IF4E_MOUSE - dbPTM
IF4E_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF4E_MOUSE
UniProt AC P63073
Protein Name Eukaryotic translation initiation factor 4E
Gene Name Eif4e
Organism Mus musculus (Mouse).
Sequence Length 217
Subcellular Localization Cytoplasm, P-body. Cytoplasm .
Protein Description 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..
Protein Sequence MATVEPETTPTTNPPPAEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENRDAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MATVEPETT
------CCCCCCCCC
21.98-
3Phosphorylation-----MATVEPETTP
-----CCCCCCCCCC
24.8925293948
8PhosphorylationMATVEPETTPTTNPP
CCCCCCCCCCCCCCC
49.1125293948
9PhosphorylationATVEPETTPTTNPPP
CCCCCCCCCCCCCCC
19.5825293948
11PhosphorylationVEPETTPTTNPPPAE
CCCCCCCCCCCCCCH
36.7925293948
12PhosphorylationEPETTPTTNPPPAEE
CCCCCCCCCCCCCHH
47.1025293948
22PhosphorylationPPAEEEKTESNQEVA
CCCHHHCCCCCCCCC
48.1826643407
24PhosphorylationAEEEKTESNQEVANP
CHHHCCCCCCCCCCH
49.3926643407
34PhosphorylationEVANPEHYIKHPLQN
CCCCHHHHCCCCCCC
15.2526643407
54MalonylationFFKNDKSKTWQANLR
EEECCCCCCHHHHHH
60.5726320211
119UbiquitinationRWLITLNKQQRRSDL
EEEEECCHHHHHHHH
51.42-
119AcetylationRWLITLNKQQRRSDL
EEEEECCHHHHHHHH
51.4222826441
119MalonylationRWLITLNKQQRRSDL
EEEEECCHHHHHHHH
51.4226320211
159MalonylationAVVNVRAKGDKIAIW
EEEEEEECCCEEEEE
58.0126320211
162MalonylationNVRAKGDKIAIWTTE
EEEECCCEEEEEEEE
42.5826320211
170GlutathionylationIAIWTTECENRDAVT
EEEEEEEECCCCHHH
5.4324333276
206MalonylationSHADTATKSGSTTKN
CCCCCCCCCCCCCCC
50.8126320211
207PhosphorylationHADTATKSGSTTKNR
CCCCCCCCCCCCCCE
33.3526160508
209PhosphorylationDTATKSGSTTKNRFV
CCCCCCCCCCCCEEC
39.7418805096
210PhosphorylationTATKSGSTTKNRFVV
CCCCCCCCCCCEECC
45.3626160508
211PhosphorylationATKSGSTTKNRFVV-
CCCCCCCCCCEECC-
28.1923140645

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
209SPhosphorylationKinasePRKCAP04409
GPS
209SPhosphorylationKinaseKPCAP20444
PhosphoELM
209SPhosphorylationKinaseMNK1Q9BUB5
PSP
209SPhosphorylationKinaseMKNK1O08605
PhosphoELM
209SPhosphorylationKinaseMKNK2Q8CDB0
Uniprot
209SPhosphorylationKinasePKC-FAMILY-GPS
209SPhosphorylationKinasePKC-Uniprot
210TPhosphorylationKinaseMKNK1Q9BUB5
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF4E_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of IF4E_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4G1_HUMANEIF4G1physical
12149653
IF4E_MOUSEEif4ephysical
12149653
IF4G3_MOUSEEif4g3physical
16899032
DCC_MOUSEDccphysical
20434207
4EBP2_MOUSEEif4ebp2physical
8939971
4EBP2_MOUSEEif4ebp2physical
20347422
4EBP1_MOUSEEif4ebp1physical
20971826
IF4G1_MOUSEEif4g1physical
20971826
4ET_MOUSEEif4enif1physical
25923732

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF4E_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Roles of mitogen-activated protein kinase signal-integrating kinases1 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).
Cited for: PHOSPHORYLATION AT SER-209 BY MKNK2.

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