UniProt ID | EF1A1_DROME | |
---|---|---|
UniProt AC | P08736 | |
Protein Name | Elongation factor 1-alpha 1 {ECO:0000312|FlyBase:FBgn0284245} | |
Gene Name | eEF1alpha1 {ECO:0000312|FlyBase:FBgn0284245} | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 463 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.. | |
Protein Sequence | MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTNMPWFKGWKVERKEGNADGKTLIDALDAILPPARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYVAGDSKANPPKGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKAVNFKDASGGKVTKAAEKATKGKK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
23 | Phosphorylation | VDSGKSTTTGHLIYK CCCCCCCCCCEEEEE | 37.56 | 27794539 | |
29 | Phosphorylation | TTTGHLIYKCGGIDK CCCCEEEEECCCCCH | 13.44 | 19429919 | |
30 | Acetylation | TTGHLIYKCGGIDKR CCCEEEEECCCCCHH | 21.29 | 19608861 | |
41 | Acetylation | IDKRTIEKFEKEAQE CCHHHHHHHHHHHHH | 55.78 | 19608861 | |
44 | Acetylation | RTIEKFEKEAQEMGK HHHHHHHHHHHHCCC | 62.57 | 19608861 | |
55 | Acetylation | EMGKGSFKYAWVLDK HCCCCCHHHHHHHHH | 35.44 | 19608861 | |
172 | Acetylation | ARYEEIKKEVSSYIK HHHHHHHHHHHHHHH | 69.84 | 19608861 | |
255 | Acetylation | LPLQDVYKIGGIGTV CCHHHEEEECCCEEE | 34.42 | 19608861 | |
269 | Phosphorylation | VPVGRVETGVLKPGT EECCEEECCCCCCCE | 29.72 | 21082442 | |
276 | Phosphorylation | TGVLKPGTVVVFAPA CCCCCCCEEEEEECC | 20.75 | 21082442 | |
286 | Phosphorylation | VFAPANITTEVKSVE EEECCCCCCEEEEEH | 19.40 | 21082442 | |
301 | 5-glutamyl glycerylphosphorylethanolamine | MHHEALQEAVPGDNV HHHHHHHHHCCCCCC | 53.11 | - | |
301 | Formation of an isopeptide bond | MHHEALQEAVPGDNV HHHHHHHHHCCCCCC | 53.11 | 8500545 | |
330 | Acetylation | GYVAGDSKANPPKGA CCCCCCCCCCCCCCC | 57.85 | 21791702 | |
374 | 5-glutamyl glycerylphosphorylethanolamine | HIACKFAEIKEKVDR HHHHHHHHHHHHHHH | 58.70 | - | |
374 | Formation of an isopeptide bond | HIACKFAEIKEKVDR HHHHHHHHHHHHHHH | 58.70 | - | |
383 | Phosphorylation | KEKVDRRSGKTTEEN HHHHHHCCCCCCCCC | 45.60 | 25749252 | |
386 | Phosphorylation | VDRRSGKTTEENPKF HHHCCCCCCCCCCCE | 42.86 | 21082442 | |
392 | Acetylation | KTTEENPKFIKSGDA CCCCCCCCEEECCCE | 71.89 | 21791702 | |
395 | Acetylation | EENPKFIKSGDAAIV CCCCCEEECCCEEEE | 52.06 | 21791702 | |
432 | Phosphorylation | AVRDMRQTVAVGVIK HHHCHHHHHEEEEEE | 10.48 | 18511481 | |
439 | Ubiquitination | TVAVGVIKAVNFKDA HHEEEEEEECCCCCC | 43.82 | 31113955 | |
444 | Acetylation | VIKAVNFKDASGGKV EEEECCCCCCCCCCC | 47.37 | 21791702 | |
447 | Phosphorylation | AVNFKDASGGKVTKA ECCCCCCCCCCCCHH | 59.20 | 27626673 |
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 EF1A1_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EF1A1_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 EF1A1_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
F206_DROME | CG9288 | physical | 14605208 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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