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P63073 (IF4E_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 4E

Short name=eIF-4E
Short name=eIF4E
Short name=mRNA cap-binding protein
Alternative name(s):
eIF-4F 25 kDa subunit
Gene names
Name:Eif4e
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development By similarity. Its translation stimulation activity is repressed by binding to the complex CYFIP1-FMR1. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap. Ref.6

Subunit structure

eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4E is also known to interact with other partners. The interaction with EIF4ENIF1 mediates the import into the nucleus. Hypophosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Rapamycin can attenuate insulin stimulation, mediated by FKBPs. Interacts mutually exclusive with EIF4A1 or EIF4A2. Binds to MKNK2 in nucleus By similarity. Interacts with NGDN and PIWIL2. Component of the CYFIP1-EIF4E-FMR1 complex composed of CYFIP, EIF4E and FMR1. Interacts directly with CYFIP1. Interacts with LIMD1, WTIP and AJUBA By similarity. Interacts with APOBEC3G in an RNA-dependent manner. Interacts with LARP1 By similarity. Interacts with CLOCK. Ref.4 Ref.6 Ref.7 Ref.8

Subcellular location

CytoplasmP-body By similarity. Cytoplasm Ref.8.

Post-translational modification

Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex By similarity.

Sequence similarities

Belongs to the eukaryotic initiation factor 4E family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CYFIP1Q7L5762EBI-2000006,EBI-1048143From a different organism.
Cyfip1Q7TMB85EBI-2000006,EBI-772928
Eif4g1Q6NZJ64EBI-2000006,EBI-8175606

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 217216Eukaryotic translation initiation factor 4E
PRO_0000193635

Regions

Region37 – 404EIF4EBP1/2/3 binding
Region56 – 5727-methylguanosine-containing mRNA cap binding
Region73 – 775EIF4EBP1/2/3 binding
Region102 – 10327-methylguanosine-containing mRNA cap binding
Region132 – 1398EIF4EBP1/2/3 binding
Region157 – 16267-methylguanosine-containing mRNA cap binding
Region205 – 20737-methylguanosine-containing mRNA cap binding

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2091Phosphoserine; by PKC and MKNK2 Ref.5

Experimental info

Mutagenesis731W → A: Binding to CYFIP1 reduced by 70%. Ref.6
Sequence conflict701E → L no nucleotide entry Ref.1

Secondary structure

................................. 217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63073 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: FC61D0FB337BCD8F

FASTA21725,053
        10         20         30         40         50         60 
MATVEPETTP TTNPPPAEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL 

        70         80         90        100        110        120 
RLISKFDTVE DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ 

       130        140        150        160        170        180 
QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG DKIAIWTTEC ENRDAVTHIG 

       190        200        210 
RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV 

« Hide

References

« Hide 'large scale' references
[1]"A mammalian translation initiation factor can substitute for its yeast homologue in vivo."
Altmann M., Mueller P.P., Pelletier J., Sonenberg N., Trachsel H.
J. Biol. Chem. 264:12145-12147(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Multiple mRNAs encode the murine translation initiation factor eIF-4E."
Jaramillo M., Pelletier J., Edery I., Nielsen P.J., Sonenberg N.
J. Biol. Chem. 266:10446-10451(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon and Mammary gland.
[4]"Translational control by neuroguidin, a eukaryotic initiation factor 4E and CPEB binding protein."
Jung M.-Y., Lorenz L., Richter J.D.
Mol. Cell. Biol. 26:4277-4287(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGDN.
[5]"Roles of mitogen-activated protein kinase signal-integrating kinases 1 and 2 in oxidant-mediated eIF4E phosphorylation."
Shenberger J.S., Zhang L., Hughlock M.K., Ueda T., Watanabe-Fukunaga R., Fukunaga R.
Int. J. Biochem. Cell Biol. 39:1828-1842(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-209 BY MKNK2.
[6]"The fragile X syndrome protein represses activity-dependent translation through CYFIP1, a new 4E-BP."
Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F., De Rubeis S., Di Marino D., Mohr E., Massimi M., Falconi M., Witke W., Costa-Mattioli M., Sonenberg N., Achsel T., Bagni C.
Cell 134:1042-1054(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CYFIP1 AND FMR1, MUTAGENESIS OF TRP-73.
[7]"MILI, a PIWI-interacting RNA-binding protein, is required for germ Line stem cell self-renewal and appears to positively regulate translation."
Unhavaithaya Y., Hao Y., Beyret E., Yin H., Kuramochi-Miyagawa S., Nakano T., Lin H.
J. Biol. Chem. 284:6507-6519(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIWIL2.
[8]"Circadian proteins CLOCK and BMAL1 in the chromatoid body, a RNA processing granule of male germ cells."
Peruquetti R.L., de Mateo S., Sassone-Corsi P.
PLoS ONE 7:E42695-E42695(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CLOCK.
[9]"Cocrystal structure of the messenger RNA 5' cap-binding protein (eIF4E) bound to 7-methyl-GDP."
Marcotrigiano J., Gingras A.-C., Sonenberg N., Burley S.K.
Cell 89:951-961(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 28-217 IN COMPLEX WITH MRNA CAP ANALOG.
[10]"Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G."
Marcotrigiano J., Gingras A.-C., Sonenberg N., Burley S.K.
Mol. Cell 3:707-716(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 28-217 IN COMPLEX WITH MRNA CAP ANALOG AND EIF4EBP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61731 mRNA. Translation: AAA37545.1.
BC010759 mRNA. Translation: AAH10759.1.
BC085087 mRNA. Translation: AAH85087.1.
PIRA34295.
I49644.
RefSeqNP_031943.3. NM_007917.3.
UniGeneMm.3941.
Mm.488704.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ1X-ray2.20A/B28-217[»]
1EJ4X-ray2.25A28-217[»]
1EJHX-ray2.20A/B/C/D28-217[»]
1L8BX-ray1.80A/B28-217[»]
ProteinModelPortalP63073.
SMRP63073. Positions 1-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199420. 10 interactions.
DIPDIP-42768N.
IntActP63073. 6 interactions.
MINTMINT-1856981.
STRING10090.ENSMUSP00000029803.

Chemistry

BindingDBP63073.
ChEMBLCHEMBL6148.

PTM databases

PhosphoSiteP63073.

2D gel databases

REPRODUCTION-2DPAGEP63073.

Proteomic databases

PaxDbP63073.
PRIDEP63073.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029803; ENSMUSP00000029803; ENSMUSG00000028156.
GeneID13684.
KEGGmmu:13684.
UCSCuc008rnn.1. mouse.

Organism-specific databases

CTD1977.
MGIMGI:95305. Eif4e.

Phylogenomic databases

eggNOGCOG5053.
HOGENOMHOG000186751.
HOVERGENHBG006130.
InParanoidP63073.
KOK03259.
OMANDENTAP.
OrthoDBEOG7QRQVM.
PhylomeDBP63073.
TreeFamTF101526.

Gene expression databases

BgeeP63073.
CleanExMM_EIF4E.
GenevestigatorP63073.

Family and domain databases

Gene3D3.30.760.10. 1 hit.
InterProIPR023398. TIF_eIF4e-like_dom.
IPR001040. TIF_eIF_4E.
IPR019770. TIF_eIF_4E_CS.
[Graphical view]
PANTHERPTHR11960. PTHR11960. 1 hit.
PfamPF01652. IF4E. 1 hit.
[Graphical view]
SUPFAMSSF55418. SSF55418. 1 hit.
PROSITEPS00813. IF4E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63073.
NextBio284446.
PROP63073.
SOURCESearch...

Entry information

Entry nameIF4E_MOUSE
AccessionPrimary (citable) accession number: P63073
Secondary accession number(s): P20415
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries