EIF4E2
entrez
9470
canonical
uniprot
O60573
canonical
ensembl
ENSG00000135930
resolver
ensp
ENSP00000258416
resolver
ensp
ENSP00000386424
resolver
ensp
ENSP00000386983
resolver
ensp
ENSP00000386996
resolver
ensp
ENSP00000387336
resolver
ensp
ENSP00000390904
resolver
ensp
ENSP00000508671
resolver
enst
ENST00000409322
resolver
enst
ENST00000409394
resolver
enst
ENST00000409514
resolver
enst
ENST00000687222
resolver
genesymbol
EIF4E2
resolver
genesymbol_syn
EIF4EL3
resolver
hgnc
HGNC:3293
resolver
uniprot
A0A8I5KSA5
resolver
uniprot
B8ZZ50
resolver
uniprot
B8ZZJ9
resolver
uniprot
B8ZZL3
resolver
uniprot
B9A023
resolver
uniprot
O75349
resolver
uniprot
Q53RG0
resolver
uniprot
Q59FE1
resolver
uniprot_entry
A0A8I5KSA5_HUMAN
resolver
uniprot_entry
B8ZZ50_HUMAN
resolver
uniprot_entry
B8ZZL3_HUMAN
resolver
uniprot_entry
B9A023_HUMAN
resolver
uniprot_entry
IF4E2_HUMAN
resolver
uniprot_entry
Q53RG0_HUMAN
resolver
uniprot_entry
Q59FE1_HUMAN
resolver
uniprot_sec
B8ZZJ9
resolver
uniprot_sec
O75349
resolver
amino_acid_sequence
MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP
uniprot
proteins
function
FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation (PubMed:17368478, PubMed:22751931, PubMed:25624349, PubMed:33581076, PubMed:9582349). In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity). In P-bodies, component of a complex that promotes miRNA-mediated translational repression (PubMed:28487484). Involved in virus-induced host response by mediating miRNA MIR34A-induced translational silencing which controls IFNB1 production by a negative feedback mechanism (PubMed:28487484, PubMed:33581076). {ECO:0000250|UniProtKB:Q8BMB3, ECO:0000269|PubMed:17368478, ECO:0000269|PubMed:22751931, ECO:0000269|PubMed:25624349, ECO:0000269|PubMed:28487484, ECO:0000269|PubMed:33581076, ECO:0000269|PubMed:9582349}.; FUNCTION: Component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931, PubMed:35878012). In association with GIGYF2, assists ribosome-associated quality control (RQC) by sequestering the mRNA cap, blocking ribosome initiation and decreasing the translational load on problematic messages. Part of a pathway that works in parallel to RQC-mediated degradation of the stalled nascent polypeptide. GIGYF2 and EIF4E2 work downstream and independently of ZNF598, which seems to work as a scaffold that can recruit them to faulty mRNA even if alternative recruitment mechanisms may exist (PubMed:32726578). {ECO:0000269|PubMed:22751931, ECO:0000269|PubMed:32726578, ECO:0000269|PubMed:35878012}.; FUNCTION: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 infection, the interaction with non-structural protein 2 (nsp2) with GIGYF2 enhances GIGYF2 binding to EIF4E2 and increases repression of translation initiation of genes involved in antiviral innate immune response such as IFNB1. {ECO:0000269|PubMed:35878012}.
uniprot
proteins
mass_dalton
28362
uniprot
proteins
mutagenesis
MUTAGEN 63; /note="W->A: Unable to bind capped mRNA."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 95; /note="W->A: Ability to bind capped mRNA reduced to 40% of wild-type."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 121; /note="K->R: Does not affect ubiquitination by ARIH1; when associated with R-130; R-134 and R-222."; /evidence="ECO:0000269|PubMed:25624349"; MUTAGEN 124..126; /note="WED->FAA: Unable to bind capped mRNA."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 124; /note="W->A: Ability to bind capped mRNA reduced to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 124; /note="W->F: Ability to bind capped mRNA reduced to 13% of wild-type."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 125; /note="E->A: Ability to bind capped mRNA reduced to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 126; /note="D->A: Slight reduction in ability to bind capped mRNA."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 130; /note="K->R: Does not affect ubiquitination by ARIH1; when associated with R-121; R-134 and R-222."; /evidence="ECO:0000269|PubMed:25624349"; MUTAGEN 134; /note="K->R: Does not affect ubiquitination by ARIH1; when associated with R-121; R-130 and R-222."; /evidence="ECO:0000269|PubMed:25624349"; MUTAGEN 135; /note="W->A: Unable to bind capped mRNA."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 148; /note="W->A: Unable to bind capped mRNA."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 183; /note="W->A: Ability to bind capped mRNA reduced to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 183; /note="W->F: Unable to bind capped mRNA."; /evidence="ECO:0000269|PubMed:9582349"; MUTAGEN 222; /note="K->R: Does not affect ubiquitination by ARIH1; when associated with R-121; R-130 and R-134."; /evidence="ECO:0000269|PubMed:25624349
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by ARIH1 (PubMed:14623119, PubMed:25624349). The consequences of ubiquitination are however unclear: according to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report ubiquitination leads to its subsequent degradation (PubMed:14623119). {ECO:0000269|PubMed:14623119, ECO:0000269|PubMed:25624349}.; PTM: ISGylation enhances its cap structure-binding activity and translation-inhibition activity. {ECO:0000269|PubMed:17289916}.
uniprot
proteins
protein_family
Eukaryotic initiation factor 4E family
uniprot
proteins
pubmed
14623119
uniprot
proteins
pubmed
15153109
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17289916
uniprot
proteins
pubmed
17368478
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22751931
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23991149
uniprot
proteins
pubmed
25624349
uniprot
proteins
pubmed
28487484
uniprot
proteins
pubmed
32726578
uniprot
proteins
pubmed
33581076
uniprot
proteins
pubmed
35878012
uniprot
proteins
pubmed
9582349
uniprot
proteins
pubmed
9653160
uniprot
proteins
sequence_length
245
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23991149}. Cytoplasm, P-body {ECO:0000269|PubMed:23991149}.
uniprot
proteins