Eif4ebp2
entrez
13688
canonical
uniprot
P70445
canonical
ensembl
ENSMUSG00000020091
resolver
ensp
ENSMUSP00000020288
resolver
enst
ENSMUST00000020288
resolver
genesymbol
Eif4ebp2
resolver
uniprot
Q3UFP6
resolver
uniprot_entry
4EBP2_MOUSE
resolver
uniprot_entry
Q3UFP6_MOUSE
resolver
amino_acid_sequence
MSASAGGSHQPSQSRAIPTRTVAISDAAQLPQDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGALIEDSKVEVNNLNNLNNHDRKHAVGDEAQFEMDI
uniprot
proteins
function
FUNCTION: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation (PubMed:16237163, PubMed:17029989). Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 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 (PubMed:17029989, PubMed:20347422, PubMed:23172145). EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation (PubMed:20347422, PubMed:23172145, PubMed:24139800). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:8939971). {ECO:0000250|UniProtKB:Q13542, ECO:0000269|PubMed:16237163, ECO:0000269|PubMed:17029989, ECO:0000269|PubMed:20347422, ECO:0000269|PubMed:23172145, ECO:0000269|PubMed:24139800, ECO:0000269|PubMed:8939971}.
uniprot
proteins
mass_dalton
12898
uniprot
proteins
mutagenesis
MUTAGEN 37; /note="T->A: Impaired hyperphosphorylation."; /evidence="ECO:0000269|PubMed:20347422"; MUTAGEN 46; /note="T->A: Impaired hyperphosphorylation."; /evidence="ECO:0000269|PubMed:20347422"; MUTAGEN 70; /note="T->A: Does not greatlay affect hyperphosphorylation."; /evidence="ECO:0000269|PubMed:20347422"; MUTAGEN 99..102; /note="NNLN->ANLA: Abolishes deamidation and impaired interaction with RPTOR."; /evidence="ECO:0000269|PubMed:20347422"; MUTAGEN 99..102; /note="NNLN->DNLD: Increased interaction with RPTOR."; /evidence="ECO:0000269|PubMed:20347422"; MUTAGEN 116..120; /note="Missing: Abolishes interaction with RPTOR."; /evidence="ECO:0000269|PubMed:20347422
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-37, Thr-46, Ser-65, Thr-70 and Ser-83 is mediated by MTOR and corresponds to the hyperphosphorylated form: it abolishes binding to EIF4E by inducing folding of intrinsically disordered regions. First phosphorylated at Thr-37 and Thr-46 by MTOR, inducing folding of region encompassing residues from Pro-18 to Arg-62 of into a four-stranded beta-domain that sequesters the helical YXXXXLPhi motif into a partly buried beta-strand, blocking accessibility to EIF4E. Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000. Phosphorylated in response to insulin, EGF and PDGF. {ECO:0000250|UniProtKB:Q13542, ECO:0000269|PubMed:24139800}.; PTM: Deamidated at Asn-99 and Asn-102 to aspartate (Asp) in brain. Deamidation promotes interaction with RPTOR, subsequent phosphorylation by mTORC1 and increased translation, leading to impair kinetics of excitatory synaptic transmission. Deamidation takes place during postnatal development, when the PI3K-Akt-mTOR signaling is reduced, suggesting it acts as a compensatory mechanism to promote translation despite attenuated PI3K-Akt-mTOR signaling in neuron development (PubMed:20347422). Deamidation converts Asn residues into a mixture of Asp and isoaspartate; interactions with PCMT1 is required to prevent isoaspartate accumulation and convert isoaspartate to Asp (PubMed:20424163). {ECO:0000269|PubMed:20347422, ECO:0000269|PubMed:20424163}.
uniprot
proteins
protein_family
EIF4E-binding protein family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16237163
uniprot
proteins
pubmed
17029989
uniprot
proteins
pubmed
17273556
uniprot
proteins
pubmed
18515545
uniprot
proteins
pubmed
19175792
uniprot
proteins
pubmed
20347422
uniprot
proteins
pubmed
20424163
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23172145
uniprot
proteins
pubmed
23184952
uniprot
proteins
pubmed
24139800
uniprot
proteins
pubmed
8939971
uniprot
proteins
sequence_length
120
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18515545}. Nucleus {ECO:0000269|PubMed:18515545}.
uniprot
proteins