G3P3_YEAST - dbPTM
G3P3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID G3P3_YEAST
UniProt AC P00359
Protein Name Glyceraldehyde-3-phosphate dehydrogenase 3
Gene Name TDH3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 332
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MVRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA
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
22PhosphorylationLVMRIALSRPNVEVV
HHHHHHHCCCCEEEE		36.3528889911
43PhosphorylationITNDYAAYMFKYDST
CCCCCEEHEEEEECC		8.5621440633
46UbiquitinationDYAAYMFKYDSTHGR
CCEEHEEEEECCCCE		31.4523749301
46SuccinylationDYAAYMFKYDSTHGR
CCEEHEEEEECCCCE		31.4523954790
46AcetylationDYAAYMFKYDSTHGR
CCEEHEEEEECCCCE		31.4524489116
47PhosphorylationYAAYMFKYDSTHGRY
CEEHEEEEECCCCEE		12.1221440633
49PhosphorylationAYMFKYDSTHGRYAG
EHEEEEECCCCEECE		21.1517287358
50PhosphorylationYMFKYDSTHGRYAGE
HEEEEECCCCEECEE		26.0017287358
54PhosphorylationYDSTHGRYAGEVSHD
EECCCCEECEECCCC		24.4517287358
59PhosphorylationGRYAGEVSHDDKHII
CEECEECCCCCCEEE		19.5217287358
63SuccinylationGEVSHDDKHIIVDGK
EECCCCCCEEEECCE		42.6423954790
63UbiquitinationGEVSHDDKHIIVDGK
EECCCCCCEEEECCE		42.6423749301
63AcetylationGEVSHDDKHIIVDGK
EECCCCCCEEEECCE		42.6424489116
70AcetylationKHIIVDGKKIATYQE
CEEEECCEEEEEECC		36.2224489116
70UbiquitinationKHIIVDGKKIATYQE
CEEEECCEEEEEECC		36.2217644757
70SuccinylationKHIIVDGKKIATYQE
CEEEECCEEEEEECC		36.2223954790
71AcetylationHIIVDGKKIATYQER
EEEECCEEEEEECCC		43.0025381059
71UbiquitinationHIIVDGKKIATYQER
EEEECCEEEEEECCC		43.0017644757
74PhosphorylationVDGKKIATYQERDPA
ECCEEEEEECCCCCC		29.2521440633
87PhosphorylationPANLPWGSSNVDIAI
CCCCCCCCCCEEEEE		18.1821440633
88PhosphorylationANLPWGSSNVDIAID
CCCCCCCCCEEEEEE		36.6120377248
96PhosphorylationNVDIAIDSTGVFKEL
CEEEEEECCCHHHCH		22.4321440633
101AcetylationIDSTGVFKELDTAQK
EECCCHHHCHHHHHH		55.77-
101UbiquitinationIDSTGVFKELDTAQK
EECCCHHHCHHHHHH		55.7717644757
108UbiquitinationKELDTAQKHIDAGAK
HCHHHHHHHHHCCCC		39.8123749301
115UbiquitinationKHIDAGAKKVVITAP
HHHHCCCCEEEEECC		45.2222817900
116UbiquitinationHIDAGAKKVVITAPS
HHHCCCCEEEEECCC		41.0023749301
116AcetylationHIDAGAKKVVITAPS
HHHCCCCEEEEECCC		41.00-
120PhosphorylationGAKKVVITAPSSTAP
CCCEEEEECCCCCCC		22.3922369663
123PhosphorylationKVVITAPSSTAPMFV
EEEEECCCCCCCEEE		37.5522369663
124PhosphorylationVVITAPSSTAPMFVM
EEEECCCCCCCEEEE		27.7722369663
125PhosphorylationVITAPSSTAPMFVMG
EEECCCCCCCEEEEE		38.8325521595
137UbiquitinationVMGVNEEKYTSDLKI
EEECCCHHCCCCCEE		47.8823749301
138PhosphorylationMGVNEEKYTSDLKIV
EECCCHHCCCCCEEE		18.1127017623
139PhosphorylationGVNEEKYTSDLKIVS
ECCCHHCCCCCEEEC		27.1727017623
140PhosphorylationVNEEKYTSDLKIVSN
CCCHHCCCCCEEECC		37.5422369663
143UbiquitinationEKYTSDLKIVSNASC
HHCCCCCEEECCCCC		46.1623749301
146PhosphorylationTSDLKIVSNASCTTN
CCCCEEECCCCCCCC		30.1022369663
149PhosphorylationLKIVSNASCTTNCLA
CEEECCCCCCCCCHH		19.0822369663
151PhosphorylationIVSNASCTTNCLAPL
EECCCCCCCCCHHHH		20.6722369663
152PhosphorylationVSNASCTTNCLAPLA
ECCCCCCCCCHHHHH		28.4125521595
160UbiquitinationNCLAPLAKVINDAFG
CCHHHHHHHHHHHHC		51.8617644757
174PhosphorylationGIEEGLMTTVHSLTA
CCCCCCCHHHHHEEE		30.6122369663
175PhosphorylationIEEGLMTTVHSLTAT
CCCCCCHHHHHEEEE		11.4022369663
178PhosphorylationGLMTTVHSLTATQKT
CCCHHHHHEEEEECC		24.0722369663
180PhosphorylationMTTVHSLTATQKTVD
CHHHHHEEEEECCCC		30.5822369663
182PhosphorylationTVHSLTATQKTVDGP
HHHHEEEEECCCCCC		25.9322369663
184AcetylationHSLTATQKTVDGPSH
HHEEEEECCCCCCCC		46.2724489116
184UbiquitinationHSLTATQKTVDGPSH
HHEEEEECCCCCCCC		46.2723749301
185PhosphorylationSLTATQKTVDGPSHK
HEEEEECCCCCCCCC		17.6329136822
190PhosphorylationQKTVDGPSHKDWRGG
ECCCCCCCCCCCCCC		49.0129136822
192UbiquitinationTVDGPSHKDWRGGRT
CCCCCCCCCCCCCCC		64.4223749301
199PhosphorylationKDWRGGRTASGNIIP
CCCCCCCCCCCCCCC		28.5722369663
201PhosphorylationWRGGRTASGNIIPSS
CCCCCCCCCCCCCCC		31.5925521595
207PhosphorylationASGNIIPSSTGAAKA
CCCCCCCCCHHHHHH		30.0822369663
208PhosphorylationSGNIIPSSTGAAKAV
CCCCCCCCHHHHHHH		26.0422369663
209PhosphorylationGNIIPSSTGAAKAVG
CCCCCCCHHHHHHHH		34.8725521595
213UbiquitinationPSSTGAAKAVGKVLP
CCCHHHHHHHHHHHH		42.9723749301
217UbiquitinationGAAKAVGKVLPELQG
HHHHHHHHHHHHHHH		33.7223749301
225UbiquitinationVLPELQGKLTGMAFR
HHHHHHHHHCCEEEE		29.8923749301
227PhosphorylationPELQGKLTGMAFRVP
HHHHHHHCCEEEECC		28.5322369663
235PhosphorylationGMAFRVPTVDVSVVD
CEEEECCCCCEEEEE		26.8722369663
239PhosphorylationRVPTVDVSVVDLTVK
ECCCCCEEEEEEEEE		16.3822369663
244PhosphorylationDVSVVDLTVKLNKET
CEEEEEEEEECCCCC		15.9021440633
246UbiquitinationSVVDLTVKLNKETTY
EEEEEEEECCCCCCH		40.9023749301
249AcetylationDLTVKLNKETTYDEI
EEEEECCCCCCHHHH		67.86-
249UbiquitinationDLTVKLNKETTYDEI
EEEEECCCCCCHHHH		67.8623749301
251PhosphorylationTVKLNKETTYDEIKK
EEECCCCCCHHHHHH		32.0620377248
252PhosphorylationVKLNKETTYDEIKKV
EECCCCCCHHHHHHH		30.0222369663
253PhosphorylationKLNKETTYDEIKKVV
ECCCCCCHHHHHHHH		20.9922369663
257UbiquitinationETTYDEIKKVVKAAA
CCCHHHHHHHHHHHH		37.1523749301
258UbiquitinationTTYDEIKKVVKAAAE
CCHHHHHHHHHHHHH		58.9022817900
261UbiquitinationDEIKKVVKAAAEGKL
HHHHHHHHHHHHCCC		34.9823749301
267UbiquitinationVKAAAEGKLKGVLGY
HHHHHHCCCCEEEEC		38.2323749301
269UbiquitinationAAAEGKLKGVLGYTE
HHHHCCCCEEEECCC		50.9222817900
291PhosphorylationFLGDSHSSIFDASAG
CCCCCCCCCCCCCCC		23.1128889911
296PhosphorylationHSSIFDASAGIQLSP
CCCCCCCCCCCEECH		28.9524961812
302PhosphorylationASAGIQLSPKFVKLV
CCCCCEECHHHHEEE		15.0727214570
304UbiquitinationAGIQLSPKFVKLVSW
CCCEECHHHHEEEEE		60.4522817900
307UbiquitinationQLSPKFVKLVSWYDN
EECHHHHEEEEECCC		46.4323749301
310PhosphorylationPKFVKLVSWYDNEYG
HHHHEEEEECCCCCC		30.2917287358
312PhosphorylationFVKLVSWYDNEYGYS
HHEEEEECCCCCCCC		11.0328889911
319PhosphorylationYDNEYGYSTRVVDLV
CCCCCCCCCCHHHHH		12.8417287358
320PhosphorylationDNEYGYSTRVVDLVE
CCCCCCCCCHHHHHH		20.9917287358
331UbiquitinationDLVEHVAKA------
HHHHHHHHC------		54.2423749301
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 G3P3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of G3P3_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 G3P3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP74_YEASTSSA4physical
19536198
SSB1_YEASTSSB1physical
19536198
G3P3_YEASTTDH3physical
19343713
SIR2_YEASTSIR2genetic
19390637
HST2_YEASTHST2genetic
19390637
SHE1_YEASTSHE1genetic
20093466
AAD4_YEASTAAD4genetic
20093466
NOP6_YEASTNOP6genetic
20093466
GNTK_YEASTYDR248Cgenetic
20093466
GGA1_YEASTGGA1genetic
20093466
CP56_YEASTDIT2genetic
20093466
RL9A_YEASTRPL9Agenetic
20093466
YGK1_YEASTYGL101Wgenetic
20093466
YGI1_YEASTYGL081Wgenetic
20093466
RL8A_YEASTRPL8Agenetic
20093466
NVJ1_YEASTNVJ1genetic
20093466
G3P2_YEASTTDH2genetic
20093466
PDC5_YEASTPDC5genetic
20093466
RL37A_YEASTRPL37Agenetic
20093466
PHO84_YEASTPHO84genetic
20093466
CTK3_YEASTCTK3genetic
20093466
YMD8_YEASTYMD8genetic
20093466
AIM34_YEASTAIM34genetic
20093466
ADE_YEASTAAH1genetic
20093466
MED9_YEASTCSE2genetic
20093466
MDM12_YEASTMDM12genetic
20093466
BUB3_YEASTBUB3genetic
20093466
TYE7_YEASTTYE7genetic
20093466
YP191_YEASTYPL191Cgenetic
20093466
G3P2_YEASTTDH2genetic
21623372
COX7_YEASTCOX7genetic
21623372
CSG2_YEASTCSG2genetic
21623372
QCR2_YEASTQCR2genetic
21623372
G3P3_YEASTTDH3physical
22869137
GPP1_YEASTGPP1genetic
23891562
G3P2_YEASTTDH2genetic
23891562
CLA4_YEASTCLA4genetic
23891562
CSG2_YEASTCSG2genetic
23891562
ICE2_YEASTICE2genetic
23891562
SIR2_YEASTSIR2physical
24146631
CND2_YEASTBRN1genetic
27708008
SWC4_YEASTSWC4genetic
27708008
MCM1_YEASTMCM1genetic
27708008
IMG2_YEASTIMG2genetic
27708008
PRP6_YEASTPRP6genetic
27708008
ARP2_YEASTARP2genetic
27708008
RPB1_YEASTRPO21genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC14_YEASTCDC14genetic
27708008
NBP35_YEASTNBP35genetic
27708008
RHO3_YEASTRHO3genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
CLF1_YEASTCLF1genetic
27708008
TPT1_YEASTTPT1genetic
27708008
DEP1_YEASTDEP1genetic
27708008
ELO2_YEASTELO2genetic
27708008
NOP6_YEASTNOP6genetic
27708008
AAD4_YEASTAAD4genetic
27708008
VMS1_YEASTVMS1genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
GGA1_YEASTGGA1genetic
27708008
CP56_YEASTDIT2genetic
27708008
DOT1_YEASTDOT1genetic
27708008
YGI1_YEASTYGL081Wgenetic
27708008
YGK1_YEASTYGL101Wgenetic
27708008
RL9A_YEASTRPL9Agenetic
27708008
GPP1_YEASTGPP1genetic
27708008
ICE2_YEASTICE2genetic
27708008
G3P2_YEASTTDH2genetic
27708008
DPOD3_YEASTPOL32genetic
27708008
YK25_YEASTYKR045Cgenetic
27708008
FPS1_YEASTFPS1genetic
27708008
PFD6_YEASTYKE2genetic
27708008
CACP_YEASTCAT2genetic
27708008
CTK3_YEASTCTK3genetic
27708008
PHO84_YEASTPHO84genetic
27708008
AIM34_YEASTAIM34genetic
27708008
MDM12_YEASTMDM12genetic
27708008
LIPA_YEASTLIP5genetic
27708008
TYE7_YEASTTYE7genetic
27708008
YP191_YEASTYPL191Cgenetic
27708008
SPT20_YEASTSPT20physical
27899560
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of G3P3_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-22; SER-123; SER-124;THR-125; SER-149; THR-151; THR-152; SER-178; THR-182; SER-190;THR-199; SER-201; SER-207; SER-208; THR-209; THR-227; THR-235;SER-239; THR-252; SER-302; SER-310 AND TYR-312, 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 THR-175 AND SER-178, 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-149; SER-178 ANDSER-201, 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 THR-227, AND MASSSPECTROMETRY.

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