STE12_YEAST - dbPTM
STE12_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STE12_YEAST
UniProt AC P13574
Protein Name Protein STE12
Gene Name STE12
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 688
Subcellular Localization Nucleus.
Protein Description Binds to the DNA sequence mediating pheromone induction (called the pheromone response element = PRE) which is found in the upstream control region of several a-, alpha- and haploid-specific genes. Involved in mating of haploids and in pseudohyphae formation in diploids..
Protein Sequence MKVQITNSRTEEILKVQANNENDEVSKATPGEVEESLRLIGDLKFFLATAPVNWQENQIIRRYYLNSGQGFVSCVFWNNLYYITGTDIVKCCLYRMQKFGREVVQKKKFEEGIFSDLRNLKCGIDATLEQPKSEFLSFLFRNMCLKTQKKQKVFFWFSVAHDKLFADALERDLKRESLNQPSTTKPVNEPALSFSYDSSSDKPLYDQLLQHLDSRRPSSTTKSDNSPPKLESENFKDNELVTVTNQPLLGVGLMDDDAPESPSQINDFIPQKLIIEPNTLELNGLTEETPHDLPKNTAKGRDEEDFPLDYFPVSVEYPTEENAFDPFPPQAFTPAAPSMPISYDNVNERDSMPVNSLLNRYPYQLSVAPTFPVPPSSSRQHFMTNRDFYSSNNNKEKLVSPSDPTSYMKYDEPVMDFDESRPNENCTNAKSHNSGQQTKQHQLYSNNFQQSYPNGMVPGYYPKMPYNPMGGDPLLDQAFYGADDFFFPPEGCDNNMLYPQTATSWNVLPPQAMQPAPTYVGRPYTPNYRSTPGSAMFPYMQSSNSMQWNTAVSPYSSRAPSTTAKNYPPSTFYSQNINQYPRRRTVGMKSSQGNVPTGNKQSVGKSAKISKPLHIKTSAYQKQYKINLETKARPSAGDEDSAHPDKNKEISMPTPDSNTLVVQSEEGGAHSLEVDTNRRSDKNLPDAT
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
6Phosphorylation--MKVQITNSRTEEI
--CCEEECCCCCHHH		15.2824961812
8PhosphorylationMKVQITNSRTEEILK
CCEEECCCCCHHHHE		31.7421551504
10PhosphorylationVQITNSRTEEILKVQ
EEECCCCCHHHHEEE		37.4824961812
26PhosphorylationNNENDEVSKATPGEV
CCCCCCHHHCCCCHH		17.9628889911
29PhosphorylationNDEVSKATPGEVEES
CCCHHHCCCCHHHHH		35.2517330950
36PhosphorylationTPGEVEESLRLIGDL
CCCHHHHHHHHHHCE		12.8021440633
174SumoylationDALERDLKRESLNQP
HHHHHHHHHHHCCCC		59.41-
214PhosphorylationQLLQHLDSRRPSSTT
HHHHHHHHCCCCCCC		36.2328889911
218PhosphorylationHLDSRRPSSTTKSDN
HHHHCCCCCCCCCCC		38.2117287358
219PhosphorylationLDSRRPSSTTKSDNS
HHHCCCCCCCCCCCC		42.6621551504
223PhosphorylationRPSSTTKSDNSPPKL
CCCCCCCCCCCCCCC		39.6722369663
226PhosphorylationSTTKSDNSPPKLESE
CCCCCCCCCCCCCCC		47.7922369663
232PhosphorylationNSPPKLESENFKDNE
CCCCCCCCCCCCCCC		48.5619823750
261PhosphorylationMDDDAPESPSQINDF
CCCCCCCCHHHHHHC		28.8828889911
263PhosphorylationDDAPESPSQINDFIP
CCCCCCHHHHHHCCC		53.6321440633
279PhosphorylationKLIIEPNTLELNGLT
CEEECCCEEEECCCC		32.1222369663
286PhosphorylationTLELNGLTEETPHDL
EEEECCCCCCCCCCC		32.9222369663
289PhosphorylationLNGLTEETPHDLPKN
ECCCCCCCCCCCCCC		21.4922369663
376PhosphorylationPTFPVPPSSSRQHFM
CCCCCCCCCCCHHCC		34.5728889911
377PhosphorylationTFPVPPSSSRQHFMT
CCCCCCCCCCHHCCC		35.0028889911
378PhosphorylationFPVPPSSSRQHFMTN
CCCCCCCCCHHCCCC		40.0528889911
400PhosphorylationNNKEKLVSPSDPTSY
CCCCCCCCCCCCCCC		29.1722369663
402PhosphorylationKEKLVSPSDPTSYMK
CCCCCCCCCCCCCCC		49.0322890988
405PhosphorylationLVSPSDPTSYMKYDE
CCCCCCCCCCCCCCC		37.1622890988
406PhosphorylationVSPSDPTSYMKYDEP
CCCCCCCCCCCCCCC		28.7222890988
407PhosphorylationSPSDPTSYMKYDEPV
CCCCCCCCCCCCCCC		10.4922890988
408OxidationPSDPTSYMKYDEPVM
CCCCCCCCCCCCCCC		3.0415665377
409SumoylationSDPTSYMKYDEPVMD
CCCCCCCCCCCCCCC		41.12-
410PhosphorylationDPTSYMKYDEPVMDF
CCCCCCCCCCCCCCC		14.7121440633
451PhosphorylationYSNNFQQSYPNGMVP
HCCCCHHHCCCCCCC		31.6028889911
525PhosphorylationTYVGRPYTPNYRSTP
CCCCCCCCCCCCCCC		14.0328889911
542PhosphorylationAMFPYMQSSNSMQWN
CCCCCCCCCCCCEEE		18.2419779198
553PhosphorylationMQWNTAVSPYSSRAP
CEEEEECCCCCCCCC		18.6927017623
565AcetylationRAPSTTAKNYPPSTF
CCCCCCCCCCCCCHH		55.7224489116
567PhosphorylationPSTTAKNYPPSTFYS
CCCCCCCCCCCHHCC		18.8027017623
570PhosphorylationTAKNYPPSTFYSQNI
CCCCCCCCHHCCCCC		27.0127017623
574PhosphorylationYPPSTFYSQNINQYP
CCCCHHCCCCCCCCC		16.7424961812
580PhosphorylationYSQNINQYPRRRTVG
CCCCCCCCCCCCCCC		8.3324961812
585PhosphorylationNQYPRRRTVGMKSSQ
CCCCCCCCCCCCCCC		21.4324961812
589AcetylationRRRTVGMKSSQGNVP
CCCCCCCCCCCCCCC		40.8125381059
590PhosphorylationRRTVGMKSSQGNVPT
CCCCCCCCCCCCCCC		20.9928889911
591PhosphorylationRTVGMKSSQGNVPTG
CCCCCCCCCCCCCCC		36.2728889911
597PhosphorylationSSQGNVPTGNKQSVG
CCCCCCCCCCCCCCC		49.4528889911
602PhosphorylationVPTGNKQSVGKSAKI
CCCCCCCCCCCCCEE		34.1523749301
635PhosphorylationLETKARPSAGDEDSA
CCCCCCCCCCCCCCC		39.0528132839
641PhosphorylationPSAGDEDSAHPDKNK
CCCCCCCCCCCCCCC		26.8228132839
651PhosphorylationPDKNKEISMPTPDSN
CCCCCCCCCCCCCCC		21.5719779198
654PhosphorylationNKEISMPTPDSNTLV
CCCCCCCCCCCCEEE		30.9628889911
657PhosphorylationISMPTPDSNTLVVQS
CCCCCCCCCEEEEEC		32.6828889911
659PhosphorylationMPTPDSNTLVVQSEE
CCCCCCCEEEEECCC		25.5328889911
664PhosphorylationSNTLVVQSEEGGAHS
CCEEEEECCCCCEEE		26.4628889911
671PhosphorylationSEEGGAHSLEVDTNR
CCCCCEEEEEEECCC		26.2019779198
680PhosphorylationEVDTNRRSDKNLPDA
EEECCCCCCCCCCCC		50.1030377154
682AcetylationDTNRRSDKNLPDAT-
ECCCCCCCCCCCCC-		62.7224489116
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 STE12_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STE12_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 STE12_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DIG2_YEASTDIG2physical
10688190
IMB3_YEASTPSE1physical
11909949
TEC1_YEASTTEC1physical
9036858
KSS1_YEASTKSS1physical
14734536
DIG1_YEASTDIG1physical
10825185
DIG2_YEASTDIG2physical
10825185
KSS1_YEASTKSS1physical
9744865
DIG1_YEASTDIG1physical
9343403
DIG2_YEASTDIG2physical
9343403
DIG2_YEASTDIG2physical
12590263
DIG1_YEASTDIG1physical
12590263
EF1A_YEASTTEF2physical
12590263
METK1_YEASTSAM1physical
12590263
RL23A_YEASTRPL23Aphysical
12590263
RL23B_YEASTRPL23Aphysical
12590263
RS3A1_YEASTRPS1Aphysical
12590263
RS3A2_YEASTRPS1Bphysical
12590263
METK2_YEASTSAM2physical
12590263
RL1A_YEASTRPL1Bphysical
12590263
RL1B_YEASTRPL1Bphysical
12590263
SCW4_YEASTSCW4physical
12590263
MAS5_YEASTYDJ1physical
12590263
VATB_YEASTVMA2physical
12590263
TEC1_YEASTTEC1physical
9234690
DIG2_YEASTDIG2physical
9094309
DIG1_YEASTDIG1physical
9094309
FLO8_YEASTFLO8physical
15485921
MSS11_YEASTMSS11physical
15485921
FAR1_YEASTFAR1genetic
8649392
FLO11_YEASTFLO11genetic
9436998
FLO8_YEASTFLO8genetic
10064592
OCH1_YEASTOCH1genetic
10535982
KAPR_YEASTBCY1genetic
10373537
RAS2_YEASTRAS2genetic
9055077
STE11_YEASTSTE11genetic
9055077
STE12_YEASTSTE12genetic
9055077
ISW1_YEASTISW1physical
16554755
DIG1_YEASTDIG1physical
16554755
DIG1_YEASTDIG1physical
16782869
DIG2_YEASTDIG2physical
16782869
TEC1_YEASTTEC1physical
16782869
ASH1_YEASTASH1genetic
9566907
PHD1_YEASTPHD1genetic
9566907
FLO8_YEASTFLO8genetic
15466424
MSS11_YEASTMSS11genetic
15466424
IRA1_YEASTIRA1genetic
10064592
RPA49_YEASTRPA49physical
18467557
OSH3_YEASTOSH3genetic
12054531
DIG1_YEASTDIG1physical
20489023
DIG2_YEASTDIG2physical
20489023
TEC1_YEASTTEC1physical
20489023
SLT2_YEASTSLT2physical
20489023
TEC1_YEASTTEC1physical
20584076
SFL1_YEASTSFL1genetic
20421603
KAPC_YEASTTPK3genetic
20421603
PHD1_YEASTPHD1genetic
22124158
SPO14_YEASTSPO14genetic
12702348
IMB3_YEASTPSE1physical
23541588
MSA1_YEASTMSA1physical
24732795
MSA2_YEASTMSA2physical
24732795
UPC2_YEASTUPC2genetic
26448198
PP2B1_YEASTCNA1physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STE12_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 THR-29; SER-223; SER-226;SER-261; THR-289 AND SER-400, 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-226; THR-289 ANDSER-400, 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-218 AND SER-226, 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 THR-29; SER-226 AND SER-400,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-400, AND MASSSPECTROMETRY.

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