ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome (PubMed:20156963). In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. As a result, promotes cell proliferation and growth (PubMed:20156963)
eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with PAIP1, EIF4E and UPF2.
Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact with NOM1. Interacts with PDCD4; this interferes with the interaction between EIF4A and EIF4G.
Interacts with RBM4. Interacts with DDX3X in an RNA-independent manner (PubMed:18596238). Interacts with PKP1 (via N-terminus); the interaction promotes EIF4A1 recruitment to the cap-dependent translation complex and EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369).
Interacts with CEP112 (PubMed:39349455)
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL69
No mutation information available.
Genes with an experimentally identified or computationally predicted synthetic-lethal relationship to EIF4A1, aggregated across our SSL data sources. Click any partner node to view that gene’s page.
Nodes and edges are coloured by the SSL data source. Partners appearing in more than one source are shown in grey.
No clinical trials information available.