UniProt ID | ATPG_YEAST | |
---|---|---|
UniProt AC | P38077 | |
Protein Name | ATP synthase subunit gamma, mitochondrial | |
Gene Name | ATP3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 311 | |
Subcellular Localization |
Mitochondrion. Mitochondrion inner membrane Peripheral membrane protein. |
|
Protein Description | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.. | |
Protein Sequence | MLSRIVSNNATRSVMCHQAQVGILYKTNPVRTYATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKISAKKMDEAEQLFYKNAETKNLDVEATETGAPKELIVAITSDKGLCGSIHSQLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSINGIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDPVSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDLFEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRYSILYNRTRQAVITNELVDIITGASSLG | |
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 |
---|---|---|---|---|---|
85 | Phosphorylation | DEAEQLFYKNAETKN HHHHHHHHHCCCCCC | 16.36 | 25882841 | |
86 | Acetylation | EAEQLFYKNAETKNL HHHHHHHHCCCCCCC | 42.20 | 24489116 | |
90 | Phosphorylation | LFYKNAETKNLDVEA HHHHCCCCCCCCEEE | 23.87 | 27017623 | |
91 | Acetylation | FYKNAETKNLDVEAT HHHCCCCCCCCEEEC | 47.20 | 24489116 | |
98 | Phosphorylation | KNLDVEATETGAPKE CCCCEEECCCCCCCE | 22.15 | 27017623 | |
100 | Phosphorylation | LDVEATETGAPKELI CCEEECCCCCCCEEE | 34.00 | 27017623 | |
122 | Phosphorylation | GLCGSIHSQLAKAVR CCHHHHHHHHHHHHH | 25.81 | 27214570 | |
142 | Phosphorylation | QPNADIVTIGDKIKM CCCCCEEECCHHHHH | 21.41 | 28889911 | |
146 | Acetylation | DIVTIGDKIKMQLLR CEEECCHHHHHHHHH | 38.73 | 24489116 | |
148 | Acetylation | VTIGDKIKMQLLRTH EECCHHHHHHHHHHC | 26.74 | 24489116 | |
176 | Phosphorylation | DAPTFQESALIADKL CCCCHHHHHHHHHHH | 20.00 | 24909858 | |
182 | Acetylation | ESALIADKLLSVMKA HHHHHHHHHHHHHHH | 42.16 | 24489116 | |
185 | Phosphorylation | LIADKLLSVMKAGTY HHHHHHHHHHHHCCC | 30.51 | 24909858 | |
219 | Acetylation | EKPIFNAKTIEQSPS CCCCCCCEECEECCC | 51.65 | 24489116 | |
224 | Phosphorylation | NAKTIEQSPSFGKFE CCEECEECCCCCEEE | 15.10 | 27717283 | |
226 | Phosphorylation | KTIEQSPSFGKFEID EECEECCCCCEEEEC | 52.45 | 27214570 | |
229 | Acetylation | EQSPSFGKFEIDTDA EECCCCCEEEECCCC | 37.50 | 24489116 | |
284 | Phosphorylation | AGDMINRYSILYNRT HHHHHHHHHHHHHHH | 8.79 | 22369663 | |
285 | Phosphorylation | GDMINRYSILYNRTR HHHHHHHHHHHHHHC | 11.68 | 22369663 | |
288 | Phosphorylation | INRYSILYNRTRQAV HHHHHHHHHHHCCCH | 10.83 | 22369663 | |
297 | Phosphorylation | RTRQAVITNELVDII HHCCCHHHHHHHHHH | 18.95 | 22369663 | |
305 | Phosphorylation | NELVDIITGASSLG- HHHHHHHHCHHHCC- | 27.34 | 22369663 | |
308 | Phosphorylation | VDIITGASSLG---- HHHHHCHHHCC---- | 27.69 | 22369663 | |
309 | Phosphorylation | DIITGASSLG----- HHHHCHHHCC----- | 36.25 | 22369663 |
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 ATPG_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATPG_YEAST !! |
* 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 ATPG_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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