| UniProt ID | EIF3E_MOUSE | |
|---|---|---|
| UniProt AC | P60229 | |
| Protein Name | Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004} | |
| Gene Name | Eif3e | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 445 | |
| Subcellular Localization | Cytoplasm . Nucleus, PML body . | |
| 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. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins.. | |
| Protein Sequence | MAEYDLTTRIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY | |
| 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 | ------MAEYDLTTR ------CCCCCCHHH | 24.85 | - | |
| 35 | Acetylation | VKEIYNEKELLQGKL HHHHHCHHHHHCCHH | 50.45 | 23954790 | |
| 35 | Ubiquitination | VKEIYNEKELLQGKL HHHHHCHHHHHCCHH | 50.45 | 22790023 | |
| 82 | Ubiquitination | TTVVAQLKQLQAETE HHHHHHHHHHHHHCC | 36.56 | 22790023 | |
| 88 | Phosphorylation | LKQLQAETEPIVKMF HHHHHHHCCCHHHHH | 50.51 | 22802335 | |
| 93 | Ubiquitination | AETEPIVKMFEDPET HHCCCHHHHHCCHHH | 38.29 | 22790023 | |
| 100 | Phosphorylation | KMFEDPETTRQMQST HHHCCHHHHHHHHHC | 32.44 | 22802335 | |
| 101 | Phosphorylation | MFEDPETTRQMQSTR HHCCHHHHHHHHHCC | 19.76 | 25168779 | |
| 106 | Phosphorylation | ETTRQMQSTRDGRML HHHHHHHHCCCCHHH | 21.77 | 25168779 | |
| 107 | Phosphorylation | TTRQMQSTRDGRMLF HHHHHHHCCCCHHHH | 18.85 | 25168779 | |
| 263 | Phosphorylation | YLTTAVITNKDVRKR HHHHHHHCCHHHHHH | 29.62 | 21454597 | |
| 265 | Malonylation | TTAVITNKDVRKRRQ HHHHHCCHHHHHHHH | 49.29 | 26320211 | |
| 265 | Acetylation | TTAVITNKDVRKRRQ HHHHHCCHHHHHHHH | 49.29 | 23954790 | |
| 275 | Malonylation | RKRRQVLKDLVKVIQ HHHHHHHHHHHHHHH | 50.59 | 26320211 | |
| 275 | Acetylation | RKRRQVLKDLVKVIQ HHHHHHHHHHHHHHH | 50.59 | 23236377 | |
| 275 | Ubiquitination | RKRRQVLKDLVKVIQ HHHHHHHHHHHHHHH | 50.59 | - | |
| 387 | Ubiquitination | LDAKIDSKLGHVVMG CCCCCCCCCCCEEEC | 55.53 | 22790023 | |
| 399 | Phosphorylation | VMGNNAVSPYQQVIE EECCCCCCHHHHHHH | 18.58 | 27087446 | |
| 401 | Phosphorylation | GNNAVSPYQQVIEKT CCCCCCHHHHHHHHH | 12.22 | 26643407 | |
| 407 | Ubiquitination | PYQQVIEKTKSLSFR HHHHHHHHHHCCCHH | 50.56 | 22790023 | |
| 409 | Malonylation | QQVIEKTKSLSFRSQ HHHHHHHHCCCHHHH | 61.54 | 26320211 | |
| 409 | Ubiquitination | QQVIEKTKSLSFRSQ HHHHHHHHCCCHHHH | 61.54 | - | |
| 410 | Phosphorylation | QVIEKTKSLSFRSQM HHHHHHHCCCHHHHH | 34.18 | 26643407 | |
| 412 | Phosphorylation | IEKTKSLSFRSQMLA HHHHHCCCHHHHHHH | 26.21 | 26745281 | |
| 415 | Phosphorylation | TKSLSFRSQMLAMNI HHCCCHHHHHHHHHH | 20.24 | 26643407 | |
| 430 | Phosphorylation | EKKLNQNSRSEAPNW HHHHCCCCCCCCCCC | 27.67 | 26643407 | |
| 432 | Phosphorylation | KLNQNSRSEAPNWAT HHCCCCCCCCCCCCC | 37.62 | 26643407 | |
| 439 | Phosphorylation | SEAPNWATQDSGFY- CCCCCCCCCCCCCC- | 25.23 | 17525332 | |
| 442 | Phosphorylation | PNWATQDSGFY---- CCCCCCCCCCC---- | 22.45 | 25619855 | |
| 445 | Phosphorylation | ATQDSGFY------- CCCCCCCC------- | 22.59 | 15592455 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of EIF3E_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EIF3E_MOUSE !! | ||||||
* 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 EIF3E_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439, AND MASSSPECTROMETRY. | |
