SSK1_YEAST - dbPTM
SSK1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSK1_YEAST
UniProt AC Q07084
Protein Name Osmolarity two-component system protein SSK1
Gene Name SSK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 712
Subcellular Localization Cytoplasm .
Protein Description Final receptor of the SLN1-YPD1-SSK1 two-component regulatory system, which controls activity of the HOG1 pathway in response to changes in the osmolarity of the extracellular environment. Under normal osmotic conditions, maintained in a phosphorylated and inactive state by the phosphorelay intermediate protein YPD1. Under conditions of high osmolarity, the histidine kinase SLN1 is no longer active and the unphosphorylated form of SSK1 interacts with and activates SSK2 and SSK22, two MAPKKKs that further stimulate the PBS2-HOG1 MAPKK-MAPK cascade. Unphosphorylated SSK1 is subsequently degraded by the UBC7-dependent ubiquitin-proteasome system to down-regulate the HOG1 pathway after completion of the osmotic adaptation..
Protein Sequence MLNSALLWKVWLRIDNSTDEVNQPIAVQFDEIDTVDDLKSRFFQKLSSTRWREINDNASIAIGLYAPKFDNQADNTSSNNTNDNSCRSKSNGAGSGANLSVNSNTKSSVSPTAGSFGLSKDLAKDRNVLQHPKPTQKRGALYDAFAAVPTVAATTNVDFPPNEAPMLSPQRPYSTSPKQFPATTKSPLLRFASVSPYPKFHSDNQIMASAGLTYVSPHNKNKYTRPLIRKGLNFTTESVNDCTYKIIFEPDELAINIYKELFGTMGSQPASQPLLIFSNVNLRQDVPPLDILNVVDYVPTNEEISQQKTQPTDHGAVGVFHLDDHISPGEQGLKQTIGDKADLKGKDGNSSPQEFKLITDEEQLRRASQELKDEEKDAESPWQAILLLPKGYKGGVDFRNKPVAHTDSSFNNEDTITHSELEVNTGSPSQESGSLNEAGIGITQPMSEVQRRKEDVTPASPILTSSQTPHYSNSLYNAPFAVSSPPDPLPNLFTTTSEKVFPKINVLIVEDNVINQAILGSFLRKHKISYKLAKNGQEAVNIWKEGGLHLIFMDLQLPVLSGIEAAKQIRDFEKQNGIGIQKSLNNSHSNLEKGTSKRFSQAPVIIVALTASNSQMDKRKALLSGCNDYLTKPVNLHWLSKKITEWGCMQALIDFDSWKQGESRMTDSVLVKSPQKPIAPSNPHSFKQATSMTPTHSPVRKNSNLSPTQIEL
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
77PhosphorylationDNQADNTSSNNTNDN
CCCCCCCCCCCCCCC		37.0028889911
88PhosphorylationTNDNSCRSKSNGAGS
CCCCCCCCCCCCCCC		44.7728889911
90PhosphorylationDNSCRSKSNGAGSGA
CCCCCCCCCCCCCCC		41.5722369663
95PhosphorylationSKSNGAGSGANLSVN
CCCCCCCCCCCEEEC		33.9122369663
107PhosphorylationSVNSNTKSSVSPTAG
EECCCCCCCCCCCCC		33.6522369663
108PhosphorylationVNSNTKSSVSPTAGS
ECCCCCCCCCCCCCC		28.3329688323
110PhosphorylationSNTKSSVSPTAGSFG
CCCCCCCCCCCCCCC		20.6222369663
112PhosphorylationTKSSVSPTAGSFGLS
CCCCCCCCCCCCCCC		35.8222369663
115PhosphorylationSVSPTAGSFGLSKDL
CCCCCCCCCCCCHHH		17.4321440633
155PhosphorylationVPTVAATTNVDFPPN
CCEEEEECCCCCCCC		28.6321440633
168PhosphorylationPNEAPMLSPQRPYST
CCCCCCCCCCCCCCC		16.8521440633
173PhosphorylationMLSPQRPYSTSPKQF
CCCCCCCCCCCCCCC		27.1121440633
174PhosphorylationLSPQRPYSTSPKQFP
CCCCCCCCCCCCCCC		25.7021440633
175PhosphorylationSPQRPYSTSPKQFPA
CCCCCCCCCCCCCCC		43.1121440633
176PhosphorylationPQRPYSTSPKQFPAT
CCCCCCCCCCCCCCC		24.9421440633
183PhosphorylationSPKQFPATTKSPLLR
CCCCCCCCCCCCCCC		34.6922369663
184PhosphorylationPKQFPATTKSPLLRF
CCCCCCCCCCCCCCE		31.4721440633
186PhosphorylationQFPATTKSPLLRFAS
CCCCCCCCCCCCEEC		20.7722369663
193PhosphorylationSPLLRFASVSPYPKF
CCCCCEECCCCCCCC		22.0322369663
195PhosphorylationLLRFASVSPYPKFHS
CCCEECCCCCCCCCC		19.0722369663
197PhosphorylationRFASVSPYPKFHSDN
CEECCCCCCCCCCCC		16.1422369663
213PhosphorylationIMASAGLTYVSPHNK
EECCCCCEEECCCCC		22.4324961812
216PhosphorylationSAGLTYVSPHNKNKY
CCCCEEECCCCCCCC		15.2724961812
327PhosphorylationFHLDDHISPGEQGLK
EECCCCCCCCHHHHH		24.3520377248
336PhosphorylationGEQGLKQTIGDKADL
CHHHHHHCCCCHHHH		25.9130377154
350PhosphorylationLKGKDGNSSPQEFKL
HCCCCCCCCHHHHEE		49.2625521595
351PhosphorylationKGKDGNSSPQEFKLI
CCCCCCCCHHHHEEC		34.3022369663
368PhosphorylationEEQLRRASQELKDEE
HHHHHHHHHHHHHHH		23.5225533186
380PhosphorylationDEEKDAESPWQAILL
HHHHCCCCHHHHHCC		32.9122369663
460PhosphorylationKEDVTPASPILTSSQ
HCCCCCCCCCCCCCC		17.4228889911
474PhosphorylationQTPHYSNSLYNAPFA
CCCCCCCCCCCCCEE		26.7021551504
476PhosphorylationPHYSNSLYNAPFAVS
CCCCCCCCCCCEEEC		14.7527738172
484PhosphorylationNAPFAVSSPPDPLPN
CCCEEECCCCCCCCC		33.5828889911
554PhosphorylationGLHLIFMDLQLPVLS
CEEEEEEECCHHHHC		22.108808622
583PhosphorylationNGIGIQKSLNNSHSN
HCCCCCHHCCCCCCC		21.6919823750
587PhosphorylationIQKSLNNSHSNLEKG
CCHHCCCCCCCCCCC		27.5025752575
589PhosphorylationKSLNNSHSNLEKGTS
HHCCCCCCCCCCCCC		42.8219823750
666PhosphorylationKQGESRMTDSVLVKS
HCCCCCCCCEEEECC		24.8230377154
668PhosphorylationGESRMTDSVLVKSPQ
CCCCCCCEEEECCCC		14.2621440633
673PhosphorylationTDSVLVKSPQKPIAP
CCEEEECCCCCCCCC		25.6917330950
681PhosphorylationPQKPIAPSNPHSFKQ
CCCCCCCCCCCCHHC		54.7119795423
685PhosphorylationIAPSNPHSFKQATSM
CCCCCCCCHHCCCCC		35.0819823750
690PhosphorylationPHSFKQATSMTPTHS
CCCHHCCCCCCCCCC		19.2823749301
691PhosphorylationHSFKQATSMTPTHSP
CCHHCCCCCCCCCCC		24.5521440633
693PhosphorylationFKQATSMTPTHSPVR
HHCCCCCCCCCCCCC		25.4619823750
695PhosphorylationQATSMTPTHSPVRKN
CCCCCCCCCCCCCCC		26.3119823750
697PhosphorylationTSMTPTHSPVRKNSN
CCCCCCCCCCCCCCC		27.8019823750
703PhosphorylationHSPVRKNSNLSPTQI
CCCCCCCCCCCCCCC		42.0322369663
706PhosphorylationVRKNSNLSPTQIEL-
CCCCCCCCCCCCCC-		30.1022369663
708PhosphorylationKNSNLSPTQIEL---
CCCCCCCCCCCC---		38.5122890988
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
-KUbiquitinationE3 ubiquitin ligaseUFD4P33202
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSK1_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 SSK1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EST1_YEASTEST1physical
11805837
SSK2_YEASTSSK2physical
11805837
SSK22_YEASTSSK22physical
11805837
YPD1_YEASTYPD1physical
9882653
YPD1_YEASTYPD1physical
11073911
SSK2_YEASTSSK2physical
9482735
SSK2_YEASTSSK2physical
7624781
YPD1_YEASTYPD1physical
15628880
STE11_YEASTSTE11genetic
10980703
STE20_YEASTSTE20genetic
10980703
CDC42_YEASTCDC42genetic
10980703
SHO1_YEASTSHO1genetic
10980703
SHO1_YEASTSHO1genetic
9744864
STE20_YEASTSTE20genetic
9744864
STE50_YEASTSTE50genetic
9744864
STE11_YEASTSTE11genetic
14595107
GPI7_YEASTLAS21genetic
11922108
SHO1_YEASTSHO1genetic
15773992
SSK2_YEASTSSK2physical
16554755
STE11_YEASTSTE11genetic
16920868
STE50_YEASTSTE50genetic
17318632
SSK2_YEASTSSK2physical
18467557
YPD1_YEASTYPD1physical
18719252
TPS1_YEASTTPS1genetic
19269370
BEM1_YEASTBEM1genetic
19269370
STE50_YEASTSTE50genetic
19269370
CG23_YEASTCLB3genetic
19269370
YPD1_YEASTYPD1genetic
19269370
PTPA1_YEASTRRD1genetic
19269370
SAC1_YEASTSAC1genetic
19269370
RIC1_YEASTRIC1genetic
19269370
MSG5_YEASTMSG5genetic
19269370
CLA4_YEASTCLA4genetic
19269370
YPD1_YEASTYPD1physical
18573873
SSK2_YEASTSSK2physical
18573873
SSK1_YEASTSSK1physical
18573873
SNT1_YEASTSNT1genetic
18931302
MNN10_YEASTMNN10genetic
18931302
HOS2_YEASTHOS2genetic
18931302
SIF2_YEASTSIF2genetic
18931302
HOG1_YEASTHOG1genetic
19536204
SHO1_YEASTSHO1genetic
20121702
SP110_YEASTSPC110physical
20489023
SSK2_YEASTSSK2physical
21118957
YPD1_YEASTYPD1physical
21118957
TAT1_YEASTTAT1genetic
20526336
STE50_YEASTSTE50genetic
10980703
SSK2_YEASTSSK2physical
22615397
STE11_YEASTSTE11genetic
12052881
SHO1_YEASTSHO1genetic
12052881
SNF1_YEASTSNF1genetic
26394309
MNN2_YEASTMNN2genetic
27708008
AIM4_YEASTAIM4genetic
27708008
MNN10_YEASTMNN10genetic
27708008
SERB_YEASTSER2genetic
27708008
MED20_YEASTSRB2genetic
27708008
DHOM_YEASTHOM6genetic
27708008
RFX1_YEASTRFX1genetic
27708008
MSC1_YEASTMSC1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
TKT1_YEASTTKL1genetic
27708008
CTF4_YEASTCTF4genetic
27708008
MMS1_YEASTMMS1genetic
27708008
SHO1_YEASTSHO1genetic
27001830
STE11_YEASTSTE11genetic
27001830
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SSK1_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-110; THR-112; SER-186;SER-193; SER-195; SER-327; SER-350; SER-460; SER-484; SER-703 ANDSER-706, 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-186; SER-351; THR-693AND SER-697, 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-368; SER-673; THR-693;THR-695 AND SER-697, AND MASS 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-380 AND SER-673, ANDMASS 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-110 AND SER-706, ANDMASS SPECTROMETRY.

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