| UniProt ID | IF4E_HUMAN | |
|---|---|---|
| UniProt AC | P06730 | |
| Protein Name | Eukaryotic translation initiation factor 4E | |
| Gene Name | EIF4E | |
| Organism | Homo sapiens (Human). | |
| 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. 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 | MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MATVEPETT ------CCCCCCCCC | 21.98 | 19413330 | |
| 3 | Phosphorylation | -----MATVEPETTP -----CCCCCCCCCC | 24.89 | 22199227 | |
| 5 (in isoform 3) | Phosphorylation | - | 32.82 | 24043423 | |
| 6 (in isoform 3) | Phosphorylation | - | 39.64 | 24043423 | |
| 8 | Phosphorylation | MATVEPETTPTPNPP CCCCCCCCCCCCCCC | 49.11 | 23401153 | |
| 9 | Phosphorylation | ATVEPETTPTPNPPT CCCCCCCCCCCCCCC | 24.41 | 25159151 | |
| 11 | Phosphorylation | VEPETTPTPNPPTTE CCCCCCCCCCCCCCH | 33.34 | 28450419 | |
| 12 (in isoform 3) | Phosphorylation | - | 53.16 | 24043423 | |
| 13 (in isoform 3) | Phosphorylation | - | 58.63 | 24043423 | |
| 16 | Phosphorylation | TPTPNPPTTEEEKTE CCCCCCCCCHHHHCC | 48.36 | 23401153 | |
| 17 | Phosphorylation | PTPNPPTTEEEKTES CCCCCCCCHHHHCCC | 47.36 | 28450419 | |
| 22 | Phosphorylation | PTTEEEKTESNQEVA CCCHHHHCCCCCCCC | 48.18 | 28450419 | |
| 24 | Phosphorylation | TEEEKTESNQEVANP CHHHHCCCCCCCCCH | 49.39 | 25159151 | |
| 34 | Phosphorylation | EVANPEHYIKHPLQN CCCCHHHHCCCCCCC | 15.25 | 28450419 | |
| 36 (in isoform 2) | Ubiquitination | - | 31.81 | - | |
| 36 | Sumoylation | ANPEHYIKHPLQNRW CCHHHHCCCCCCCCE | 31.81 | - | |
| 36 | Ubiquitination | ANPEHYIKHPLQNRW CCHHHHCCCCCCCCE | 31.81 | 21890473 | |
| 49 | Sumoylation | RWALWFFKNDKSKTW CEEEEEEECCCCCCH | 55.55 | - | |
| 53 | Phosphorylation | WFFKNDKSKTWQANL EEEECCCCCCHHHHH | 37.88 | 20170512 | |
| 54 (in isoform 2) | Ubiquitination | - | 60.57 | - | |
| 54 | Ubiquitination | FFKNDKSKTWQANLR EEECCCCCCHHHHHH | 60.57 | - | |
| 55 | Phosphorylation | FKNDKSKTWQANLRL EECCCCCCHHHHHHH | 29.87 | 23882029 | |
| 56 | Ubiquitination | KNDKSKTWQANLRLI ECCCCCCHHHHHHHH | 10.06 | 21890473 | |
| 92 | Phosphorylation | LMPGCDYSLFKDGIE CCCCCCHHHCCCCCC | 17.68 | 24719451 | |
| 101 | Sulfoxidation | FKDGIEPMWEDEKNK CCCCCCCCCCCCCCC | 3.87 | 30846556 | |
| 108 | Acetylation | MWEDEKNKRGGRWLI CCCCCCCCCCCEEEE | 64.58 | 25953088 | |
| 119 | Ubiquitination | RWLITLNKQQRRSDL EEEEECCHHHHHHHH | 51.42 | - | |
| 119 (in isoform 2) | Ubiquitination | - | 51.42 | - | |
| 119 | Acetylation | RWLITLNKQQRRSDL EEEEECCHHHHHHHH | 51.42 | 23954790 | |
| 119 | Malonylation | RWLITLNKQQRRSDL EEEEECCHHHHHHHH | 51.42 | 26320211 | |
| 159 | Acetylation | AVVNVRAKGDKIAIW EEEEEEECCCEEEEE | 58.01 | 23749302 | |
| 159 | Ubiquitination | AVVNVRAKGDKIAIW EEEEEEECCCEEEEE | 58.01 | 1672057 | |
| 162 | Sumoylation | NVRAKGDKIAIWTTE EEEECCCEEEEEEEE | 42.58 | - | |
| 162 | Ubiquitination | NVRAKGDKIAIWTTE EEEECCCEEEEEEEE | 42.58 | - | |
| 162 | Acetylation | NVRAKGDKIAIWTTE EEEECCCEEEEEEEE | 42.58 | 25953088 | |
| 168 | O-linked_Glycosylation | DKIAIWTTECENREA CEEEEEEEEECCHHH | 24.52 | 30677218 | |
| 173 | Methylation | WTTECENREAVTHIG EEEEECCHHHHHHHH | 15.80 | - | |
| 177 | O-linked_Glycosylation | CENREAVTHIGRVYK ECCHHHHHHHHHHHH | 18.15 | 30677218 | |
| 183 | Phosphorylation | VTHIGRVYKERLGLP HHHHHHHHHHHHCCC | 13.03 | 19835603 | |
| 193 (in isoform 2) | Ubiquitination | - | 3.17 | - | |
| 197 | Phosphorylation | PPKIVIGYQSHADTA CCEEEEEEECCCCCC | 8.84 | 28152594 | |
| 199 | Phosphorylation | KIVIGYQSHADTATK EEEEEEECCCCCCCC | 16.50 | 24719451 | |
| 203 | Phosphorylation | GYQSHADTATKSGST EEECCCCCCCCCCCC | 36.69 | 26074081 | |
| 205 | Phosphorylation | QSHADTATKSGSTTK ECCCCCCCCCCCCCC | 28.03 | 26074081 | |
| 206 | Sumoylation | SHADTATKSGSTTKN CCCCCCCCCCCCCCC | 50.81 | - | |
| 206 | Ubiquitination | SHADTATKSGSTTKN CCCCCCCCCCCCCCC | 50.81 | - | |
| 206 | Malonylation | SHADTATKSGSTTKN CCCCCCCCCCCCCCC | 50.81 | 26320211 | |
| 207 | Phosphorylation | HADTATKSGSTTKNR CCCCCCCCCCCCCCE | 33.35 | 26074081 | |
| 209 | Phosphorylation | DTATKSGSTTKNRFV CCCCCCCCCCCCEEC | 39.74 | 19934253 | |
| 210 | Phosphorylation | TATKSGSTTKNRFVV CCCCCCCCCCCEECC | 45.36 | 26074081 | |
| 211 | Phosphorylation | ATKSGSTTKNRFVV- CCCCCCCCCCEECC- | 28.19 | 26074081 | |
| 212 | Sumoylation | TKSGSTTKNRFVV-- CCCCCCCCCEECC-- | 46.33 | - | |
| 230 | Phosphorylation | -------------------- -------------------- | 24719451 | ||
| 237 (in isoform 2) | Ubiquitination | - | - | ||
| 242 | Phosphorylation | -------------------------------- -------------------------------- | 24719451 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 209 | S | Phosphorylation | Kinase | MKNK1 | Q9BUB5 | PhosphoELM |
| 209 | S | Phosphorylation | Kinase | MNK1 ISO2 | Q9BUB5-2 | PSP |
| 209 | S | Phosphorylation | Kinase | MKNK1 | O08605 | GPS |
| 209 | S | Phosphorylation | Kinase | MNK2 | Q9HBH9 | PSP |
| 209 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
| 209 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IF4E_HUMAN !! | ||||||
* 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_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 615091 | Autism 19 (AUTS19) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Acetylation | |
| Reference | PubMed |
| "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 | |
| Reference | PubMed |
| "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. | |
| "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. | |
| "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. | |
