TOS4_YEAST - dbPTM
TOS4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOS4_YEAST
UniProt AC Q06266
Protein Name Protein TOS4
Gene Name TOS4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 489
Subcellular Localization Nucleus .
Protein Description Binds to the promoters of genes with functions important for the G1/S (start) transition; primarily genes involved in pheromone response, polarized growth and transcription..
Protein Sequence MSSQFPSSPYRTVDPYSPPNYKQQPNCPSSNYEKAGKTASESIGNFGKGDYPTPFPSSSIGRVSSPVRSNKVDAIPSSPAFPGQLAETSPKFSSKLSSPSRHTRVINAELDPSKISTITVGRNSSQCDVALCKNKFISRVHASITYLPQTNEVKIHCFSMNGLIVTYRKQFDCYQLKDTMNNNNRAYRLVPRFSNEKCVKEIQDEGGFINFTLEEGDTVYMTYYKGIMLDFRQVLLRISLKEKNSSSEPLRFEKKAEFESESETKHMGSIRKHPLIFTDTSMDRPKKILKDSNKISIGSDSGVAERMLNHFLNSKSSPLSSVSSVDHEEQTLRQDSLSSDKNPMTMKKPKLNKRVLPSKPKKSVKENLDELSRRNIDVMHLQHILTNHLAFANVQQTPLFQLQQVNSQISELSRDELRSILSDAKCVGVIYRHGKDAAGKPLDEEYFYDLENDDDYERRNLVSSLKGGRTGLRSCRRTHKQYFWKKPAK
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
7Phosphorylation-MSSQFPSSPYRTVD
-CCCCCCCCCCCCCC		45.2827017623
8PhosphorylationMSSQFPSSPYRTVDP
CCCCCCCCCCCCCCC		26.6228132839
17PhosphorylationYRTVDPYSPPNYKQQ
CCCCCCCCCCCCCCC		38.9925752575
21PhosphorylationDPYSPPNYKQQPNCP
CCCCCCCCCCCCCCC		18.8927017623
22UbiquitinationPYSPPNYKQQPNCPS
CCCCCCCCCCCCCCC		49.4423749301
34UbiquitinationCPSSNYEKAGKTASE
CCCCCHHHCCCCHHH		52.6723749301
37UbiquitinationSNYEKAGKTASESIG
CCHHHCCCCHHHHHC		45.8623749301
40PhosphorylationEKAGKTASESIGNFG
HHCCCCHHHHHCCCC		36.7925752575
48AcetylationESIGNFGKGDYPTPF
HHHCCCCCCCCCCCC		44.4624489116
58PhosphorylationYPTPFPSSSIGRVSS
CCCCCCCCCCCCCCC		26.6427017623
59PhosphorylationPTPFPSSSIGRVSSP
CCCCCCCCCCCCCCC		33.1421440633
64PhosphorylationSSSIGRVSSPVRSNK
CCCCCCCCCCCCCCC		27.8023749301
65PhosphorylationSSIGRVSSPVRSNKV
CCCCCCCCCCCCCCC		25.2621440633
69PhosphorylationRVSSPVRSNKVDAIP
CCCCCCCCCCCCCCC		41.0320377248
77PhosphorylationNKVDAIPSSPAFPGQ
CCCCCCCCCCCCCCC		42.7221440633
78PhosphorylationKVDAIPSSPAFPGQL
CCCCCCCCCCCCCCC		18.2017563356
88PhosphorylationFPGQLAETSPKFSSK
CCCCCCCCCCCHHHH		44.7323749301
89PhosphorylationPGQLAETSPKFSSKL
CCCCCCCCCCHHHHC		20.0025752575
93PhosphorylationAETSPKFSSKLSSPS
CCCCCCHHHHCCCCC		32.4628889911
94PhosphorylationETSPKFSSKLSSPSR
CCCCCHHHHCCCCCC		40.5223749301
97PhosphorylationPKFSSKLSSPSRHTR
CCHHHHCCCCCCCCE		43.8917287358
98PhosphorylationKFSSKLSSPSRHTRV
CHHHHCCCCCCCCEE		37.0120377248
100PhosphorylationSSKLSSPSRHTRVIN
HHHCCCCCCCCEEEE		38.3517287358
103PhosphorylationLSSPSRHTRVINAEL
CCCCCCCCEEEECCC		26.0624961812
114UbiquitinationNAELDPSKISTITVG
ECCCCHHHCCEEEEC		46.1717644757
150PhosphorylationSITYLPQTNEVKIHC
EEEECCCCCEEEEEE		31.2628889911
154UbiquitinationLPQTNEVKIHCFSMN
CCCCCEEEEEEEEEC		22.1317644757
197UbiquitinationVPRFSNEKCVKEIQD
ECCCCCHHHHHHHCC		48.8823749301
247PhosphorylationLKEKNSSSEPLRFEK
HCCCCCCCCCCCCEE		42.9528889911
260PhosphorylationEKKAEFESESETKHM
EEHHHHCCCCCCCCC		52.3127017623
264PhosphorylationEFESESETKHMGSIR
HHCCCCCCCCCCCCC		35.2127017623
269PhosphorylationSETKHMGSIRKHPLI
CCCCCCCCCCCCCEE		16.2027017623
272UbiquitinationKHMGSIRKHPLIFTD
CCCCCCCCCCEEEEC		48.1517644757
278PhosphorylationRKHPLIFTDTSMDRP
CCCCEEEECCCCCCC		31.2321551504
286UbiquitinationDTSMDRPKKILKDSN
CCCCCCCHHHHHCCC		54.0317644757
287UbiquitinationTSMDRPKKILKDSNK
CCCCCCHHHHHCCCC		56.8217644757
316PhosphorylationNHFLNSKSSPLSSVS
HHHHHCCCCCCCCCC		36.6927017623
317PhosphorylationHFLNSKSSPLSSVSS
HHHHCCCCCCCCCCC		33.3321551504
336PhosphorylationEQTLRQDSLSSDKNP
HHHHHHHHCCCCCCC		23.0821551504
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 TOS4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOS4_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 TOS4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BEM1_YEASTBEM1genetic
19269370
MNN10_YEASTMNN10genetic
19269370
BUB1_YEASTBUB1genetic
19269370
STE20_YEASTSTE20genetic
19269370
ATG17_YEASTATG17genetic
19269370
BUB1_YEASTBUB1genetic
21127252
PP2C1_YEASTPTC1genetic
21127252
CHA4_YEASTCHA4genetic
21127252
RTG3_YEASTRTG3genetic
21127252
UPC2_YEASTUPC2genetic
21127252
BEM1_YEASTBEM1genetic
21987634
VPS52_YEASTVPS52genetic
21987634
AIM44_YEASTAIM44genetic
21987634
HST1_YEASTHST1genetic
22333912
RPD3_YEASTRPD3genetic
22333912
SWI5_YEASTSWI5genetic
27708008
UBP3_YEASTUBP3genetic
27708008
VPS53_YEASTVPS53genetic
27708008
GSH1_YEASTGSH1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
COXM1_YEASTCMC1genetic
27708008
PET8_YEASTPET8genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
AIM44_YEASTAIM44genetic
27708008
MSS18_YEASTMSS18genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOS4_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-17; SER-40; SER-77;SER-78; SER-94; SER-97 AND SER-98, 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-78; SER-97 AND SER-98,AND MASS 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-97; SER-98 AND SER-100,AND MASS SPECTROMETRY.

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