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P06730 (IF4E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 4E

Short name=eIF-4E
Short name=eIF4E
Alternative name(s):
eIF-4F 25 kDa subunit
mRNA cap-binding protein
Gene names
Name:EIF4E
Synonyms:EIF4EL1, EIF4F
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. 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.26 Ref.29

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. Interacts with NGDN and PIWIL2. Component of the CYFIP1-EIF4E-FMR1 complex composed of CYFIP, EIF4E and FMR1. Interacts directly with CYFIP1. Interacts with CLOCK By similarity. Interacts with Lassa virus Z protein. Binds to MKNK2 in nucleus. Interacts with LIMD1, WTIP and AJUBA. Interacts with APOBEC3G in an RNA-dependent manner. Interacts with LARP1. Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.23 Ref.24 Ref.29

Subcellular location

CytoplasmP-body. Cytoplasm By similarity Ref.24.

Post-translational modification

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

Involvement in disease

Autism 19 (AUTS19) [MIM:615091]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. A heterozygous single-nucleotide insertion has been found in families affected by autism. The variant results in increased promoter activity and is involved in disease pathogenesis through EIF4E deregulation (Ref.22). Ref.22

A chromosomal aberration involving EIF4E has been found in a patient with classic autism. Translocation t45(q23q31.3). The breakpoint on chromosome 4 is located 56 kb downstream of EIF4E (Ref.22).

Sequence similarities

Belongs to the eukaryotic initiation factor 4E family.

Caution

Was originally thought to be phosphorylated on Ser-53 (Ref.9); this was later shown to be wrong (Ref.13).

Mass spectrometry

Molecular mass is 24964.3 Da from positions 2 - 217. Determined by ESI. Ref.30

Molecular mass is 24960 Da from positions 2 - 217. Determined by ESI. Ref.31

Ontologies

Keywords
   Biological processHost-virus interaction
Protein biosynthesis
Translation regulation
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 14673156. Source: UniProtKB

RNA metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA poly(A) tail shortening

Traceable author statement. Source: Reactome

positive regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 14673156. Source: UniProtKB

regulation of translation

Inferred from direct assay Ref.26. Source: UniProtKB

translation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentRISC complex

Inferred from direct assay Ref.24. Source: MGI

chromatoid body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic mRNA processing body

Inferred from direct assay Ref.24. Source: MGI

cytoplasmic stress granule

Inferred from direct assay PubMed 21883093. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 4F complex

Inferred from direct assay Ref.26. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

mRNA cap binding complex

Inferred from direct assay Ref.29. Source: UniProtKB

   Molecular_functionRNA cap binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

translation initiation factor activity

Inferred from direct assay Ref.26. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06730-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P06730-2)

The sequence of this isoform differs from the canonical sequence as follows:
     133-133: T → TRWDLAMLPRLVSNFWPQVILPLQPPKVLELQ
Note: No experimental confirmation available.
Isoform 3 (identifier: P06730-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MATVEP → MLDLTSRGQVGTSRRMAEAACSAHFL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21 Ref.30
Chain2 – 217216Eukaryotic translation initiation factor 4E
PRO_0000193634

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 Ref.21
Modified residue2091Phosphoserine; by PKC and MKNK2 Ref.12 Ref.13 Ref.18

Natural variations

Alternative sequence1 – 66MATVEP → MLDLTSRGQVGTSRRMAEAA CSAHFL in isoform 3.
VSP_043591
Alternative sequence1331T → TRWDLAMLPRLVSNFWPQVI LPLQPPKVLELQ in isoform 2.
VSP_042014

Experimental info

Mutagenesis531S → A or D: No effect on phosphorylation level nor incorporation into eIF4F complex. Ref.10 Ref.11
Mutagenesis731W → A: Abolishes binding to EIF4EBP1. Ref.26
Mutagenesis1021W → L: Decrease in mRNA cap binding; when associated with A-105. Ref.8
Mutagenesis1031E → A: No effect. Ref.8
Mutagenesis1041D → A: No effect. Ref.8
Mutagenesis1051E → A: Decrease in mRNA cap binding; when associated with L-102. Ref.8
Mutagenesis1191K → A: Higher affinity for EIF4G1. Ref.30
Sequence conflict1271D → N in AAH12611. Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: B869B8DE615E699D

FASTA21725,097
        10         20         30         40         50         60 
MATVEPETTP TPNPPTTEEE 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 ENREAVTHIG 

       190        200        210 
RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV 

« Hide

Isoform 2 [UniParc].

Checksum: 3869E3249A241190
Show »

FASTA24828,778
Isoform 3 [UniParc].

Checksum: D4925235C678DE08
Show »

FASTA23727,260

References

« Hide 'large scale' references
[1]"Amino acid sequence of the mRNA cap-binding protein from human tissues."
Rychlik W., Domier L.L., Gardner P.R., Hellmann G.M., Rhoads R.E.
Proc. Natl. Acad. Sci. U.S.A. 84:945-949(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]Erratum
Rychlik W., Domier L.L., Gardner P.R., Hellmann G.M., Rhoads R.E.
Proc. Natl. Acad. Sci. U.S.A. 89:1148-1148(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 108 AND 189.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Small intestine.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Brain and Testis.
[6]"Transcriptome analysis of human gastric cancer."
Oh J.H., Yang J.O., Hahn Y., Kim M.R., Byun S.S., Jeon Y.J., Kim J.M., Song K.S., Noh S.M., Kim S., Yoo H.S., Kim Y.S., Kim N.S.
Mamm. Genome 16:942-954(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-214 (ISOFORM 2).
Tissue: Myeloma.
[7]"Phosphorylation of the proto-oncogene product eukaryotic initiation factor 4E is a common cellular response to tumor necrosis factor."
Marino M.W., Feld L.J., Jaffe E.A., Pfeffer L.M., Han Y.-M., Donner D.B.
J. Biol. Chem. 266:2685-2688(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[8]"Combination of Trp and Glu residues for recognition of mRNA cap structure. Analysis of m7G base recognition site of human cap binding protein (IF-4E) by site-directed mutagenesis."
Ueda H., Iyo H., Doi M., Inoue M., Ishida T., Morioka H., Tanaka T., Nishikawa S., Uesugi S.
FEBS Lett. 280:207-210(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-102; GLU-103; ASP-104 AND GLU-105.
[9]"Phosphorylation site of eukaryotic initiation factor 4E."
Rychlik W., Russ M.A., Rhoads R.E.
J. Biol. Chem. 262:10434-10437(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[10]"Characterization of wild-type and Ser53 mutant eukaryotic initiation factor 4E overexpression in mammalian cells."
Kaufman R.J., Murtha-Riel P., Pittman D.D., Davies M.V.
J. Biol. Chem. 268:11902-11909(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-53.
[11]"Role of Ser-53 phosphorylation in the activity of human translation initiation factor eIF-4E in mammalian and yeast cells."
Zhang Y., Klein H.L., Schneider R.J.
Gene 163:283-288(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-53.
[12]"Phosphorylation of eukaryotic protein synthesis initiation factor 4E at Ser-209."
Joshi B., Cai A.L., Keiper B.D., Minich W.B., Mendez R., Beach C.M., Stepinski J., Stolarski R., Darzynkiewicz E., Rhoads R.E.
J. Biol. Chem. 270:14597-14603(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-209.
[13]"Serine 209, not serine 53, is the major site of phosphorylation in initiation factor eIF-4E in serum-treated Chinese hamster ovary cells."
Flynn A., Proud C.G.
J. Biol. Chem. 270:21684-21688(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-209.
[14]"Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E."
Haghighat A., Mader S., Pause A., Sonenberg N.
EMBO J. 14:5701-5709(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4G AND EIF4EBP1.
[15]"A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E."
Dostie J., Ferraiuolo M., Pause A., Adam S.A., Sonenberg N.
EMBO J. 19:3142-3156(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4ENIF1.
Tissue: Fetal brain and Placenta.
[16]"Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E."
Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N.
EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY MKNK1.
[17]"Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo."
Li W., Belsham G.J., Proud C.G.
J. Biol. Chem. 276:29111-29115(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4A1 AND EIF4A2.
[18]"The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-209 BY MKNK2.
[19]"The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization."
Scheper G.C., Parra J.L., Wilson M., Van Kollenburg B., Vertegaal A.C.O., Han Z.-G., Proud C.G.
Mol. Cell. Biol. 23:5692-5705(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MKNK2.
[20]"Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies."
Wichroski M.J., Robb G.B., Rana T.M.
PLoS Pathog. 2:E41-E41(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APOBEC3G.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[22]"Deregulation of EIF4E: a novel mechanism for autism."
Neves-Pereira M., Mueller B., Massie D., Williams J.H., O'Brien P.C., Hughes A., Shen S.B., Clair D.S., Miedzybrodzka Z.
J. Med. Genet. 46:759-765(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AUTS19, CHROMOSOMAL TRANSLOCATION.
[23]"The RNA binding protein Larp1 regulates cell division, apoptosis and cell migration."
Burrows C., Abd Latip N., Lam S.J., Carpenter L., Sawicka K., Tzolovsky G., Gabra H., Bushell M., Glover D.M., Willis A.E., Blagden S.P.
Nucleic Acids Res. 38:5542-5553(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LARP1.
[24]"LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing."
James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M., Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J., Longmore G.D., Bushell M., Sharp T.V.
Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMD1; WTIP AND AJUBA.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Translational homeostasis via the mRNA cap-binding protein, eIF4E."
Yanagiya A., Suyama E., Adachi H., Svitkin Y.V., Aza-Blanc P., Imataka H., Mikami S., Martineau Y., Ronai Z.A., Sonenberg N.
Mol. Cell 46:847-858(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-73.
[27]"Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region."
Tomoo K., Shen X., Okabe K., Nozoe Y., Fukuhara S., Morino S., Ishida T., Taniguchi T., Hasegawa H., Terashima A., Sasaki M., Katsuya Y., Kitamura K., Miyoshi H., Ishikawa M., Miura K.
Biochem. J. 362:539-544(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MRNA CAP ANALOGS.
[28]"Backbone resonance assignment of human eukaryotic translation initiation factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and a 17-amino acid peptide derived from human eIF4GII."
Miura T., Shiratori Y., Shimma N.
J. Biomol. NMR 27:279-280(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH EIF4G3 AND MRNA CAP ANALOGS.
[29]"Structural basis for mRNA cap-binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods."
Tomoo K., Matsushita Y., Fujisaki H., Abiko F., Shen X., Taniguchi T., Miyagawa H., Kitamura K., Miura K., Ishida T.
Biochim. Biophys. Acta 1753:191-208(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-217 IN COMPLEX WITH MRNA CAP ANALOG AND EIF4EBP1, FUNCTION, INTERACTION WITH EIF4EBP1; EIF4EBP2 AND EIF4EBP3.
[30]"Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands."
Volpon L., Osborne M.J., Topisirovic I., Siddiqui N., Borden K.L.B.
EMBO J. 25:5138-5149(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY, MUTAGENESIS OF LYS-119.
[31]"Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives."
Brown C.J., McNae I., Fischer P.M., Walkinshaw M.D.
J. Mol. Biol. 372:7-15(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH MRNA CAP ANALOGS, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15353 mRNA. Translation: AAC13647.1.
AK300982 mRNA. Translation: BAH13387.1.
AC019131 Genomic DNA. No translation available.
AC093836 Genomic DNA. No translation available.
BC012611 mRNA. Translation: AAH12611.1.
BC035166 mRNA. Translation: AAH35166.1.
BC043226 mRNA. Translation: AAH43226.1.
BM849222 mRNA. No translation available.
PIRA26411.
RefSeqNP_001124150.1. NM_001130678.1.
NP_001124151.1. NM_001130679.1.
NP_001959.1. NM_001968.3.
UniGeneHs.249718.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IPBX-ray2.00A1-217[»]
1IPCX-ray2.00A1-217[»]
1WKWX-ray2.10A27-217[»]
2GPQNMR-A1-217[»]
2V8WX-ray2.30A/E1-217[»]
2V8XX-ray2.30A/E1-217[»]
2V8YX-ray2.10A/E1-217[»]
2W97X-ray2.29A/B1-217[»]
3AM7X-ray2.20A27-217[»]
3TF2X-ray2.10A/B/C/D1-217[»]
3U7XX-ray2.10A/B1-217[»]
4AZAX-ray2.16A/C1-217[»]
4BEAX-ray2.57A1-217[»]
4DT6X-ray2.60A1-217[»]
4DUMX-ray2.95A1-217[»]
ProteinModelPortalP06730.
SMRP06730. Positions 1-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108292. 39 interactions.
DIPDIP-22N.
IntActP06730. 30 interactions.
MINTMINT-85626.
STRING9606.ENSP00000280892.

Chemistry

BindingDBP06730.
ChEMBLCHEMBL4848.

PTM databases

PhosphoSiteP06730.

Polymorphism databases

DMDM1352435.

2D gel databases

OGPP06730.
REPRODUCTION-2DPAGEIPI00027485.

Proteomic databases

PaxDbP06730.
PRIDEP06730.

Protocols and materials databases

DNASU1977.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280892; ENSP00000280892; ENSG00000151247. [P06730-3]
ENST00000450253; ENSP00000389624; ENSG00000151247. [P06730-1]
ENST00000505992; ENSP00000425561; ENSG00000151247. [P06730-2]
GeneID1977.
KEGGhsa:1977.
UCSCuc003hue.2. human. [P06730-1]
uc011cea.1. human. [P06730-3]
uc011ceb.1. human. [P06730-2]

Organism-specific databases

CTD1977.
GeneCardsGC04M099799.
H-InvDBHIX0039231.
HGNCHGNC:3287. EIF4E.
HPACAB004077.
CAB016316.
HPA051311.
MIM133440. gene.
615091. phenotype.
neXtProtNX_P06730.
Orphanet106. Autism.
PharmGKBPA27714.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5053.
HOGENOMHOG000186751.
HOVERGENHBG006130.
KOK03259.
OMANDENTAP.
OrthoDBEOG7QRQVM.
PhylomeDBP06730.
TreeFamTF101526.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_6900. Immune System.
REACT_71. Gene Expression.
SignaLinkP06730.

Gene expression databases

ArrayExpressP06730.
BgeeP06730.
CleanExHS_EIF4E.
GenevestigatorP06730.

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

ChiTaRSEIF4E. human.
EvolutionaryTraceP06730.
GeneWikiEIF4E.
GenomeRNAi1977.
NextBio7999.
PROP06730.
SOURCESearch...

Entry information

Entry nameIF4E_HUMAN
AccessionPrimary (citable) accession number: P06730
Secondary accession number(s): B7Z6V1, D6RCQ6, Q96E95
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM