PSS_YEAST - dbPTM
PSS_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSS_YEAST
UniProt AC P08456
Protein Name CDP-diacylglycerol--serine O-phosphatidyltransferase
Gene Name CHO1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 276
Subcellular Localization Microsome membrane
Multi-pass membrane protein. Endoplasmic reticulum membrane
Multi-pass membrane protein. Mitochondrion outer membrane
Multi-pass membrane protein.
Protein Description
Protein Sequence MVESDEDFAPQEFPHTDTDVIVNEHRDENDGYASDEVGGTLSRRASSIFSINTTPLAPPNATDIQKFTSDEHHFSMMRNLHMADYITMLNGFSGFYSIVSCLRFTLTGKPHYVQRAHFFILLGMCFDFLDGRVARLRNRSSLMGQELDSLADLVSFGVAPAAIAFAIGFQTTFDVMILSFFVLCGLARLARFNVTVAQLPKDSSTGKSKYFEGLPMPTTLALVLGMAYCVRKGLIFDNIPFGIFREDQILEFHPIILVFFIHGCGMISKSLKIPKP
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
4Phosphorylation----MVESDEDFAPQ
----CCCCCCCCCCC		34.5822369663
16PhosphorylationAPQEFPHTDTDVIVN
CCCCCCCCCCCEEEC		40.6122369663
18PhosphorylationQEFPHTDTDVIVNEH
CCCCCCCCCEEECCC		33.0622369663
32PhosphorylationHRDENDGYASDEVGG
CCCCCCCCCCCCCCC		13.0422369663
34PhosphorylationDENDGYASDEVGGTL
CCCCCCCCCCCCCCE		26.3122369663
40PhosphorylationASDEVGGTLSRRASS
CCCCCCCCEEEHHHC		18.6822369663
42PhosphorylationDEVGGTLSRRASSIF
CCCCCCEEEHHHCCE		21.4022369663
46PhosphorylationGTLSRRASSIFSINT
CCEEEHHHCCEEEEC		23.3522369663
47PhosphorylationTLSRRASSIFSINTT
CEEEHHHCCEEEECC		27.0322369663
50PhosphorylationRRASSIFSINTTPLA
EHHHCCEEEECCCCC		17.1722369663
53PhosphorylationSSIFSINTTPLAPPN
HCCEEEECCCCCCCC		28.2822369663
54PhosphorylationSIFSINTTPLAPPNA
CCEEEECCCCCCCCC		16.3022369663
62PhosphorylationPLAPPNATDIQKFTS
CCCCCCCCCHHHHCC		40.0322890988
109AcetylationLRFTLTGKPHYVQRA
HHHHHCCCCCHHHHH		24.3224489116
201AcetylationVTVAQLPKDSSTGKS
EEEEECCCCCCCCCC		77.9924489116
201UbiquitinationVTVAQLPKDSSTGKS
EEEEECCCCCCCCCC		77.9923749301
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 PSS_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSS_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 PSS_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PGPS1_YEASTPGS1genetic
8666200
DS1P1_YEASTLCB3genetic
9419344
TRPF_YEASTTRP1genetic
10705462
TRPD_YEASTTRP4genetic
10705462
TAT1_YEASTTAT1genetic
10705462
TAT2_YEASTTAT2genetic
10705462
SUR1_YEASTSUR1genetic
20979339
IPT1_YEASTIPT1genetic
20979339
SCS7_YEASTSCS7genetic
20979339
SUR1_YEASTSUR1genetic
23062277
CSG2_YEASTCSG2genetic
23062277
IPT1_YEASTIPT1genetic
23062277
CDC50_YEASTCDC50genetic
24390140
RHO1_YEASTRHO1genetic
28167678
KPC1_YEASTPKC1genetic
28167678
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSS_YEAST

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Related Literatures of Post-Translational Modification
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-4; TYR-32; SER-34;SER-46; SER-47; SER-50; THR-53 AND THR-54, 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-46 AND SER-47, 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-4; SER-34; SER-42;SER-46; SER-47 AND SER-50, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-42, AND MASSSPECTROMETRY.

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