ZEO1_YEAST - dbPTM
ZEO1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZEO1_YEAST
UniProt AC Q08245
Protein Name Protein ZEO1
Gene Name ZEO1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 113
Subcellular Localization Cell membrane
Peripheral membrane protein .
Protein Description Acts antagonistically to MID2 in signaling cell wall stress to the PKC1-MPK1 cell integrity pathway..
Protein Sequence MSEIQNKAETAAQDVQQKLEETKESLQNKGQEVKEQAEASIDNLKNEATPEAEQVKKEEQNIADGVEQKKTEAANKVEETKKQASAAVSEKKETKKEGGFLKKLNRKIASIFN
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------MSEIQNKAE
------CHHHHHHHH		43.3324909858
2Acetylation------MSEIQNKAE
------CHHHHHHHH		43.3315665377
7Succinylation-MSEIQNKAETAAQD
-CHHHHHHHHHHHHH		31.0923954790
72-Hydroxyisobutyrylation-MSEIQNKAETAAQD
-CHHHHHHHHHHHHH		31.09-
7Ubiquitination-MSEIQNKAETAAQD
-CHHHHHHHHHHHHH		31.0924961812
7Acetylation-MSEIQNKAETAAQD
-CHHHHHHHHHHHHH		31.0922865919
10PhosphorylationEIQNKAETAAQDVQQ
HHHHHHHHHHHHHHH		31.9522369663
182-HydroxyisobutyrylationAAQDVQQKLEETKES
HHHHHHHHHHHHHHH		40.55-
18SuccinylationAAQDVQQKLEETKES
HHHHHHHHHHHHHHH		40.5523954790
18AcetylationAAQDVQQKLEETKES
HHHHHHHHHHHHHHH		40.5524489116
18UbiquitinationAAQDVQQKLEETKES
HHHHHHHHHHHHHHH		40.5523749301
22PhosphorylationVQQKLEETKESLQNK
HHHHHHHHHHHHHHH		30.6422369663
232-HydroxyisobutyrylationQQKLEETKESLQNKG
HHHHHHHHHHHHHHH		48.89-
23SuccinylationQQKLEETKESLQNKG
HHHHHHHHHHHHHHH		48.8923954790
23UbiquitinationQQKLEETKESLQNKG
HHHHHHHHHHHHHHH		48.8923749301
23AcetylationQQKLEETKESLQNKG
HHHHHHHHHHHHHHH		48.8924489116
25PhosphorylationKLEETKESLQNKGQE
HHHHHHHHHHHHHHH		36.4922369663
29UbiquitinationTKESLQNKGQEVKEQ
HHHHHHHHHHHHHHH		49.3523749301
292-HydroxyisobutyrylationTKESLQNKGQEVKEQ
HHHHHHHHHHHHHHH		49.35-
29SuccinylationTKESLQNKGQEVKEQ
HHHHHHHHHHHHHHH		49.3523954790
29AcetylationTKESLQNKGQEVKEQ
HHHHHHHHHHHHHHH		49.3522865919
34UbiquitinationQNKGQEVKEQAEASI
HHHHHHHHHHHHHHH		43.2723749301
34SuccinylationQNKGQEVKEQAEASI
HHHHHHHHHHHHHHH		43.2723954790
34AcetylationQNKGQEVKEQAEASI
HHHHHHHHHHHHHHH		43.2724489116
40PhosphorylationVKEQAEASIDNLKNE
HHHHHHHHHHHHHHC		23.2122369663
45SuccinylationEASIDNLKNEATPEA
HHHHHHHHHCCCHHH		60.0223954790
45UbiquitinationEASIDNLKNEATPEA
HHHHHHHHHCCCHHH		60.0223749301
45AcetylationEASIDNLKNEATPEA
HHHHHHHHHCCCHHH		60.0224489116
49PhosphorylationDNLKNEATPEAEQVK
HHHHHCCCHHHHHHH		18.5822369663
56UbiquitinationTPEAEQVKKEEQNIA
CHHHHHHHHHHHHHH		54.9123749301
56AcetylationTPEAEQVKKEEQNIA
CHHHHHHHHHHHHHH		54.9124489116
57AcetylationPEAEQVKKEEQNIAD
HHHHHHHHHHHHHHH		68.5724489116
57UbiquitinationPEAEQVKKEEQNIAD
HHHHHHHHHHHHHHH		68.5723749301
69UbiquitinationIADGVEQKKTEAANK
HHHHHHHHHHHHHHH		48.4323749301
692-HydroxyisobutyrylationIADGVEQKKTEAANK
HHHHHHHHHHHHHHH		48.43-
69AcetylationIADGVEQKKTEAANK
HHHHHHHHHHHHHHH		48.4325381059
70UbiquitinationADGVEQKKTEAANKV
HHHHHHHHHHHHHHH		51.8222817900
71PhosphorylationDGVEQKKTEAANKVE
HHHHHHHHHHHHHHH		37.5821551504
76AcetylationKKTEAANKVEETKKQ
HHHHHHHHHHHHHHH		46.4222865919
76UbiquitinationKKTEAANKVEETKKQ
HHHHHHHHHHHHHHH		46.4223749301
81UbiquitinationANKVEETKKQASAAV
HHHHHHHHHHHHHHH		46.2822106047
812-HydroxyisobutyrylationANKVEETKKQASAAV
HHHHHHHHHHHHHHH		46.28-
81AcetylationANKVEETKKQASAAV
HHHHHHHHHHHHHHH		46.2825381059
82UbiquitinationNKVEETKKQASAAVS
HHHHHHHHHHHHHHH		59.5223749301
85PhosphorylationEETKKQASAAVSEKK
HHHHHHHHHHHHHHH		17.8022369663
89PhosphorylationKQASAAVSEKKETKK
HHHHHHHHHHHHHHH		38.6822369663
91AcetylationASAAVSEKKETKKEG
HHHHHHHHHHHHHHC		48.6924489116
91UbiquitinationASAAVSEKKETKKEG
HHHHHHHHHHHHHHC		48.6923749301
91SuccinylationASAAVSEKKETKKEG
HHHHHHHHHHHHHHC		48.6923954790
912-HydroxyisobutyrylationASAAVSEKKETKKEG
HHHHHHHHHHHHHHC		48.69-
92AcetylationSAAVSEKKETKKEGG
HHHHHHHHHHHHHCC		67.5724489116
92UbiquitinationSAAVSEKKETKKEGG
HHHHHHHHHHHHHCC		67.5724961812
94PhosphorylationAVSEKKETKKEGGFL
HHHHHHHHHHHCCHH		57.1928889911
95UbiquitinationVSEKKETKKEGGFLK
HHHHHHHHHHCCHHH		50.3322817900
96UbiquitinationSEKKETKKEGGFLKK
HHHHHHHHHCCHHHH		69.8522817900
1022-HydroxyisobutyrylationKKEGGFLKKLNRKIA
HHHCCHHHHHHHHHH		53.61-
102UbiquitinationKKEGGFLKKLNRKIA
HHHCCHHHHHHHHHH		53.6122817900
102AcetylationKKEGGFLKKLNRKIA
HHHCCHHHHHHHHHH		53.6125381059
103UbiquitinationKEGGFLKKLNRKIAS
HHCCHHHHHHHHHHH		53.8122817900
107UbiquitinationFLKKLNRKIASIFN-
HHHHHHHHHHHHCC-		41.3623749301
110PhosphorylationKLNRKIASIFN----
HHHHHHHHHCC----		31.0521440633
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 ZEO1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
25SPhosphorylation

15665377
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 ZEO1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAC7_YEASTSAC7genetic
12949174
CALM_YEASTCMD1physical
16554755
MTC1_YEASTMTC1physical
16554755
MOT3_YEASTMOT3physical
18719252
MID2_YEASTMID2genetic
12949174
HSP71_YEASTSSA1physical
22940862
PMA1_YEASTPMA1genetic
23891562
SAC7_YEASTSAC7genetic
23891562
SRO7_YEASTSRO7genetic
23891562
SEC9_YEASTSEC9genetic
23891562
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZEO1_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: PROTEIN SEQUENCE OF 2-29 AND 35-69, ACETYLATION [LARGE SCALE ANALYSIS]AT SER-2, PHOSPHORYLATION AT SER-2; SER-25; SER-40 AND THR-49, ANDMASS SPECTROMETRY.
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 THR-22; SER-25; SER-40 ANDTHR-49, AND MASS 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-25; SER-40 AND THR-49,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-25 AND THR-49, AND MASSSPECTROMETRY.
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase.";
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
Mol. Cell. Proteomics 6:1896-1906(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-40 AND THR-49,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-25; SER-40 AND THR-49,AND MASS 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: PROTEIN SEQUENCE OF 2-29 AND 35-69, ACETYLATION [LARGE SCALE ANALYSIS]AT SER-2, PHOSPHORYLATION AT SER-2; SER-25; SER-40 AND THR-49, ANDMASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PROTEIN SEQUENCE OF 35-69, UBIQUITINATION [LARGE SCALE ANALYSIS] ATLYS-45 AND LYS-57, AND MASS SPECTROMETRY.

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