| UniProt ID | ADH2_YEAST | |
|---|---|---|
| UniProt AC | P00331 | |
| Protein Name | Alcohol dehydrogenase 2 | |
| Gene Name | ADH2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 348 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols.. | |
| Protein Sequence | MSIPETQKAIIFYESNGKLEHKDIPVPKPKPNELLINVKYSGVCHTDLHAWHGDWPLPTKLPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGYTHDGSFQEYATADAVQAAHIPQGTDLAEVAPILCAGITVYKALKSANLRAGHWAAISGAAGGLGSLAVQYAKAMGYRVLGIDGGPGKEELFTSLGGEVFIDFTKEKDIVSAVVKATNGGAHGIINVSVSEAAIEASTRYCRANGTVVLVGLPAGAKCSSDVFNHVVKSISIVGSYVGNRADTREALDFFARGLVKSPIKVVGLSSLPEIYEKMEKGQIAGRYVVDTSK | |
| 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 | ------MSIPETQKA ------CCCCCCCEE | 47.02 | 9298649 | |
| 2 | Phosphorylation | ------MSIPETQKA ------CCCCCCCEE | 47.02 | 19823750 | |
| 6 | Phosphorylation | --MSIPETQKAIIFY --CCCCCCCEEEEEE | 29.98 | 19823750 | |
| 15 | Phosphorylation | KAIIFYESNGKLEHK EEEEEEEECCCEEEC | 39.23 | 29734811 | |
| 22 | Acetylation | SNGKLEHKDIPVPKP ECCCEEECCCCCCCC | 48.23 | 25381059 | |
| 28 | Ubiquitination | HKDIPVPKPKPNELL ECCCCCCCCCCCCEE | 66.94 | 23749301 | |
| 39 | Ubiquitination | NELLINVKYSGVCHT CCEEEEEEEECCCCC | 29.25 | 22817900 | |
| 60 | Ubiquitination | GDWPLPTKLPLVGGH CCCCCCCCCCEECCC | 46.28 | 23749301 | |
| 81 | Ubiquitination | VGMGENVKGWKIGDY EECCCCCCCCEECCC | 71.31 | 23749301 | |
| 84 | Ubiquitination | GENVKGWKIGDYAGI CCCCCCCEECCCCCC | 45.54 | 23749301 | |
| 92 | Ubiquitination | IGDYAGIKWLNGSCM ECCCCCCEEECCCEE | 44.72 | 17644757 | |
| 212 | Phosphorylation | PGKEELFTSLGGEVF CCHHHHHHCCCCEEE | 35.35 | 28889911 | |
| 213 | Phosphorylation | GKEELFTSLGGEVFI CHHHHHHCCCCEEEE | 20.06 | 28889911 | |
| 223 | Phosphorylation | GEVFIDFTKEKDIVS CEEEEECCCHHHHEE | 34.25 | 28889911 | |
| 226 | Acetylation | FIDFTKEKDIVSAVV EEECCCHHHHEEEEE | 55.07 | 25381059 | |
| 249 | Phosphorylation | GIINVSVSEAAIEAS EEEEEEHHHHHHHHH | 17.63 | 18407956 | |
| 279 | Phosphorylation | PAGAKCSSDVFNHVV CCCCCCCHHHHHHHH | 47.46 | - | |
| 287 | Ubiquitination | DVFNHVVKSISIVGS HHHHHHHHHHHEECC | 40.77 | 17644757 | |
| 288 | Phosphorylation | VFNHVVKSISIVGSY HHHHHHHHHHEECCC | 15.23 | 17330950 | |
| 290 | Phosphorylation | NHVVKSISIVGSYVG HHHHHHHHEECCCCC | 20.50 | 21082442 | |
| 294 | Phosphorylation | KSISIVGSYVGNRAD HHHHEECCCCCCCCC | 13.02 | 17287358 | |
| 295 | Phosphorylation | SISIVGSYVGNRADT HHHEECCCCCCCCCH | 13.37 | 29136822 | |
| 302 | Phosphorylation | YVGNRADTREALDFF CCCCCCCHHHHHHHH | 29.44 | 17287358 | |
| 315 | Ubiquitination | FFARGLVKSPIKVVG HHHHCCCCCCCEEEE | 56.40 | 23749301 | |
| 316 | Phosphorylation | FARGLVKSPIKVVGL HHHCCCCCCCEEEEC | 25.12 | 17330950 | |
| 319 | Ubiquitination | GLVKSPIKVVGLSSL CCCCCCCEEEECCCC | 33.96 | 22817900 | |
| 325 | Phosphorylation | IKVVGLSSLPEIYEK CEEEECCCCHHHHHH | 53.65 | 29734811 | |
| 332 | Ubiquitination | SLPEIYEKMEKGQIA CCHHHHHHHHCCCCC | 35.07 | 22817900 | |
| 332 | Acetylation | SLPEIYEKMEKGQIA CCHHHHHHHHCCCCC | 35.07 | 24489116 | |
| 335 | Ubiquitination | EIYEKMEKGQIAGRY HHHHHHHCCCCCEEE | 53.25 | 22817900 | |
| 335 | Acetylation | EIYEKMEKGQIAGRY HHHHHHHCCCCCEEE | 53.25 | 25381059 | |
| 348 | Ubiquitination | RYVVDTSK------- EEEEECCC------- | 67.46 | 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 ADH2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ADH2_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 ADH2_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| LAM5_YEAST | YFL042C | physical | 10688190 | |
| ADR1_YEAST | ADR1 | genetic | 3302603 | |
| ADH3_YEAST | ADH3 | genetic | 22033067 | |
| ADH4_YEAST | ADH4 | genetic | 22033067 | |
| ADH5_YEAST | ADH5 | genetic | 22033067 | |
| FADH_YEAST | SFA1 | genetic | 22033067 | |
| GPR1_YEAST | GPR1 | genetic | 27708008 | |
| ATG9_YEAST | ATG9 | genetic | 27708008 | |
| NKP1_YEAST | NKP1 | genetic | 27708008 | |
| CSN12_YEAST | YJR084W | genetic | 27708008 | |
| NAA38_YEAST | MAK31 | genetic | 27708008 | |
| THRC_YEAST | THR4 | genetic | 27708008 | |
| MNN10_YEAST | MNN10 | genetic | 27708008 | |
| VAM7_YEAST | VAM7 | genetic | 27708008 | |
| MUP1_YEAST | MUP1 | genetic | 27708008 | |
| YHK5_YEAST | YHR045W | genetic | 27708008 | |
| RS30A_YEAST | RPS30A | genetic | 27708008 | |
| RS30B_YEAST | RPS30A | genetic | 27708008 | |
| YL413_YEAST | INA1 | genetic | 27708008 | |
| SUCA_YEAST | LSC1 | genetic | 27708008 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins."; Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.; Electrophoresis 18:1347-1360(1997). Cited for: ACETYLATION AT SER-2. | |
| 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-288; SER-290 ANDSER-316, 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-290; SER-294 ANDTHR-302, AND MASS SPECTROMETRY. | |
| "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-316, 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-290, AND MASSSPECTROMETRY. | |