8 exons and 7 introns.

5 alternatives for transcript splicing.

50kDa; 463 amino acids contains tRNA binding sites, GTP binding and hydrolysis sites and putative actin binding sites (see figure above).

In mice and humans, eEF1A2 is expressed only in normal tissues of the brain, heart and skeletal muscle. Expression is found in tumours of the breast, lung and ovary.

Diffusely cytoplasmic and nuclear.

This protein is an isoform of the alpha subunit of the elongation factor-1 complex. There are two known isoforms of protein elongation factor eEF1A (eEF1A1 and eEF1A2). eEF1A proteins are GTP-binding proteins that interact with amino-acylated tRNA and recruit them to the ribosome during the elongation phase of protein translation. In addition, eEF1A2 binds to and stimulates the lipid kinase activity of phosphatidylinositol 4-kinase beta, the enzyme that catalyzes the generation of phosphatidylinositol 4-phosphate from phosphatidylinositol. eEF1A2 also activates the Akt serine/threonine kinase and can stimulate actin remodeling and increase the rate of cell invasion and migration in vitro.

EEF1A2 is highly homologous to the EEF1A1. EEF1A2 and EEF1A1 share greater than 90% DNA sequence and amino acid identity. The GTP binding and hydrolysis domains also have homology to the Ras GTPase.

Inactivation of mouse EEF1A2 leads to immunodeficiency, neuromuscular abnormalities and death by 30 days of age.