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Protein

Eukaryotic translation initiation factor 4E-binding protein 1

Gene

Eif4ebp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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:7629182).By similarity1 Publication

GO - Molecular functioni

  • eukaryotic initiation factor 4E binding Source: MGI
  • translation repressor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protein synthesis inhibitor

Keywords - Biological processi

Translation regulation

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4E-binding protein 1
Short name:
4E-BP1
Short name:
eIF4E-binding protein 1
Alternative name(s):
Phosphorylated heat- and acid-stable protein regulated by insulin 1
Short name:
PHAS-I
Gene namesi
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:103267. Eif4ebp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mice lacking both Eif4ebp1 and Eif4ebp2 display increased their sensitivity to diet-induced obesity (PubMed:17273556). Mice lacking both Eif4ebp1 and Eif4ebp2 show defects in myelopoiesis: mice display an increased number of immature granulocytic precursors, associated with a decreased number of mature granulocytic elements (PubMed:19175792).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi113 – 1131F → A: Impaired interaction with RPTOR. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 117116Eukaryotic translation initiation factor 4E-binding protein 1PRO_0000190514Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei36 – 361PhosphothreonineCombined sources
Modified residuei40 – 401PhosphothreonineCombined sources
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei45 – 451PhosphothreonineCombined sources
Modified residuei49 – 491PhosphothreonineBy similarity
Modified residuei53 – 531PhosphotyrosineBy similarity
Modified residuei64 – 641PhosphoserineCombined sources
Modified residuei69 – 691PhosphothreonineCombined sources
Modified residuei82 – 821PhosphoserineBy similarity
Modified residuei95 – 951PhosphoserineCombined sources
Modified residuei99 – 991PhosphoserineCombined sources
Modified residuei100 – 1001PhosphoserineCombined sources
Modified residuei111 – 1111PhosphoserineBy similarity

Post-translational modificationi

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.1 Publication
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.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ60876.
MaxQBiQ60876.
PaxDbiQ60876.
PeptideAtlasiQ60876.
PRIDEiQ60876.

PTM databases

iPTMnetiQ60876.
PhosphoSiteiQ60876.

Expressioni

Tissue specificityi

Highest expression in fat cells.1 Publication

Gene expression databases

BgeeiENSMUSG00000031490.
GenevisibleiQ60876. MM.

Interactioni

Subunit structurei

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:7629182). Interacts (via TOS motif) with RPTOR; promoting phosphorylation by mTORC1 (PubMed:24139800).2 Publications

GO - Molecular functioni

  • eukaryotic initiation factor 4E binding Source: MGI

Protein-protein interaction databases

BioGridi199421. 2 interactions.
DIPiDIP-32577N.
IntActiQ60876. 3 interactions.
MINTiMINT-203831.
STRINGi10090.ENSMUSP00000033880.

Structurei

3D structure databases

ProteinModelPortaliQ60876.
SMRiQ60876. Positions 16-82.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi53 – 597YXXXXLphi motifBy similarity
Motifi113 – 1175TOS motif1 Publication

Domaini

The TOS motif mediates interaction with RPTOR, leading to promote phosphorylation by mTORC1 complex.1 Publication

Sequence similaritiesi

Belongs to the eIF4E-binding protein family.Curated

Phylogenomic databases

eggNOGiENOG410J2Z0. Eukaryota.
ENOG4112779. LUCA.
GeneTreeiENSGT00390000013843.
HOGENOMiHOG000231190.
HOVERGENiHBG050425.
InParanoidiQ60876.
KOiK07205.
OMAiTEPSQNH.
OrthoDBiEOG091G0ZHJ.
PhylomeDBiQ60876.
TreeFamiTF101530.

Family and domain databases

InterProiIPR008606. EIF4EBP.
[Graphical view]
PfamiPF05456. eIF_4EBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60876-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAGSSCSQT PSRAIPTRRV ALGDGVQLPP GDYSTTPGGT LFSTTPGGTR
60 70 80 90 100
IIYDRKFLME CRNSPVAKTP PKDLPAIPGV TSPTSDEPPM QASQSQLPSS
110
PEDKRAGGEE SQFEMDI
Length:117
Mass (Da):12,325
Last modified:January 23, 2007 - v3
Checksum:i3458D5687468A7EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931S → N in BAB28612 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28656 mRNA. Translation: AAA88818.1.
AK013033 mRNA. Translation: BAB28612.1.
AK169979 mRNA. Translation: BAE41494.1.
AK170031 mRNA. Translation: BAE41521.1.
BC002045 mRNA. Translation: AAH02045.1.
CCDSiCCDS22214.1.
PIRiA57396.
RefSeqiNP_031944.3. NM_007918.3.
UniGeneiMm.6700.

Genome annotation databases

EnsembliENSMUST00000033880; ENSMUSP00000033880; ENSMUSG00000031490.
GeneIDi13685.
KEGGimmu:13685.
UCSCiuc009lih.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28656 mRNA. Translation: AAA88818.1.
AK013033 mRNA. Translation: BAB28612.1.
AK169979 mRNA. Translation: BAE41494.1.
AK170031 mRNA. Translation: BAE41521.1.
BC002045 mRNA. Translation: AAH02045.1.
CCDSiCCDS22214.1.
PIRiA57396.
RefSeqiNP_031944.3. NM_007918.3.
UniGeneiMm.6700.

3D structure databases

ProteinModelPortaliQ60876.
SMRiQ60876. Positions 16-82.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199421. 2 interactions.
DIPiDIP-32577N.
IntActiQ60876. 3 interactions.
MINTiMINT-203831.
STRINGi10090.ENSMUSP00000033880.

PTM databases

iPTMnetiQ60876.
PhosphoSiteiQ60876.

Proteomic databases

EPDiQ60876.
MaxQBiQ60876.
PaxDbiQ60876.
PeptideAtlasiQ60876.
PRIDEiQ60876.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033880; ENSMUSP00000033880; ENSMUSG00000031490.
GeneIDi13685.
KEGGimmu:13685.
UCSCiuc009lih.1. mouse.

Organism-specific databases

CTDi1978.
MGIiMGI:103267. Eif4ebp1.

Phylogenomic databases

eggNOGiENOG410J2Z0. Eukaryota.
ENOG4112779. LUCA.
GeneTreeiENSGT00390000013843.
HOGENOMiHOG000231190.
HOVERGENiHBG050425.
InParanoidiQ60876.
KOiK07205.
OMAiTEPSQNH.
OrthoDBiEOG091G0ZHJ.
PhylomeDBiQ60876.
TreeFamiTF101530.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ60876.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031490.
GenevisibleiQ60876. MM.

Family and domain databases

InterProiIPR008606. EIF4EBP.
[Graphical view]
PfamiPF05456. eIF_4EBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei4EBP1_MOUSE
AccessioniPrimary (citable) accession number: Q60876
Secondary accession number(s): Q3TDS8, Q9CZ40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.