| UniProt ID | EIF3I_MOUSE | |
|---|---|---|
| UniProt AC | Q9QZD9 | |
| Protein Name | Eukaryotic translation initiation factor 3 subunit I {ECO:0000255|HAMAP-Rule:MF_03008} | |
| Gene Name | Eif3i | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 325 | |
| 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. 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.. | |
| Protein Sequence | MKPILLQGHERSITQIKYNREGDLLFTVAKDPIVNVWYSVNGERLGTYMGHTGAVWCVDADWDTKHVLTGSADNSCRLWDCETGKQLALLKTNSAVRTCGFDFGGNIIMFSTDKQMGYQCFVSFFDLRDPSQIDSNEPYMKIPCNDSKITSAVWGPLGECVIAGHESGELNQYSAKSGEVLVNVKEHSRQINDIQLSRDMTMFVTASKDNTAKLFDSTTLEHQKTFRTERPVNSAALSPNYDHVVLGGGQEAMDVTTTSTRIGKFEARFFHLAFEEEFGRVKGHFGPINSVAFHPDGKSYSSGGEDGYVRIHYFDPQYFEFEFEA | |
| 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 | Ubiquitination | ------MKPILLQGH ------CCCEEECCC | 40.54 | - | |
| 2 | Acetylation | ------MKPILLQGH ------CCCEEECCC | 40.54 | 22826441 | |
| 76 | S-nitrosocysteine | TGSADNSCRLWDCET ECCCCCCCEEEECCC | 5.34 | - | |
| 76 | S-nitrosylation | TGSADNSCRLWDCET ECCCCCCCEEEECCC | 5.34 | 21278135 | |
| 85 | Ubiquitination | LWDCETGKQLALLKT EEECCCCCEEEEEEC | 49.94 | - | |
| 85 | Acetylation | LWDCETGKQLALLKT EEECCCCCEEEEEEC | 49.94 | 22826441 | |
| 91 | Acetylation | GKQLALLKTNSAVRT CCEEEEEECCCCCHH | 46.65 | 23954790 | |
| 144 | Glutathionylation | EPYMKIPCNDSKITS CCCEECCCCCCHHEE | 11.42 | 24333276 | |
| 176 | Ubiquitination | ELNQYSAKSGEVLVN CCCEEECCCCCEEEE | 53.72 | - | |
| 218 | Phosphorylation | TAKLFDSTTLEHQKT CCCCCCCCCCEEECE | 36.93 | 18779572 | |
| 219 | Phosphorylation | AKLFDSTTLEHQKTF CCCCCCCCCEEECEE | 33.82 | - | |
| 224 | Ubiquitination | STTLEHQKTFRTERP CCCCEEECEECCCCC | 52.09 | - | |
| 264 | Acetylation | TTSTRIGKFEARFFH ECCCCEEEEEEEHHH | 37.35 | - | |
| 264 | Ubiquitination | TTSTRIGKFEARFFH ECCCCEEEEEEEHHH | 37.35 | 27667366 | |
| 282 | Ubiquitination | EEEFGRVKGHFGPIN HHHHCCCCCCCCCCC | 45.36 | - | |
| 298 | Ubiquitination | VAFHPDGKSYSSGGE EEECCCCCCCCCCCC | 54.31 | - | |
| 301 | Phosphorylation | HPDGKSYSSGGEDGY CCCCCCCCCCCCCCE | 29.60 | 26525534 | |
| 302 | Phosphorylation | PDGKSYSSGGEDGYV CCCCCCCCCCCCCEE | 42.45 | 26525534 | |
| 308 | Phosphorylation | SSGGEDGYVRIHYFD CCCCCCCEEEEEEEC | 10.01 | - |
| 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 EIF3I_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EIF3I_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 EIF3I_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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