EC Number   |
General Information |
Reference |
|---|
   2.3.2.8 | evolution |
arginyltransferase (ATE1) is an evolutionary conserved enzyme |
760135 |
| 2.3.2.8 | physiological function |
arginyltransferase 1 (Ate1) mediates protein arginylation, a protein posttranslational modification (PTM) in eukaryotic cells. Ate1 is required to suppress mutation frequency in yeast and mammalian cells during DNA-damaging conditions such as ultraviolet irradiation. Ate1 and arginylation are upregulated during stress and are responsible for cell death, role of Ate1/arginylation in stress response, overview. Ate1 is essential for the suppression of mutagenesis during DNA-damaging stress. Growth arrest and cell death during stress could be interpreted as a mechanism to prevent incorporation of damaged genetic material or transmission of mutation to the subsequent generations |
-, 759021 |
| 2.3.2.8 | physiological function |
arginyltransferase ATE1 can modulate the hypertrophic growth of myocytes induced by Ang II. Physiological importance of ATE1 in higher eukaryotes |
760135 |
| 2.3.2.8 | physiological function |
arginyltransferases (ATE) mediates N-terminal arginylation of secondary destabilizing residues (D, E, Cox) |
759770 |
| 2.3.2.8 | more |
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively |
759302 |
| 2.3.2.8 | evolution |
ATE1 Arg-transferase is an evolutionarily conserved protein present in all eukaryotes from fungi to animals |
-, 758964 |
| 2.3.2.8 | physiological function |
ATE1 Arg-transferase is the key enzyme in the Arg/N-end rule pathway. ATE1 is required for degradation of regulators of G protein signaling (RGS) proteins and GPCR signaling, regulation, overview. Essential role of N-terminal arginylation in neural tube development. The crucial role of ATE1 in neural tube development is directly related to proper turn-over of the RGS4 protein, which participate in the oxygen-sensing mechanism in the cells. Degradation of the RGS4 protein by ATE1 is closely associated with the migration or differentiation of neural crest cells during embryogenesis. Neural crest cells migrate into the heart and vessels |
-, 758964 |
| 2.3.2.8 | physiological function |
Ate1 plays a role in the regulation of cytoskeleton and is essential for cardiovascular development and angiogenesis |
706443 |
| 2.3.2.8 | malfunction |
Ate1- null cells are almost completely lacking focal actin adhesion sites at the substrate-attached surface and are only weakly adhesive. In vitro polymerization assays with actin purified from ate1-null cells reveal a diminished polymerization capacity in comparixadson to wild-type actin. Chemotaxis of aggregation-competent ate1-/- null cells is impaired in three-dimensional compared with two-dimensional environments |
-, 759753 |
| 2.3.2.8 | malfunction |
ATE1-null mice show severe intracerebral hemorrhages and cystic space near the neural tubes. The ATE1-/- brain shows defective G-protein signaling. Reduced mitosis in ATE1-/- neuroepithelium and a significantly higher nitric oxide concentration in ATE1-/- brain are observed. In ATE1-null murine embryos, neural-tube genesis is severely defective, and this problem may be the primary cause of embryonic mortality of the mutant mice. ATE1 expression is more prominent in the embryonic brain and spinal cord than in the heart. ATE1-null embryonic brain shows stabilized regulators of G protein signaling (RGS) proteins, defective G protein signaling, and a higher concentration of NO. Proliferation of ATE1-/- neuroepithelial cells in the developing primary neural tube is significantly impaired. Stabilized RGS proteins in ATE1-null mice and reduced activities of downstream effectors, overview |
-, 758964 |
