GPD2_YEAST - dbPTM
GPD2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPD2_YEAST
UniProt AC P41911
Protein Name Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrial
Gene Name GPD2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 440
Subcellular Localization Cytoplasm. Mitochondrion.
Protein Description Catalyzes the production of glycerol under anaerobic growth conditions. Glycerol production serves as a redox sink by consuming the excess cytosolic NADH during anaerobic metabolism..
Protein Sequence MLAVRRLTRYTFLKRTHPVLYTRRAYKILPSRSTFLRRSLLQTQLHSKMTAHTNIKQHKHCHEDHPIRRSDSAVSIVHLKRAPFKVTVIGSGNWGTTIAKVIAENTELHSHIFEPEVRMWVFDEKIGDENLTDIINTRHQNVKYLPNIDLPHNLVADPDLLHSIKGADILVFNIPHQFLPNIVKQLQGHVAPHVRAISCLKGFELGSKGVQLLSSYVTDELGIQCGALSGANLAPEVAKEHWSETTVAYQLPKDYQGDGKDVDHKILKLLFHRPYFHVNVIDDVAGISIAGALKNVVALACGFVEGMGWGNNASAAIQRLGLGEIIKFGRMFFPESKVETYYQESAGVADLITTCSGGRNVKVATYMAKTGKSALEAEKELLNGQSAQGIITCREVHEWLQTCELTQEFPLFEAVYQIVYNNVRMEDLPEMIEELDIDDE
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
70PhosphorylationEDHPIRRSDSAVSIV
CCCCCCCCCCCEEEE		26.5222369663
72PhosphorylationHPIRRSDSAVSIVHL
CCCCCCCCCEEEEEE		31.6422369663
75PhosphorylationRRSDSAVSIVHLKRA
CCCCCCEEEEEECCC		20.7122369663
80AcetylationAVSIVHLKRAPFKVT
CEEEEEECCCCEEEE		31.4724489116
80UbiquitinationAVSIVHLKRAPFKVT
CEEEEEECCCCEEEE		31.4717644757
85UbiquitinationHLKRAPFKVTVIGSG
EECCCCEEEEEEECC		35.6217644757
100UbiquitinationNWGTTIAKVIAENTE
CHHHHHHHHHHHCCC		30.2617644757
125UbiquitinationRMWVFDEKIGDENLT
EEEEEECCCCCCCHH		54.5617644757
143UbiquitinationNTRHQNVKYLPNIDL
HCCCCCCCCCCCCCC		48.9317644757
165UbiquitinationPDLLHSIKGADILVF
HHHHHHCCCCCEEEE		51.5717644757
184UbiquitinationQFLPNIVKQLQGHVA
HHHHHHHHHHCCCCC		41.3017644757
201AcetylationVRAISCLKGFELGSK
HHHHHHHCCCCCCHH		66.9224489116
207PhosphorylationLKGFELGSKGVQLLS
HCCCCCCHHHHHHHH		38.5727017623
243PhosphorylationEVAKEHWSETTVAYQ
HHHHHHHCCEEEEEE		27.2919684113
253AcetylationTVAYQLPKDYQGDGK
EEEEECCCCCCCCCC		77.1124489116
260AcetylationKDYQGDGKDVDHKIL
CCCCCCCCCCCHHHH		60.3624489116
265AcetylationDGKDVDHKILKLLFH
CCCCCCHHHHHHHHC		45.3224489116
268AcetylationDVDHKILKLLFHRPY
CCCHHHHHHHHCCCC		46.7624489116
327UbiquitinationLGLGEIIKFGRMFFP
HCHHHHHHHCCCCCC		47.6417644757
327AcetylationLGLGEIIKFGRMFFP
HCHHHHHHHCCCCCC		47.6424489116
337UbiquitinationRMFFPESKVETYYQE
CCCCCHHHHHHHHHC		42.2917644757
369UbiquitinationKVATYMAKTGKSALE
EEEEEEHHHCHHHHH		41.0823749301
372UbiquitinationTYMAKTGKSALEAEK
EEEHHHCHHHHHHHH		37.4722817900
379UbiquitinationKSALEAEKELLNGQS
HHHHHHHHHHHCCCC		61.7915699485
379AcetylationKSALEAEKELLNGQS
HHHHHHHHHHHCCCC		61.7924489116
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 GPD2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPD2_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 GPD2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNA1_YEASTGNA1physical
10688190
H2A2_YEASTHTA2physical
16554755
IF5A1_YEASTHYP2physical
16554755
ZUO1_YEASTZUO1physical
16554755
AHP1_YEASTAHP1physical
16554755
STM1_YEASTSTM1physical
16554755
FPS1_YEASTFPS1genetic
15611083
MRP8_YEASTMRP8physical
18719252
NAP1_YEASTNAP1physical
18719252
RIM11_YEASTRIM11physical
18719252
GPD1_YEASTGPD1genetic
18408719
FUMH_YEASTFUM1genetic
21623372
PROA_YEASTPRO2genetic
21623372
PPT2_YEASTPPT2genetic
21623372
TPS2_YEASTTPS2genetic
21623372
METX_YEASTYML082Wgenetic
21623372
KCS1_YEASTKCS1genetic
21623372
GPP2_YEASTGPP2genetic
21623372
ARE1_YEASTARE1genetic
21623372
PDX3_YEASTPDX3genetic
21623372
GPD1_YEASTGPD1genetic
21623372
ETR1_YEASTETR1genetic
21623372
FADH_YEASTSFA1genetic
21623372
TKT1_YEASTTKL1genetic
21623372
ARGJ_YEASTARG7genetic
21623372
AATC_YEASTAAT2genetic
21623372
DHSO1_YEASTSOR1genetic
21720823
GRE3_YEASTGRE3genetic
21720823
ADH1_YEASTADH1genetic
22161213
PDC1_YEASTPDC1genetic
22161213
STL1_YEASTSTL1genetic
23801122
MAL12_YEASTMAL12genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
EIF3J_YEASTHCR1genetic
27708008
LTE1_YEASTLTE1genetic
27708008
PEX22_YEASTPEX22genetic
27708008
BUD31_YEASTBUD31genetic
27708008
PEX19_YEASTPEX19genetic
27708008
VAM6_YEASTVAM6genetic
27708008
TAPT1_YEASTEMP65genetic
27708008
YFF2_YEASTYFL052Wgenetic
27708008
MED5_YEASTNUT1genetic
27708008
PEX14_YEASTPEX14genetic
27708008
STF2_YEASTSTF2genetic
27708008
VMA21_YEASTVMA21genetic
27708008
UBCX_YEASTPEX4genetic
27708008
SNF6_YEASTSNF6genetic
27708008
THIK_YEASTPOT1genetic
27708008
DAL81_YEASTDAL81genetic
27708008
MNN11_YEASTMNN11genetic
27708008
PEX2_YEASTPEX2genetic
27708008
CBT1_YEASTCBT1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
PEX13_YEASTPEX13genetic
27708008
COA4_YEASTCOA4genetic
27708008
PEX12_YEASTPEX12genetic
27708008
FUS2_YEASTFUS2genetic
27708008
TDA1_YEASTTDA1genetic
27708008
PUB1_YEASTPUB1genetic
27708008
APP1_YEASTAPP1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
SRO7_YEASTSRO7genetic
27708008
UBA3_YEASTUBA3genetic
27708008
CACO2_HUMANCALCOCO2physical
27107014
CEP70_HUMANCEP70physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPD2_YEAST

loading...

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-70; SER-72 AND SER-75,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-72 AND SER-75, AND MASSSPECTROMETRY.
"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-70; SER-72 AND SER-75,AND MASS SPECTROMETRY.
"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-72 AND SER-75, AND MASSSPECTROMETRY.
"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-72 AND SER-75, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory