IGO2_YEAST - dbPTM
IGO2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IGO2_YEAST
UniProt AC Q9P305
Protein Name mRNA stability protein IGO2
Gene Name IGO2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 131
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Required for TORC1 to properly control gene expression and chronological life span. Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway..
Protein Sequence MSEDLSPTSSRVDLSNPHGFTKEGVDLSKLSPQELKLYKMYGKLPSKKDLLRHKMQDRQYFDSGDYALKKAGVIKSDDVIVNNSSNNLPVTNPSGLRESIIRRRMSSSSGGDSISRQGSISSGPPPRSPNK
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
2Acetylation------MSEDLSPTS
------CCCCCCCCC		39.5622814378
2Phosphorylation------MSEDLSPTS
------CCCCCCCCC		39.5622369663
6Phosphorylation--MSEDLSPTSSRVD
--CCCCCCCCCCCCC		38.1522369663
8PhosphorylationMSEDLSPTSSRVDLS
CCCCCCCCCCCCCCC		35.6422369663
9PhosphorylationSEDLSPTSSRVDLSN
CCCCCCCCCCCCCCC		21.3822369663
10PhosphorylationEDLSPTSSRVDLSNP
CCCCCCCCCCCCCCC		38.5124909858
15PhosphorylationTSSRVDLSNPHGFTK
CCCCCCCCCCCCCCC		43.8022369663
21PhosphorylationLSNPHGFTKEGVDLS
CCCCCCCCCCCCCHH		32.5522369663
22AcetylationSNPHGFTKEGVDLSK
CCCCCCCCCCCCHHH		50.6524489116
28PhosphorylationTKEGVDLSKLSPQEL
CCCCCCHHHCCHHHH		27.3824961812
31PhosphorylationGVDLSKLSPQELKLY
CCCHHHCCHHHHHHH		28.4225752575
36AcetylationKLSPQELKLYKMYGK
HCCHHHHHHHHHHCC		49.3624489116
38PhosphorylationSPQELKLYKMYGKLP
CHHHHHHHHHHCCCC		7.6627017623
39AcetylationPQELKLYKMYGKLPS
HHHHHHHHHHCCCCC		35.7625381059
60PhosphorylationHKMQDRQYFDSGDYA
HHHHCHHHHCCCCHH		15.3922890988
63PhosphorylationQDRQYFDSGDYALKK
HCHHHHCCCCHHHHH		24.5422369663
66PhosphorylationQYFDSGDYALKKAGV
HHHCCCCHHHHHCCC		19.8422890988
69AcetylationDSGDYALKKAGVIKS
CCCCHHHHHCCCCCC		32.1924489116
84PhosphorylationDDVIVNNSSNNLPVT
CCEEEECCCCCCCCC		29.2822369663
85PhosphorylationDVIVNNSSNNLPVTN
CEEEECCCCCCCCCC		31.6822369663
91PhosphorylationSSNNLPVTNPSGLRE
CCCCCCCCCCCCHHH		39.2022369663
94PhosphorylationNLPVTNPSGLRESII
CCCCCCCCCHHHHHH		53.1628132839
99PhosphorylationNPSGLRESIIRRRMS
CCCCHHHHHHHHHHH		19.5123749301
106PhosphorylationSIIRRRMSSSSGGDS
HHHHHHHHCCCCCCC		25.8422369663
107PhosphorylationIIRRRMSSSSGGDSI
HHHHHHHCCCCCCCC		21.1222369663
108PhosphorylationIRRRMSSSSGGDSIS
HHHHHHCCCCCCCCC		26.2022369663
109PhosphorylationRRRMSSSSGGDSISR
HHHHHCCCCCCCCCC		49.0622369663
113PhosphorylationSSSSGGDSISRQGSI
HCCCCCCCCCCCCCC		26.2422369663
115PhosphorylationSSGGDSISRQGSISS
CCCCCCCCCCCCCCC		23.6222369663
119PhosphorylationDSISRQGSISSGPPP
CCCCCCCCCCCCCCC		15.8022369663
121PhosphorylationISRQGSISSGPPPRS
CCCCCCCCCCCCCCC		30.8222369663
122PhosphorylationSRQGSISSGPPPRSP
CCCCCCCCCCCCCCC		54.3622369663
128PhosphorylationSSGPPPRSPNK----
CCCCCCCCCCC----		38.3022369663
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 IGO2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IGO2_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 IGO2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHH1_YEASTDHH1genetic
20471941
CCR4_YEASTCCR4genetic
20471941
XRN1_YEASTXRN1genetic
20471941
CCR4_YEASTCCR4genetic
21289492
DHH1_YEASTDHH1genetic
21289492
LSM1_YEASTLSM1genetic
21289492
LSM6_YEASTLSM6genetic
21289492
PAT1_YEASTPAT1genetic
21289492
PP2A1_YEASTPPH21genetic
23273919
2ABA_YEASTCDC55genetic
23273919
2ABA_YEASTCDC55genetic
23792549
SWE1_YEASTSWE1genetic
23861665
MPIP_YEASTMIH1genetic
23861665
RIM15_YEASTRIM15genetic
23861665
CDK1_YEASTCDC28genetic
23861665
ZDS1_YEASTZDS1genetic
23861665
ZDS2_YEASTZDS2genetic
23861665
ZDS1_YEASTZDS1genetic
24800822
DID2_YEASTDID2genetic
27708008
MLH1_YEASTMLH1genetic
27708008
RAD14_YEASTRAD14genetic
27708008
RCR1_YEASTRCR1genetic
27708008
NAA38_YEASTMAK31genetic
27708008
MCM21_YEASTMCM21genetic
27708008
DLDH_YEASTLPD1genetic
27708008
PALF_YEASTRIM8genetic
27708008
MON1_YEASTMON1genetic
27708008
BUB1_YEASTBUB1genetic
27708008
YOR1_YEASTYOR1genetic
27708008
RL17B_YEASTRPL17Bgenetic
27708008
DHOM_YEASTHOM6genetic
27708008
YL149_YEASTYLR149Cgenetic
27708008
ARV1_YEASTARV1genetic
27708008
EFM7_YEASTNNT1genetic
27708008
BUD8_YEASTBUD8genetic
27708008
SUR7_YEASTSUR7genetic
27708008
YMP8_YEASTYMR018Wgenetic
27708008
RSF1_YEASTRSF1genetic
27708008
CSM3_YEASTCSM3genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
MSO1_YEASTMSO1genetic
27708008
PHO80_YEASTPHO80genetic
27708008
AIM39_YEASTAIM39genetic
27708008
CHL1_YEASTCHL1genetic
27708008
RAD1_YEASTRAD1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
PCL8_YEASTPCL8genetic
27708008
2ABA_YEASTCDC55genetic
28600888
WHI5_YEASTWHI5genetic
28600888
STB1_YEASTSTB1genetic
28600888
2ABA_YEASTCDC55genetic
26356805
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IGO2_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-6,AND MASS SPECTROMETRY.
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-6; SER-9; SER-63;SER-106; SER-107; SER-108 AND SER-109, 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-106; SER-108 ANDSER-128, 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-63, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-6,AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-107, ANDMASS SPECTROMETRY.

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