STB3_YEAST - dbPTM
STB3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STB3_YEAST
UniProt AC Q12427
Protein Name Protein STB3
Gene Name STB3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 513
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MSENQKEVSPPQAISVKSEASSSIFSKPISTSSPAGLAAAQRVTPGKLSTLLLEMGPLAIRHITQTLCLDIPCFKDLSSSKQRRLIMSAMESGDKEKSVVFEKIGWGQWSAKRVDPANFDKELEATNFANAKVKDLISQESQRRKSNNSNSNSGGKVEMPMKVEHNITNIDGATTPPTAVASTTIPVNIKRSKSPLAAANVVYIDENALASEDEDEEFDEDDHHLHYQNKSRNSSNNFGKSSNGDPYSFGRRRSQVVFADSTPENIEHEIIAQKIRPLLRNRRRSSIKPHTPFISKLNTHQDSSYLSPNTTSTTTPSNNNSNSNQAKIDLEKLTATSEPTSRRASRLSVSKESSIRSTLFPNKNYLIVTTNPNSKATSVSTSPKLEEQMNVSSNPIVLSDKEKHRVASQHLNGESSPQLVPHSHHQPHSDTDEEDWESIGAASLRNNSLAPNIDSVASSTNGVVSPKPTNPSFTNSQNGDIEPPLQHDQQKHEQQPRNGEDNSAAFLLMSLKS
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
9PhosphorylationSENQKEVSPPQAISV
CCCCCCCCCCCCEEE		31.7722369663
18PhosphorylationPQAISVKSEASSSIF
CCCEEECCCCCCHHC		35.9229688323
21PhosphorylationISVKSEASSSIFSKP
EEECCCCCCHHCCCC		22.1429688323
22PhosphorylationSVKSEASSSIFSKPI
EECCCCCCHHCCCCC		34.2029688323
23PhosphorylationVKSEASSSIFSKPIS
ECCCCCCHHCCCCCC		25.7629688323
30PhosphorylationSIFSKPISTSSPAGL
HHCCCCCCCCCHHHH		30.6622369663
31PhosphorylationIFSKPISTSSPAGLA
HCCCCCCCCCHHHHH		33.6622369663
32PhosphorylationFSKPISTSSPAGLAA
CCCCCCCCCHHHHHH		27.7728132839
33PhosphorylationSKPISTSSPAGLAAA
CCCCCCCCHHHHHHH		20.8922369663
138PhosphorylationAKVKDLISQESQRRK
HHHHHHHCHHHHHHH		34.8819823750
141PhosphorylationKDLISQESQRRKSNN
HHHHCHHHHHHHHCC		22.7328889911
146PhosphorylationQESQRRKSNNSNSNS
HHHHHHHHCCCCCCC		39.1622369663
149PhosphorylationQRRKSNNSNSNSGGK
HHHHHCCCCCCCCCC		45.9822369663
151PhosphorylationRKSNNSNSNSGGKVE
HHHCCCCCCCCCCEE		31.9921440633
153PhosphorylationSNNSNSNSGGKVEMP
HCCCCCCCCCCEECC		49.0620377248
168PhosphorylationMKVEHNITNIDGATT
EEEEECEECCCCCCC		31.2922369663
174PhosphorylationITNIDGATTPPTAVA
EECCCCCCCCCCCCE		45.4222369663
175PhosphorylationTNIDGATTPPTAVAS
ECCCCCCCCCCCCEE		27.0822369663
178PhosphorylationDGATTPPTAVASTTI
CCCCCCCCCCEECEE		34.6622369663
182PhosphorylationTPPTAVASTTIPVNI
CCCCCCEECEECCEE		21.3422369663
183PhosphorylationPPTAVASTTIPVNIK
CCCCCEECEECCEEE		21.0022369663
184PhosphorylationPTAVASTTIPVNIKR
CCCCEECEECCEEEC		22.3122369663
211PhosphorylationIDENALASEDEDEEF
ECCCCCCCCCCCCCC		46.5621440633
231PhosphorylationHLHYQNKSRNSSNNF
CCCCCCCCCCCCCCC		44.2224909858
234PhosphorylationYQNKSRNSSNNFGKS
CCCCCCCCCCCCCCC		33.0824909858
235PhosphorylationQNKSRNSSNNFGKSS
CCCCCCCCCCCCCCC		39.0619823750
248PhosphorylationSSNGDPYSFGRRRSQ
CCCCCCCCCCCCCCE		26.9821551504
254PhosphorylationYSFGRRRSQVVFADS
CCCCCCCCEEEECCC		26.0522369663
261PhosphorylationSQVVFADSTPENIEH
CEEEECCCCCCCHHH		42.2922369663
262PhosphorylationQVVFADSTPENIEHE
EEEECCCCCCCHHHH		34.8622369663
285PhosphorylationLLRNRRRSSIKPHTP
HHHCCCHHCCCCCCC		34.3024930733
286PhosphorylationLRNRRRSSIKPHTPF
HHCCCHHCCCCCCCC		32.5922369663
291PhosphorylationRSSIKPHTPFISKLN
HHCCCCCCCCHHHCC		28.5528132839
295PhosphorylationKPHTPFISKLNTHQD
CCCCCCHHHCCCCCC		31.3122369663
303PhosphorylationKLNTHQDSSYLSPNT
HCCCCCCCCCCCCCC		17.8227017623
307PhosphorylationHQDSSYLSPNTTSTT
CCCCCCCCCCCCCCC		14.1023749301
315PhosphorylationPNTTSTTTPSNNNSN
CCCCCCCCCCCCCCC		25.4721440633
334PhosphorylationKIDLEKLTATSEPTS
EEEHHHHHCCCCCCC		38.6722890988
336PhosphorylationDLEKLTATSEPTSRR
EHHHHHCCCCCCCHH		28.5222890988
337PhosphorylationLEKLTATSEPTSRRA
HHHHHCCCCCCCHHH		38.8322369663
340PhosphorylationLTATSEPTSRRASRL
HHCCCCCCCHHHHHC		30.7122369663
341PhosphorylationTATSEPTSRRASRLS
HCCCCCCCHHHHHCC		30.4022369663
345PhosphorylationEPTSRRASRLSVSKE
CCCCHHHHHCCCCCC		31.7628889911
348PhosphorylationSRRASRLSVSKESSI
CHHHHHCCCCCCCCC		24.2020377248
350PhosphorylationRASRLSVSKESSIRS
HHHHCCCCCCCCCCC		27.5921440633
369PhosphorylationNKNYLIVTTNPNSKA
CCCEEEEECCCCCCC		17.5428132839
370PhosphorylationKNYLIVTTNPNSKAT
CCEEEEECCCCCCCC		37.4722369663
374PhosphorylationIVTTNPNSKATSVST
EEECCCCCCCCCCCC		25.5622369663
377PhosphorylationTNPNSKATSVSTSPK
CCCCCCCCCCCCCHH		33.1422369663
378PhosphorylationNPNSKATSVSTSPKL
CCCCCCCCCCCCHHH		20.9422369663
380PhosphorylationNSKATSVSTSPKLEE
CCCCCCCCCCHHHHH		23.9620377248
381PhosphorylationSKATSVSTSPKLEEQ
CCCCCCCCCHHHHHH		47.0620377248
382PhosphorylationKATSVSTSPKLEEQM
CCCCCCCCHHHHHHC		16.7222369663
392PhosphorylationLEEQMNVSSNPIVLS
HHHHCCCCCCCEECC		21.2822369663
393PhosphorylationEEQMNVSSNPIVLSD
HHHCCCCCCCEECCH		42.2022369663
399PhosphorylationSSNPIVLSDKEKHRV
CCCCEECCHHHHHHH		35.4222369663
401AcetylationNPIVLSDKEKHRVAS
CCEECCHHHHHHHHH		66.3524489116
403AcetylationIVLSDKEKHRVASQH
EECCHHHHHHHHHHH		42.3124489116
408PhosphorylationKEKHRVASQHLNGES
HHHHHHHHHHCCCCC		18.4419779198
415PhosphorylationSQHLNGESSPQLVPH
HHHCCCCCCCCCCCC		49.0321440633
416PhosphorylationQHLNGESSPQLVPHS
HHCCCCCCCCCCCCC		16.6228889911
423PhosphorylationSPQLVPHSHHQPHSD
CCCCCCCCCCCCCCC		19.3228889911
429PhosphorylationHSHHQPHSDTDEEDW
CCCCCCCCCCCHHHH		49.2221440633
431PhosphorylationHHQPHSDTDEEDWES
CCCCCCCCCHHHHHH		48.6121440633
438PhosphorylationTDEEDWESIGAASLR
CCHHHHHHHHHHHHH		23.2819779198
448PhosphorylationAASLRNNSLAPNIDS
HHHHHCCCCCCCCHH		29.4730377154
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 STB3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STB3_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 STB3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRPE_YEASTTRP2physical
16554755
EF3A_YEASTYEF3physical
16554755
HSC82_YEASTHSC82physical
16554755
SCH9_YEASTSCH9genetic
20385783
HOS2_YEASTHOS2genetic
20385783
RPD3_YEASTRPD3genetic
20385783
PP2A2_YEASTPPH22genetic
20385783
SFP1_YEASTSFP1genetic
20385783
SDS3_YEASTSDS3genetic
21730963
SDS3_YEASTSDS3physical
21730963
RNH1_YEASTRNH1genetic
22195970
UTP22_YEASTUTP22genetic
27818142
GPR1_YEASTGPR1genetic
27708008
RXT3_YEASTRXT3genetic
27708008
CDC24_YEASTCDC24genetic
27708008
APC11_YEASTAPC11genetic
27708008
CDC4_YEASTCDC4genetic
27708008
YPT1_YEASTYPT1genetic
27708008
TEL2_YEASTTEL2genetic
27708008
GPI12_YEASTGPI12genetic
27708008
YBY9_YEASTYBR139Wgenetic
27708008
NPL4_YEASTNPL4genetic
27708008
YB70_YEASTYBR220Cgenetic
27708008
RL35A_YEASTRPL35Agenetic
27708008
RL35B_YEASTRPL35Agenetic
27708008
MSH4_YEASTMSH4genetic
27708008
CSK2B_YEASTCKB1genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
SGF73_YEASTSGF73genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
DNM1_YEASTDNM1genetic
27708008
SWI6_YEASTSWI6genetic
27708008
DATI_YEASTDAT1genetic
27708008
MSC1_YEASTMSC1genetic
27708008
SPO1_YEASTSPO1genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
SFL1_YEASTSFL1genetic
27708008
RAD1_YEASTRAD1genetic
27708008
ELP4_YEASTELP4genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STB3_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-9; SER-33; THR-175;SER-235; SER-254; SER-382; SER-415 AND SER-416, 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-234 AND SER-235, ANDMASS 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-254, AND MASSSPECTROMETRY.

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