Eif4e
entrez
13684
canonical
uniprot
P63073
canonical
ensembl
ENSMUSG00000028156
resolver
ensp
ENSMUSP00000029803
resolver
ensp
ENSMUSP00000143104
resolver
ensp
ENSMUSP00000215471
resolver
enst
ENSMUST00000029803
resolver
enst
ENSMUST00000196990
resolver
genesymbol
Eif4e
resolver
uniprot
A0A0G2JFB4
resolver
uniprot
P20415
resolver
uniprot
Q3TK95
resolver
uniprot
Q8C470
resolver
uniprot_entry
A0A0G2JFB4_MOUSE
resolver
uniprot_entry
IF4E_MOUSE
resolver
uniprot_entry
Q3TK95_MOUSE
resolver
uniprot_entry
Q8C470_MOUSE
resolver
uniprot_sec
P20415
resolver
amino_acid_sequence
MATVEPETTPTTNPPPAEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENRDAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
uniprot
proteins
function
FUNCTION: Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:18805096, PubMed:25456498, PubMed:31042468, PubMed:36843541, PubMed:8577715). Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:18805096). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (By similarity). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:18805096, PubMed:25456498). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap (PubMed:18805096). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (PubMed:25456498). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (By similarity). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). As well as its roles in translation, also involved in mRNA nucleocytoplasmic transport (PubMed:8577715). Its role in mRNA export from the nucleus to the cytoplasm relies on its ability to bind the m7G cap of RNAs and on the presence of the 50-nucleotide EIF4E sensitivity element (4ESE) in the 3'UTR of sensitive transcripts (PubMed:17074885). Interaction with the 4ESE is mediated by LRPPRC which binds simultaneously to both EIF4E and the 4ESE, thereby acting as a platform for assembly for the RNA export complex (PubMed:19262567, PubMed:28325843). EIF4E-dependent mRNA export is independent of ongoing protein or RNA synthesis and is also NFX1-independent but is XPO1-dependent with LRPPRC interacting with XPO1 to form an EIF4E-dependent mRNA export complex (PubMed:17074885). Alters the composition of the cytoplasmic face of the nuclear pore to promote RNA export by reducing RANBP2 expression, relocalizing nucleoporin NUP214 and increasing expression of RANBP1 and RNA export factors DDX19 and GLE1 (PubMed:22902403). Promotes the nuclear export of cyclin CCND1 mRNA (PubMed:11500381, PubMed:15574771, PubMed:18391071, PubMed:8577715). Promotes the nuclear export of NOS2/iNOS mRNA (By similarity). Promotes the nuclear export of MDM2 mRNA (By similarity). Also promotes the export of additional mRNAs, including others involved in the cell cycle (PubMed:17074885). In the nucleus, binds to capped splice factor-encoding mRNAs and stimulates their nuclear export to enhance splice factor production by increasing their cytoplasmic availability to the translation machinery (PubMed:36843541). May also regulate splicing through interaction with the spliceosome in an RNA and m7G cap-dependent manner (PubMed:36843541). Also binds to some pre-mRNAs and may play a role in their recruitment to the spliceosome (PubMed:36843541). Promotes steady-state capping of a subset of coding and non-coding RNAs by mediating nuclear export of capping machinery mRNAs including RNMT, RNGTT and RAMAC to enhance their translation (PubMed:33055213). Stimulates mRNA 3'-end processing by promoting the expression of several core cleavage complex factors required for mRNA cleavage and polyadenylation, and may also have a direct effect through its interaction with the CPSF3 cleavage enzyme (PubMed:31042468). Rescues cells from apoptosis by promoting activation of serine/threonine-protein kinase AKT1 through mRNA export of NBS1 which potentiates AKT1 phosphorylation and also through mRNA export of AKT1 effectors, allowing for increased production of these proteins (PubMed:18391071). {ECO:0000250|UniProtKB:P06730, ECO:0000250|UniProtKB:P63074, ECO:0000269|PubMed:11500381, ECO:0000269|PubMed:15574771, ECO:0000269|PubMed:17074885, ECO:0000269|PubMed:18391071, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19262567, ECO:0000269|PubMed:22902403, ECO:0000269|PubMed:25456498, ECO:0000269|PubMed:28325843, ECO:0000269|PubMed:31042468, ECO:0000269|PubMed:33055213, ECO:0000269|PubMed:36843541, ECO:0000269|PubMed:8577715}.
uniprot
proteins
mass_dalton
25053
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="S->A: No increase in protein levels of ODC1 or CCND1 in NIH 3T3 cells overexpressing the mutant in comparison to a 3-fold increase in cells overexpressing the wild-type. Abolishes stimulation of splice factor synthesis. Abolishes binding to mRNAs in the nucleus and impairs nuclear pore complex reprogramming and mRNA export. Does not affect interaction with HHEX."; /evidence="ECO:0000269|PubMed:12554669, ECO:0000269|PubMed:22902403, ECO:0000269|PubMed:36843541, ECO:0000269|PubMed:8577715"; MUTAGEN 56; /note="W->A: Abolishes mRNA nuclear export. Impairs nuclear pore complex reprogramming. No effect on interaction with PML or viral Z protein but reduces binding to the mRNA cap. Capable of AKT1 activation. Does not impair interaction with HHEX or HOXA9."; /evidence="ECO:0000269|PubMed:11500381, ECO:0000269|PubMed:11575918, ECO:0000269|PubMed:12554669, ECO:0000269|PubMed:15657436, ECO:0000269|PubMed:17074885, ECO:0000269|PubMed:18391071, ECO:0000269|PubMed:22902403"; MUTAGEN 69; /note="V->A: Reduces interaction with LRPPRC. Abolishes interaction with LRPPRC and abolishes CCND1 mRNA export; when associated with A-73."; /evidence="ECO:0000269|PubMed:19262567"; MUTAGEN 73; /note="W->A: Binding to CYFIP1 reduced by 70%. Does not affect mRNA nuclear export or nuclear pore complex reprogramming. Does not affect affinity for mRNA cap. Reduces interaction with LRPPRC. Reduces affinity for PML and viral Z protein. Abolishes AKT1 activation. Abolishes interaction with HHEX. Inhibits interaction with HOXA9. Abolishes interaction with LRPPRC and abolishes CCND1 mRNA export; when associated with A-69."; /evidence="ECO:0000269|PubMed:11500381, ECO:0000269|PubMed:11575918, ECO:0000269|PubMed:12554669, ECO:0000269|PubMed:15657436, ECO:0000269|PubMed:17074885, ECO:0000269|PubMed:18391071, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19262567, ECO:0000269|PubMed:22902403"; MUTAGEN 157; /note="R->E: Abolishes binding to the 4ESE element in mRNAs; when associated with E-159 and E-162."; /evidence="ECO:0000269|PubMed:28325843"; MUTAGEN 159; /note="K->E: Abolishes binding to the 4ESE element in mRNAs; when associated with E-157 and E-162."; /evidence="ECO:0000269|PubMed:28325843"; MUTAGEN 162; /note="K->E: Abolishes binding to the 4ESE element in mRNAs; when associated with E-157 and E-159."; /evidence="ECO:0000269|PubMed:28325843"; MUTAGEN 209..210; /note="ST->AA: Abolishes phosphorylation, abrogates the ability to transform cells and impairs nuclear export of CCND1 but does not affect subcellular location."; /evidence="ECO:0000269|PubMed:15574771"; MUTAGEN 209; /note="S->A: Abolishes phosphorylation and abrogates the ability to transform cells."; /evidence="ECO:0000269|PubMed:15574771"; MUTAGEN 209; /note="S->D: Abolishes phosphorylation and abrogates the ability to transform cells."; /evidence="ECO:0000269|PubMed:15574771
uniprot
proteins
post_translational_modification
PTM: Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex (By similarity). Phosphorylation also enhances its mRNA transport function (PubMed:15574771). Phosphorylation at Ser-209 is not essential for protein synthesis (By similarity). {ECO:0000250|UniProtKB:P06730, ECO:0000269|PubMed:15574771}.
uniprot
proteins
protein_family
Eukaryotic initiation factor 4E family
uniprot
proteins
pubmed
10394359
uniprot
proteins
pubmed
11500381
uniprot
proteins
pubmed
11575918
uniprot
proteins
pubmed
12554669
uniprot
proteins
pubmed
15247416
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15574771
uniprot
proteins
pubmed
15657436
uniprot
proteins
pubmed
16705177
uniprot
proteins
pubmed
16835235
uniprot
proteins
pubmed
17074885
uniprot
proteins
pubmed
17689282
uniprot
proteins
pubmed
18391071
uniprot
proteins
pubmed
18515545
uniprot
proteins
pubmed
18805096
uniprot
proteins
pubmed
19114715
uniprot
proteins
pubmed
19262567
uniprot
proteins
pubmed
2037592
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22900038
uniprot
proteins
pubmed
22902403
uniprot
proteins
pubmed
25456498
uniprot
proteins
pubmed
2663851
uniprot
proteins
pubmed
27065194
uniprot
proteins
pubmed
28325843
uniprot
proteins
pubmed
31042468
uniprot
proteins
pubmed
33055213
uniprot
proteins
pubmed
36843541
uniprot
proteins
pubmed
8577715
uniprot
proteins
pubmed
9200613
uniprot
proteins
sequence_length
217
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:P06730}. Cytoplasm {ECO:0000269|PubMed:15574771, ECO:0000269|PubMed:18515545, ECO:0000269|PubMed:22900038}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P06730}. Nucleus {ECO:0000269|PubMed:18515545}. Nucleus speckle {ECO:0000250|UniProtKB:P06730}. Nucleus, nuclear body {ECO:0000269|PubMed:15574771}. Note=Interaction with EIF4ENIF1/4E-T is required for localization to processing bodies (P-bodies). Imported in the nucleus via interaction with EIF4ENIF1/4E-T via a piggy-back mechanism (By similarity). Sequestered in the nucleus by EIF4EBP1 and EIF4EBP2 (PubMed:18515545). {ECO:0000250|UniProtKB:P06730, ECO:0000269|PubMed:18515545}.
uniprot
proteins