UniProt ID | STV1_YEAST | |
---|---|---|
UniProt AC | P37296 | |
Protein Name | V-type proton ATPase subunit a, Golgi isoform | |
Gene Name | STV1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 890 | |
Subcellular Localization |
Endosome membrane Multi-pass membrane protein. Golgi apparatus 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 Golgi- and endosome-residing V-ATPase complexes. Enzymes containing this subunit have a 4-fold lower ratio of proton transport to ATP hydrolysis than complexes containing the vacuolar isoform and do not dissociate V1 and V0 in response to glucose depletion. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.. | |
Protein Sequence | MNQEEAIFRSADMTYVQLYIPLEVIREVTFLLGKMSVFMVMDLNKDLTAFQRGYVNQLRRFDEVERMVGFLNEVVEKHAAETWKYILHIDDEGNDIAQPDMADLINTMEPLSLENVNDMVKEITDCESRARQLDESLDSLRSKLNDLLEQRQVIFECSKFIEVNPGIAGRATNPEIEQEERDVDEFRMTPDDISETLSDAFSFDDETPQDRGALGNDLTRNQSVEDLSFLEQGYQHRYMITGSIRRTKVDILNRILWRLLRGNLIFQNFPIEEPLLEGKEKVEKDCFIIFTHGETLLKKVKRVIDSLNGKIVSLNTRSSELVDTLNRQIDDLQRILDTTEQTLHTELLVIHDQLPVWSAMTKREKYVYTTLNKFQQESQGLIAEGWVPSTELIHLQDSLKDYIETLGSEYSTVFNVILTNKLPPTYHRTNKFTQAFQSIVDAYGIATYKEINAGLATVVTFPFMFAIMFGDMGHGFILFLMALFLVLNERKFGAMHRDEIFDMAFTGRYVLLLMGAFSVYTGLLYNDIFSKSMTIFKSGWQWPSTFRKGESIEAKKTGVYPFGLDFAWHGTDNGLLFSNSYKMKLSILMGYAHMTYSFMFSYINYRAKNSKVDIIGNFIPGLVFMQSIFGYLSWAIVYKWSKDWIKDDKPAPGLLNMLINMFLAPGTIDDQLYSGQAKLQVVLLLAALVCVPWLLLYKPLTLRRLNKNGGGGRPHGYQSVGNIEHEEQIAQQRHSAEGFQGMIISDVASVADSINESVGGGEQGPFNFGDVMIHQVIHTIEFCLNCISHTASYLRLWALSLAHAQLSSVLWDMTISNAFSSKNSGSPLAVMKVVFLFAMWFVLTVCILVFMEGTSAMLHALRLHWVEAMSKFFEGEGYAYEPFSFRAIIE | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MNQEEAIF -------CCHHHHHH | 12.02 | 22814378 | |
143 | Ubiquitination | SLDSLRSKLNDLLEQ HHHHHHHHHHHHHHH | 44.89 | 17644757 | |
159 | Ubiquitination | QVIFECSKFIEVNPG HHHHHCCCCEECCCC | 63.12 | 17644757 | |
172 | Phosphorylation | PGIAGRATNPEIEQE CCCCCCCCCHHHHHH | 50.36 | 27214570 | |
189 | Phosphorylation | DVDEFRMTPDDISET CHHHHCCCHHHHHHH | 21.22 | 28889911 | |
194 | Phosphorylation | RMTPDDISETLSDAF CCCHHHHHHHHHHHC | 31.36 | 30377154 | |
196 | Phosphorylation | TPDDISETLSDAFSF CHHHHHHHHHHHCCC | 25.44 | 27738172 | |
198 | Phosphorylation | DDISETLSDAFSFDD HHHHHHHHHHCCCCC | 34.02 | 28889911 | |
202 | Phosphorylation | ETLSDAFSFDDETPQ HHHHHHCCCCCCCCC | 29.50 | 27214570 | |
219 | Phosphorylation | GALGNDLTRNQSVED CCCCCCCCCCCCHHH | 30.36 | 28889911 | |
223 | Phosphorylation | NDLTRNQSVEDLSFL CCCCCCCCHHHHHHH | 30.90 | 22369663 | |
228 | Phosphorylation | NQSVEDLSFLEQGYQ CCCHHHHHHHHHHCC | 39.86 | 22369663 | |
234 | Phosphorylation | LSFLEQGYQHRYMIT HHHHHHHCCEEEEEC | 10.80 | 29136822 | |
537 | Ubiquitination | SKSMTIFKSGWQWPS HCCCEEECCCCCCCC | 44.18 | 17644757 | |
548 | Ubiquitination | QWPSTFRKGESIEAK CCCCCCCCCCCEECH | 63.94 | 17644757 | |
551 | Phosphorylation | STFRKGESIEAKKTG CCCCCCCCEECHHCC | 34.10 | 21126336 | |
586 | Phosphorylation | NSYKMKLSILMGYAH CCHHHHHHHHHHCCH | 14.25 | 27017623 | |
596 | Phosphorylation | MGYAHMTYSFMFSYI HHCCHHHHHHHHHHH | 7.73 | 27017623 | |
605 | Phosphorylation | FMFSYINYRAKNSKV HHHHHHHHCCCCCCE | 11.46 | 27017623 | |
707 | Ubiquitination | LTLRRLNKNGGGGRP HHHHHCCCCCCCCCC | 62.65 | 17644757 |
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 STV1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STV1_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 STV1_YEAST !! |
Kegg Drug | ||||||
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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-223 AND SER-228, ANDMASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND MASSSPECTROMETRY. | |
"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 SER-223, AND MASSSPECTROMETRY. |