| UniProt ID | IF2B_DROME | |
|---|---|---|
| UniProt AC | P41375 | |
| Protein Name | Eukaryotic translation initiation factor 2 subunit 2 | |
| Gene Name | eIF2beta {ECO:0000312|FlyBase:FBgn0004926} | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 312 | |
| Subcellular Localization | ||
| Protein Description | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This preinitiation complex mediates ribosomal recognition of a start codon during the scanning process of the leader region.. | |
| Protein Sequence | MDAEDGFDPTLLKKKKKKKTTFDLDAALGLEDDTKKEDPQDEASAEGGAAAEEDNLDLESFGKKKKKKKKPFNMDEIEAAIPSFGGDDVAASEEPEEEEINLDMDFSMAKKKKKSKKKELDELFADQADDDKSEDKENDEDNSSTWFGSDRDYTYDELLKRVFEIILDKNPDMAAGRKPKFVMRPPQVLRVGTKKTSFANFMDIAKTLHRLPKHLLDFLLAELGTSGSMDGNQQLIIKGRFQPKQIENVLRRYIKEYVTCHTCRSPETILQKDTRLFFLQCESCGSRCSVASIKSGFQAVTGKRAAIRAKTT | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | EDPQDEASAEGGAAA CCCCHHHHHCCCHHH | 25.46 | 19429919 | |
| 133 | Phosphorylation | DQADDDKSEDKENDE HHCCCCCCCCCCCCC | 59.01 | 21082442 | |
| 143 | Phosphorylation | KENDEDNSSTWFGSD CCCCCCCCCCCCCCC | 41.28 | 19429919 | |
| 144 | Phosphorylation | ENDEDNSSTWFGSDR CCCCCCCCCCCCCCC | 35.59 | 19429919 | |
| 145 | Phosphorylation | NDEDNSSTWFGSDRD CCCCCCCCCCCCCCC | 25.32 | 19429919 | |
| 244 | Acetylation | IKGRFQPKQIENVLR EEECCCHHHHHHHHH | 53.80 | 21791702 | |
| 265 | Phosphorylation | VTCHTCRSPETILQK HCCCCCCCHHHHHCC | 29.27 | 19429919 | |
| 268 | Phosphorylation | HTCRSPETILQKDTR CCCCCHHHHHCCCCE | 30.30 | 19429919 | |
| 286 | Phosphorylation | LQCESCGSRCSVASI EEECCCCCCEEHHHH | 34.15 | 21082442 | |
| 289 | Phosphorylation | ESCGSRCSVASIKSG CCCCCCEEHHHHHHC | 21.43 | 22817900 |
| 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 IF2B_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IF2B_DROME !! | ||||||
* 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 IF2B_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| NFS1_DROME | CG12264 | physical | 22036573 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND THR-145, ANDMASS SPECTROMETRY. | |
| "An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY. | |