EIF4EBP1
entrez
1978
canonical
uniprot
Q13541
canonical
ensembl
ENSG00000187840
resolver
ensp
ENSP00000340691
resolver
enst
ENST00000338825
resolver
genesymbol
EIF4EBP1
resolver
hgnc
HGNC:3288
resolver
uniprot
B2R502
resolver
uniprot
D3DSW8
resolver
uniprot
Q6IBN3
resolver
uniprot_entry
4EBP1_HUMAN
resolver
uniprot_sec
B2R502
resolver
uniprot_sec
D3DSW8
resolver
uniprot_sec
Q6IBN3
resolver
amino_acid_sequence
MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI
uniprot
proteins
function
FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. {ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:7935836}.
uniprot
proteins
mass_dalton
12580
uniprot
proteins
mutagenesis
MUTAGEN 37; /note="T->A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-46; A-65 and A-70."; /evidence="ECO:0000269|PubMed:22578813"; MUTAGEN 46; /note="T->A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-65 and A-70."; /evidence="ECO:0000269|PubMed:22578813"; MUTAGEN 57; /note="K->R: Impaired ubiquitination by the BCR(KLHL25) complex."; /evidence="ECO:0000269|PubMed:22578813"; MUTAGEN 59..60; /note="LM->AA: Abolishes eIF4E-binding. Increased ubiquitination by the BCR(KLHL25) complex."; /evidence="ECO:0000269|PubMed:22578813"; MUTAGEN 65; /note="S->A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-46 and A-70."; /evidence="ECO:0000269|PubMed:22578813"; MUTAGEN 69; /note="K->R: Does not affect ubiquitination by the BCR(KLHL25) complex."; /evidence="ECO:0000269|PubMed:22578813"; MUTAGEN 70; /note="T->A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-46 and A-65."; /evidence="ECO:0000269|PubMed:22578813"; MUTAGEN 105; /note="K->R: Does not affect ubiquitination by the BCR(KLHL25) complex."; /evidence="ECO:0000269|PubMed:22578813"; MUTAGEN 113; /note="Q->A: Reduced interaction with RPTOR."; /evidence="ECO:0000269|PubMed:29236692
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF (PubMed:12588975, PubMed:12747827, PubMed:22578813, PubMed:24403073, PubMed:29236692, PubMed:7935836, PubMed:9465032). Phosphorylation at Thr-37, Thr-46, Ser-65 and Thr-70, corresponding to the hyperphosphorylated form, is regulated by mTORC1 and abolishes binding to EIF4E (PubMed:12588975, PubMed:12747827, PubMed:22578813, PubMed:24403073, PubMed:29236692, PubMed:7935836, PubMed:9465032). {ECO:0000269|PubMed:12588975, ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:24403073, ECO:0000269|PubMed:29236692, ECO:0000269|PubMed:7935836, ECO:0000269|PubMed:9465032}.; PTM: Ubiquitinated: when eIF4E levels are low, hypophosphorylated form is ubiquitinated by the BCR(KLHL25) complex, leading to its degradation and serving as a homeostatic mechanism to maintain translation and prevent eIF4E inhibition when eIF4E levels are low. Not ubiquitinated when hyperphosphorylated (at Thr-37, Thr-46, Ser-65 and Thr-70) or associated with eIF4E. {ECO:0000269|PubMed:22578813}.
uniprot
proteins
protein_family
EIF4E-binding protein family
uniprot
proteins
pubmed
12150926
uniprot
proteins
pubmed
12588975
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12747827
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16271312
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17368478
uniprot
proteins
pubmed
17487921
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17631896
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22578813
uniprot
proteins
pubmed
22684010
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24403073
uniprot
proteins
pubmed
25702871
uniprot
proteins
pubmed
29236692
uniprot
proteins
pubmed
29750193
uniprot
proteins
pubmed
7935836
uniprot
proteins
pubmed
8521827
uniprot
proteins
pubmed
9465032
uniprot
proteins
pubmed
9684899
uniprot
proteins
sequence_length
118
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22684010}. Nucleus {ECO:0000269|PubMed:22684010}. Note=Localization to the nucleus is unaffected by phosphorylation status. {ECO:0000250|UniProtKB:Q60876}.
uniprot
proteins