GTS1_YEAST - dbPTM
GTS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GTS1_YEAST
UniProt AC P40956
Protein Name Protein GTS1
Gene Name GTS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 396
Subcellular Localization Nucleus .
Protein Description Appears to modulate the timing of budding to obtain an appropriate cell size independent of the DNA replication cycle. Transcription factor involved in both heat resistance and flocculation..
Protein Sequence MRFRSSSHSLKHVDRELKELINSSENANKCGECGNFYPTWCSVNLGVFLCGRCASVHRKVFGSRDDDAFSNVKSLSMDRWTREDIDELVSLGGNKGNARFWNPKNVPFPFDGDDDKAIVEHYIRDKYILGKFRYDEIKPEDFGSRMDDFDGESDRFDERNRSRSRSRSHSFYKGGHNRSDYGGSRDSFQSSGSRYSRQLAELKDMGFGDTNKNLDALSSAHGNINRAIDYLEKSSSSRNSVSAAATTSTPPLPRRRATTSGPQPAIFDGTNVITPDFTSNSASFVQAKPAVFDGTLQQYYDPATGMIYVDQQQYAMAMQQQQQQQQQLAVAQAQAQAQAQAQAQVQAQAQAQAQAQAQAQQIQMQQLQMQQQQQAPLSFQQMSQGGNLPQGYFYTQ
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
5Phosphorylation---MRFRSSSHSLKH
---CCCCCCCHHHHH		33.2217287358
6Phosphorylation--MRFRSSSHSLKHV
--CCCCCCCHHHHHH		28.0117287358
7Phosphorylation-MRFRSSSHSLKHVD
-CCCCCCCHHHHHHH		20.5224909858
9PhosphorylationRFRSSSHSLKHVDRE
CCCCCCHHHHHHHHH		40.8524961812
18UbiquitinationKHVDRELKELINSSE
HHHHHHHHHHHHCCC		45.8023749301
73UbiquitinationDDAFSNVKSLSMDRW
CCHHHCCHHCCCCCC		50.3524961812
90PhosphorylationEDIDELVSLGGNKGN
HHHHHHHHCCCCCCC		33.6428889911
95UbiquitinationLVSLGGNKGNARFWN
HHHCCCCCCCCCCCC		57.7423749301
116AcetylationPFDGDDDKAIVEHYI
CCCCCCHHHHHHHHH		47.1924489116
153PhosphorylationMDDFDGESDRFDERN
CCCCCCCCHHCCHHH		39.3522369663
168PhosphorylationRSRSRSRSHSFYKGG
HHHHCCCCCCCCCCC		25.4023749301
170PhosphorylationRSRSRSHSFYKGGHN
HHCCCCCCCCCCCCC		31.3625005228
179PhosphorylationYKGGHNRSDYGGSRD
CCCCCCCCCCCCCHH		40.2722369663
181PhosphorylationGGHNRSDYGGSRDSF
CCCCCCCCCCCHHHH		25.3222369663
184PhosphorylationNRSDYGGSRDSFQSS
CCCCCCCCHHHHHCC		28.6622369663
187PhosphorylationDYGGSRDSFQSSGSR
CCCCCHHHHHCCCCH		24.8722369663
190PhosphorylationGSRDSFQSSGSRYSR
CCHHHHHCCCCHHHH		34.3622369663
191PhosphorylationSRDSFQSSGSRYSRQ
CHHHHHCCCCHHHHH		29.9722369663
193PhosphorylationDSFQSSGSRYSRQLA
HHHHCCCCHHHHHHH		29.9622369663
212AcetylationMGFGDTNKNLDALSS
CCCCCCCCCHHHHHH		62.0624489116
218PhosphorylationNKNLDALSSAHGNIN
CCCHHHHHHHCCCHH		27.4822369663
219PhosphorylationKNLDALSSAHGNINR
CCHHHHHHHCCCHHH		25.7422369663
230PhosphorylationNINRAIDYLEKSSSS
CHHHHHHHHHHCCCC		15.6221440633
233UbiquitinationRAIDYLEKSSSSRNS
HHHHHHHHCCCCCCC		53.7123749301
234PhosphorylationAIDYLEKSSSSRNSV
HHHHHHHCCCCCCCC		26.5222369663
235PhosphorylationIDYLEKSSSSRNSVS
HHHHHHCCCCCCCCC		43.3222369663
236PhosphorylationDYLEKSSSSRNSVSA
HHHHHCCCCCCCCCC		40.1722369663
237PhosphorylationYLEKSSSSRNSVSAA
HHHHCCCCCCCCCCH		37.1122369663
240PhosphorylationKSSSSRNSVSAAATT
HCCCCCCCCCCHHCC		19.1522369663
242PhosphorylationSSSRNSVSAAATTST
CCCCCCCCCHHCCCC		16.4122890988
246PhosphorylationNSVSAAATTSTPPLP
CCCCCHHCCCCCCCC		19.2922890988
247PhosphorylationSVSAAATTSTPPLPR
CCCCHHCCCCCCCCC		26.3622890988
248PhosphorylationVSAAATTSTPPLPRR
CCCHHCCCCCCCCCC		34.2622890988
249PhosphorylationSAAATTSTPPLPRRR
CCHHCCCCCCCCCCC		27.1722369663
258PhosphorylationPLPRRRATTSGPQPA
CCCCCCCCCCCCCCC		21.4922369663
259PhosphorylationLPRRRATTSGPQPAI
CCCCCCCCCCCCCCC		30.6022369663
260PhosphorylationPRRRATTSGPQPAIF
CCCCCCCCCCCCCCC		44.0922369663
270PhosphorylationQPAIFDGTNVITPDF
CCCCCCCCCEECCCC		28.3222369663
274PhosphorylationFDGTNVITPDFTSNS
CCCCCEECCCCCCCC		16.7222369663
278PhosphorylationNVITPDFTSNSASFV
CEECCCCCCCCCCHH		34.0922369663
279PhosphorylationVITPDFTSNSASFVQ
EECCCCCCCCCCHHC		28.8729734811
281PhosphorylationTPDFTSNSASFVQAK
CCCCCCCCCCHHCCC		25.6722369663
283PhosphorylationDFTSNSASFVQAKPA
CCCCCCCCHHCCCCE		26.2722369663
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 GTS1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GTS1_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 GTS1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G3P3_YEASTTDH3physical
12135496
MDL1_YEASTMDL1physical
9914482
YCFI_YEASTYCF1physical
9914482
PRP5_YEASTPRP5genetic
8622683
PRP9_YEASTPRP9genetic
8622683
PRP11_YEASTPRP11genetic
8622683
PRP21_YEASTPRP21genetic
8622683
SFI1_YEASTSFI1physical
16911513
YAP6_YEASTYAP6physical
11283351
YHX7_YEASTYHR177Wphysical
11283351
POG1_YEASTPOG1physical
11283351
RT16_YEASTMRPS16physical
11283351
SLA1_YEASTSLA1physical
17449140
PAN1_YEASTPAN1physical
17449140
RV167_YEASTRVS167physical
18719252
RGM1_YEASTRGM1physical
18719252
POG1_YEASTPOG1physical
18719252
NAF1_YEASTNAF1physical
18719252
AP18B_YEASTYAP1802physical
18719252
AP18A_YEASTYAP1801physical
18719252
PBP1_YEASTPBP1physical
18719252
LSB3_YEASTLSB3physical
18719252
DIG1_YEASTDIG1physical
18719252
GTS1_YEASTGTS1physical
19345193
RNT1_YEASTRNT1physical
17534422
CUS1_YEASTCUS1genetic
8622683
SLA1_YEASTSLA1physical
18208507
CLC1_YEASTCLC1physical
18208507
BSP1_YEASTBSP1physical
18208507
PAN1_YEASTPAN1physical
18208507
YSC84_YEASTYSC84physical
18208507
AP18B_YEASTYAP1802physical
18208507
SLA2_YEASTSLA2physical
18208507
SLA1_YEASTSLA1genetic
18208507
PDR3_YEASTPDR3genetic
20959818
HSP71_YEASTSSA1physical
21307595
HSP72_YEASTSSA2physical
21307595
CYC8_YEASTCYC8physical
21512249
SNF1_YEASTSNF1genetic
21127252
VDAC1_YEASTPOR1genetic
21821937
FHP_YEASTYHB1genetic
21821937
UBI4P_YEASTUBI4physical
16007098
SLA1_YEASTSLA1genetic
27708008
BSC2_YEASTBSC2genetic
27708008
MSS11_YEASTMSS11genetic
26711350
SAP30_YEASTSAP30genetic
26711350
MSN1_YEASTMSN1genetic
26711350
SNF5_YEASTSNF5genetic
26711350
FLO8_YEASTFLO8genetic
26711350
4ET_HUMANEIF4ENIF1physical
27107014
HM20A_HUMANHMG20Aphysical
27107014
DVL2_HUMANDVL2physical
27107014
RHXF2_HUMANRHOXF2physical
27107014
RFOX2_HUMANRBFOX2physical
27107014
TFG_HUMANTFGphysical
27107014
DAZP2_HUMANDAZAP2physical
27107014
CA094_HUMANC1orf94physical
27107014
CRX_HUMANCRXphysical
27107014
RBPMS_HUMANRBPMSphysical
27107014
NFYA_HUMANNFYAphysical
27107014
CPSF7_HUMANCPSF7physical
27107014
DMRTB_HUMANDMRTB1physical
27107014
UBC9_HUMANUBE2Iphysical
27107014
ANKH1_HUMANANKHD1physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GTS1_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-90; SER-153; SER-184;SER-187; SER-218; THR-249 AND SER-281, 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-179 AND SER-184, 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-5; SER-6; SER-7 ANDSER-184, AND MASS SPECTROMETRY.
"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-170, AND MASSSPECTROMETRY.

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