| UniProt ID | VPH1_YEAST | |
|---|---|---|
| UniProt AC | P32563 | |
| Protein Name | V-type proton ATPase subunit a, vacuolar isoform | |
| Gene Name | VPH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 840 | |
| Subcellular Localization |
Vacuole membrane Multi-pass membrane protein . |
|
| Protein Description | Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in vacuolar V-ATPase complexes. Enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.. | |
| Protein Sequence | MAEKEEAIFRSAEMALVQFYIPQEISRDSAYTLGQLGLVQFRDLNSKVRAFQRTFVNEIRRLDNVERQYRYFYSLLKKHDIKLYEGDTDKYLDGSGELYVPPSGSVIDDYVRNASYLEERLIQMEDATDQIEVQKNDLEQYRFILQSGDEFFLKGDNTDSTSYMDEDMIDANGENIAAAIGASVNYVTGVIARDKVATLEQILWRVLRGNLFFKTVEIEQPVYDVKTREYKHKNAFIVFSHGDLIIKRIRKIAESLDANLYDVDSSNEGRSQQLAKVNKNLSDLYTVLKTTSTTLESELYAIAKELDSWFQDVTREKAIFEILNKSNYDTNRKILIAEGWIPRDELATLQARLGEMIARLGIDVPSIIQVLDTNHTPPTFHRTNKFTAGFQSICDCYGIAQYREINAGLPTIVTFPFMFAIMFGDMGHGFLMTLAALSLVLNEKKINKMKRGEIFDMAFTGRYIILLMGVFSMYTGFLYNDIFSKTMTIFKSGWKWPDHWKKGESITATSVGTYPIGLDWAWHGTENALLFSNSYKMKLSILMGFIHMTYSYFFSLANHLYFNSMIDIIGNFIPGLLFMQGIFGYLSVCIVYKWAVDWVKDGKPAPGLLNMLINMFLSPGTIDDELYPHQAKVQVFLLLMALVCIPWLLLVKPLHFKFTHKKKSHEPLPSTEADASSEDLEAQQLISAMDADDAEEEEVGSGSHGEDFGDIMIHQVIHTIEFCLNCVSHTASYLRLWALSLAHAQLSSVLWTMTIQIAFGFRGFVGVFMTVALFAMWFALTCAVLVLMEGTSAMLHSLRLHWVESMSKFFVGEGLPYEPFAFEYKDMEVAVASASSSASS | |
| 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 | ------MAEKEEAIF ------CHHHHHHHH | 36.25 | 22814378 | |
| 4 | Ubiquitination | ----MAEKEEAIFRS ----CHHHHHHHHHH | 51.85 | 24961812 | |
| 77 | 2-Hydroxyisobutyrylation | RYFYSLLKKHDIKLY HHHHHHHHHCCCEEE | 54.04 | - | |
| 90 | Ubiquitination | LYEGDTDKYLDGSGE EEECCCCCCCCCCCC | 50.21 | 17644757 | |
| 135 | Ubiquitination | TDQIEVQKNDLEQYR CCCEEECCCCHHHHH | 58.57 | 23749301 | |
| 135 | Acetylation | TDQIEVQKNDLEQYR CCCEEECCCCHHHHH | 58.57 | 24489116 | |
| 226 | Ubiquitination | EQPVYDVKTREYKHK ECCEEECCCCEEECC | 38.68 | 24961812 | |
| 226 | Succinylation | EQPVYDVKTREYKHK ECCEEECCCCEEECC | 38.68 | 23954790 | |
| 226 | Acetylation | EQPVYDVKTREYKHK ECCEEECCCCEEECC | 38.68 | 24489116 | |
| 226 | 2-Hydroxyisobutyrylation | EQPVYDVKTREYKHK ECCEEECCCCEEECC | 38.68 | - | |
| 231 | Ubiquitination | DVKTREYKHKNAFIV ECCCCEEECCCEEEE | 43.26 | 19722269 | |
| 233 | Ubiquitination | KTREYKHKNAFIVFS CCCEEECCCEEEEEE | 45.91 | 19722269 | |
| 247 | Ubiquitination | SHGDLIIKRIRKIAE ECHHHHHHHHHHHHH | 34.48 | 17644757 | |
| 251 | Ubiquitination | LIIKRIRKIAESLDA HHHHHHHHHHHHHCC | 43.85 | 23749301 | |
| 276 | Ubiquitination | GRSQQLAKVNKNLSD CHHHHHHHHCCCHHH | 55.74 | 23749301 | |
| 279 | Ubiquitination | QQLAKVNKNLSDLYT HHHHHHCCCHHHHHH | 63.35 | 23749301 | |
| 279 | Acetylation | QQLAKVNKNLSDLYT HHHHHHCCCHHHHHH | 63.35 | 24489116 | |
| 290 | Phosphorylation | DLYTVLKTTSTTLES HHHHHHHHCCCCHHH | 23.09 | 22369663 | |
| 291 | Phosphorylation | LYTVLKTTSTTLESE HHHHHHHCCCCHHHH | 23.61 | 22369663 | |
| 292 | Phosphorylation | YTVLKTTSTTLESEL HHHHHHCCCCHHHHH | 25.32 | 22369663 | |
| 293 | Phosphorylation | TVLKTTSTTLESELY HHHHHCCCCHHHHHH | 33.05 | 22369663 | |
| 294 | Phosphorylation | VLKTTSTTLESELYA HHHHCCCCHHHHHHH | 28.44 | 22369663 | |
| 297 | Phosphorylation | TTSTTLESELYAIAK HCCCCHHHHHHHHHH | 35.69 | 22369663 | |
| 300 | Phosphorylation | TTLESELYAIAKELD CCHHHHHHHHHHHHH | 7.60 | 22369663 | |
| 304 | Ubiquitination | SELYAIAKELDSWFQ HHHHHHHHHHHHHHH | 53.34 | 17644757 | |
| 317 | Acetylation | FQDVTREKAIFEILN HHHCHHHHHHHHHHH | 43.42 | 24489116 | |
| 325 | Acetylation | AIFEILNKSNYDTNR HHHHHHHHCCCCCCC | 36.31 | 24489116 | |
| 333 | Ubiquitination | SNYDTNRKILIAEGW CCCCCCCCEEEEECC | 43.89 | 17644757 | |
| 491 | Acetylation | SKTMTIFKSGWKWPD HCCEEECCCCCCCCC | 44.18 | 24489116 | |
| 495 | Acetylation | TIFKSGWKWPDHWKK EECCCCCCCCCCHHC | 52.99 | 24489116 | |
| 671 | Phosphorylation | SHEPLPSTEADASSE CCCCCCCCCCCCCCH | 33.00 | 28889911 | |
| 676 | Phosphorylation | PSTEADASSEDLEAQ CCCCCCCCCHHHHHH | 34.50 | 28889911 | |
| 677 | Phosphorylation | STEADASSEDLEAQQ CCCCCCCCHHHHHHH | 36.53 | 27214570 |
| 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 VPH1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPH1_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 VPH1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-671; SER-676 ANDSER-677, AND MASS SPECTROMETRY. | |
