3) show high preference for the peptides containing N-terminal D and E. ATE1-4 do not appear to target peptides containing N-terminal E. At the same time all four isoforms, to a various degree, show prominent reactivity with the peptides bearing N-terminal C. Even more strikingly, ATE1-1, unlike any other ATE1 isoforms, appears to be reactive with additional N-terminal sites not seen with other ATE1 isoforms, including Q and, weakly, H. Thus, it appears that N-terminal target site specificity of ATE1-1 may be broader than other ATE1 isoforms and potentially include non-canonical N-terminal residues. The four ATE1 isoforms also show different reactivity with the peptides bearing side chain target sites. In the case of ATE1-1 and ATE1-2, the signal with these peptides containing side chain target sites is substantially lower or absent compared to the peptides containing favorable N-terminal target sites. Side chain arginylation of one of these peptides with ATE1-2 in solution. It appears likely that the peptide array format is unfavorable for side chain targeting by these ATE1 isoforms. Isozyme ATE1-1 catalyzes arginylation of non-canonical residues. Identification of the arginylation-favorable sequence motif Mus musculus ?
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Synonyms

EC Number Synonyms Comment Organism
2.3.2.8 Ate1
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 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.8 37
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 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.8 7.4
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 assay at Mus musculus

General Information

EC Number General Information Comment Organism
2.3.2.8 additional information estimation of the scope and evolutionary conservation of the N-terminal arginylome, analysis to a shorter list of likely arginylation targets with likely conserved regulation across mammals, these protein targets may be highly regulated by N-terminal arginylation in vivo, overview Mus musculus
2.3.2.8 physiological function protein arginylation, mediated by the arginyltransferase ATE1, is a posttranslational modification that is essential for mammalian embryogenesis, regulates many fundamental biological processes, and targets a large number of proteins in vivo. In mammals, ATE1 is represented by four homologous isoforms ATE1-1, 2, 3, and 4, generated by alternative splicing from a single gene and reported in different studies to have varying activity, substrate specificity, and tissue-specific expression. In addition to N-terminal arginylation, ATE1 can also add arginine to the acidic side chains of Asp and Glu on the mid-chain sites of intact proteins Mus musculus