This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976). (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection. Inhibited by plitidepsin, a chemical compound extracted from the ascidian Aplidium albicans. Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA (PubMed:12426392, PubMed:12426393). Interacts with PARP1 and TXK (PubMed:17177976). Interacts with KARS1 (PubMed:18029264). May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7) (By similarity). Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation. Interacts with ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner. Interacts with PPP1R16B (PubMed:26497934). Interacts with SPHK1 and SPHK2; both interactions increase SPHK1 and SPHK2 kinase activity (PubMed:18263879). Colocalizes with DLC1 at actin-rich regions in the cell periphery (PubMed:19158340). Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens (PubMed:8650580). Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B (PubMed:26497934). Brain, placenta, lung, liver, kidney, pancreas but barely detectable in heart and skeletal muscle. By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress. ISGylated. Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2 (PubMed:26497934). Trimethylated at Lys-79 by EEF1AKMT1 (PubMed:26545399). Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation (PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2 (PubMed:25144183). Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs (PubMed:28520920). Trimethylated at Gly-2 by METTL13 (PubMed:30143613). Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is predominant (PubMed:30143613, PubMed:30612740). Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. Extended N-terminus. Probable cloning artifact.