Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginyl-tRNAArg + protein | Mus musculus | - |
tRNAArg + L-arginyl-[protein] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q9Z2A5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginyl-tRNAArg + protein | - |
Mus musculus | tRNAArg + L-arginyl-[protein] | - |
? | |
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 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
Ate1 | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Mus musculus |
General Information | Comment | Organism |
---|---|---|
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 |
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 |