| UniProt ID | ATP7_YEAST | |
|---|---|---|
| UniProt AC | P30902 | |
| Protein Name | ATP synthase subunit d, mitochondrial | |
| Gene Name | ATP7 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 174 | |
| Subcellular Localization | Mitochondrion. Mitochondrion inner membrane. | |
| 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(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.. | |
| Protein Sequence | MSLAKSAANKLDWAKVISSLRITGSTATQLSSFKKRNDEARRQLLELQSQPTEVDFSHYRSVLKNTSVIDKIESYVKQYKPVKIDASKQLQVIESFEKHAMTNAKETESLVSKELKDLQSTLDNIQSARPFDELTVDDLTKIKPEIDAKVEEMVKKGKWDVPGYKDRFGNLNVM | |
| 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 | ------MSLAKSAAN ------CCHHHHHHH | 36.71 | 1832157 | |
| 10 | Acetylation | LAKSAANKLDWAKVI HHHHHHHHCHHHHHH | 43.00 | 24489116 | |
| 15 | Acetylation | ANKLDWAKVISSLRI HHHCHHHHHHHHCEE | 35.53 | 24489116 | |
| 18 | Phosphorylation | LDWAKVISSLRITGS CHHHHHHHHCEECCC | 26.72 | 24961812 | |
| 19 | Phosphorylation | DWAKVISSLRITGST HHHHHHHHCEECCCC | 15.56 | 24961812 | |
| 23 | Phosphorylation | VISSLRITGSTATQL HHHHCEECCCCHHHH | 20.74 | 27214570 | |
| 25 | Phosphorylation | SSLRITGSTATQLSS HHCEECCCCHHHHHH | 13.25 | 27214570 | |
| 26 | Phosphorylation | SLRITGSTATQLSSF HCEECCCCHHHHHHH | 34.76 | 24961812 | |
| 31 | Phosphorylation | GSTATQLSSFKKRND CCCHHHHHHHHHCCH | 24.74 | 27214570 | |
| 32 | Phosphorylation | STATQLSSFKKRNDE CCHHHHHHHHHCCHH | 50.07 | 27214570 | |
| 34 | Acetylation | ATQLSSFKKRNDEAR HHHHHHHHHCCHHHH | 53.42 | 24489116 | |
| 34 | Succinylation | ATQLSSFKKRNDEAR HHHHHHHHHCCHHHH | 53.42 | 23954790 | |
| 67 | Phosphorylation | RSVLKNTSVIDKIES HHHHHCCHHHHHHHH | 26.86 | 28889911 | |
| 71 | Acetylation | KNTSVIDKIESYVKQ HCCHHHHHHHHHHHH | 36.93 | 24489116 | |
| 77 | Acetylation | DKIESYVKQYKPVKI HHHHHHHHHHCCEEE | 39.41 | 24489116 | |
| 88 | Acetylation | PVKIDASKQLQVIES CEEECHHHHHHHHHH | 57.67 | 24489116 | |
| 95 | Phosphorylation | KQLQVIESFEKHAMT HHHHHHHHHHHHHCC | 27.81 | 27214570 | |
| 98 | Acetylation | QVIESFEKHAMTNAK HHHHHHHHHHCCCHH | 34.35 | 24489116 | |
| 105 | Acetylation | KHAMTNAKETESLVS HHHCCCHHHHHHHHH | 68.21 | 24489116 | |
| 105 | Succinylation | KHAMTNAKETESLVS HHHCCCHHHHHHHHH | 68.21 | 23954790 | |
| 109 | Phosphorylation | TNAKETESLVSKELK CCHHHHHHHHHHHHH | 41.30 | 27214570 | |
| 112 | Phosphorylation | KETESLVSKELKDLQ HHHHHHHHHHHHHHH | 26.21 | 28889911 | |
| 113 | Acetylation | ETESLVSKELKDLQS HHHHHHHHHHHHHHH | 60.63 | 24489116 | |
| 116 | Acetylation | SLVSKELKDLQSTLD HHHHHHHHHHHHHHH | 58.44 | 24489116 | |
| 120 | Phosphorylation | KELKDLQSTLDNIQS HHHHHHHHHHHHHHH | 37.93 | 21440633 | |
| 149 | Acetylation | IKPEIDAKVEEMVKK CCHHHHHHHHHHHHC | 46.56 | 24489116 | |
| 158 | Acetylation | EEMVKKGKWDVPGYK HHHHHCCCCCCCCCC | 49.45 | 24489116 |
| 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 ATP7_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATP7_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 ATP7_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "ATP synthase of yeast mitochondria. Characterization of subunit d andsequence analysis of the structural gene ATP7."; Norais N., Prome D., Velours J.; J. Biol. Chem. 266:16541-16549(1991). Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. | |
