| UniProt ID | VATH_YEAST | |
|---|---|---|
| UniProt AC | P41807 | |
| Protein Name | V-type proton ATPase subunit H | |
| Gene Name | VMA13 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 478 | |
| Subcellular Localization |
Vacuole membrane Peripheral membrane protein. |
|
| Protein Description | Vacuolar ATPases regulate the organelle acidity. This subunit is essential for activity, but not assembly, of the enzyme complex.. | |
| Protein Sequence | MGATKILMDSTHFNEIRSIIRSRSVAWDALARSEELSEIDASTAKALESILVKKNIGDGLSSSNNAHSGFKVNGKTLIPLIHLLSTSDNEDCKKSVQNLIAELLSSDKYGDDTVKFFQEDPKQLEQLFDVSLKGDFQTVLISGFNVVSLLVQNGLHNVKLVEKLLKNNNLINILQNIEQMDTCYVCIRLLQELAVIPEYRDVIWLHEKKFMPTLFKILQRATDSQLATRIVATNSNHLGIQLQYHSLLLIWLLTFNPVFANELVQKYLSDFLDLLKLVKITIKEKVSRLCISIILQCCSTRVKQHKKVIKQLLLLGNALPTVQSLSERKYSDEELRQDISNLKEILENEYQELTSFDEYVAELDSKLLCWSPPHVDNGFWSDNIDEFKKDNYKIFRQLIELLQAKVRNGDVNAKQEKIIIQVALNDITHVVELLPESIDVLDKTGGKADIMELLNHSDSRVKYEALKATQAIIGYTFK | |
| 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 |
|---|---|---|---|---|---|
| 22 | Phosphorylation | EIRSIIRSRSVAWDA HHHHHHHHHHHHHHH | 20.64 | 30377154 | |
| 24 | Phosphorylation | RSIIRSRSVAWDALA HHHHHHHHHHHHHHH | 19.89 | 28889911 | |
| 45 | Acetylation | EIDASTAKALESILV HCCHHHHHHHHHHHH | 54.30 | 24489116 | |
| 45 | Ubiquitination | EIDASTAKALESILV HCCHHHHHHHHHHHH | 54.30 | 17644757 | |
| 49 | Phosphorylation | STAKALESILVKKNI HHHHHHHHHHHHCCC | 23.28 | 21440633 | |
| 53 | Acetylation | ALESILVKKNIGDGL HHHHHHHHCCCCCCC | 36.34 | 24489116 | |
| 53 | Succinylation | ALESILVKKNIGDGL HHHHHHHHCCCCCCC | 36.34 | 23954790 | |
| 54 | Ubiquitination | LESILVKKNIGDGLS HHHHHHHCCCCCCCC | 46.44 | 17644757 | |
| 61 | Phosphorylation | KNIGDGLSSSNNAHS CCCCCCCCCCCCCCC | 36.93 | 21440633 | |
| 62 | Phosphorylation | NIGDGLSSSNNAHSG CCCCCCCCCCCCCCC | 41.97 | 21440633 | |
| 63 | Phosphorylation | IGDGLSSSNNAHSGF CCCCCCCCCCCCCCC | 30.63 | 21440633 | |
| 68 | Phosphorylation | SSSNNAHSGFKVNGK CCCCCCCCCCEECCE | 43.44 | 21440633 | |
| 71 | Acetylation | NNAHSGFKVNGKTLI CCCCCCCEECCEEHH | 38.01 | 24489116 | |
| 71 | Ubiquitination | NNAHSGFKVNGKTLI CCCCCCCEECCEEHH | 38.01 | 17644757 | |
| 75 | Ubiquitination | SGFKVNGKTLIPLIH CCCEECCEEHHHHHH | 34.65 | 17644757 | |
| 93 | Ubiquitination | TSDNEDCKKSVQNLI CCCCHHHHHHHHHHH | 61.48 | 17644757 | |
| 94 | Ubiquitination | SDNEDCKKSVQNLIA CCCHHHHHHHHHHHH | 63.29 | 17644757 | |
| 95 | Phosphorylation | DNEDCKKSVQNLIAE CCHHHHHHHHHHHHH | 17.90 | 21126336 | |
| 105 | Phosphorylation | NLIAELLSSDKYGDD HHHHHHHCCCCCCCC | 49.46 | 21126336 | |
| 108 | Acetylation | AELLSSDKYGDDTVK HHHHCCCCCCCCCHH | 53.75 | 24489116 | |
| 163 | Acetylation | HNVKLVEKLLKNNNL CHHHHHHHHHHCCCH | 52.20 | 24489116 | |
| 208 | Acetylation | DVIWLHEKKFMPTLF CHHHHCCCCCHHHHH | 40.33 | 24489116 | |
| 216 | Acetylation | KFMPTLFKILQRATD CCHHHHHHHHHHHCC | 45.69 | 24489116 | |
| 222 | Phosphorylation | FKILQRATDSQLATR HHHHHHHCCCHHCCC | 38.07 | 22369663 | |
| 224 | Phosphorylation | ILQRATDSQLATRIV HHHHHCCCHHCCCHH | 23.80 | 22369663 | |
| 228 | Phosphorylation | ATDSQLATRIVATNS HCCCHHCCCHHHCCC | 29.53 | 22369663 | |
| 310 | Ubiquitination | KQHKKVIKQLLLLGN HHHHHHHHHHHHHCC | 37.57 | 17644757 | |
| 329 | Ubiquitination | VQSLSERKYSDEELR HHHHHHCCCCHHHHH | 45.08 | 17644757 | |
| 414 | Acetylation | RNGDVNAKQEKIIIQ HCCCCCHHHEEEEEE | 54.51 | 24489116 | |
| 457 | Phosphorylation | IMELLNHSDSRVKYE HHHHHCCCCCHHHHH | 35.89 | 30377154 | |
| 459 | Phosphorylation | ELLNHSDSRVKYEAL HHHCCCCCHHHHHHH | 41.82 | 30377154 | |
| 467 | Ubiquitination | RVKYEALKATQAIIG HHHHHHHHHHHHHHC | 57.33 | 23749301 |
| 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 VATH_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VATH_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 VATH_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| 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 SER-24; SER-49 AND SER-61,AND MASS SPECTROMETRY. | |
