STE11_YEAST - dbPTM
STE11_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STE11_YEAST
UniProt AC P23561
Protein Name Serine/threonine-protein kinase STE11
Gene Name STE11
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 717
Subcellular Localization
Protein Description Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases..
Protein Sequence MEQTQTAEGTDLLIGDEKTNDLPFVQLFLEEIGCTQYLDSFIQCNLVTEEEIKYLDKDILIALGVNKIGDRLKILRKSKSFQRDKRIEQVNRLKNLMEKVSSLSTATLSMNSELIPEKHCVIFILNDGSAKKVNVNGCFNADSIKKRLIRRLPHELLATNSNGEVTKMVQDYDVFVLDYTKNVLHLLYDVELVTICHANDRVEKNRLIFVSKDQTPSDKAISTSKKLYLRTLSALSQVGPSSSNLLAQNKGISHNNAEGKLRIDNTEKDRIRQIFNQRPPSEFISTNLAGYFPHTDMKRLQKTMRESFRHSARLSIAQRRPLSAESNNIGDILLKHSNAVDMALLQGLDQTRLSSKLDTTKIPKLAHKRPEDNDAISNQLELLSVESGEEEDHDFFGEDSDIVSLPTKIATPKNWLKGACIGSGSFGSVYLGMNAHTGELMAVKQVEIKNNNIGVPTDNNKQANSDENNEQEEQQEKIEDVGAVSHPKTNQNIHRKMVDALQHEMNLLKELHHENIVTYYGASQEGGNLNIFLEYVPGGSVSSMLNNYGPFEESLITNFTRQILIGVAYLHKKNIIHRDIKGANILIDIKGCVKITDFGISKKLSPLNKKQNKRASLQGSVFWMSPEVVKQTATTAKADIWSTGCVVIEMFTGKHPFPDFSQMQAIFKIGTNTTPEIPSWATSEGKNFLRKAFELDYQYRPSALELLQHPWLDAHII
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
4Phosphorylation----MEQTQTAEGTD
----CCCCCCCCCCC
18.0030377154
101PhosphorylationKNLMEKVSSLSTATL
HHHHHHHHHCCHHHH
36.3128889911
105PhosphorylationEKVSSLSTATLSMNS
HHHHHCCHHHHCCCC
29.0228889911
215PhosphorylationIFVSKDQTPSDKAIS
EEECCCCCCCCCCCC
34.5928889911
231PhosphorylationSKKLYLRTLSALSQV
CHHHHHHHHHHHHHH
23.5928889911
233PhosphorylationKLYLRTLSALSQVGP
HHHHHHHHHHHHHCC
26.9330377154
236PhosphorylationLRTLSALSQVGPSSS
HHHHHHHHHHCCCHH
23.6525371407
241PhosphorylationALSQVGPSSSNLLAQ
HHHHHCCCHHHHHHH
40.2320377248
242PhosphorylationLSQVGPSSSNLLAQN
HHHHCCCHHHHHHHC
26.7824961812
243PhosphorylationSQVGPSSSNLLAQNK
HHHCCCHHHHHHHCC
35.5221551504
281PhosphorylationIFNQRPPSEFISTNL
HHHCCCCHHHHCCCC
48.0610837245
285PhosphorylationRPPSEFISTNLAGYF
CCCHHHHCCCCCCCC
19.3010837245
286PhosphorylationPPSEFISTNLAGYFP
CCHHHHCCCCCCCCC
29.4510837245
315PhosphorylationFRHSARLSIAQRRPL
HHHHHHHHHHHHCCC
15.4328889911
323PhosphorylationIAQRRPLSAESNNIG
HHHHCCCCCCCCCHH
32.4517330950
326PhosphorylationRRPLSAESNNIGDIL
HCCCCCCCCCHHHHH
34.5925752575
384PhosphorylationSNQLELLSVESGEEE
HHHHHEEEECCCCCC
36.1421440633
387PhosphorylationLELLSVESGEEEDHD
HHEEEECCCCCCCCC
49.7227214570
423PhosphorylationLKGACIGSGSFGSVY
CCCCEECCCCCCCEE
16.0227017623
425PhosphorylationGACIGSGSFGSVYLG
CCEECCCCCCCEEEE
28.2927017623
428PhosphorylationIGSGSFGSVYLGMNA
ECCCCCCCEEEEEEC
12.9427017623
465PhosphorylationDNNKQANSDENNEQE
CCCCCCCCCCCCHHH
49.6825521595
485PhosphorylationIEDVGAVSHPKTNQN
HHHHHHCCCCCCCCH
33.2721551504
616PhosphorylationKKQNKRASLQGSVFW
HHHCCCHHHCCCEEE
25.8420377248
620PhosphorylationKRASLQGSVFWMSPE
CCHHHCCCEEECCHH
10.9420377248
661PhosphorylationKHPFPDFSQMQAIFK
CCCCCCHHHHHHHHC
31.9321440633

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
281SPhosphorylationKinaseSTE20Q03497
GPS
285SPhosphorylationKinaseSTE20Q03497
GPS
286TPhosphorylationKinaseSTE20Q03497
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STE11_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 STE11_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STE50_YEASTSTE50physical
10688190
CDC37_YEASTCDC37physical
10664467
STE50_YEASTSTE50physical
9742096
STE5_YEASTSTE5physical
8052657
CDC37_YEASTCDC37physical
14742721
HSP73_YEASTSSA3physical
14742721
HSP82_YEASTHSP82physical
14742721
BUD6_YEASTBUD6physical
9632790
KSS1_YEASTKSS1physical
7851759
STE5_YEASTSTE5physical
7851759
STE5_YEASTSTE5physical
9335587
HSP82_YEASTHSP82physical
9802897
STE50_YEASTSTE50physical
14573615
STE11_YEASTSTE11physical
14573615
STE5_YEASTSTE5physical
10593609
PBS2_YEASTPBS2physical
15200959
STE11_YEASTSTE11physical
7851759
STE11_YEASTSTE11physical
15327964
STE50_YEASTSTE50physical
15327964
STE7_YEASTSTE7physical
15456892
STE11_YEASTSTE11physical
15544813
STE11_YEASTSTE11physical
15689513
STE50_YEASTSTE50physical
15544813
STE50_YEASTSTE50physical
15689513
STE5_YEASTSTE5physical
11370856
STE11_YEASTSTE11physical
11370856
HSC82_YEASTHSC82physical
9802897
PBS2_YEASTPBS2physical
12853477
STE11_YEASTSTE11physical
8052657
STE50_YEASTSTE50physical
10397774
PBS2_YEASTPBS2physical
9180081
STE7_YEASTSTE7physical
8159759
FUS3_YEASTFUS3physical
15713635
FUS3_YEASTFUS3physical
8062390
STE5_YEASTSTE5physical
8062390
CG12_YEASTCLN2genetic
9148934
HLR1_YEASTHLR1genetic
11532139
LRE1_YEASTLRE1genetic
11532139
APC10_YEASTDOC1genetic
12724382
OCH1_YEASTOCH1genetic
10535982
STE12_YEASTSTE12genetic
2193847
STE12_YEASTSTE12genetic
9286665
HSP82_YEASTHSP82genetic
9802897
NOT4_YEASTMOT2genetic
8164669
STE50_YEASTSTE50physical
16554755
CSK21_YEASTCKA1physical
16554755
STE50_YEASTSTE50physical
16429126
STE50_YEASTSTE50physical
16337230
PTK2_YEASTPTK2physical
16319894
KCC2_YEASTCMK2physical
16319894
SHO1_YEASTSHO1physical
16778768
STE50_YEASTSTE50physical
11283351
SSK2_YEASTSSK2genetic
16885417
CDC37_YEASTCDC37physical
17573546
STE5_YEASTSTE5physical
17952059
STE11_YEASTSTE11physical
18092817
URE2_YEASTURE2physical
18467557
STE11_YEASTSTE11physical
18431466
STE50_YEASTSTE50physical
18431466
MAS5_YEASTYDJ1physical
18829866
HSP82_YEASTHSP82physical
18829866
HSC82_YEASTHSC82physical
18829866
HSP77_YEASTSSC1physical
18829866
STE11_YEASTSTE11physical
18618697
STE50_YEASTSTE50physical
18618697
STE20_YEASTSTE20genetic
19793923
WSC3_YEASTWSC3genetic
11532139
GPD1_YEASTGPD1genetic
12724381
FPS1_YEASTFPS1genetic
12724381
EBS1_YEASTEBS1physical
20489023
IFH1_YEASTIFH1physical
20489023
PABP_YEASTPAB1physical
20489023
PBP4_YEASTPBP4physical
20489023
STE50_YEASTSTE50physical
20489023
IF4F1_YEASTTIF4631physical
20489023
STE50_YEASTSTE50physical
20826334
STE5_YEASTSTE5physical
21118957
STE11_YEASTSTE11physical
21118957
STE50_YEASTSTE50physical
21118957
GBB_YEASTSTE4genetic
10049917
STE5_YEASTSTE5genetic
10049917
STE7_YEASTSTE7genetic
10049917
STE12_YEASTSTE12genetic
10049917
GPA1_YEASTGPA1genetic
10049917
SST2_YEASTSST2genetic
10049917
STE50_YEASTSTE50genetic
10049917
FUS3_YEASTFUS3genetic
10049917
KSS1_YEASTKSS1genetic
10049917
CG12_YEASTCLN2genetic
10049917
CGS5_YEASTCLB5genetic
10049917
CG13_YEASTCLN3genetic
10049917
MCM1_YEASTMCM1genetic
10049917
SYPM_YEASTAIM10physical
21460040
IF5A2_YEASTANB1physical
21460040
GLRX4_YEASTGRX4physical
21460040
HGH1_YEASTHGH1physical
21460040
RDS2_YEASTRDS2physical
21460040
RIM11_YEASTRIM11physical
21460040
RPAC2_YEASTRPC19physical
21460040
IF4A_YEASTTIF2physical
21460040
YIG1_YEASTYIG1physical
21460040
STE50_YEASTSTE50physical
21863494
STE12_YEASTSTE12genetic
22114773
PBS2_YEASTPBS2genetic
22114773
FUS3_YEASTFUS3genetic
22114773
BNI1_YEASTBNI1genetic
22114773
STE20_YEASTSTE20genetic
22114773
CANB_YEASTCNB1genetic
22114773
CRZ1_YEASTCRZ1genetic
22114773
BCK1_YEASTBCK1genetic
22114773
SLT2_YEASTSLT2genetic
22114773
KCC2_YEASTCMK2genetic
22114773
PTK2_YEASTPTK2genetic
22114773
TAB1_HUMANTAB1genetic
8638164
M3K7_HUMANMAP3K7genetic
8638164
MP2K1_XENLAmap2k1physical
8208535
STE50_YEASTSTE50physical
23658712
STE50_YEASTSTE50physical
8816472
STE11_YEASTSTE11physical
8816472
STE5_YEASTSTE5physical
8816472
STE7_YEASTSTE7physical
8816472
FUS3_YEASTFUS3physical
8816472
BEM4_YEASTBEM4physical
25384973
SSK1_YEASTSSK1genetic
27001830
SSK1_YEASTSSK1genetic
25356552
MKK1_YEASTMKK1physical
26787465
LSM1_YEASTLSM1genetic
26447709
PAT1_YEASTPAT1genetic
26447709

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STE11_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-241; SER-323; SER-326AND SER-387, 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-323, AND MASSSPECTROMETRY.
"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-323, AND MASSSPECTROMETRY.

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