MKS1_YEAST - dbPTM
MKS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MKS1_YEAST
UniProt AC P34072
Protein Name Negative regulator of RAS-cAMP pathway
Gene Name MKS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 584
Subcellular Localization Nucleus.
Protein Description Negative regulator of Ras-cAMP pathway. Involved in transcriptional regulation of galactose-inducible genes..
Protein Sequence MSREAFDVPNIGTNKFLKVTPNLFTPERLNLFDDVELYLTLIKASKCVEQGERLHNISWRILNKAVLKEHNINRSKKRDGVKNIYYVLNPNNKQPIKPKQAAVKQPPLQKANLPPTTAKQNVLTRPMTSPAIAQGAHDRSLDNPNSTNNDVKNDVAPNRQFSKSTTSGLFSNFADKYQKMKNVNHVANKEEPQTIITGFDTSTVITKKPLQSRRSRSPFQHIGDMNMNCIDNETSKSTSPTLENMGSRKSSFPQKESLFGRPRSYKNDQNGQLSLSKTSSRKGKNKIFFSSEDEDSDWDSVSNDSEFYADEDDEEYDDYNEEEADQYYRRQWDKLLFAKNQQNLDSTKSSVSSANTINSNTSHDPVRKSLLSGLFLSEANSNSNNHNTAHSEYASKHVSPTPQSSHSNIGPQPQQNPPSANGIKQQKPSLKTSNVTALASLSPPQPSNNERLSMDIQKDFKTDNESNHLYESNAPLTAQTILPTALSTHMFLPNNIHQQRMAIATGSNTRHRFSRRQSMDIPSKNRNTGFLKTRMEISEEEKMVRTISRLDNTSIANSNGNGNDDTSNQRTEALGRKTSNGGRI
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
2Phosphorylation------MSREAFDVP
------CCCCCCCCC		38.5422369663
25PhosphorylationKVTPNLFTPERLNLF
EECCCCCCHHHHCCC		27.6628889911
124PhosphorylationTAKQNVLTRPMTSPA
CCCCCCCCCCCCCHH		28.5729734811
128PhosphorylationNVLTRPMTSPAIAQG
CCCCCCCCCHHHHCC		33.9528889911
129PhosphorylationVLTRPMTSPAIAQGA
CCCCCCCCHHHHCCC		13.1928889911
140PhosphorylationAQGAHDRSLDNPNST
HCCCCCCCCCCCCCC		46.2422369663
146PhosphorylationRSLDNPNSTNNDVKN
CCCCCCCCCCCHHCC		33.5023749301
147PhosphorylationSLDNPNSTNNDVKND
CCCCCCCCCCHHCCC		44.6822369663
162PhosphorylationVAPNRQFSKSTTSGL
CCCCCCCCHHHCCCH		19.8421551504
164PhosphorylationPNRQFSKSTTSGLFS
CCCCCCHHHCCCHHH		35.4022369663
165PhosphorylationNRQFSKSTTSGLFSN
CCCCCHHHCCCHHHH		28.8120377248
166PhosphorylationRQFSKSTTSGLFSNF
CCCCHHHCCCHHHHH		28.0822369663
167PhosphorylationQFSKSTTSGLFSNFA
CCCHHHCCCHHHHHH		33.3222369663
194PhosphorylationANKEEPQTIITGFDT
CCCCCCCEEEECCCC		25.6827017623
197PhosphorylationEEPQTIITGFDTSTV
CCCCEEEECCCCCCE		28.1327017623
201PhosphorylationTIITGFDTSTVITKK
EEEECCCCCCEEECC		24.8427017623
202PhosphorylationIITGFDTSTVITKKP
EEECCCCCCEEECCC		23.6327017623
203PhosphorylationITGFDTSTVITKKPL
EECCCCCCEEECCCC		20.3027017623
206PhosphorylationFDTSTVITKKPLQSR
CCCCCEEECCCCCCC		28.7827017623
215PhosphorylationKPLQSRRSRSPFQHI
CCCCCCCCCCCCCCH		35.6828889911
217PhosphorylationLQSRRSRSPFQHIGD
CCCCCCCCCCCCHHH		31.1725704821
235PhosphorylationNCIDNETSKSTSPTL
CCCCCCCCCCCCCCH		20.5928889911
237PhosphorylationIDNETSKSTSPTLEN
CCCCCCCCCCCCHHH		33.6122369663
238PhosphorylationDNETSKSTSPTLENM
CCCCCCCCCCCHHHC		42.3222369663
239PhosphorylationNETSKSTSPTLENMG
CCCCCCCCCCHHHCC		23.9922369663
241PhosphorylationTSKSTSPTLENMGSR
CCCCCCCCHHHCCCC		46.6122369663
247PhosphorylationPTLENMGSRKSSFPQ
CCHHHCCCCCCCCCC		26.2622369663
250PhosphorylationENMGSRKSSFPQKES
HHCCCCCCCCCCHHH		35.7828152593
251PhosphorylationNMGSRKSSFPQKESL
HCCCCCCCCCCHHHH		43.9419823750
257PhosphorylationSSFPQKESLFGRPRS
CCCCCHHHHCCCCCC		35.7124961812
264PhosphorylationSLFGRPRSYKNDQNG
HHCCCCCCCCCCCCC		43.0422369663
265PhosphorylationLFGRPRSYKNDQNGQ
HCCCCCCCCCCCCCC		18.3222369663
274PhosphorylationNDQNGQLSLSKTSSR
CCCCCCEEECCCCCC		23.7822369663
276PhosphorylationQNGQLSLSKTSSRKG
CCCCEEECCCCCCCC		30.4322369663
346PhosphorylationKNQQNLDSTKSSVSS
HCCCCCCCCCCCHHH		40.6828889911
352PhosphorylationDSTKSSVSSANTINS
CCCCCCHHHCHHCCC		26.1921551504
353PhosphorylationSTKSSVSSANTINSN
CCCCCHHHCHHCCCC		24.3121440633
356PhosphorylationSSVSSANTINSNTSH
CCHHHCHHCCCCCCC		22.6621440633
359PhosphorylationSSANTINSNTSHDPV
HHCHHCCCCCCCCHH		37.3228889911
361PhosphorylationANTINSNTSHDPVRK
CHHCCCCCCCCHHHH		27.5320377248
362PhosphorylationNTINSNTSHDPVRKS
HHCCCCCCCCHHHHH		30.0920377248
399PhosphorylationEYASKHVSPTPQSSH
HHHHHHCCCCCCCCC		23.8321440633
401PhosphorylationASKHVSPTPQSSHSN
HHHHCCCCCCCCCCC		26.8421440633
404PhosphorylationHVSPTPQSSHSNIGP
HCCCCCCCCCCCCCC		31.0821440633
405PhosphorylationVSPTPQSSHSNIGPQ
CCCCCCCCCCCCCCC		26.2019823750
407PhosphorylationPTPQSSHSNIGPQPQ
CCCCCCCCCCCCCCC		31.9019779198
419PhosphorylationQPQQNPPSANGIKQQ
CCCCCCCCCCCCCCC		35.3121440633
429PhosphorylationGIKQQKPSLKTSNVT
CCCCCCCCCCCCCCE		49.9229734811
436PhosphorylationSLKTSNVTALASLSP
CCCCCCCEEEHHCCC		21.8722369663
440PhosphorylationSNVTALASLSPPQPS
CCCEEEHHCCCCCCC		30.1722369663
442PhosphorylationVTALASLSPPQPSNN
CEEEHHCCCCCCCCC		31.8522369663
447PhosphorylationSLSPPQPSNNERLSM
HCCCCCCCCCCCCCC		47.2222369663
505PhosphorylationQQRMAIATGSNTRHR
HHHHHHHCCCCHHHC		34.7222369663
507PhosphorylationRMAIATGSNTRHRFS
HHHHHCCCCHHHCCC		30.5822369663
509PhosphorylationAIATGSNTRHRFSRR
HHHCCCCHHHCCCCC		29.5622369663
518PhosphorylationHRFSRRQSMDIPSKN
HCCCCCCCCCCCCCC		19.3322369663
523PhosphorylationRQSMDIPSKNRNTGF
CCCCCCCCCCCCCCC		42.7822369663
546PhosphorylationEEEKMVRTISRLDNT
HHHHHHHHHHHHCCC		16.3421440633
548PhosphorylationEKMVRTISRLDNTSI
HHHHHHHHHHCCCCC		26.6123749301
553PhosphorylationTISRLDNTSIANSNG
HHHHHCCCCCCCCCC		22.6022369663
554PhosphorylationISRLDNTSIANSNGN
HHHHCCCCCCCCCCC		26.4222369663
558PhosphorylationDNTSIANSNGNGNDD
CCCCCCCCCCCCCCC		36.7722369663
566PhosphorylationNGNGNDDTSNQRTEA
CCCCCCCCCCHHHHH		32.2322369663
567PhosphorylationGNGNDDTSNQRTEAL
CCCCCCCCCHHHHHH		37.6522369663
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
518SPhosphorylationKinasePKA-Uniprot
-KUbiquitinationE3 ubiquitin ligaseGRR1P24814
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MKS1_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 MKS1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED15_YEASTGAL11genetic
8386801
URE2_YEASTURE2genetic
10511541
DPOD_YEASTPOL3genetic
12759774
RTG2_YEASTRTG2genetic
14536080
BMH1_YEASTBMH1physical
16429126
RTG2_YEASTRTG2physical
16429126
RTG2_YEASTRTG2physical
16093347
GRR1_YEASTGRR1physical
16093347
CSK22_YEASTCKA2physical
20489023
KOG1_YEASTKOG1physical
20489023
MYO2_YEASTMYO2physical
20489023
RTG2_YEASTRTG2physical
20489023
RTG3_YEASTRTG3physical
20489023
TOR1_YEASTTOR1physical
20489023
TOR2_YEASTTOR2physical
20489023
GLN3_YEASTGLN3genetic
20489023
GAT1_YEASTGAT1genetic
20489023
ATC1_YEASTPMR1genetic
20489023
NPR1_YEASTNPR1genetic
20489023
TAP42_YEASTTAP42genetic
20489023
TOR1_YEASTTOR1genetic
20489023
RTG1_YEASTRTG1genetic
20526336
YPT31_YEASTYPT31genetic
20526336
SLT2_YEASTSLT2genetic
20526336
RV167_YEASTRVS167genetic
20526336
VPS27_YEASTVPS27genetic
20526336
SUR1_YEASTSUR1genetic
20526336
SFT2_YEASTSFT2genetic
20526336
THRC_YEASTTHR4genetic
20526336
AP18A_YEASTYAP1801genetic
20526336
SRO77_YEASTSRO77genetic
20526336
KOG1_YEASTKOG1physical
22043304
RTG2_YEASTRTG2physical
23711018
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MKS1_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-25; THR-165; SER-217;SER-239; SER-247; SER-251; SER-264; SER-274; SER-276; SER-442; THR-509AND SER-518, 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-164 AND SER-264, 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-264, 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-247, AND MASSSPECTROMETRY.
"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-442, AND MASSSPECTROMETRY.

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