ADH1_YEAST - dbPTM
ADH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADH1_YEAST
UniProt AC P00330
Protein Name Alcohol dehydrogenase 1
Gene Name ADH1
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 primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols..
Protein Sequence MSIPETQKGVIFYESHGKLEYKDIPVPKPKANELLINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGYTHDGSFQQYATADAVQAAHIPQGTDLAQVAPILCAGITVYKALKSANLMAGHWVAISGAAGGLGSLAVQYAKAMGYRVLGIDGGEGKEELFRSIGGEVFIDFTKEKDIVGAVLKATDGGAHGVINVSVSEAAIEASTRYVRANGTTVLVGMPAGAKCCSDVFNQVVKSISIVGSYVGNRADTREALDFFARGLVKSPIKVVGLSTLPEIYEKMEKGQIVGRYVVDTSK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSIPETQKG
------CCCCCCCCC		47.0229136822
2Acetylation------MSIPETQKG
------CCCCCCCCC		47.02320000
6Phosphorylation--MSIPETQKGVIFY
--CCCCCCCCCEEEE		30.1729136822
8SuccinylationMSIPETQKGVIFYES
CCCCCCCCCEEEEEE		63.6723954790
8UbiquitinationMSIPETQKGVIFYES
CCCCCCCCCEEEEEE		63.6724961812
8AcetylationMSIPETQKGVIFYES
CCCCCCCCCEEEEEE		63.6724489116
15PhosphorylationKGVIFYESHGKLEYK
CCEEEEEECCCEEEE		26.5917287358
18UbiquitinationIFYESHGKLEYKDIP
EEEEECCCEEEEECC		32.4924961812
18AcetylationIFYESHGKLEYKDIP
EEEEECCCEEEEECC		32.4924489116
21PhosphorylationESHGKLEYKDIPVPK
EECCCEEEEECCCCC		25.1328889911
22AcetylationSHGKLEYKDIPVPKP
ECCCEEEEECCCCCC		39.5424489116
22SuccinylationSHGKLEYKDIPVPKP
ECCCEEEEECCCCCC		39.5423954790
22UbiquitinationSHGKLEYKDIPVPKP
ECCCEEEEECCCCCC		39.5422817900
28SuccinylationYKDIPVPKPKANELL
EEECCCCCCCCCEEE		60.4223954790
28AcetylationYKDIPVPKPKANELL
EEECCCCCCCCCEEE		60.4224489116
28UbiquitinationYKDIPVPKPKANELL
EEECCCCCCCCCEEE		60.4223749301
30AcetylationDIPVPKPKANELLIN
ECCCCCCCCCEEEEE		70.7124489116
30SuccinylationDIPVPKPKANELLIN
ECCCCCCCCCEEEEE		70.7123954790
30UbiquitinationDIPVPKPKANELLIN
ECCCCCCCCCEEEEE		70.7117644757
39UbiquitinationNELLINVKYSGVCHT
CEEEEEEEEECCCCC		29.2523749301
46PhosphorylationKYSGVCHTDLHAWHG
EEECCCCCCHHHCCC		34.8221440633
60UbiquitinationGDWPLPVKLPLVGGH
CCCCCCEEECEECCC		42.3123749301
81SuccinylationVGMGENVKGWKIGDY
EECCCCCCCCEECCC		71.3123954790
81UbiquitinationVGMGENVKGWKIGDY
EECCCCCCCCEECCC		71.3123749301
81AcetylationVGMGENVKGWKIGDY
EECCCCCCCCEECCC		71.3124489116
84SuccinylationGENVKGWKIGDYAGI
CCCCCCCEECCCCCC		45.5423954790
84UbiquitinationGENVKGWKIGDYAGI
CCCCCCCEECCCCCC		45.5423749301
84AcetylationGENVKGWKIGDYAGI
CCCCCCCEECCCCCC		45.5424489116
92UbiquitinationIGDYAGIKWLNGSCM
ECCCCCCEEECCCEE		44.7217644757
161UbiquitinationCAGITVYKALKSANL
HHHHHHHHHHHHCCC		42.7922817900
164UbiquitinationITVYKALKSANLMAG
HHHHHHHHHCCCCCC		53.0023749301
165PhosphorylationTVYKALKSANLMAGH
HHHHHHHHCCCCCCE		24.2021440633
177PhosphorylationAGHWVAISGAAGGLG
CCEEEEECCCCCCHH		16.7921440633
192UbiquitinationSLAVQYAKAMGYRVL
HHHHHHHHHCCCEEE		33.6923749301
207AcetylationGIDGGEGKEELFRSI
EEECCCCHHHHHHHH		43.6524489116
207UbiquitinationGIDGGEGKEELFRSI
EEECCCCHHHHHHHH		43.6523749301
207SuccinylationGIDGGEGKEELFRSI
EEECCCCHHHHHHHH		43.6523954790
213PhosphorylationGKEELFRSIGGEVFI
CHHHHHHHHCCEEEE		20.4617287358
223PhosphorylationGEVFIDFTKEKDIVG
CEEEEECCCCCCEEE		34.2517287358
224AcetylationEVFIDFTKEKDIVGA
EEEEECCCCCCEEEE		63.8624489116
224UbiquitinationEVFIDFTKEKDIVGA
EEEEECCCCCCEEEE		63.8617644757
224SuccinylationEVFIDFTKEKDIVGA
EEEEECCCCCCEEEE		63.8623954790
226AcetylationFIDFTKEKDIVGAVL
EEECCCCCCEEEEEE		55.0724489116
226UbiquitinationFIDFTKEKDIVGAVL
EEECCCCCCEEEEEE		55.0724961812
226SuccinylationFIDFTKEKDIVGAVL
EEECCCCCCEEEEEE		55.0723954790
234UbiquitinationDIVGAVLKATDGGAH
CEEEEEEEECCCCCC		42.5122106047
249PhosphorylationGVINVSVSEAAIEAS
CEEEEEHHHHHHHHH		17.6328889911
265PhosphorylationRYVRANGTTVLVGMP
EEEECCCCEEEECCC		17.3428152593
266PhosphorylationYVRANGTTVLVGMPA
EEECCCCEEEECCCC		17.1528152593
276UbiquitinationVGMPAGAKCCSDVFN
ECCCCCCHHHHHHHH		34.5523749301
279PhosphorylationPAGAKCCSDVFNQVV
CCCCHHHHHHHHHHH		46.4028152593
287UbiquitinationDVFNQVVKSISIVGS
HHHHHHHHHHHHEEC		43.1223749301
288PhosphorylationVFNQVVKSISIVGSY
HHHHHHHHHHHEECC		15.2317330950
290PhosphorylationNQVVKSISIVGSYVG
HHHHHHHHHEECCCC		20.5021082442
294PhosphorylationKSISIVGSYVGNRAD
HHHHHEECCCCCCCC		13.0217287358
295PhosphorylationSISIVGSYVGNRADT
HHHHEECCCCCCCCH		13.3729136822
302PhosphorylationYVGNRADTREALDFF
CCCCCCCHHHHHHHH		29.4417287358
315SuccinylationFFARGLVKSPIKVVG
HHHHCCCCCCCEEEE		56.4023954790
315UbiquitinationFFARGLVKSPIKVVG
HHHHCCCCCCCEEEE		56.4023749301
315AcetylationFFARGLVKSPIKVVG
HHHHCCCCCCCEEEE		56.4024489116
316PhosphorylationFARGLVKSPIKVVGL
HHHCCCCCCCEEEEE		25.1217330950
319UbiquitinationGLVKSPIKVVGLSTL
CCCCCCCEEEEECCH		33.9623749301
319AcetylationGLVKSPIKVVGLSTL
CCCCCCCEEEEECCH		33.9624489116
319SuccinylationGLVKSPIKVVGLSTL
CCCCCCCEEEEECCH		33.9623954790
324PhosphorylationPIKVVGLSTLPEIYE
CCEEEEECCHHHHHH		23.2025521595
325PhosphorylationIKVVGLSTLPEIYEK
CEEEEECCHHHHHHH		51.9125521595
330PhosphorylationLSTLPEIYEKMEKGQ
ECCHHHHHHHHHCCC		14.0828889911
332UbiquitinationTLPEIYEKMEKGQIV
CHHHHHHHHHCCCEE		35.0723749301
332AcetylationTLPEIYEKMEKGQIV
CHHHHHHHHHCCCEE		35.0724489116
332SuccinylationTLPEIYEKMEKGQIV
CHHHHHHHHHCCCEE		35.0723954790
335SuccinylationEIYEKMEKGQIVGRY
HHHHHHHCCCEEEEE		53.2523954790
335UbiquitinationEIYEKMEKGQIVGRY
HHHHHHHCCCEEEEE		53.2523749301
335AcetylationEIYEKMEKGQIVGRY
HHHHHHHCCCEEEEE		53.2524489116
342PhosphorylationKGQIVGRYVVDTSK-
CCCEEEEEEEECCC-		10.0121440633
347PhosphorylationGRYVVDTSK------
EEEEEECCC------		31.7221440633
348UbiquitinationRYVVDTSK-------
EEEEECCC-------		67.4617644757
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 ADH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADH1_YEAST !!
Disease-associated PTM Sites based on SAP

* 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 ADH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADH2_YEASTADH2genetic
9836432
ADH5_YEASTADH5genetic
18408719
ADH1_YEASTADH1physical
19343713
FAB1_YEASTFAB1genetic
20526336
TPM1_YEASTTPM1genetic
20526336
BCK1_YEASTBCK1genetic
20526336
SMY1_YEASTSMY1genetic
20526336
RV161_YEASTRVS161genetic
20526336
IRE1_YEASTIRE1genetic
20526336
PEX11_YEASTPEX11genetic
20526336
SRO7_YEASTSRO7genetic
20526336
ADH2_YEASTADH2genetic
22033067
ADH3_YEASTADH3genetic
22033067
ADH4_YEASTADH4genetic
22033067
ADH5_YEASTADH5genetic
22033067
FADH_YEASTSFA1genetic
22033067
ADH1_YEASTADH1physical
25157460
RHC31_YEASTAOS1physical
21036361
ATG18_YEASTATG18physical
21036361
ECM1_YEASTECM1physical
21036361
ESA1_YEASTESA1physical
21036361
FAR11_YEASTFAR11physical
21036361
FTH1_YEASTFTH1physical
21036361
FUN19_YEASTFUN19physical
21036361
ISW2_YEASTISW2physical
21036361
LEUC_YEASTLEU1physical
21036361
MED7_YEASTMED7physical
21036361
MYO4_YEASTMYO4physical
21036361
ADH2_YEASTADH2physical
21036361
ADH3_YEASTADH3physical
21036361
PRR1_YEASTPRR1physical
21036361
SNX3_YEASTSNX3physical
21036361
ADH1_YEASTADH1physical
26743849
PMP1_YEASTPMP1physical
26404137
PCH2_HUMANTRIP13physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADH1_YEAST

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The primary structure of yeast alcohol dehydrogenase.";
Joernvall H.;
Eur. J. Biochem. 72:425-442(1977).
Cited for: PROTEIN SEQUENCE OF 2-348, ACETYLATION AT SER-2, AND VARIANT ILE-236.
Phosphorylation
ReferencePubMed
"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-316 AND THR-325, 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-316, AND MASSSPECTROMETRY.
"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-15; SER-213 AND THR-223,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 SER-316, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory