EIF4A1

Eukaryotic initiation factor 4A-I UniProt accession P60842

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)

Source: UniProt

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

Source: UniProt
Cytoplasm, perinuclear region, Cell membrane, Cytoplasm, Stress granule
Source: UniProt
  • ISG15 antiviral mechanism
  • L13a-mediated translational silencing of Ceruloplasmin expression
  • Deadenylation of mRNA
  • Translation initiation complex formation
  • Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S
  • Ribosomal scanning and start codon recognition
  • GTP hydrolysis and joining of the 60S ribosomal subunit
  • M-decay: degradation of maternal mRNAs by maternally stored factors
  • Z-decay: degradation of maternal mRNAs by zygotically expressed factors
Source: Reactome via UniProt

Mutations

No mutation information available.

Synthetic Lethal Network

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.

BioGRID SLOrth SynLethDB MexDrugs Multi-source
Sources: BioGRID, SLOrth, SynLethDB, MexDrugs

Clinical Trials

No clinical trials information available.