SOK1_YEAST - dbPTM
SOK1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SOK1_YEAST
UniProt AC P40317
Protein Name Protein SOK1
Gene Name SOK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 901
Subcellular Localization Nucleus.
Protein Description High copy suppressor of a cyclic AMP-dependent protein kinase mutant..
Protein Sequence MDQPRTHSGPTTASNPAPSSTNSSSAPSATNSKQERSSSSLSKPSSVVPSKDSPDGDAIAKTQAAALKNDMKSGDTSTLDGSSQNIIPNRASMQKYIDQSSDLLSRSSGVITPSMSLNASTNATNNDSSGNSANSSDLKIPIDRDNTIFKTFDTKTGQFLKNDDNEEEIRRNNKVDSIPPKNIYTNINNPSPSPPPSSKQPPSASAPQLPPATEPHKEQAAQQQPPGNASNFLRIFSNKKMRSHSVPTILHSSLRKLSSHNQYYRNQNILLNHPTPSGISKKKFSRNHHQPYLHSNNPLSSNPLSLKRAIFLNQQISGNASTNANNDNINNSTATSMTNQSFLSSSNFDLTLEDRINYIKATPTPVPFPPINLQGLKEIDLQEILKNPQLRHDIIFDPLLQFRPNLDGERGNKKRQLANIYWNDVQNEIYVYSKRPEIFQYNRSRLVPLFDTLRDVLLTIVPQKESPMINNVLDTELNIQELLKGSLIMSNLSGWLADLFKHHCAPMRDPWVDKMSNKFKEAERDSSLTRLIEGLRLVFQILETMKLDIANHQIRILRPALLSNAVEFEKQYFNTLIASKRVNLNTSLLWFDKKFNENVTAGLVRNPSSITIPDVYNICIRSIINLLSCRKMVREYPTPLSFDHARLILLRADIRQIVCILVCRLLFQQLVANDPSMDKATKEYVIHTYSTKRLKNEIISIITDEHGNCRWTKNTMSIAVHLCKVIDDLHREYDNNGSCEQARRPQLPSLDNSKITFAKSWLSKQTQPLSEVYGVLENRVFKSLEDAIFNRSECTIDGRVKQDFVYLYNTNNGNVGSTNTLSTTTDTASVKISPSLMSPSKTSTTTPTGNAIASRGLFAATELEEFENVYRHLYALINLHWSVFGPHYIEMLGDKVNKKGI
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--MDQPRTHSGPTTA
--CCCCCCCCCCCCC		27.3822369663
8PhosphorylationMDQPRTHSGPTTASN
CCCCCCCCCCCCCCC		45.9422369663
11PhosphorylationPRTHSGPTTASNPAP
CCCCCCCCCCCCCCC		38.2222369663
12PhosphorylationRTHSGPTTASNPAPS
CCCCCCCCCCCCCCC		31.0822369663
14PhosphorylationHSGPTTASNPAPSST
CCCCCCCCCCCCCCC		41.0522369663
19PhosphorylationTASNPAPSSTNSSSA
CCCCCCCCCCCCCCC		52.4822369663
20PhosphorylationASNPAPSSTNSSSAP
CCCCCCCCCCCCCCC		30.4622369663
37PhosphorylationTNSKQERSSSSLSKP
CCCCCHHCCCCCCCC		33.5429136822
38PhosphorylationNSKQERSSSSLSKPS
CCCCHHCCCCCCCCC		30.1219779198
39PhosphorylationSKQERSSSSLSKPSS
CCCHHCCCCCCCCCC		36.2229136822
40PhosphorylationKQERSSSSLSKPSSV
CCHHCCCCCCCCCCC		38.3129136822
42PhosphorylationERSSSSLSKPSSVVP
HHCCCCCCCCCCCCC		44.4623749301
45PhosphorylationSSSLSKPSSVVPSKD
CCCCCCCCCCCCCCC		39.2319779198
50PhosphorylationKPSSVVPSKDSPDGD
CCCCCCCCCCCCCCH		37.1722369663
51AcetylationPSSVVPSKDSPDGDA
CCCCCCCCCCCCCHH		57.0424489116
53PhosphorylationSVVPSKDSPDGDAIA
CCCCCCCCCCCHHHH		28.7322369663
72UbiquitinationAALKNDMKSGDTSTL
HHHHCCCCCCCCCCC		54.9019722269
92PhosphorylationNIIPNRASMQKYIDQ
CCCCCHHHHHHHHHH		20.6425752575
95UbiquitinationPNRASMQKYIDQSSD
CCHHHHHHHHHHHHH		35.2219722269
95AcetylationPNRASMQKYIDQSSD
CCHHHHHHHHHHHHH		35.2224489116
100PhosphorylationMQKYIDQSSDLLSRS
HHHHHHHHHHHHHHC		23.2830377154
101PhosphorylationQKYIDQSSDLLSRSS
HHHHHHHHHHHHHCC		27.0127214570
107PhosphorylationSSDLLSRSSGVITPS
HHHHHHHCCCCCCCC		28.2427017623
161AcetylationTKTGQFLKNDDNEEE
CCCCCCCCCCCCHHH		60.6724489116
177PhosphorylationRRNNKVDSIPPKNIY
HHHCCCCCCCCCCCC		39.7330377154
185PhosphorylationIPPKNIYTNINNPSP
CCCCCCCCCCCCCCC		26.3121126336
191PhosphorylationYTNINNPSPSPPPSS
CCCCCCCCCCCCCCC		39.8822369663
193PhosphorylationNINNPSPSPPPSSKQ
CCCCCCCCCCCCCCC		55.1422369663
197PhosphorylationPSPSPPPSSKQPPSA
CCCCCCCCCCCCCCC		56.8122369663
198PhosphorylationSPSPPPSSKQPPSAS
CCCCCCCCCCCCCCC		40.8722369663
230PhosphorylationQQPPGNASNFLRIFS
HCCCCCHHHHHHHHC		31.9219779198
243PhosphorylationFSNKKMRSHSVPTIL
HCCCCHHCCCCCHHH		19.3329136822
245PhosphorylationNKKMRSHSVPTILHS
CCCHHCCCCCHHHHH		30.9117330950
248PhosphorylationMRSHSVPTILHSSLR
HHCCCCCHHHHHHHH		33.7329136822
258PhosphorylationHSSLRKLSSHNQYYR
HHHHHHHHHCCHHHH		32.3621440633
275PhosphorylationNILLNHPTPSGISKK
CEECCCCCCCCCCCC		23.6423749301
285PhosphorylationGISKKKFSRNHHQPY
CCCCCCCCCCCCCCC		40.8424961812
292PhosphorylationSRNHHQPYLHSNNPL
CCCCCCCCCCCCCCC		15.5224961812
295PhosphorylationHHQPYLHSNNPLSSN
CCCCCCCCCCCCCCC		35.3924961812
300PhosphorylationLHSNNPLSSNPLSLK
CCCCCCCCCCCCCHH		29.3524961812
301PhosphorylationHSNNPLSSNPLSLKR
CCCCCCCCCCCCHHH		50.5824961812
307AcetylationSSNPLSLKRAIFLNQ
CCCCCCHHHHHHCCC		36.0925381059
833PhosphorylationDTASVKISPSLMSPS
CCCEEEECHHHCCCC		11.6128889911
835PhosphorylationASVKISPSLMSPSKT
CEEEECHHHCCCCCC		29.8819795423
838PhosphorylationKISPSLMSPSKTSTT
EECHHHCCCCCCCCC		31.1719823750
840PhosphorylationSPSLMSPSKTSTTTP
CHHHCCCCCCCCCCC		41.0621440633
842PhosphorylationSLMSPSKTSTTTPTG
HHCCCCCCCCCCCCC		35.3328889911
846PhosphorylationPSKTSTTTPTGNAIA
CCCCCCCCCCCCHHH		20.9523749301
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 SOK1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SOK1_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 SOK1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZUO1_YEASTZUO1physical
16554755
EIF3J_YEASTHCR1physical
16554755
PRS6A_YEASTRPT5physical
18757749
CDC24_YEASTCDC24genetic
27708008
STU1_YEASTSTU1genetic
27708008
PRP6_YEASTPRP6genetic
27708008
ORC2_YEASTORC2genetic
27708008
SEC18_YEASTSEC18genetic
27708008
TAF12_YEASTTAF12genetic
27708008
SEC7_YEASTSEC7genetic
27708008
RPB7_YEASTRPB7genetic
27708008
COG3_YEASTCOG3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
MOB2_YEASTMOB2genetic
27708008
STT3_YEASTSTT3genetic
27708008
PRS8_YEASTRPT6genetic
27708008
CDC20_YEASTCDC20genetic
27708008
COPB2_YEASTSEC27genetic
27708008
DBF2_YEASTDBF2genetic
27708008
TEL2_YEASTTEL2genetic
27708008
MPPA_YEASTMAS2genetic
27708008
STS1_YEASTSTS1genetic
27708008
PRP21_YEASTPRP21genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
FIP1_YEASTFIP1genetic
27708008
PRI2_YEASTPRI2genetic
27708008
RSC4_YEASTRSC4genetic
27708008
PRP19_YEASTPRP19genetic
27708008
NOC3_YEASTNOC3genetic
27708008
NSE1_YEASTNSE1genetic
27708008
TIM14_YEASTPAM18genetic
27708008
BOS1_YEASTBOS1genetic
27708008
SMC4_YEASTSMC4genetic
27708008
SEC13_YEASTSEC13genetic
27708008
RU1C_YEASTYHC1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
SC61A_YEASTSEC61genetic
27708008
POB3_YEASTPOB3genetic
27708008
MCM1_YEASTMCM1genetic
27708008
SEC12_YEASTSEC12genetic
27708008
TOA1_YEASTTOA1genetic
27708008
APC5_YEASTAPC5genetic
27708008
SEC62_YEASTSEC62genetic
27708008
NAB3_YEASTNAB3genetic
27708008
NSL1_YEASTNSL1genetic
27708008
PRP4_YEASTPRP4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SOK1_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-40; SER-53; SER-191;SER-193 AND SER-245, 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-245, 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-245, AND MASSSPECTROMETRY.

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