ALE1_YEAST - dbPTM
ALE1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALE1_YEAST
UniProt AC Q08548
Protein Name Lysophospholipid acyltransferase
Gene Name ALE1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 619
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Microsome membrane
Multi-pass membrane protein.
Protein Description Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids. Preferentially acylates lysophosphocholine, but also lysophosphoethanolamine and lysophosphatidylglycerol..
Protein Sequence MYNPVDAVLTKIITNYGIDSFTLRYAICLLGSFPLNAILKRIPEKRIGLKCCFIISMSMFYLFGVLNLVSGFRTLFISTMFTYLISRFYRSKFMPHLNFMFVMGHLAINHIHAQFLNEQTQTTVDITSSQMVLAMKLTSFAWSYYDGSCTSESDFKDLTEHQKSRAVRGHPPLLKFLAYAFFYSTLLTGPSFDYADFDSWLNCEMFRDLPESKKPMRRHHPGERRQIPKNGKLALWKVVQGLAWMILSTLGMKHFPVKYVLDKDGFPTRSFIFRIHYLFLLGFIHRFKYYAAWTISEGSCILCGLGYNGYDSKTQKIRWDRVRNIDIWTVETAQNTREMLEAWNMNTNKWLKYSVYLRVTKKGKKPGFRSTLFTFLTSAFWHGTRPGYYLTFATGALYQTCGKIYRRNFRPIFLREDGVTPLPSKKIYDLVGIYAIKLAFGYMVQPFIILDLKPSLMVWGSVYFYVHIIVAFSFFLFRGPYAKQVTEFFKSKQPKEIFIRKQKKLEKDISASSPNLGGILKAKIEHEKGKTAEEEEMNLGIPPIELEKWDNAKEDWEDFCKDYKEWRNKNGLEIEEENLSKAFERFKQEFSNAASGSGERVRKMSFSGYSPKPISKKEE
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
164PhosphorylationDLTEHQKSRAVRGHP
HCHHHHHHHHHCCCH		20.9219795423
289PhosphorylationGFIHRFKYYAAWTIS
HHHHHHHHHEEEEEC		8.8127017623
290PhosphorylationFIHRFKYYAAWTISE
HHHHHHHHEEEEECC		7.1627017623
294PhosphorylationFKYYAAWTISEGSCI
HHHHEEEEECCCCEE		15.2027017623
353PhosphorylationNTNKWLKYSVYLRVT
CCCCCEEEEEEEEEC		10.9521551504
354PhosphorylationTNKWLKYSVYLRVTK
CCCCEEEEEEEEECC		11.6021551504
356PhosphorylationKWLKYSVYLRVTKKG
CCEEEEEEEEECCCC		5.2621551504
360PhosphorylationYSVYLRVTKKGKKPG
EEEEEEECCCCCCCC		22.1721551504
420PhosphorylationFLREDGVTPLPSKKI
EEECCCCCCCCCCHH		25.3319795423
424PhosphorylationDGVTPLPSKKIYDLV
CCCCCCCCCHHHHHH		55.0219795423
507AcetylationRKQKKLEKDISASSP
CCHHHHHCCCCCCCC		71.4524489116
510PhosphorylationKKLEKDISASSPNLG
HHHHCCCCCCCCCHH		32.0322890988
512PhosphorylationLEKDISASSPNLGGI
HHCCCCCCCCCHHHH		39.2725521595
513PhosphorylationEKDISASSPNLGGIL
HCCCCCCCCCHHHHH		19.9522369663
591PhosphorylationERFKQEFSNAASGSG
HHHHHHHHHHCCCCC		25.4724961812
595PhosphorylationQEFSNAASGSGERVR
HHHHHHCCCCCCCCE		30.9521551504
597PhosphorylationFSNAASGSGERVRKM
HHHHCCCCCCCCEEC		34.6828889911
605PhosphorylationGERVRKMSFSGYSPK
CCCCEECCCCCCCCC		21.2122369663
607PhosphorylationRVRKMSFSGYSPKPI
CCEECCCCCCCCCCC		29.5222369663
609PhosphorylationRKMSFSGYSPKPISK
EECCCCCCCCCCCCC		22.1722369663
610PhosphorylationKMSFSGYSPKPISKK
ECCCCCCCCCCCCCC		29.9422369663
615PhosphorylationGYSPKPISKKEE---
CCCCCCCCCCCC---		46.3222369663
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 ALE1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALE1_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 ALE1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLSC_YEASTSLC1genetic
16269340
PMA1_YEASTPMA1genetic
16269340
ATC1_YEASTPMR1genetic
16269340
RGP1_YEASTRGP1genetic
16269340
RIC1_YEASTRIC1genetic
16269340
CHO2_YEASTCHO2genetic
16269340
PLSC_YEASTSLC1genetic
17890783
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALE1_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-512; SER-513; SER-605;SER-607 AND SER-610, 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-605, 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-605, 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-513 AND SER-605, ANDMASS 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-513, 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-607 AND SER-610, ANDMASS SPECTROMETRY.

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