Eukaryotic translation initiation factor 4E

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P63073 (IF4E_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Nonphosphorylated 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 By similarity. Ref.4 Ref.6 Ref.7
Subcellular location	Cytoplasm › P-body By similarity.
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.

Ontologies

Keywords
Biological process	Protein biosynthesis Translation regulation
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara lung development Inferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	RNA-induced silencing complex Inferred from electronic annotation. Source: Compara chromatoid body Inferred from direct assay PubMed 22792342. Source: MGI cytoplasmic mRNA processing body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic stress granule Inferred from sequence or structural similarity. Source: UniProtKB eukaryotic translation initiation factor 4F complex Inferred from electronic annotation. Source: Compara mRNA cap binding complex Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	translation initiation factor activity Inferred from direct assay PubMed 16289705. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CYFIP1	Q7L576	2	EBI-2000006,EBI-1048143	From a different organism.
Cyfip1	Q7TMB8	5	EBI-2000006,EBI-772928

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 217

216

Eukaryotic translation initiation factor 4E

PRO_0000193635

Regions

Region

37 – 40

EIF4EBP1/2/3 binding

Region

56 – 57

7-methylguanosine-containing mRNA cap binding

Region

73 – 77

EIF4EBP1/2/3 binding

Region

102 – 103

7-methylguanosine-containing mRNA cap binding

Region

132 – 139

EIF4EBP1/2/3 binding

Region

157 – 162

7-methylguanosine-containing mRNA cap binding

Region

205 – 207

7-methylguanosine-containing mRNA cap binding

Amino acid modifications

Modified residue

209

Phosphoserine; by PKC and MKNK2 Ref.5

Experimental info

Mutagenesis

W → A: Binding to CYFIP1 reduced by 70%. Ref.6

Sequence conflict

E → L no nucleotide entry Ref.1

Secondary structure

217

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P63073 [UniParc].

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

217

25,053

        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' referencesShow '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]	"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.
[9]	"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.

IPI

IPI00119057.

PIR

A34295.
I49644.

RefSeq

NP_031943.3. NM_007917.3.

UniGene

Mm.3941.
Mm.488704.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EJ1	X-ray	2.20	A/B	28-217	[»]
1EJ4	X-ray	2.25	A	28-217	[»]
1EJH	X-ray	2.20	A/B/C/D	28-217	[»]
1L8B	X-ray	1.80	A/B	28-217	[»]

ProteinModelPortal

P63073.

SMR

P63073. Positions 1-217.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42768N.

IntAct

P63073. 4 interactions.

MINT

MINT-1856981.

STRING

10090.ENSMUSP00000029803.

PTM databases

PhosphoSite

P63073.

2D gel databases

REPRODUCTION-2DPAGE

P63073.

Proteomic databases

PaxDb

P63073.

PRIDE

P63073.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029803; ENSMUSP00000029803; ENSMUSG00000028156.

GeneID

13684.

KEGG

mmu:13684.

UCSC

uc008rnn.1. mouse.

Organism-specific databases

CTD

1977.

MGI

MGI:95305. Eif4e.

Phylogenomic databases

eggNOG

COG5053.

HOGENOM

HOG000186751.

HOVERGEN

HBG006130.

InParanoid

P63073.

K03259.

OMA

KIAIWTA.

OrthoDB

EOG48GW45.

Gene expression databases

ArrayExpress

P63073.

Bgee

P63073.

CleanEx

MM_EIF4E.

Genevestigator

P63073.

GermOnline

ENSMUSG00000028156. Mus musculus.

Family and domain databases

Gene3D

3.30.760.10. 1 hit.

InterPro

IPR023398. TIF_eIF4e-like_dom.
IPR001040. TIF_eIF_4E.
IPR019770. TIF_eIF_4E_CS.
[Graphical view]

PANTHER

PTHR11960. PTHR11960. 1 hit.

Pfam

PF01652. IF4E. 1 hit.
[Graphical view]

SUPFAM

SSF55418. TIF_eIF_4E. 1 hit.

PROSITE

PS00813. IF4E. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P63073.

ChEMBL

CHEMBL6148.

EvolutionaryTrace

P63073.

NextBio

284446.

SOURCE

Search...

Entry information

Entry name

IF4E_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Translation initiation factors

List of translation initiation factor entries

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents