SYG1_YEAST - dbPTM
SYG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYG1_YEAST
UniProt AC P40528
Protein Name Protein SYG1
Gene Name SYG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 902
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description May function in G-protein coupled signal transduction..
Protein Sequence MKFADHLTESAIPEWRDKYIDYKVGKKKLRRYKEKLDAEEEQSSSYRSWMPSVSVYQTAFQQREPGKSRSDGDYRSGPAFKKDYSALQREFVADFIEDWLISFQLSKCNEFYLWLLKECDKKFEVLQSQLHYYSLQKNYERDNLNRSSSNVDMSTSLYAAGLAGRSDSRVNSIDSDSRSVMYGSMPCTKEAKKPRLSLLAYCQKVLKDNRLLPSWPKRGFSLLQDLRQDASSRGRETFAFGASFLETMTTTQARNLLSNAIIEYYLYLQLVKSFRDINVTGFRKMVKKFDKTCHTRELTTFMSYARTHYTLFKHADANVQLVAQKMQQITSSQPTPTSELSSAQRDKEPITWLETQITEWFTTALTNSPKDRKHNTHKLKKLTIQYSISEQMVHRNNRSIVQMLVVGLGIGVSMTLITYTLYLGISSEETSFTHKILFPLWGGWYMVLLIAFLFLVNCFIWHRTGINYRFIMLGEIQSKNGTQFFNNDFATSKIPLKLYFLTFFIVPCAVCSMLSFALEKLTPLGFLYIGIVSFLFLCPSGLIPYWDKVVHTRKWLVVTLIRLMMSGFFPVEFGDFFLGDIICSLTYSIADIAMFFCVYSHTPNNLCGSSHSRAMGVLSCLPSYWRFMQCLRRFADSGDWFPHLLNAAKYTLGIAYNATLCAYRLSDRSEQRRTPFIVCATLNSILTSAWDLVMDWSFAHNTTSYNWLLRDDLYLAGKKNWENGSYSFSRKLVYYFAMIWDILIRFEWIVYAIAPQTIQQSAVTSFILALLEVLRRFVWIIFRVENEHVANVHLFRVTGDAPLPYPIAQVGDDSMDSSDLGSKAFSSLNDIPITPSHDNNPHSFAEPMPAYRGTFRRRSSVFENISRSIPWAHATDFQRPTVNTVDDRSPETDSESEVESIM
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
35UbiquitinationKLRRYKEKLDAEEEQ
HHHHHHHHCCHHHHH		47.7323749301
43PhosphorylationLDAEEEQSSSYRSWM
CCHHHHHCHHHHHHC		25.2422369663
44PhosphorylationDAEEEQSSSYRSWMP
CHHHHHCHHHHHHCC		30.9622369663
45PhosphorylationAEEEQSSSYRSWMPS
HHHHHCHHHHHHCCC		29.7922369663
46PhosphorylationEEEQSSSYRSWMPSV
HHHHCHHHHHHCCCC		15.6021440633
82UbiquitinationRSGPAFKKDYSALQR
CCCHHHHCCHHHHHH		56.2823749301
102PhosphorylationFIEDWLISFQLSKCN
HHHHHHHHHHHHCCC		12.5519779198
106PhosphorylationWLISFQLSKCNEFYL
HHHHHHHHCCCHHHH		25.1230377154
147PhosphorylationERDNLNRSSSNVDMS
HHCCCCCCCCCCCHH		36.7222369663
148PhosphorylationRDNLNRSSSNVDMST
HCCCCCCCCCCCHHH		23.7722369663
149PhosphorylationDNLNRSSSNVDMSTS
CCCCCCCCCCCHHHH		41.9622369663
153OxidationRSSSNVDMSTSLYAA
CCCCCCCHHHHHHHH		4.0215665377
154PhosphorylationSSSNVDMSTSLYAAG
CCCCCCHHHHHHHHH		15.4730377154
155PhosphorylationSSNVDMSTSLYAAGL
CCCCCHHHHHHHHHH		19.0030377154
156PhosphorylationSNVDMSTSLYAAGLA
CCCCHHHHHHHHHHC		16.4530377154
166PhosphorylationAAGLAGRSDSRVNSI
HHHHCCCCCCCCCCC		38.7321440633
168PhosphorylationGLAGRSDSRVNSIDS
HHCCCCCCCCCCCCC		39.1023749301
172PhosphorylationRSDSRVNSIDSDSRS
CCCCCCCCCCCCCCH		25.5621440633
175PhosphorylationSRVNSIDSDSRSVMY
CCCCCCCCCCCHHHC		35.5021440633
177PhosphorylationVNSIDSDSRSVMYGS
CCCCCCCCCHHHCCC		30.3322369663
179PhosphorylationSIDSDSRSVMYGSMP
CCCCCCCHHHCCCCC		18.3922369663
182PhosphorylationSDSRSVMYGSMPCTK
CCCCHHHCCCCCCCC		12.1428889911
184PhosphorylationSRSVMYGSMPCTKEA
CCHHHCCCCCCCCCC		11.3219779198
335PhosphorylationQITSSQPTPTSELSS
HHHCCCCCCHHHHCC		31.4019779198
341PhosphorylationPTPTSELSSAQRDKE
CCCHHHHCCCCCCCC		21.4119779198
342PhosphorylationTPTSELSSAQRDKEP
CCHHHHCCCCCCCCC		40.8319779198
351PhosphorylationQRDKEPITWLETQIT
CCCCCCCCCHHHHHH		34.4127017623
362PhosphorylationTQITEWFTTALTNSP
HHHHHHHHHHHHCCC		16.5427017623
363PhosphorylationQITEWFTTALTNSPK
HHHHHHHHHHHCCCC		15.3627017623
366PhosphorylationEWFTTALTNSPKDRK
HHHHHHHHCCCCCCC		31.0527017623
368PhosphorylationFTTALTNSPKDRKHN
HHHHHHCCCCCCCCC		28.2627017623
376PhosphorylationPKDRKHNTHKLKKLT
CCCCCCCHHHHCHHE		21.8028889911
419PhosphorylationVSMTLITYTLYLGIS
HHHHHHHHHHHHCCC		6.4325521595
431PhosphorylationGISSEETSFTHKILF
CCCCCCCCCCCCHHH		31.2825521595
805PhosphorylationTGDAPLPYPIAQVGD
ECCCCCCCCCCCCCC		18.2319779198
814PhosphorylationIAQVGDDSMDSSDLG
CCCCCCCCCCHHHHC		29.2723749301
817PhosphorylationVGDDSMDSSDLGSKA
CCCCCCCHHHHCCHH		19.6723749301
818PhosphorylationGDDSMDSSDLGSKAF
CCCCCCHHHHCCHHH		32.3723749301
822PhosphorylationMDSSDLGSKAFSSLN
CCHHHHCCHHHHCCC		28.2719779198
834PhosphorylationSLNDIPITPSHDNNP
CCCCCCCCCCCCCCC		17.2421440633
859PhosphorylationRGTFRRRSSVFENIS
CCCCCCCHHHHHHHH		29.1017330950
860PhosphorylationGTFRRRSSVFENISR
CCCCCCHHHHHHHHH		29.0717330950
868PhosphorylationVFENISRSIPWAHAT
HHHHHHHCCCCCCCC		26.6428889911
875PhosphorylationSIPWAHATDFQRPTV
CCCCCCCCCCCCCCC		27.7219779198
889PhosphorylationVNTVDDRSPETDSES
CCCCCCCCCCCCCHH		33.8019795423
892PhosphorylationVDDRSPETDSESEVE
CCCCCCCCCCHHHHH		48.4821440633
894PhosphorylationDRSPETDSESEVESI
CCCCCCCCHHHHHHC		50.9021440633
896PhosphorylationSPETDSESEVESIM-
CCCCCCHHHHHHCC-		51.3921440633
900PhosphorylationDSESEVESIM-----
CCHHHHHHCC-----		29.1821440633
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 SYG1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYG1_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 SYG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBB_YEASTSTE4physical
7592711
SYG1_YEASTSYG1physical
18467557
RS8A_YEASTRPS8Agenetic
20093466
RS8B_YEASTRPS8Agenetic
20093466
TPS1_YEASTTPS1genetic
20093466
PP2C1_YEASTPTC1genetic
20093466
SPT3_YEASTSPT3genetic
20093466
ZRT1_YEASTZRT1genetic
20093466
CGR1_YEASTCGR1genetic
20093466
DBF2_YEASTDBF2genetic
20093466
HAL5_YEASTHAL5genetic
20093466
CYP7_YEASTCPR7genetic
20093466
TOR1_YEASTTOR1genetic
20093466
MTAP_YEASTMEU1genetic
20093466
YPT6_YEASTYPT6genetic
20093466
NU188_YEASTNUP188genetic
20093466
SRC1_YEASTSRC1genetic
20093466
AIM34_YEASTAIM34genetic
20093466
MRE11_YEASTMRE11genetic
20093466
MAS5_YEASTYDJ1genetic
20093466
SUR1_YEASTSUR1genetic
20093466
YPK9_YEASTYPK9genetic
22457822
SYG1_YEASTSYG1physical
22615397
SSB1_YEASTSSB1physical
22940862
HSP72_YEASTSSA2physical
22940862
HAL5_YEASTHAL5genetic
22282571
VMA21_YEASTVMA21genetic
27708008
UBX2_YEASTUBX2genetic
27708008
DEP1_YEASTDEP1genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
TPS1_YEASTTPS1genetic
27708008
RV161_YEASTRVS161genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
CGR1_YEASTCGR1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
HAL5_YEASTHAL5genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
RS3A1_YEASTRPS1Agenetic
27708008
ATP18_YEASTATP18genetic
27708008
AIM34_YEASTAIM34genetic
27708008
RIM13_YEASTRIM13genetic
27708008
MRE11_YEASTMRE11genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
IRA2_YEASTIRA2genetic
27708008
SUR1_YEASTSUR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYG1_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-44; SER-149; SER-172;SER-179; SER-859 AND SER-860, 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-859 AND SER-860, 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-149, 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-859 AND SER-860, ANDMASS SPECTROMETRY.

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