Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA.
In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family. In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family. Contains 3 WHEP-TRS domains.
The WHEP-TRS domain is involved in RNA binding.
Phosphorylated at Ser-886 by CDK5 in a IFN-gamma-dependent manner; this phosphorylation activates assembly of the GAIT (IFN-gamma-activated inhibitor of translation) complex, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells.
Detection of Glutamyl Prolyl tRNA synthetase in Immunoprecipitates of 293T whole cell lysate (1 mg for IP, 20% of IP loaded) using ab157129 at 6 µg/mg lysate for IP (Lane 1) and at 1 µg/ml for subsequent Western blot detection. Lane 2 represents control IgG IP. Detection: Chemiluminescence with an exposure time of 3 seconds.