Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Eukaryotic translation initiation factor 4E  

UniProtKB / Swiss-Prot ID :  IF4E_HUMAN

Gene Name (Synonyms) : 
EIF4E, EIF4EL1, EIF4F  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, P-body. 

Protein Function :  Its translation stimulation activity is repressed by binding to the complex CYFIP1-FMR1 (By similarity). 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. 

Protein Sequence MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVE...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEEECCCCCCCHHHHCCCCEEECCHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATVEP
---CCCCCC
21.98UniProtKB
Link-
9PhosphothreonineEPETTPTPN
CCCCCCCCC
24.41HPRD
Link-
9PhosphothreonineEPETTPTPN
CCCCCCCCC
24.41Phosphositeplus
Link-
22PhosphothreonineEEEKTESNQ
CCCCCCCCC
48.18HPRD
Link-
36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EHYIKHPLQ
CCCCCCCCC
31.81Phosphositeplus
Link
53PhosphoserineKNDKSKTWQ
CCCCCCCHH
37.88HPRD
Link
53PhosphoserineKNDKSKTWQ
CCCCCCCHH
37.88PhosphoELM
Link
53PhosphoserineKNDKSKTWQ
CCCCCCCHH
37.88Phosphositeplus
Link
159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NVRAKGDKI
EEECCCCEE
58.01Phosphositeplus
Link
183PhosphotyrosineIGRVYKERL
HHHHHHHHH
13.03Phosphositeplus
Link
209PhosphoserineTKSGSTTKN
HCCCCCCCC
39.74Phosphositeplus
Link
209Phosphoserine (MKNK1)TKSGSTTKN
HCCCCCCCC
39.74HPRD
Link
209Phosphoserine (MKNK2)TKSGSTTKN
HCCCCCCCC
39.74HPRD
Link
209Phosphoserine (Mnk1;Mnk2)TKSGSTTKN
HCCCCCCCC
39.74PhosphoELM
Link
209Phosphoserine (PRKCA)TKSGSTTKN
HCCCCCCCC
39.74HPRD
Link
209Phosphoserine (PRKCB)TKSGSTTKN
HCCCCCCCC
39.74HPRD
Link
209Phosphoserine (PRKCG)TKSGSTTKN
HCCCCCCCC
39.74HPRD
Link
209Phosphoserine; by PKC and MKNK2.TKSGSTTKN
HCCCCCCCC
39.74UniProtKB
Link
210PhosphothreonineKSGSTTKNR
CCCCCCCCE
45.36Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IF4G1_HUMANphysical interactionMINT-17286MINT7651417
4EBP1_HUMANphysical interactionMINT-19056MINT7935836
4EBP1_HUMANphysical interactionMINT-19057MINT7935836
4ET_HUMANcolocalizationMINT-1956046MINT16467844
4EBP1_HUMANphysical interaction
physical interaction
direct interaction
physical interaction
physical interaction
EBI-74102
EBI-760300
EBI-9351
intact10772338
16189514
15153109
17353931
7651417
IF4G1_HUMANdirect interaction
physical interaction
EBI-928154
EBI-464760
intact15153109
15361857
4EBP2_HUMANdirect interactionEBI-935146
intact15153109
IF4A1_HUMANphysical interactionEBI-1071340
intact17353931
EMX2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-399863
EBI-399857
EBI-399
intact15247416
15247416
15247416
15247416
PML_HUMANin vitroHPRD:00591HPRD11500381
IF4E_HUMANin vitro
in vivo
HPRD:00591HPRD12482586
RS20_HUMANENSP00000280892STRING
RS5_HUMANENSP00000280892STRING
RS18_HUMANENSP00000280892STRING
EIF3D_HUMANENSP00000280892STRING
IF5_HUMANENSP00000280892STRING
EIF3E_HUMANENSP00000280892STRING
RS19_HUMANENSP00000280892STRING
KS6B1_HUMANENSP00000280892STRING
CCND1_HUMANENSP00000280892STRING
RS13_HUMANENSP00000280892STRING
RS12_HUMANENSP00000280892STRING
2A5D_HUMANENSP00000280892STRING
RS15_HUMANENSP00000280892STRING
RS25_HUMANENSP00000280892STRING
EIF3K_HUMANENSP00000280892STRING
RS4Y1_HUMANENSP00000280892STRING
INS_HUMANENSP00000280892STRING
INS_HUMANENSP00000280892STRING
RS16_HUMANENSP00000280892STRING
IF2G_HUMANENSP00000280892STRING
EIF3G_HUMANENSP00000280892STRING
IF2A_HUMANENSP00000280892STRING
EIF3J_HUMANENSP00000280892STRING
IF4B_HUMANENSP00000280892STRING
RHEB_HUMANENSP00000280892STRING
DDX6_HUMANENSP00000280892STRING
IF4G3_HUMANENSP00000280892STRING
IF4H_HUMANENSP00000280892STRING
PML_HUMANENSP00000280892STRING
RS11_HUMANENSP00000280892STRING
RL13A_HUMANENSP00000280892STRING
RS27A_HUMANENSP00000280892STRING
UBIQ_HUMANENSP00000280892STRING
REN3B_HUMANENSP00000280892STRING
EIF3H_HUMANENSP00000280892STRING
RS3_HUMANENSP00000280892STRING
UBIM_HUMANENSP00000280892STRING
RS30_HUMANENSP00000280892STRING
NXF1_HUMANENSP00000280892STRING
RS23_HUMANENSP00000280892STRING
ANKH1_HUMANENSP00000280892STRING
ANKH1_HUMANENSP00000280892STRING
ANKH1_HUMANENSP00000280892STRING
RS9_HUMANENSP00000280892STRING
RPTOR_HUMANENSP00000280892STRING
EIF3F_HUMANENSP00000280892STRING
EIF3F_HUMANENSP00000280892STRING
RS14_HUMANENSP00000280892STRING
PABP1_HUMANENSP00000280892STRING
SLBP_HUMANENSP00000280892STRING
RS15A_HUMANENSP00000280892STRING
IF4G1_HUMANENSP00000280892STRING
IF4A2_HUMANENSP00000280892STRING
NCBP2_HUMANENSP00000280892STRING
4ET_HUMANENSP00000280892STRING
THOC4_HUMANENSP00000280892STRING
EIF3C_HUMANENSP00000280892STRING
RS7_HUMANENSP00000280892STRING
IF4G2_HUMANENSP00000280892STRING
4EBP1_HUMANENSP00000280892STRING
RS2_HUMANENSP00000280892STRING
ATP7A_HUMANENSP00000280892STRING
RS17_HUMANENSP00000280892STRING
RS3A_HUMANENSP00000280892STRING
RSSA_HUMANENSP00000280892STRING
RS26_HUMANENSP00000280892STRING
RS28_HUMANENSP00000280892STRING
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Disease Reference
Kegg disease
OMIM disease
615091Autism 19 (AUTS19)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation of eukaryotic protein synthesis initiation factor 4Eat 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).
Cited for: PHOSPHORYLATION AT SER-209.
"Serine 209, not serine 53, is the major site of phosphorylation ininitiation factor eIF-4E in serum-treated Chinese hamster ovarycells.";
Flynn A., Proud C.G.;
J. Biol. Chem. 270:21684-21688(1995).
Cited for: PHOSPHORYLATION AT SER-209.
"The mitogen-activated protein kinase signal-integrating kinase Mnk2is a eukaryotic initiation factor 4E kinase with high levels of basalactivity in mammalian cells.";
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
Mol. Cell. Biol. 21:743-754(2001).
Cited for: PHOSPHORYLATION AT SER-209 BY MKNK2.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures