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Reviewed, UniProtKB/Swiss-Prot O60573 (IF4E2_HUMAN)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Eukaryotic translation initiation factor 4E type 2
      Short name=eIF-4E type 2
      Short name=eIF4E type 2
Alternative name(s):
    mRNA cap-binding protein type 3
    Eukaryotic translation initiation factor 4E-like 3
    Eukaryotic translation initiation factor 4E homologous protein
    mRNA cap-binding protein 4EHP
    eIF4E-like protein 4E-LP
Gene names
Name: EIF4E2
Synonyms: EIF4EL3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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 eIF4G. eIF4E is also known to interact with other partners By similarity. EIF4E2 interacts with EIF4EBP1, EIF4EBP2 and EIF4EBP3 but not with eIF4G.

Sequence similarities

Belongs to the eukaryotic initiation factor 4E family.

Ontologies

Keywords
   Biological processProtein biosynthesis
Translation regulation
   LigandRNA-binding
   Molecular functionInitiation factor
   Technical term3D-structure
Gene Ontology (GO)
   Biological processregulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

translational initiation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionRNA cap binding Ref.1

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: IntAct

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF4EBP1Q135411EBI-398610,EBI-74090
TRAF6Q9Y4K31EBI-398610,EBI-359276

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Eukaryotic translation initiation factor 4E type 2
PRO_0000193664

Experimental info

Mutagenesis631W → A: Unable to bind capped mRNA.
Mutagenesis951W → A: Ability to bind capped mRNA reduced to 40% of wild-type.
Mutagenesis124 – 1263WED → FAA: Unable to bind capped mRNA.
Mutagenesis1241W → A: Ability to bind capped mRNA reduced to less than 10% of wild-type.
Mutagenesis1241W → F: Ability to bind capped mRNA reduced to 13% of wild-type.
Mutagenesis1251E → A: Ability to bind capped mRNA reduced to less than 10% of wild-type.
Mutagenesis1261D → A: Slight reduction in ability to bind capped mRNA.
Mutagenesis1351W → A: Unable to bind capped mRNA.
Mutagenesis1481W → A: Unable to bind capped mRNA.
Mutagenesis1831W → A: Ability to bind capped mRNA reduced to less than 10% of wild-type.
Mutagenesis1831W → F: Unable to bind capped mRNA.
Sequence conflict1 – 2727MNNKF…STQKD → MMTVGTMIRMKKTAHRKI Ref.3

Secondary structure

.......................... 245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60573-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 3D3075BFA48B3C12

FASTA24528,362
        10         20         30         40         50         60 
MNNKFDALKD DDSGDHDQNE ENSTQKDGEK EKTERDKNQS SSKRKAVVPG PAEHPLQYNY 

        70         80         90        100        110        120 
TFWYSRRTPG RPTSSQSYEQ NIKQIGTFAS VEQFWRFYSH MVRPGDLTGH SDFHLFKEGI 

       130        140        150        160        170        180 
KPMWEDDANK NGGKWIIRLR KGLASRCWEN LILAMLGEQF MVGEEICGAV VSVRFQEDII 

       190        200        210        220        230        240 
SIWNKTASDQ ATTARIRDTL RRVLNLPPNT IMEYKTHTDS IKMPGRLGPQ RLLFQNLWKP 


RLNVP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein."
Rom E., Kim H.C., Gingras A.-C., Marcotrigiano J., Favre D., Olsen H., Burley S.K., Sonenberg N.
J. Biol. Chem. 273:13104-13109(1998) [PubMed: 9582349] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, 3D-STRUCTURE MODELING, MUTAGENESIS.
Tissue: Follicular cell.
[2]"Characterization of mammalian eIF4E-family members."
Joshi B., Cameron A., Jagus R.
Eur. J. Biochem. 271:2189-2203(2004) [PubMed: 15153109] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EIF4EBP1; EIF4EBP2 AND EIF4EBP3.
Tissue: Mammary gland.
[3]"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed: 9653160] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle, Urinary bladder and Uterus.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF047695 mRNA. Translation: AAC18565.1.
AF068117 mRNA. Translation: AAC19374.1.
AF038957 mRNA. Translation: AAC39871.1.
BC005392 mRNA. Translation: AAH05392.1.
BC005874 mRNA. Translation: AAH05874.1.
BC021226 mRNA. Translation: AAH21226.1.
BC021690 mRNA. Translation: AAH21690.1.
IPIIPI00744211.
RefSeqNP_004837.1.
UniGeneHs.292026

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2JGBX-ray1.70A45-234[»]
2JGCX-ray2.40A45-234[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO60573. 7 interactions.

Proteomic databases

PRIDEO60573.

Genome annotation databases

EnsemblENSG00000135930. Homo sapiens. [Contig view]
GeneID9470.
KEGGhsa:9470.

Organism-specific databases

GeneCardsGC02P233123.
H-InvDBHIX0002926.
HIX0059993.
HGNCHGNC:3293. EIF4E2.
HPAHPA019253.
MIM605895. gene.
PharmGKBPA27720.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO60573.
OMAO60573. LWKPRLN.

Gene expression databases

ArrayExpressO60573.
BgeeO60573.
CleanExHS_EIF4E2.
GermOnlineENSG00000135930. Homo sapiens.

Family and domain databases

InterProIPR001040. TIF_eIF_4E.
IPR019770. TIF_eIF_4E_CS.
[Graphical view]
Gene3DG3DSA:3.30.760.10. TIF_eIF_4E. 1 hit.
PANTHERPTHR11960. TIF_eIF_4E. 1 hit.
PfamPF01652. IF4E. 1 hit.
[Graphical view]
ProDomPD003697. TIF_eIF_4E. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00813. IF4E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio35490.
SOURCESearch...

Entry information

Entry nameIF4E2_HUMAN
AccessionPrimary (citable) accession number: O60573
Secondary accession number(s): O75349
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) 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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents