| UniProt ID | VAC8_YEAST | |
|---|---|---|
| UniProt AC | P39968 | |
| Protein Name | Vacuolar protein 8 | |
| Gene Name | VAC8 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 578 | |
| Subcellular Localization |
Vacuole membrane Lipid-anchor . |
|
| Protein Description | Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.. | |
| Protein Sequence | MGSCCSCLKDSSDEASVSPIADNEREAVTLLLGYLEDKDQLDFYSGGPLKALTTLVYSDNLNLQRSAALAFAEITEKYVRQVSREVLEPILILLQSQDPQIQVAACAALGNLAVNNENKLLIVEMGGLEPLINQMMGDNVEVQCNAVGCITNLATRDDNKHKIATSGALIPLTKLAKSKHIRVQRNATGALLNMTHSEENRKELVNAGAVPVLVSLLSSTDPDVQYYCTTALSNIAVDEANRKKLAQTEPRLVSKLVSLMDSPSSRVKCQATLALRNLASDTSYQLEIVRAGGLPHLVKLIQSDSIPLVLASVACIRNISIHPLNEGLIVDAGFLKPLVRLLDYKDSEEIQCHAVSTLRNLAASSEKNRKEFFESGAVEKCKELALDSPVSVQSEISACFAILALADVSKLDLLEANILDALIPMTFSQNQEVSGNAAAALANLCSRVNNYTKIIEAWDRPNEGIRGFLIRFLKSDYATFEHIALWTILQLLESHNDKVEDLVKNDDDIINGVRKMADVTFERLQRSGIDVKNPGSNNNPSSNDNNSNNNDTGSEHQPVEDASLELYNITQQILQFLH | |
| 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 | N-myristoyl glycine | ------MGSCCSCLK ------CCCCCCCCC | 29.41 | - | |
| 2 | Myristoylation | ------MGSCCSCLK ------CCCCCCCCC | 29.41 | 9490720 | |
| 4 | S-palmitoylation | ----MGSCCSCLKDS ----CCCCCCCCCCC | 1.31 | 19453970 | |
| 5 | S-palmitoylation | ---MGSCCSCLKDSS ---CCCCCCCCCCCC | 3.26 | 19453970 | |
| 7 | S-palmitoylation | -MGSCCSCLKDSSDE -CCCCCCCCCCCCCC | 3.23 | 19453970 | |
| 11 | Phosphorylation | CCSCLKDSSDEASVS CCCCCCCCCCCCCCC | 37.79 | 22890988 | |
| 12 | Phosphorylation | CSCLKDSSDEASVSP CCCCCCCCCCCCCCC | 49.99 | 22890988 | |
| 16 | Phosphorylation | KDSSDEASVSPIADN CCCCCCCCCCCCCCC | 22.53 | 22369663 | |
| 18 | Phosphorylation | SSDEASVSPIADNER CCCCCCCCCCCCCHH | 14.21 | 22369663 | |
| 29 | Phosphorylation | DNEREAVTLLLGYLE CCHHHHHHHHHHHHC | 20.80 | 19823750 | |
| 34 | Phosphorylation | AVTLLLGYLEDKDQL HHHHHHHHHCCHHHC | 13.59 | 19823750 | |
| 77 | Ubiquitination | AFAEITEKYVRQVSR HHHHHHHHHHHHHHH | 40.16 | 23749301 | |
| 174 | Ubiquitination | GALIPLTKLAKSKHI CCHHHHHHHHHCCCC | 54.88 | 23749301 | |
| 174 | Acetylation | GALIPLTKLAKSKHI CCHHHHHHHHHCCCC | 54.88 | 24489116 | |
| 244 | Ubiquitination | VDEANRKKLAQTEPR CCHHHHHHHHCCCHH | 45.90 | 23749301 | |
| 255 | Acetylation | TEPRLVSKLVSLMDS CCHHHHHHHHHHHCC | 45.49 | 24489116 | |
| 258 | Phosphorylation | RLVSKLVSLMDSPSS HHHHHHHHHHCCCCH | 28.54 | 27017623 | |
| 264 | Phosphorylation | VSLMDSPSSRVKCQA HHHHCCCCHHHHHHH | 34.43 | 27017623 | |
| 282 | Phosphorylation | LRNLASDTSYQLEIV HHHHCCCCCEEEEEE | 27.17 | 28889911 | |
| 370 | Ubiquitination | ASSEKNRKEFFESGA HCCHHHHHHHHHCCH | 69.16 | 23749301 | |
| 515 | Acetylation | DIINGVRKMADVTFE HHHHHHHHHHHHCHH | 35.71 | 25381059 | |
| 515 | Ubiquitination | DIINGVRKMADVTFE HHHHHHHHHHHHCHH | 35.71 | 23749301 | |
| 527 | Phosphorylation | TFERLQRSGIDVKNP CHHHHHHCCCCCCCC | 27.43 | 24961812 | |
| 536 | Phosphorylation | IDVKNPGSNNNPSSN CCCCCCCCCCCCCCC | 37.33 | 19823750 | |
| 541 | Phosphorylation | PGSNNNPSSNDNNSN CCCCCCCCCCCCCCC | 43.85 | 19823750 | |
| 542 | Phosphorylation | GSNNNPSSNDNNSNN CCCCCCCCCCCCCCC | 49.84 | 19823750 | |
| 547 | Phosphorylation | PSSNDNNSNNNDTGS CCCCCCCCCCCCCCC | 47.38 | 19823750 | |
| 552 | Phosphorylation | NNSNNNDTGSEHQPV CCCCCCCCCCCCCCH | 44.74 | 19823750 | |
| 554 | Phosphorylation | SNNNDTGSEHQPVED CCCCCCCCCCCCHHH | 33.72 | 19823750 | |
| 563 | Phosphorylation | HQPVEDASLELYNIT CCCHHHHHHHHHHHH | 34.40 | 19823750 | |
| 567 | Phosphorylation | EDASLELYNITQQIL HHHHHHHHHHHHHHH | 8.64 | 19823750 | |
| 570 | Phosphorylation | SLELYNITQQILQFL HHHHHHHHHHHHHHC | 15.70 | 19823750 |
| 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 VAC8_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VAC8_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 VAC8_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Myristoylation | |
| Reference | PubMed |
| "Vac8p, a vacuolar protein with armadillo repeats, functions in bothvacuole inheritance and protein targeting from the cytoplasm tovacuole."; Wang Y.-X., Catlett N.L., Weisman L.S.; J. Cell Biol. 140:1063-1074(1998). Cited for: FUNCTION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4; CYS-5 ANDCYS-7, MUTAGENESIS OF 4-CYS--CYS-7, AND SUBCELLULAR LOCATION. | |
| 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 AND SER-18, 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-16, AND MASSSPECTROMETRY. | |
