| UniProt ID | EIF3F_HUMAN | |
|---|---|---|
| UniProt AC | O00303 | |
| Protein Name | Eukaryotic translation initiation factor 3 subunit F {ECO:0000255|HAMAP-Rule:MF_03005} | |
| Gene Name | EIF3F {ECO:0000255|HAMAP-Rule:MF_03005} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 357 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. [PubMed: 17581632] | |
| Protein Sequence | MATPAVPVSAPPATPTPVPAAAPASVPAPTPAPAAAPVPAAAPASSSDPAAAAAATAAPGQTPASAQAPAQTPAPALPGPALPGPFPGGRVVRLHPVILASIVDSYERRNEGAARVIGTLLGTVDKHSVEVTNCFSVPHNESEDEVAVDMEFAKNMYELHKKVSPNELILGWYATGHDITEHSVLIHEYYSREAPNPIHLTVDTSLQNGRMSIKAYVSTLMGVPGRTMGVMFTPLTVKYAYYDTERIGVDLIMKTCFSPNRVIGLSSDLQQVGGASARIQDALSTVLQYAEDVLSGKVSADNTVGRFLMSLVNQVPKIVPDDFETMLNSNINDLLMVTYLANLTQSQIALNEKLVNL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MATPAVPVS ------CCCCCCCCC | 23.45 | 17322308 | |
| 46 | Phosphorylation | PAAAPASSSDPAAAA CCCCCCCCCCHHHHH | 40.65 | 19245811 | |
| 101 | Phosphorylation | LHPVILASIVDSYER EEHHHHHHHHHHHHH | 21.50 | 28152594 | |
| 105 | Phosphorylation | ILASIVDSYERRNEG HHHHHHHHHHHHCHH | 20.28 | 28152594 | |
| 106 | Phosphorylation | LASIVDSYERRNEGA HHHHHHHHHHHCHHH | 14.70 | 28152594 | |
| 119 | Phosphorylation | GAARVIGTLLGTVDK HHHHHHHHHHHCCCC | 14.00 | 19245811 | |
| 126 | Ubiquitination | TLLGTVDKHSVEVTN HHHHCCCCCCEEEEE | 33.18 | 21963094 | |
| 132 | Phosphorylation | DKHSVEVTNCFSVPH CCCCEEEEECEECCC | 16.86 | 26126808 | |
| 136 | Phosphorylation | VEVTNCFSVPHNESE EEEEECEECCCCCCC | 36.62 | 28985074 | |
| 142 | Phosphorylation | FSVPHNESEDEVAVD EECCCCCCCCCEEEC | 56.52 | 27050516 | |
| 154 | Ubiquitination | AVDMEFAKNMYELHK EECHHHHHHHHHHHH | 47.79 | 21963094 | |
| 161 | Acetylation | KNMYELHKKVSPNEL HHHHHHHHCCCCCCE | 68.45 | 26051181 | |
| 161 | 2-Hydroxyisobutyrylation | KNMYELHKKVSPNEL HHHHHHHHCCCCCCE | 68.45 | - | |
| 161 | Ubiquitination | KNMYELHKKVSPNEL HHHHHHHHCCCCCCE | 68.45 | 21963094 | |
| 214 | Ubiquitination | QNGRMSIKAYVSTLM CCCCEEHHHHHHHHH | 26.76 | - | |
| 214 | Acetylation | QNGRMSIKAYVSTLM CCCCEEHHHHHHHHH | 26.76 | 26051181 | |
| 216 | Phosphorylation | GRMSIKAYVSTLMGV CCEEHHHHHHHHHCC | 7.02 | 20068231 | |
| 218 | Phosphorylation | MSIKAYVSTLMGVPG EEHHHHHHHHHCCCC | 11.80 | 23532336 | |
| 219 | Phosphorylation | SIKAYVSTLMGVPGR EHHHHHHHHHCCCCC | 15.66 | 20068231 | |
| 221 | Sulfoxidation | KAYVSTLMGVPGRTM HHHHHHHHCCCCCCC | 5.28 | 30846556 | |
| 228 | Sulfoxidation | MGVPGRTMGVMFTPL HCCCCCCCEEEEEEE | 3.52 | 21406390 | |
| 233 | Phosphorylation | RTMGVMFTPLTVKYA CCCEEEEEEEEEEEE | 10.17 | - | |
| 238 | Ubiquitination | MFTPLTVKYAYYDTE EEEEEEEEEEEECCH | 20.94 | 21963094 | |
| 238 | Acetylation | MFTPLTVKYAYYDTE EEEEEEEEEEEECCH | 20.94 | 19608861 | |
| 241 | Phosphorylation | PLTVKYAYYDTERIG EEEEEEEEECCHHHC | 9.97 | 28152594 | |
| 242 | Phosphorylation | LTVKYAYYDTERIGV EEEEEEEECCHHHCC | 14.28 | 25839225 | |
| 244 | Phosphorylation | VKYAYYDTERIGVDL EEEEEECCHHHCCEE | 15.84 | 28152594 | |
| 253 | Sulfoxidation | RIGVDLIMKTCFSPN HHCCEEEHHHCCCCC | 3.70 | 21406390 | |
| 254 | Acetylation | IGVDLIMKTCFSPNR HCCEEEHHHCCCCCC | 34.84 | 26051181 | |
| 254 | Ubiquitination | IGVDLIMKTCFSPNR HCCEEEHHHCCCCCC | 34.84 | 21963094 | |
| 255 | Phosphorylation | GVDLIMKTCFSPNRV CCEEEHHHCCCCCCE | 11.03 | 22167270 | |
| 258 | Phosphorylation | LIMKTCFSPNRVIGL EEHHHCCCCCCEEEE | 24.34 | 22167270 | |
| 261 | Methylation | KTCFSPNRVIGLSSD HHCCCCCCEEEECCC | 25.47 | - | |
| 266 | Phosphorylation | PNRVIGLSSDLQQVG CCCEEEECCCHHHHC | 19.32 | 23927012 | |
| 267 | Phosphorylation | NRVIGLSSDLQQVGG CCEEEECCCHHHHCC | 47.59 | 23927012 | |
| 276 | Phosphorylation | LQQVGGASARIQDAL HHHHCCHHHHHHHHH | 22.73 | 23403867 | |
| 295 | Phosphorylation | QYAEDVLSGKVSADN HHHHHHHCCCCCCCC | 36.09 | 20068231 | |
| 297 | Ubiquitination | AEDVLSGKVSADNTV HHHHHCCCCCCCCHH | 29.64 | - | |
| 299 | Phosphorylation | DVLSGKVSADNTVGR HHHCCCCCCCCHHHH | 33.13 | 21406692 | |
| 303 | Phosphorylation | GKVSADNTVGRFLMS CCCCCCCHHHHHHHH | 25.53 | 21406692 | |
| 309 | Sulfoxidation | NTVGRFLMSLVNQVP CHHHHHHHHHHHCCC | 2.40 | 21406390 | |
| 310 | Phosphorylation | TVGRFLMSLVNQVPK HHHHHHHHHHHCCCC | 31.17 | 21406692 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 46 | S | Phosphorylation | Kinase | CDK11B | P21127 | PSP |
| 46 | S | Phosphorylation | Kinase | CDK19 | Q9BWU1 | PSP |
| 119 | T | Phosphorylation | Kinase | CDK19 | Q9BWU1 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXO32 | Q969P5 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXO33 | Q7Z6M2 | PMID:18354498 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EIF3F_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 EIF3F_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry."; Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.; Mol. Cell. Proteomics 6:1135-1146(2007). Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,PHOSPHORYLATION AT SER-258, AND MASS SPECTROMETRY. | |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASSSPECTROMETRY. | |
| "Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry."; Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.; Mol. Cell. Proteomics 6:1135-1146(2007). Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,PHOSPHORYLATION AT SER-258, AND MASS SPECTROMETRY. | |
