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 | ||
* 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 | ||||||
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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. |