| UniProt ID | VATA_YEAST | |
|---|---|---|
| UniProt AC | P17255 | |
| Protein Name | V-type proton ATPase catalytic subunit A | |
| Gene Name | VMA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1071 | |
| Subcellular Localization | Endomembrane system . Vacuole membrane . Membranes of various intracellular acidic compartments. | |
| Protein Description | Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit.; PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.. | |
| Protein Sequence | MAGAIENARKEIKRISLEDHAESEYGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETIYDGIQRPLKAIKEESQSIYIPRGIDTPALDRTIKWQFTPGKFQVGDHISGGDIYGSVFENSLISSHKILLPPRSRGTITWIAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHKSDSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVVSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVHNCGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADSTGDVKHAVSSSKFFEPSRGEKEVHGEFEKLLSTMQERFAESTD | |
| 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 | ------MAGAIENAR ------CCCHHHHHH | 27.68 | 22814378 | |
| 16 | Phosphorylation | RKEIKRISLEDHAES HHHHHCCCHHHHCHH | 29.73 | 28889911 | |
| 51 | Ubiquitination | CAMYELVKVGHDNLV HHHHHHHHCCCCCCC | 55.94 | 17644757 | |
| 68 | Ubiquitination | VIRIDGDKATIQVYE EEEECCCCEEEEEEH | 53.62 | 17644757 | |
| 89 | Phosphorylation | VGDPVLRTGKPLSVE CCCCEECCCCCEEEE | 45.45 | 22369663 | |
| 91 | Ubiquitination | DPVLRTGKPLSVELG CCEECCCCCEEEEEC | 42.02 | 24961812 | |
| 94 | Phosphorylation | LRTGKPLSVELGPGL ECCCCCEEEEECCCH | 23.28 | 21440633 | |
| 104 | Phosphorylation | LGPGLMETIYDGIQR ECCCHHHHHHHHCHH | 15.75 | 21440633 | |
| 106 | Phosphorylation | PGLMETIYDGIQRPL CCHHHHHHHHCHHHH | 18.61 | 22369663 | |
| 114 | Ubiquitination | DGIQRPLKAIKEESQ HHCHHHHHHHHHHHC | 51.23 | 17644757 | |
| 117 | Ubiquitination | QRPLKAIKEESQSIY HHHHHHHHHHHCCEE | 61.36 | 23749301 | |
| 117 | Acetylation | QRPLKAIKEESQSIY HHHHHHHHHHHCCEE | 61.36 | 24489116 | |
| 117 | 2-Hydroxyisobutyrylation | QRPLKAIKEESQSIY HHHHHHHHHHHCCEE | 61.36 | - | |
| 117 | Succinylation | QRPLKAIKEESQSIY HHHHHHHHHHHCCEE | 61.36 | 23954790 | |
| 120 | Phosphorylation | LKAIKEESQSIYIPR HHHHHHHHCCEECCC | 30.25 | 21440633 | |
| 122 | Phosphorylation | AIKEESQSIYIPRGI HHHHHHCCEECCCCC | 27.00 | 21440633 | |
| 131 | Phosphorylation | YIPRGIDTPALDRTI ECCCCCCCCCCCCEE | 14.45 | 22369663 | |
| 139 | Acetylation | PALDRTIKWQFTPGK CCCCCEEEEEECCCE | 34.04 | 24489116 | |
| 139 | 2-Hydroxyisobutyrylation | PALDRTIKWQFTPGK CCCCCEEEEEECCCE | 34.04 | - | |
| 143 | Phosphorylation | RTIKWQFTPGKFQVG CEEEEEECCCEEEEC | 18.94 | 21440633 | |
| 146 | Ubiquitination | KWQFTPGKFQVGDHI EEEECCCEEEECCCC | 33.55 | 23749301 | |
| 146 | Acetylation | KWQFTPGKFQVGDHI EEEECCCEEEECCCC | 33.55 | 24489116 | |
| 166 | Phosphorylation | YGSVFENSLISSHKI CCCHHCCCCCCCCEE | 21.63 | 17287358 | |
| 172 | Ubiquitination | NSLISSHKILLPPRS CCCCCCCEEECCCCC | 36.68 | 17644757 | |
| 179 | Phosphorylation | KILLPPRSRGTITWI EEECCCCCCCCEEEE | 40.61 | 22369663 | |
| 182 | Phosphorylation | LPPRSRGTITWIAPA CCCCCCCCEEEEEEC | 17.70 | 22369663 | |
| 184 | Phosphorylation | PRSRGTITWIAPAGE CCCCCCEEEEEECCE | 15.62 | 22369663 | |
| 192 | Phosphorylation | WIAPAGEYTLDEKIL EEEECCEEECCCEEE | 16.22 | 22369663 | |
| 193 | Phosphorylation | IAPAGEYTLDEKILE EEECCEEECCCEEEE | 24.35 | 22369663 | |
| 206 | Ubiquitination | LEVEFDGKKSDFTLY EEEEECCEECCEEEE | 51.45 | 17644757 | |
| 206 | Acetylation | LEVEFDGKKSDFTLY EEEEECCEECCEEEE | 51.45 | 24489116 | |
| 207 | Ubiquitination | EVEFDGKKSDFTLYH EEEECCEECCEEEEE | 61.87 | 17644757 | |
| 207 | Acetylation | EVEFDGKKSDFTLYH EEEECCEECCEEEEE | 61.87 | 24489116 | |
| 207 | 2-Hydroxyisobutyrylation | EVEFDGKKSDFTLYH EEEECCEECCEEEEE | 61.87 | - | |
| 227 | Ubiquitination | VPRPVTEKLSADYPL CCCCCCCCCCCCCCC | 38.07 | 17644757 | |
| 227 | Acetylation | VPRPVTEKLSADYPL CCCCCCCCCCCCCCC | 38.07 | 24489116 | |
| 263 | Ubiquitination | PGAFGCGKTVISQSL CCCCCCCHHHHHHHH | 43.63 | 17644757 | |
| 267 | Phosphorylation | GCGKTVISQSLSKYS CCCHHHHHHHHHHCC | 14.91 | 30377154 | |
| 276 | Phosphorylation | SLSKYSNSDAIIYVG HHHHCCCCCEEEEEE | 23.60 | 21440633 | |
| 309 | Ubiquitination | ENIEVGNKVMGKDGR ECEEECCEEECCCCC | 27.89 | 22817900 | |
| 313 | Ubiquitination | VGNKVMGKDGRPREV ECCEEECCCCCCCCE | 38.62 | 22817900 | |
| 313 | Acetylation | VGNKVMGKDGRPREV ECCEEECCCCCCCCE | 38.62 | 24489116 | |
| 329 | Phosphorylation | KLPRGRETMYSVVQK ECCCCHHHHHHHHHH | 21.76 | 21440633 | |
| 336 | Ubiquitination | TMYSVVQKSQHRAHK HHHHHHHHHHHHHCC | 40.24 | 22817900 | |
| 336 | Acetylation | TMYSVVQKSQHRAHK HHHHHHHHHHHHHCC | 40.24 | 24489116 | |
| 344 | Phosphorylation | SQHRAHKSDSSREVP HHHHHCCCCCCCCHH | 32.62 | 22369663 | |
| 346 | Phosphorylation | HRAHKSDSSREVPEL HHHCCCCCCCCHHHH | 38.08 | 22369663 | |
| 347 | Phosphorylation | RAHKSDSSREVPELL HHCCCCCCCCHHHHH | 37.13 | 23749301 | |
| 355 | Ubiquitination | REVPELLKFTCNATH CCHHHHHHHHHCCCC | 51.78 | 17644757 | |
| 355 | Acetylation | REVPELLKFTCNATH CCHHHHHHHHHCCCC | 51.78 | 24489116 | |
| 376 | Phosphorylation | PRSVRRLSRTIKGVE HHHHHHHHHHCCCCE | 26.09 | 17287358 | |
| 407 | Ubiquitination | GRIVELVKEVSKSYP CCHHHHHHHHHHHCC | 66.09 | 23749301 | |
| 407 | Acetylation | GRIVELVKEVSKSYP CCHHHHHHHHHHHCC | 66.09 | 24489116 | |
| 411 | Ubiquitination | ELVKEVSKSYPISEG HHHHHHHHHCCCCCC | 60.22 | 23749301 | |
| 411 | Acetylation | ELVKEVSKSYPISEG HHHHHHHHHCCCCCC | 60.22 | 24489116 | |
| 411 | Succinylation | ELVKEVSKSYPISEG HHHHHHHHHCCCCCC | 60.22 | 23954790 | |
| 448 | Phosphorylation | TIEARDLSLLGSHVR EEEHHHHHHHHHHHH | 26.32 | 22369663 | |
| 452 | Phosphorylation | RDLSLLGSHVRKATY HHHHHHHHHHHHCCC | 20.83 | 22369663 | |
| 456 | Ubiquitination | LLGSHVRKATYQTYA HHHHHHHHCCCCCCC | 43.95 | 17644757 | |
| 478 | Acetylation | HFFDYMQKSKFHLTI CHHHHHHHCCCCEEE | 38.80 | 24489116 | |
| 480 | Acetylation | FDYMQKSKFHLTIEG HHHHHHCCCCEEECH | 43.78 | 24489116 | |
| 480 | 2-Hydroxyisobutyrylation | FDYMQKSKFHLTIEG HHHHHHCCCCEEECH | 43.78 | - | |
| 489 | Ubiquitination | HLTIEGPKVLAYLLG CEEECHHHHHHHHHH | 61.82 | 17644757 | |
| 517 | Phosphorylation | SVDSRDTSLMERVTE ECCCCCCCHHHHHHH | 29.97 | 28889911 | |
| 528 | Acetylation | RVTEYAEKLNLCAEY HHHHHHHHHCCCHHH | 34.21 | 24489116 | |
| 536 | Ubiquitination | LNLCAEYKDRKEPQV HCCCHHHCCCCCCCH | 42.43 | 23749301 | |
| 536 | Acetylation | LNLCAEYKDRKEPQV HCCCHHHCCCCCCCH | 42.43 | 24489116 | |
| 545 | Acetylation | RKEPQVAKTVNLYSK CCCCCHHHHHHHHHH | 54.90 | 22865919 | |
| 552 | Ubiquitination | KTVNLYSKVVRGNGI HHHHHHHHHHCCCCH | 31.06 | 23749301 | |
| 552 | Acetylation | KTVNLYSKVVRGNGI HHHHHHHHHHCCCCH | 31.06 | 24489116 | |
| 552 | 2-Hydroxyisobutyrylation | KTVNLYSKVVRGNGI HHHHHHHHHHCCCCH | 31.06 | - | |
| 580 | Ubiquitination | IVGLGFLKDGVKNIP HHHHCCCCCCCCCCC | 50.61 | 15699485 | |
| 584 | Ubiquitination | GFLKDGVKNIPSFLS CCCCCCCCCCCCHHC | 55.47 | 24961812 | |
| 588 | Phosphorylation | DGVKNIPSFLSTDNI CCCCCCCCHHCCCCC | 34.71 | 25752575 | |
| 592 | Phosphorylation | NIPSFLSTDNIGTRE CCCCHHCCCCCCCCH | 34.90 | 19779198 | |
| 600 | Phosphorylation | DNIGTRETFLAGLID CCCCCCHHHHHHHHC | 22.21 | 22369663 | |
| 608 | Phosphorylation | FLAGLIDSDGYVTDE HHHHHHCCCCCEECC | 26.41 | 22369663 | |
| 611 | Phosphorylation | GLIDSDGYVTDEHGI HHHCCCCCEECCCCC | 12.74 | 22369663 | |
| 613 | Phosphorylation | IDSDGYVTDEHGIKA HCCCCCEECCCCCEE | 27.47 | 22369663 | |
| 623 | 2-Hydroxyisobutyrylation | HGIKATIKTIHTSVR CCCEEEEEEHHHHHH | 36.75 | - | |
| 623 | Acetylation | HGIKATIKTIHTSVR CCCEEEEEEHHHHHH | 36.75 | 24489116 | |
| 652 | Acetylation | SVNAEPAKVDMNGTK EECCEEEEECCCCCC | 49.86 | 24489116 | |
| 679 | Phosphorylation | DVLLNVLSKCAGSKK HHHHHHHHHHCCCCC | 22.77 | 15665377 | |
| 686 | Acetylation | SKCAGSKKFRPAPAA HHHCCCCCCCCCCHH | 48.58 | 25381059 | |
| 770 | Phosphorylation | KEPIMKRTTLVANTS CCCCHHCEEEEECCC | 20.97 | 28889911 | |
| 771 | Phosphorylation | EPIMKRTTLVANTSN CCCHHCEEEEECCCC | 24.22 | 28889911 | |
| 776 | Phosphorylation | RTTLVANTSNMPVAA CEEEEECCCCCCCHH | 16.25 | 28889911 | |
| 777 | Phosphorylation | TTLVANTSNMPVAAR EEEEECCCCCCCHHH | 30.82 | 28889911 | |
| 803 | Ubiquitination | EYFRDQGKNVSMIAD HHHHHCCCCCEEEEC | 48.84 | 23749301 | |
| 806 | Phosphorylation | RDQGKNVSMIADSSS HHCCCCCEEEECCHH | 17.54 | 21126336 | |
| 812 | Phosphorylation | VSMIADSSSRWAEAL CEEEECCHHHHHHHH | 25.19 | 27017623 | |
| 813 | Phosphorylation | SMIADSSSRWAEALR EEEECCHHHHHHHHH | 35.47 | 27017623 | |
| 842 | Ubiquitination | FPAYLGAKLASFYER CCHHHHHHHHHHHHH | 42.67 | 23749301 | |
| 845 | Phosphorylation | YLGAKLASFYERAGK HHHHHHHHHHHHHCC | 38.51 | 22369663 | |
| 852 | Ubiquitination | SFYERAGKAVALGSP HHHHHHCCEECCCCC | 38.41 | 23749301 | |
| 858 | Phosphorylation | GKAVALGSPDRTGSV CCEECCCCCCCCCCE | 25.20 | 22369663 | |
| 899 | Ubiquitination | VFWGLDKKLAQRKHF HHHCCCHHHHHHCCC | 49.04 | 22817900 | |
| 904 | Ubiquitination | DKKLAQRKHFPSINT CHHHHHHCCCCCCCC | 37.20 | 22817900 | |
| 911 | Phosphorylation | KHFPSINTSVSYSKY CCCCCCCCCCCHHHH | 28.92 | 28889911 | |
| 915 | Phosphorylation | SINTSVSYSKYTNVL CCCCCCCHHHHHHHH | 13.66 | 21440633 | |
| 917 | Ubiquitination | NTSVSYSKYTNVLNK CCCCCHHHHHHHHHH | 48.11 | 23749301 | |
| 917 | Acetylation | NTSVSYSKYTNVLNK CCCCCHHHHHHHHHH | 48.11 | 24489116 | |
| 924 | Ubiquitination | KYTNVLNKFYDSNYP HHHHHHHHHHCCCCC | 40.93 | 23749301 | |
| 928 | Phosphorylation | VLNKFYDSNYPEFPV HHHHHHCCCCCCCHH | 27.21 | 28889911 | |
| 941 | Ubiquitination | PVLRDRMKEILSNAE HHHHHHHHHHHHCHH | 42.36 | 23749301 | |
| 941 | Acetylation | PVLRDRMKEILSNAE HHHHHHHHHHHHCHH | 42.36 | 24489116 | |
| 959 | Ubiquitination | QVVQLVGKSALSDSD HHHHHHHHHHCCCCC | 25.69 | 24961812 | |
| 1014 | Acetylation | SYHDEAQKAVANGAN HCCHHHHHHHHCCCC | 52.45 | 24489116 | |
| 1023 | Phosphorylation | VANGANWSKLADSTG HHCCCCHHHHHCCCC | 20.00 | 22369663 | |
| 1024 | Ubiquitination | ANGANWSKLADSTGD HCCCCHHHHHCCCCC | 39.03 | 23749301 | |
| 1024 | Acetylation | ANGANWSKLADSTGD HCCCCHHHHHCCCCC | 39.03 | 24489116 | |
| 1028 | Phosphorylation | NWSKLADSTGDVKHA CHHHHHCCCCCCCHH | 28.78 | 22369663 | |
| 1029 | Phosphorylation | WSKLADSTGDVKHAV HHHHHCCCCCCCHHH | 37.64 | 22369663 | |
| 1033 | Ubiquitination | ADSTGDVKHAVSSSK HCCCCCCCHHHHHCC | 30.50 | 23749301 | |
| 1033 | Acetylation | ADSTGDVKHAVSSSK HCCCCCCCHHHHHCC | 30.50 | 24489116 | |
| 1033 | 2-Hydroxyisobutyrylation | ADSTGDVKHAVSSSK HCCCCCCCHHHHHCC | 30.50 | - | |
| 1040 | Ubiquitination | KHAVSSSKFFEPSRG CHHHHHCCCCCCCCC | 56.89 | 22817900 | |
| 1040 | Acetylation | KHAVSSSKFFEPSRG CHHHHHCCCCCCCCC | 56.89 | 24489116 | |
| 1049 | Ubiquitination | FEPSRGEKEVHGEFE CCCCCCCCCHHHHHH | 68.79 | 24961812 | |
| 1049 | Acetylation | FEPSRGEKEVHGEFE CCCCCCCCCHHHHHH | 68.79 | 24489116 | |
| 1057 | Ubiquitination | EVHGEFEKLLSTMQE CHHHHHHHHHHHHHH | 61.11 | 24961812 | |
| 1057 | Acetylation | EVHGEFEKLLSTMQE CHHHHHHHHHHHHHH | 61.11 | 24489116 | |
| 1069 | Phosphorylation | MQERFAESTD----- HHHHHHHCCC----- | 34.15 | 21551504 | |
| 1070 | Phosphorylation | QERFAESTD------ HHHHHHCCC------ | 36.91 | 21440633 |
| 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 VATA_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VATA_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 VATA_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-16; THR-131; SER-448;THR-771; SER-777; SER-845; SER-858 AND SER-928, AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-376, ANDMASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND MASSSPECTROMETRY. | |
