YM54_YEAST - dbPTM
YM54_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YM54_YEAST
UniProt AC Q04336
Protein Name Uncharacterized protein YMR196W
Gene Name YMR196W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1088
Subcellular Localization
Protein Description
Protein Sequence MNKLRDKFVDSTVEEERLRENRNHEKYWYRWGPYLSERSWATVREDYSLNGDAWSNFPFEHANARVFRWGEDGLFGVSDNKQLVCMNVALWNGKDERLKERLFGLTGPQGNHGEDVKELYFYLDNTPTHSYMKALYKYPFKKAFPYKELVQKNGERGYEDKEFEVYDIDGLYRDSETGDNPYFDVFFEMAKDDENPSELNFRLTIHNRSKIDSGELYIAPQLFFRNTWAFDGTRTKDKPLLERDAEAANLINMTHKKYGNCQMVFQPSPGGFSSGTNEEEEDKEVEDIDPLLLFTDNESNLVKLFNEEKNPSEYTKDAFEEYLVQGKTDAVNPENKGTKACAVYHFKNIPPGEYVTVRYKFTNDPKNSIFKAQNLAVVDEDEFDLIFDNREEEADNFYWRITPLPISDELRNLQRQAFSGLLWTKQFYNFTYDAWYNGDANVKPRPPPNRANGRNKNWKHLYIEDILSMPDKWEYPFFASWDTAFHCIPLAMIDPEFAKRQLDLLTREWYMHPNGQIPAYEWNFNDVNPPVHAWAVYRVFKIERNMYNREDRTFLERVFQKLLLNFTWWVNRKDTEGKNVFEGGFLGLDNIGVFNRSEPLPTGGTLEQADSTGWMAFFSLQMLNIALELAKENPVYEDIASKFFEHFILISDSMSFEYATDITGEKCKEVIKQNLWNEADKFYYDAISWGDHKVQLPIRSLVGLIPLYASMTLEPSIIKQFRGFKKRVDWFVNNRPEIFDRNIASMSKKGVGERLLLSLVTKERLTAILSRLLDETEFLSPYGIRSLSKYHEKHPFEMNVNGVEYMVKYLPGESDSGMFGGNSNWRGPIWFPTSFLIMEALQRFYLYYGSDFKVECPVGSGDYLNLAEVAEELGYRMIHLFVPDENGERAIHYGDHSKFLSSDPYFRDYVPFFEYFDGDTGRGLGASHQCGWTALVAKWISDVGISCVRLPRTPRSSVATTASTESSEQGPKMKRMARRKSAKSLVNYTATILDLTEEEKRHHRIGGTHSGLTPQSSISSDKARHLMEEMNEEEGIHETVVPEDRHNFETKLIGKLKDKVKNMKVTDKAKDEDIDPMDPMSPLNKDVS
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
7Acetylation-MNKLRDKFVDSTVE
-CCHHHHHHCCCHHH		40.6324489116
197PhosphorylationAKDDENPSELNFRLT
ECCCCCHHHCEEEEE		67.3228889911
258PhosphorylationINMTHKKYGNCQMVF
HHCCCHHHCCEEEEE		20.5521551504
268PhosphorylationCQMVFQPSPGGFSSG
EEEEEECCCCCCCCC		25.9521551504
299PhosphorylationLLFTDNESNLVKLFN
EEEECCCCCHHHHHC		41.5428889911
309UbiquitinationVKLFNEEKNPSEYTK
HHHHCCCCCHHHHCH		68.9023749301
309AcetylationVKLFNEEKNPSEYTK
HHHHCCCCCHHHHCH		68.9024489116
366AcetylationYKFTNDPKNSIFKAQ
EEECCCCCCCCEEEE		67.2124489116
419PhosphorylationNLQRQAFSGLLWTKQ
HHHHHHHHCHHHHHH		31.3922369663
424PhosphorylationAFSGLLWTKQFYNFT
HHHCHHHHHHHCEEE		18.2222369663
693UbiquitinationAISWGDHKVQLPIRS
HHHCCCCCCCCCHHH		36.0924961812
758PhosphorylationVGERLLLSLVTKERL
HHHHHHHHHHCHHHH		22.2922369663
761PhosphorylationRLLLSLVTKERLTAI
HHHHHHHCHHHHHHH		32.2622369663
766PhosphorylationLVTKERLTAILSRLL
HHCHHHHHHHHHHHH		20.2022369663
770PhosphorylationERLTAILSRLLDETE
HHHHHHHHHHHCCCC		18.1222369663
816PhosphorylationYLPGESDSGMFGGNS
ECCCCCCCCCCCCCC		41.2428889911
938UbiquitinationGWTALVAKWISDVGI
HHHHHHHHHHHHCCC		37.2717644757
946PhosphorylationWISDVGISCVRLPRT
HHHHCCCEEEECCCC		10.7121440633
953PhosphorylationSCVRLPRTPRSSVAT
EEEECCCCCCCCCCC		22.5520377248
956PhosphorylationRLPRTPRSSVATTAS
ECCCCCCCCCCCCCC		30.3020377248
957PhosphorylationLPRTPRSSVATTAST
CCCCCCCCCCCCCCC		19.6322369663
960PhosphorylationTPRSSVATTASTESS
CCCCCCCCCCCCCCH		22.2722369663
961PhosphorylationPRSSVATTASTESSE
CCCCCCCCCCCCCHH		14.6322369663
963PhosphorylationSSVATTASTESSEQG
CCCCCCCCCCCHHCC		30.5222369663
964PhosphorylationSVATTASTESSEQGP
CCCCCCCCCCHHCCH		37.1122369663
966PhosphorylationATTASTESSEQGPKM
CCCCCCCCHHCCHHH		38.9822369663
967PhosphorylationTTASTESSEQGPKMK
CCCCCCCHHCCHHHH		27.9222369663
981PhosphorylationKRMARRKSAKSLVNY
HHHHHHHHHHHHHHH		38.8321440633
984PhosphorylationARRKSAKSLVNYTAT
HHHHHHHHHHHHHHH		36.9522369663
988PhosphorylationSAKSLVNYTATILDL
HHHHHHHHHHHHHHC		7.1219779198
1008PhosphorylationRHHRIGGTHSGLTPQ
HHCCCCCCCCCCCCC		13.9922369663
1010PhosphorylationHRIGGTHSGLTPQSS
CCCCCCCCCCCCCHH		35.0222369663
1013PhosphorylationGGTHSGLTPQSSISS
CCCCCCCCCCHHCCH		23.8622369663
1016PhosphorylationHSGLTPQSSISSDKA
CCCCCCCHHCCHHHH		30.7322369663
1017PhosphorylationSGLTPQSSISSDKAR
CCCCCCHHCCHHHHH		22.6522369663
1019PhosphorylationLTPQSSISSDKARHL
CCCCHHCCHHHHHHH		34.1422369663
1020PhosphorylationTPQSSISSDKARHLM
CCCHHCCHHHHHHHH		41.2722369663
1022UbiquitinationQSSISSDKARHLMEE
CHHCCHHHHHHHHHH		49.6317644757
1022AcetylationQSSISSDKARHLMEE
CHHCCHHHHHHHHHH		49.6324489116
1081PhosphorylationIDPMDPMSPLNKDVS
CCCCCCCCCCCCCCC		31.4622369663
1088PhosphorylationSPLNKDVS-------
CCCCCCCC-------		44.6428889911
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 YM54_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YM54_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 YM54_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAM10_YEASTVAM10genetic
27708008
SNF1_YEASTSNF1genetic
27708008
ACBP_YEASTACB1genetic
27708008
PRY2_YEASTPRY2genetic
27708008
SWI6_YEASTSWI6genetic
27708008
RL37A_YEASTRPL37Agenetic
27708008
YPT6_YEASTYPT6genetic
27708008
CDA1_YEASTCDA1genetic
27708008
ORM2_YEASTORM2genetic
27708008
RSF1_YEASTRSF1genetic
27708008
GYP1_YEASTGYP1genetic
27708008
SLY41_YEASTSLY41genetic
27708008
VTC3_YEASTVTC3genetic
27708008
MTHR1_YEASTMET12genetic
27708008
SPEE_YEASTSPE3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YM54_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-299; SER-957; SER-963;THR-964; SER-966; SER-984; SER-1010; THR-1013; SER-1016; SER-1019;SER-1020 AND SER-1081, 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 THR-1008; SER-1010;THR-1013; SER-1016; SER-1017; SER-1019 AND SER-1020, 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-1010, 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 THR-1013 AND SER-1020, ANDMASS SPECTROMETRY.

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