| UniProt ID | ATPB_YEAST | |
|---|---|---|
| UniProt AC | P00830 | |
| Protein Name | ATP synthase subunit beta, mitochondrial | |
| Gene Name | ATP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 511 | |
| 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. Subunits alpha and beta form the catalytic core in F(1). 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 | MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN | |
| 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 |
|---|---|---|---|---|---|
| 27 | Phosphorylation | QSAPLLSTSWKRCMA HHHCCCCCCHHHHHH | 38.28 | 21440633 | |
| 35 | Phosphorylation | SWKRCMASAAQSTPI CHHHHHHHHHHCCCC | 9.39 | 27214570 | |
| 39 | Phosphorylation | CMASAAQSTPITGKV HHHHHHHCCCCCCCE | 31.27 | 21440633 | |
| 40 | Phosphorylation | MASAAQSTPITGKVT HHHHHHCCCCCCCEE | 13.46 | 21440633 | |
| 78 | Acetylation | EIKTPQGKLVLEVAQ CCCCCCCCCHHHHHH | 30.12 | 24489116 | |
| 108 | 2-Hydroxyisobutyrylation | EGLVRGEKVLDTGGP CCEECCEEEECCCCC | 51.42 | - | |
| 108 | Acetylation | EGLVRGEKVLDTGGP CCEECCEEEECCCCC | 51.42 | 24489116 | |
| 112 | Phosphorylation | RGEKVLDTGGPISVP CCEEEECCCCCCCCC | 39.62 | 28889911 | |
| 143 | Acetylation | IDERGPIKSKLRKPI CCCCCCCCHHCCCCC | 44.67 | 24489116 | |
| 148 | Acetylation | PIKSKLRKPIHADPP CCCHHCCCCCCCCCC | 59.78 | 24489116 | |
| 196 | Methylation | FGGAGVGKTVFIQEL ECCCCCCHHHHHHHH | 38.83 | 20137074 | |
| 235 | Succinylation | NDLYREMKETGVINL CHHHHHHHHHCCEEE | 47.58 | 23954790 | |
| 235 | Acetylation | NDLYREMKETGVINL CHHHHHHHHHCCEEE | 47.58 | 24489116 | |
| 237 | Phosphorylation | LYREMKETGVINLEG HHHHHHHHCCEEEEC | 31.09 | 28889911 | |
| 310 | Phosphorylation | ALLGRIPSAVGYQPT HHHCCCCCCCCCCCC | 32.96 | 29734811 | |
| 314 | Phosphorylation | RIPSAVGYQPTLATD CCCCCCCCCCCCCCC | 12.53 | 30377154 | |
| 317 | Phosphorylation | SAVGYQPTLATDMGL CCCCCCCCCCCCHHH | 17.31 | 30377154 | |
| 334 | Methylation | ERITTTKKGSVTSVQ HHHCCCCCCCEEEEE | 55.09 | 19918266 | |
| 373 | Phosphorylation | TVLSRGISELGIYPA HHHHCCHHHCCCCCC | 29.59 | 28889911 | |
| 387 | Acetylation | AVDPLDSKSRLLDAA CCCCCCCCCHHHHHH | 38.98 | 24489116 | |
| 406 | Acetylation | EHYDVASKVQETLQT HHHHHHHHHHHHHHH | 37.89 | 24489116 | |
| 416 | Phosphorylation | ETLQTYKSLQDIIAI HHHHHHHHHHHHHHH | 22.35 | 22369663 | |
| 430 | Phosphorylation | ILGMDELSEQDKLTV HHCCHHCCHHCCHHH | 31.03 | 22369663 | |
| 434 | Ubiquitination | DELSEQDKLTVERAR HHCCHHCCHHHHHHH | 45.83 | 23749301 | |
| 468 | 2-Hydroxyisobutyrylation | PGKLVRLKDTVASFK CCCEEEHHHHHHHHH | 40.57 | - | |
| 475 | Acetylation | KDTVASFKAVLEGKY HHHHHHHHHHHCCCC | 34.78 | 24489116 | |
| 481 | Acetylation | FKAVLEGKYDNIPEH HHHHHCCCCCCCCCH | 39.80 | 24489116 | |
| 505 | Succinylation | DVVAKAEKLAAEAN- HHHHHHHHHHHHCC- | 48.57 | 23954790 |
| 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 ATPB_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATPB_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 ATPB_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| 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 THR-112; THR-237 ANDSER-373, AND MASS SPECTROMETRY. | |
