UniProt ID | ATPO_YEAST | |
---|---|---|
UniProt AC | P09457 | |
Protein Name | ATP synthase subunit 5, mitochondrial | |
Gene Name | ATP5 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 212 | |
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 | MFNRVFTRSFASSLRAAASKAAAPPPVRLFGVEGTYATALYQAAAKNSSIDAAFQSLQKVESTVKKNPKLGHLLLNPALSLKDRNSVIDAIVETHKNLDGYVVNLLKVLSENNRLGCFEKIASDFGVLNDAHNGLLKGTVTSAEPLDPKSFKRIEKALSASKLVGQGKSLKLENVVKPEIKGGLIVELGDKTVDLSISTKIQKLNKVLEDSI | |
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 |
---|---|---|---|---|---|
12 | Phosphorylation | VFTRSFASSLRAAAS HHHHHHHHHHHHHHH | 28.09 | 30377154 | |
48 | Phosphorylation | YQAAAKNSSIDAAFQ HHHHHHCCCHHHHHH | 28.15 | 27214570 | |
59 | Acetylation | AAFQSLQKVESTVKK HHHHHHHHHHHHHHH | 53.95 | 24489116 | |
62 | Phosphorylation | QSLQKVESTVKKNPK HHHHHHHHHHHHCCC | 41.30 | 27214570 | |
65 | Succinylation | QKVESTVKKNPKLGH HHHHHHHHHCCCHHH | 47.09 | 23954790 | |
65 | Acetylation | QKVESTVKKNPKLGH HHHHHHHHHCCCHHH | 47.09 | 24489116 | |
66 | Acetylation | KVESTVKKNPKLGHL HHHHHHHHCCCHHHH | 74.31 | 24489116 | |
69 | Acetylation | STVKKNPKLGHLLLN HHHHHCCCHHHHHHC | 76.21 | 24489116 | |
82 | Acetylation | LNPALSLKDRNSVID HCCCCCCCCCCHHHH | 51.79 | 24489116 | |
86 | Phosphorylation | LSLKDRNSVIDAIVE CCCCCCCHHHHHHHH | 22.73 | 25371407 | |
96 | Acetylation | DAIVETHKNLDGYVV HHHHHHCCCCCHHHH | 67.63 | 25381059 | |
120 | Acetylation | NRLGCFEKIASDFGV CCCCHHHHHHHHHCC | 24.26 | 25381059 | |
139 | Phosphorylation | HNGLLKGTVTSAEPL CCCCCCCCCCCCCCC | 21.01 | 28889911 | |
149 | Succinylation | SAEPLDPKSFKRIEK CCCCCCHHHHHHHHH | 69.09 | 23954790 | |
149 | Acetylation | SAEPLDPKSFKRIEK CCCCCCHHHHHHHHH | 69.09 | 24489116 | |
156 | Acetylation | KSFKRIEKALSASKL HHHHHHHHHHHHHHH | 52.86 | 24489116 | |
161 | Phosphorylation | IEKALSASKLVGQGK HHHHHHHHHHHCCCC | 24.13 | 23749301 | |
168 | 2-Hydroxyisobutyrylation | SKLVGQGKSLKLENV HHHHCCCCCEEECCC | 44.73 | - | |
171 | Acetylation | VGQGKSLKLENVVKP HCCCCCEEECCCCCC | 61.93 | 24489116 | |
177 | Acetylation | LKLENVVKPEIKGGL EEECCCCCCEEECCE | 32.42 | 24489116 | |
192 | Phosphorylation | IVELGDKTVDLSIST EEEECCEEEEEEHHH | 24.80 | 22890988 | |
196 | Phosphorylation | GDKTVDLSISTKIQK CCEEEEEEHHHHHHH | 15.27 | 22890988 | |
198 | Phosphorylation | KTVDLSISTKIQKLN EEEEEEHHHHHHHHH | 21.92 | 22890988 | |
199 | Phosphorylation | TVDLSISTKIQKLNK EEEEEHHHHHHHHHH | 30.42 | 22890988 |
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 ATPO_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATPO_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 ATPO_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND THR-139, AND MASSSPECTROMETRY. |