| UniProt ID | GBGE_DROME | |
|---|---|---|
| UniProt AC | Q9NFZ3 | |
| Protein Name | Guanine nucleotide-binding protein subunit gamma-e | |
| Gene Name | Ggamma30A {ECO:0000312|FlyBase:FBgn0267252} | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 72 | |
| Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side . |
|
| Protein Description | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. This subunit functions in visual transduction in the compound eye.. | |
| Protein Sequence | MDPSALQNMDRDALKKQIENMKYQASMERWPLSKSIAEMRSFIEENEKNDPLINAPDKKNNPWAEKGKCVIM | |
| 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 | ------MDPSALQNM ------CCHHHHHHC | 45.95 | 15205461 | |
| 26 | Phosphorylation | ENMKYQASMERWPLS HHHHHHHHHHHCCCH | 12.97 | 27794539 | |
| 41 | Phosphorylation | KSIAEMRSFIEENEK HHHHHHHHHHHHHHC | 29.30 | 27794539 | |
| 69 | Methylation | PWAEKGKCVIM---- CCHHCCCEEEC---- | 3.23 | 15205461 | |
| 69 | Farnesylation | PWAEKGKCVIM---- CCHHCCCEEEC---- | 3.23 | 15205461 | |
| 69 | Farnesylation | PWAEKGKCVIM---- CCHHCCCEEEC---- | 3.23 | 15205461 |
| 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 GBGE_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GBGE_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 GBGE_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GBGE_DROME !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Targeted mutagenesis of the farnesylation site of Drosophila Ggammaedisrupts membrane association of the G protein betagamma complex andaffects the light sensitivity of the visual system."; Schillo S., Belusic G., Hartmann K., Franz C., Kuhl B.,Brenner-Weiss G., Paulsen R., Huber A.; J. Biol. Chem. 279:36309-36316(2004). Cited for: ACETYLATION AT ASP-2, ISOPRENYLATION AT CYS-69, METHYLATION AT CYS-69,AND MUTAGENESIS OF CYS-69. | |
| Methylation | |
| Reference | PubMed |
| "Targeted mutagenesis of the farnesylation site of Drosophila Ggammaedisrupts membrane association of the G protein betagamma complex andaffects the light sensitivity of the visual system."; Schillo S., Belusic G., Hartmann K., Franz C., Kuhl B.,Brenner-Weiss G., Paulsen R., Huber A.; J. Biol. Chem. 279:36309-36316(2004). Cited for: ACETYLATION AT ASP-2, ISOPRENYLATION AT CYS-69, METHYLATION AT CYS-69,AND MUTAGENESIS OF CYS-69. | |
| Prenylation | |
| Reference | PubMed |
| "Targeted mutagenesis of the farnesylation site of Drosophila Ggammaedisrupts membrane association of the G protein betagamma complex andaffects the light sensitivity of the visual system."; Schillo S., Belusic G., Hartmann K., Franz C., Kuhl B.,Brenner-Weiss G., Paulsen R., Huber A.; J. Biol. Chem. 279:36309-36316(2004). Cited for: ACETYLATION AT ASP-2, ISOPRENYLATION AT CYS-69, METHYLATION AT CYS-69,AND MUTAGENESIS OF CYS-69. | |