G3P1_YEAST - dbPTM
G3P1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID G3P1_YEAST
UniProt AC P00360
Protein Name Glyceraldehyde-3-phosphate dehydrogenase 1
Gene Name TDH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 332
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MIRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSAPMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSMTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLEKEATYDQIKKAVKAAAEGPMKGVLGYTEDAVVSSDFLGDTHASIFDASAGIQLSPKFVKLISWYDNEYGYSARVVDLIEYVAKA
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
24AcetylationLRLALQRKDIEVVAV
HHHHHHCCCCEEEEE		50.5324489116
43PhosphorylationISNDYAAYMVKYDST
CCCCCEEEEEEEECC		8.3528889911
50PhosphorylationYMVKYDSTHGRYKGT
EEEEEECCCCEEECE		26.0025752575
63AcetylationGTVSHDDKHIIIDGV
CEECCCCCEEEECCE		42.6424489116
71AcetylationHIIIDGVKIATYQER
EEEECCEEEEEECCC		31.9522865919
71UbiquitinationHIIIDGVKIATYQER
EEEECCEEEEEECCC		31.9517644757
87PhosphorylationPANLPWGSLKIDVAV
CCCCCCCCEEEEEEE		23.7122369663
89UbiquitinationNLPWGSLKIDVAVDS
CCCCCCEEEEEEECC		38.2617644757
101UbiquitinationVDSTGVFKELDTAQK
ECCCCCCCCHHHHHH		55.7724961812
101AcetylationVDSTGVFKELDTAQK
ECCCCCCCCHHHHHH		55.7724489116
108UbiquitinationKELDTAQKHIDAGAK
CCHHHHHHHHHCCCC		39.8123749301
115UbiquitinationKHIDAGAKKVVITAP
HHHHCCCCEEEEECC		45.2222817900
116UbiquitinationHIDAGAKKVVITAPS
HHHCCCCEEEEECCC		41.0022817900
120PhosphorylationGAKKVVITAPSSSAP
CCCEEEEECCCCCCC		22.3922369663
123PhosphorylationKVVITAPSSSAPMFV
EEEEECCCCCCCEEE		34.1722369663
124PhosphorylationVVITAPSSSAPMFVV
EEEECCCCCCCEEEE		29.4722369663
125PhosphorylationVITAPSSSAPMFVVG
EEECCCCCCCEEEEE		40.5022369663
136PhosphorylationFVVGVNHTKYTPDKK
EEEECCCCEECCCCC		22.1222369663
137AcetylationVVGVNHTKYTPDKKI
EEECCCCEECCCCCC		39.3124489116
142AcetylationHTKYTPDKKIVSNAS
CCEECCCCCCCCCCC		45.6724489116
143UbiquitinationTKYTPDKKIVSNASC
CEECCCCCCCCCCCC		56.5817644757
146PhosphorylationTPDKKIVSNASCTTN
CCCCCCCCCCCCCCC		30.1022890988
149PhosphorylationKKIVSNASCTTNCLA
CCCCCCCCCCCCCHH		19.0822369663
151PhosphorylationIVSNASCTTNCLAPL
CCCCCCCCCCCHHHH		20.6722369663
152PhosphorylationVSNASCTTNCLAPLA
CCCCCCCCCCHHHHH		28.4122369663
160UbiquitinationNCLAPLAKVINDAFG
CCHHHHHHHHHHHHC		51.8617644757
174PhosphorylationGIEEGLMTTVHSMTA
CCCCCCCCCHHEEEE		30.6121440633
175PhosphorylationIEEGLMTTVHSMTAT
CCCCCCCCHHEEEEE		11.4022369663
178PhosphorylationGLMTTVHSMTATQKT
CCCCCHHEEEEEECC		17.3122369663
180PhosphorylationMTTVHSMTATQKTVD
CCCHHEEEEEECCCC		29.5722369663
182PhosphorylationTVHSMTATQKTVDGP
CHHEEEEEECCCCCC		22.7920377248
184AcetylationHSMTATQKTVDGPSH
HEEEEEECCCCCCCC		46.27-
184UbiquitinationHSMTATQKTVDGPSH
HEEEEEECCCCCCCC		46.2724961812
185PhosphorylationSMTATQKTVDGPSHK
EEEEEECCCCCCCCC		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
244PhosphorylationDVSVVDLTVKLEKEA
CEEEEEEEEEEEECC		15.9021440633
246UbiquitinationSVVDLTVKLEKEATY
EEEEEEEEEEECCCH		45.7717644757
249SuccinylationDLTVKLEKEATYDQI
EEEEEEEECCCHHHH		64.1923954790
249AcetylationDLTVKLEKEATYDQI
EEEEEEEECCCHHHH		64.1924489116
257AcetylationEATYDQIKKAVKAAA
CCCHHHHHHHHHHHH		29.1024489116
257SuccinylationEATYDQIKKAVKAAA
CCCHHHHHHHHHHHH		29.1023954790
291PhosphorylationFLGDTHASIFDASAG
CCCCCCHHCEECCCC		19.0417287358
302PhosphorylationASAGIQLSPKFVKLI
CCCCCCCCHHHHHHE		15.0727214570
310PhosphorylationPKFVKLISWYDNEYG
HHHHHHEECCCCCCC		29.9817287358
331SuccinylationDLIEYVAKA------
HHHHHHHHC------		44.5823954790
331AcetylationDLIEYVAKA------
HHHHHHHHC------		44.5824489116
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 G3P1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of G3P1_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 G3P1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G3P3_YEASTTDH3physical
16429126
GRP78_YEASTKAR2physical
16429126
G3P2_YEASTTDH2genetic
16941010
G3P3_YEASTTDH3genetic
16941010
SIR2_YEASTSIR2genetic
19390637
HST2_YEASTHST2genetic
19390637
YG5B_YEASTYGR250Cgenetic
20093466
SOK2_YEASTSOK2genetic
20093466
NST1_YEASTNST1genetic
20093466
G3P2_YEASTTDH2genetic
19390637
G3P3_YEASTTDH3genetic
19390637
DCOR_YEASTSPE1genetic
21623372
CDC1_YEASTCDC1genetic
27708008
ACT_YEASTACT1genetic
27708008
PRP18_YEASTPRP18genetic
27708008
MED6_YEASTMED6genetic
27708008
ORC1_YEASTORC1genetic
27708008
GOSR1_YEASTGOS1genetic
27708008
UBX2_YEASTUBX2genetic
27708008
RAS2_YEASTRAS2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of G3P1_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 TYR-43; SER-124; SER-125 ANDTHR-182, 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-199; SER-201; SER-207;SER-208; SER-291 AND SER-310, AND MASS 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 AND SER-201, ANDMASS SPECTROMETRY.

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