Q62622 · 4EBP1_RAT

  • Protein
    Eukaryotic translation initiation factor 4E-binding protein 1
  • Gene
    Eif4ebp1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 (By similarity).
Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:7939721).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentglutamatergic synapse
Cellular Componentnucleus
Cellular Componentpostsynaptic cytosol
Cellular Componentprotein-containing complex
Molecular Functioneukaryotic initiation factor 4E binding
Molecular Functionprotein phosphatase 2A binding
Molecular Functiontranslation initiation factor binding
Molecular Functiontranslation repressor activity
Biological Processcellular response to dexamethasone stimulus
Biological Processcellular response to hypoxia
Biological ProcessG1/S transition of mitotic cell cycle
Biological Processinsulin receptor signaling pathway
Biological ProcessIRES-dependent translational initiation of linear mRNA
Biological Processlung development
Biological Processnegative regulation of protein-containing complex assembly
Biological Processnegative regulation of translation
Biological Processnegative regulation of translational initiation
Biological Processpositive regulation of mitotic cell cycle
Biological Processresponse to amino acid starvation
Biological Processresponse to ethanol
Biological Processresponse to ischemia
Biological ProcessTOR signaling

Keywords

Enzyme and pathway databases

    • R-RNO-166208mTORC1-mediated signalling
    • R-RNO-72662Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S

Names & Taxonomy

Protein names

  • Recommended name
    Eukaryotic translation initiation factor 4E-binding protein 1
  • Short names
    4E-BP1; eIF4E-binding protein 1
  • Alternative names
    • Phosphorylated heat- and acid-stable protein regulated by insulin 1 (PHAS-I)

Gene names

    • Name
      Eif4ebp1

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q62622

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Note: Localization to the nucleus is unaffected by phosphorylation status.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis64Decreases phosphorylation by MAPK1 and MAPK3.

Chemistry

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00001905152-117Eukaryotic translation initiation factor 4E-binding protein 1
Modified residue36Phosphothreonine
Modified residue40Phosphothreonine
Modified residue43Phosphoserine
Modified residue45Phosphothreonine; by MTOR
Modified residue49Phosphothreonine
Modified residue53Phosphotyrosine
Cross-link56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue64Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR
Modified residue69Phosphothreonine; by MTOR
Modified residue76Phosphothreonine
Modified residue82Phosphoserine
Modified residue95Phosphoserine
Modified residue99Phosphoserine
Modified residue100Phosphoserine; by DYRK2
Modified residue111Phosphoserine

Post-translational modification

Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF. Phosphorylation at Thr-36, Thr-45, Ser-64 and Thr-69, corresponding to the hyperphosphorylated form, is regulated by mTORC1 and abolishes binding to EIF4E.
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-36, Thr-45, Ser-64 and Thr-69) or associated with eIF4E.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in all tissues examined; highest levels in fat and skeletal tissue, lowest levels in kidney.

Gene expression databases

Interaction

Subunit

Hypophosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) or mTORC1 phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation (PubMed:7939721).
Interacts (via TOS motif) with RPTOR; promoting phosphorylation by mTORC1 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, motif.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Region1-47Disordered
Compositional bias33-47Polar residues
Motif53-59YXXXXLphi motif
Region64-117Disordered
Compositional bias78-97Polar residues
Compositional bias98-117Basic and acidic residues
Motif113-117TOS motif

Domain

The TOS motif mediates interaction with RPTOR, leading to promote phosphorylation by mTORC1 complex.

Sequence similarities

Belongs to the eIF4E-binding protein family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    117
  • Mass (Da)
    12,404
  • Last updated
    2007-01-23 v3
  • Checksum
    3449D57B09FA101A
MSAGSSCSQTPSRAIPTRRVALGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVAKTPPKDLPTIPGVTSPTSDEPPMQASQSHLHSSPEDKRAGGEESQFEMDI

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8L2Q998A0A8L2Q998_RATEif4ebp1119

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Sequence conflict19in Ref. 1; AA sequence
Compositional bias33-47Polar residues
Sequence conflict69in Ref. 1; AA sequence
Sequence conflict75in Ref. 1; AA sequence
Compositional bias78-97Polar residues
Compositional bias98-117Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U05014
EMBL· GenBank· DDBJ
AAA86938.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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