| UniProt ID | EF1D_DROME | |
|---|---|---|
| UniProt AC | Q9VL18 | |
| Protein Name | Probable elongation factor 1-delta | |
| Gene Name | eEF1delta | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 256 | |
| Subcellular Localization | ||
| Protein Description | EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.. | |
| Protein Sequence | MKVEALDKFWADKSRYDLAEKRFYEGPQKVTDRSHYSPLVSEIAKAREHIQNSLEKIDGVTLDDGLNSELAKRLAQLEGEHKELKTQVSLLNELLTATVKRLETQLKLTNGVSKEPEVEAKKPEANDDDDDVDLFGSDSEEEDGEAARIREERLAAYAAKKAKKVQIIAKSNIILDVKPWDDETDLKVMETEIRKITQDGLLWGASKFVPVAFGIQKLSISCVVEDDKVSIDWLTEEIEKLEDFVQSVDIAAFNKI | |
| 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 |
|---|---|---|---|---|---|
| 34 | Phosphorylation | PQKVTDRSHYSPLVS CCCCCCCCCCHHHHH | 29.59 | 19429919 | |
| 36 | Phosphorylation | KVTDRSHYSPLVSEI CCCCCCCCHHHHHHH | 17.15 | 19429919 | |
| 37 | Phosphorylation | VTDRSHYSPLVSEIA CCCCCCCHHHHHHHH | 13.31 | 19429919 | |
| 41 | Phosphorylation | SHYSPLVSEIAKARE CCCHHHHHHHHHHHH | 30.85 | 19429919 | |
| 53 | Phosphorylation | AREHIQNSLEKIDGV HHHHHHHHHHHCCCC | 22.87 | 21082442 | |
| 56 | Ubiquitination | HIQNSLEKIDGVTLD HHHHHHHHCCCCCCC | 51.93 | 31113955 | |
| 61 | Phosphorylation | LEKIDGVTLDDGLNS HHHCCCCCCCCCCCH | 29.96 | 22668510 | |
| 86 | Phosphorylation | GEHKELKTQVSLLNE HHHHHHHHHHHHHHH | 46.99 | 28490779 | |
| 89 | Phosphorylation | KELKTQVSLLNELLT HHHHHHHHHHHHHHH | 19.81 | 19429919 | |
| 137 | Phosphorylation | DDVDLFGSDSEEEDG CCCCCCCCCCCCCCC | 30.54 | 21082442 | |
| 139 | Phosphorylation | VDLFGSDSEEEDGEA CCCCCCCCCCCCCHH | 48.91 | 21082442 |
| 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 EF1D_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EF1D_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 EF1D_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| R10AB_DROME | RpL10Ab | physical | 14605208 | |
| NACA_DROME | Nacalpha | physical | 22036573 | |
| TERA_DROME | TER94 | physical | 22036573 | |
| YC17_DROME | CG16817 | physical | 22036573 | |
| SH3BG_DROME | Sh3beta | physical | 22036573 | |
| U430_DROME | CG31712 | 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-37; SER-53; SER-137 ANDSER-139, AND MASS 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-89, AND MASSSPECTROMETRY. | |