The initiation of protein synthesis in eukaryotic cells is regulated by interactions between protein initiation factors and RNA molecules. The eukaryotic initiation factor 4E family (eIF4E) is comprised of three proteins that are involved in the early initiation of protein synthesis. eIF4E2 (eukaryotic translation initiation factor 4E family member 2), also known as 4EHP, IF4e, 4E-LP or EIF4EL3, is a ubiquitously expressed 245 amino acid protein. During early translation events, eIF4E2 recognizes and binds the 7-methylguanosine-containing mRNA cap (a cotranscriptionally added structure that conveys mRNA stability and allows for efficient RNA processing), thus initiating the unwinding of mRNA secondary structures and facilitating mRNA-ribosome binding. eIF4E2 competes with eIF4E (member 1) for cap binding and, upon modification by the ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein), exhibits increased mRNA cap affinity.