EFR3_YEAST - dbPTM
EFR3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFR3_YEAST
UniProt AC Q03653
Protein Name Protein EFR3
Gene Name EFR3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 782
Subcellular Localization
Protein Description
Protein Sequence MQLSMRMMFTPKHQKLVNQCYPTGRTTDKKPKSSETSYLLYYVNSRRSKLEKVSTYLIKRSTSDLNHRRIGNIAVTLDLMNKIVLHCKENLNVFVKDFLYIMNKVLSNNNFNNDVSVVELIELAFSSICQNLDDVLCNGDMEFVQLYQNFVDLFFKIVTERIHNDDMLLKCCIDISNTNSVSSNPQLNHFVSKSVAYTISKFQERNPKFKTLSLEAALESNLGKRLSRTQTRTIGLDKAAEDNHDLSVKALQSYFNTTETDKLNLSIRTLLRCLQSTPNKELLEFVCNGIPVQLRYIVILLLVRQLSDKDKNVNPIVSLKLMSSLLVSDVSIVGLSVLDIMRKLLNFQLKNATNKEVVAQSCITMTDLNHKTYYAEQTSDMLYELLLKLKSDTVKDVEKNAVVEDIDFLVEHITQPSISLELFIDLAHYMKNHIICLFNIVETEVPSSILFSKLYSLLRELDSHGVQKEMMEEIFDKYGKMALLSGLNYFLENVSEPEYTYYSYHLQAANFLKLNDYKSQTEYKMQTRTLFTKEDLLSYYSDTGSNKYSKKGAQILLSRDNQISTSDLLSDSQVRTTPLEYKNVPNAIFSNGKAVYDNNDFAAKQNKFDNSIDDNIEEANDTVISDANAKGSIYRFVAEDARSWKTMRATAPKVSDLKKTMNEKNIPNNMKRDGSFRGSQSVKSRVTNITFLLNELKTFSDDANKIKDPDEENIVGLDKIDVARSNSLRLAPISSLSDRSSIGNRKSFLQKTATGENQNDDFKDANEDLHSLSSRGKIFSST
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----MQLSMRMMFTP
----CCCCCCCCCCH		6.3530377154
10PhosphorylationLSMRMMFTPKHQKLV
CCCCCCCCHHHHHHH		17.3330377154
12AcetylationMRMMFTPKHQKLVNQ
CCCCCCHHHHHHHHH		56.4625381059
176PhosphorylationLKCCIDISNTNSVSS
HHHEEECCCCCCCCC		33.5819823750
178PhosphorylationCCIDISNTNSVSSNP
HEEECCCCCCCCCCH		23.2919823750
180PhosphorylationIDISNTNSVSSNPQL
EECCCCCCCCCCHHH		22.7219823750
182PhosphorylationISNTNSVSSNPQLNH
CCCCCCCCCCHHHHH		24.9919823750
183PhosphorylationSNTNSVSSNPQLNHF
CCCCCCCCCHHHHHH		50.8319823750
192PhosphorylationPQLNHFVSKSVAYTI
HHHHHHHHHHHHHHH		20.4719823750
211PhosphorylationERNPKFKTLSLEAAL
HHCCCCCCCCHHHHH		25.3927017623
213PhosphorylationNPKFKTLSLEAALES
CCCCCCCCHHHHHHC		29.4227017623
227PhosphorylationSNLGKRLSRTQTRTI
CCHHHHCCCCCCCCC		37.0017287358
229PhosphorylationLGKRLSRTQTRTIGL
HHHHCCCCCCCCCCC		30.8020377248
231PhosphorylationKRLSRTQTRTIGLDK
HHCCCCCCCCCCCHH		29.2120377248
233PhosphorylationLSRTQTRTIGLDKAA
CCCCCCCCCCCHHHH		23.8419823750
238UbiquitinationTRTIGLDKAAEDNHD
CCCCCCHHHHHCCCC		55.3123749301
372PhosphorylationMTDLNHKTYYAEQTS
EECCCCCCEEHHHHH		17.7627017623
373PhosphorylationTDLNHKTYYAEQTSD
ECCCCCCEEHHHHHH		12.8927017623
374PhosphorylationDLNHKTYYAEQTSDM
CCCCCCEEHHHHHHH		14.6427017623
378PhosphorylationKTYYAEQTSDMLYEL
CCEEHHHHHHHHHHH		20.4227017623
383PhosphorylationEQTSDMLYELLLKLK
HHHHHHHHHHHHHHC		9.6327017623
547AcetylationYSDTGSNKYSKKGAQ
HCCCCCCCCCCCCCE		53.2324489116
558PhosphorylationKGAQILLSRDNQIST
CCCEEEECCCCCCCH		33.8621440633
564PhosphorylationLSRDNQISTSDLLSD
ECCCCCCCHHHHCCC		16.4622369663
565PhosphorylationSRDNQISTSDLLSDS
CCCCCCCHHHHCCCC		28.0822369663
566PhosphorylationRDNQISTSDLLSDSQ
CCCCCCHHHHCCCCC		21.3322369663
570PhosphorylationISTSDLLSDSQVRTT
CCHHHHCCCCCCCCC		42.3819823750
572PhosphorylationTSDLLSDSQVRTTPL
HHHHCCCCCCCCCCC		27.4829136822
576PhosphorylationLSDSQVRTTPLEYKN
CCCCCCCCCCCCCCC		33.6320377248
577PhosphorylationSDSQVRTTPLEYKNV
CCCCCCCCCCCCCCC		18.4728889911
581PhosphorylationVRTTPLEYKNVPNAI
CCCCCCCCCCCCCEE		18.6219823750
582UbiquitinationRTTPLEYKNVPNAIF
CCCCCCCCCCCCEEC		41.9324961812
590PhosphorylationNVPNAIFSNGKAVYD
CCCCEECCCCEEEEC		38.2621440633
593UbiquitinationNAIFSNGKAVYDNND
CEECCCCEEEECCCC		38.6423749301
604UbiquitinationDNNDFAAKQNKFDNS
CCCCHHHHHCCCCCC		51.4823749301
607UbiquitinationDFAAKQNKFDNSIDD
CHHHHHCCCCCCCCC		52.1523749301
611PhosphorylationKQNKFDNSIDDNIEE
HHCCCCCCCCCCHHH		29.2820377248
622PhosphorylationNIEEANDTVISDANA
CHHHHHHCEEECCCC		21.3923749301
625PhosphorylationEANDTVISDANAKGS
HHHHCEEECCCCCCC		26.7417563356
630UbiquitinationVISDANAKGSIYRFV
EEECCCCCCCEEEHH		53.6623749301
632PhosphorylationSDANAKGSIYRFVAE
ECCCCCCCEEEHHHH		18.7519795423
634PhosphorylationANAKGSIYRFVAEDA
CCCCCCEEEHHHHCH		10.3320377248
643PhosphorylationFVAEDARSWKTMRAT
HHHHCHHCHHHHHHC		34.3522369663
646PhosphorylationEDARSWKTMRATAPK
HCHHCHHHHHHCCCC		12.9623749301
650PhosphorylationSWKTMRATAPKVSDL
CHHHHHHCCCCHHHH		32.8823749301
655PhosphorylationRATAPKVSDLKKTMN
HHCCCCHHHHHHHHC		43.2727017623
660PhosphorylationKVSDLKKTMNEKNIP
CHHHHHHHHCCCCCC		24.5223749301
675PhosphorylationNNMKRDGSFRGSQSV
CCCCCCCCCCCCHHH		18.9622369663
679PhosphorylationRDGSFRGSQSVKSRV
CCCCCCCCHHHHHHH		18.2822890988
681PhosphorylationGSFRGSQSVKSRVTN
CCCCCCHHHHHHHHH		32.9622890988
684PhosphorylationRGSQSVKSRVTNITF
CCCHHHHHHHHHHHH		29.8122890988
687PhosphorylationQSVKSRVTNITFLLN
HHHHHHHHHHHHHHH		21.5717330950
690PhosphorylationKSRVTNITFLLNELK
HHHHHHHHHHHHHHH		15.4217330950
697UbiquitinationTFLLNELKTFSDDAN
HHHHHHHHHCCCCHH		41.1524961812
700PhosphorylationLNELKTFSDDANKIK
HHHHHHCCCCHHHCC		39.5528889911
725PhosphorylationDKIDVARSNSLRLAP
CHHHHHHCCCCCCCC		22.4922369663
727PhosphorylationIDVARSNSLRLAPIS
HHHHHCCCCCCCCCC		19.0022369663
734PhosphorylationSLRLAPISSLSDRSS
CCCCCCCCCCCCCCC		24.9422890988
735PhosphorylationLRLAPISSLSDRSSI
CCCCCCCCCCCCCCC		32.3922369663
737PhosphorylationLAPISSLSDRSSIGN
CCCCCCCCCCCCCCC		32.6922369663
740PhosphorylationISSLSDRSSIGNRKS
CCCCCCCCCCCCCHH		31.1619684113
741PhosphorylationSSLSDRSSIGNRKSF
CCCCCCCCCCCCHHH		35.0925752575
752PhosphorylationRKSFLQKTATGENQN
CHHHHHHHCCCCCCC		19.2521440633
754PhosphorylationSFLQKTATGENQNDD
HHHHHHCCCCCCCCC		50.7021440633
771PhosphorylationDANEDLHSLSSRGKI
HHHHHHHHHHHCCCC		36.9222369663
773PhosphorylationNEDLHSLSSRGKIFS
HHHHHHHHHCCCCCC		22.4725521595
774PhosphorylationEDLHSLSSRGKIFSS
HHHHHHHHCCCCCCC		50.8025521595
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 EFR3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFR3_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 EFR3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YPP1_YEASTYPP1physical
19075114
YPP1_YEASTYPP1physical
24360784
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EFR3_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-564; THR-565; SER-566;SER-570; THR-577; SER-735; SER-737; SER-741; SER-771 AND SER-773, 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-611 AND SER-625, ANDMASS 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-227; THR-231; SER-675;SER-681; SER-771 AND SER-774, 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-643; THR-687; THR-690;SER-735 AND SER-771, 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-564 AND SER-734, ANDMASS SPECTROMETRY.
"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 THR-565, AND MASSSPECTROMETRY.

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