GPP1_YEAST - dbPTM
GPP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPP1_YEAST
UniProt AC P41277
Protein Name Glycerol-1-phosphate phosphohydrolase 1 {ECO:0000305}
Gene Name GPP1 {ECO:0000303|PubMed:8662716}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 250
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Major isoform of glycerol-1-phosphate phosphohydrolase involved in glycerol biosynthesis. Plays a role in osmoadaptation and required for adaptation to anaerobic conditions..
Protein Sequence MPLTTKPLSLKINAALFDVDGTIIISQPAIAAFWRDFGKDKPYFDAEHVIHISHGWRTYDAIAKFAPDFADEEYVNKLEGEIPEKYGEHSIEVPGAVKLCNALNALPKEKWAVATSGTRDMAKKWFDILKIKRPEYFITANDVKQGKPHPEPYLKGRNGLGFPINEQDPSKSKVVVFEDAPAGIAAGKAAGCKIVGIATTFDLDFLKEKGCDIIVKNHESIRVGEYNAETDEVELIFDDYLYAKDDLLKW
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
9PhosphorylationPLTTKPLSLKINAAL
CCCCCCEEEEECEEE		35.8222369663
58PhosphorylationHISHGWRTYDAIAKF
EEECCCEEHHHHHHH		21.1717287358
64SumoylationRTYDAIAKFAPDFAD
EEHHHHHHHCCCCCC		35.6315166219
64AcetylationRTYDAIAKFAPDFAD
EEHHHHHHHCCCCCC		35.6324489116
64UbiquitinationRTYDAIAKFAPDFAD
EEHHHHHHHCCCCCC		35.6324961812
64SumoylationRTYDAIAKFAPDFAD
EEHHHHHHHCCCCCC		35.63-
77AcetylationADEEYVNKLEGEIPE
CCHHHHHHHCCCCCH		37.5624489116
85AcetylationLEGEIPEKYGEHSIE
HCCCCCHHHCCCCEE		53.8824489116
90PhosphorylationPEKYGEHSIEVPGAV
CHHHCCCCEECCHHH		19.0121440633
115PhosphorylationKEKWAVATSGTRDMA
HHHHEEECCCCHHHH		22.5322369663
116PhosphorylationEKWAVATSGTRDMAK
HHHEEECCCCHHHHH		28.5622369663
118PhosphorylationWAVATSGTRDMAKKW
HEEECCCCHHHHHHH		24.2222369663
124AcetylationGTRDMAKKWFDILKI
CCHHHHHHHHHHHCC		43.4824489116
130UbiquitinationKKWFDILKIKRPEYF
HHHHHHHCCCCCCEE		46.6523749301
130AcetylationKKWFDILKIKRPEYF
HHHHHHHCCCCCCEE		46.6524489116
132UbiquitinationWFDILKIKRPEYFIT
HHHHHCCCCCCEEEE		61.3824961812
136PhosphorylationLKIKRPEYFITANDV
HCCCCCCEEEEHHHH		11.7219779198
139PhosphorylationKRPEYFITANDVKQG
CCCCEEEEHHHHCCC		14.9819779198
144UbiquitinationFITANDVKQGKPHPE
EEEHHHHCCCCCCCC		57.0822106047
144AcetylationFITANDVKQGKPHPE
EEEHHHHCCCCCCCC		57.08-
155UbiquitinationPHPEPYLKGRNGLGF
CCCCCCCCCCCCCCC		50.4022817900
171UbiquitinationINEQDPSKSKVVVFE
CCCCCCCCCEEEEEE		60.7322817900
172PhosphorylationNEQDPSKSKVVVFED
CCCCCCCCEEEEEEC		34.7121440633
173UbiquitinationEQDPSKSKVVVFEDA
CCCCCCCEEEEEECC		42.6723749301
188UbiquitinationPAGIAAGKAAGCKIV
CCCHHCHHHCCCEEE		30.2723749301
216UbiquitinationKGCDIIVKNHESIRV
CCCCEEECCCCCEEE		42.0223749301
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 GPP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPP1_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 GPP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPP2_YEASTGPP2genetic
11058591
YIG1_YEASTYIG1physical
11283351
YIG1_YEASTYIG1physical
18719252
HSP7F_YEASTSSE1physical
19536198
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
GPP2_YEASTGPP2genetic
18408719
INO2_YEASTINO2genetic
20093466
GPP2_YEASTGPP2genetic
20093466
CSK2B_YEASTCKB1genetic
20093466
RS23A_YEASTRPS23Agenetic
20093466
RS23B_YEASTRPS23Agenetic
20093466
UBCX_YEASTPEX4genetic
20093466
CHO2_YEASTCHO2genetic
20093466
VPS55_YEASTVPS55genetic
20093466
STE24_YEASTSTE24genetic
20093466
DCOR_YEASTSPE1genetic
20093466
NGL2_YEASTNGL2genetic
20093466
EOS1_YEASTEOS1genetic
20093466
YNB0_YEASTYNL010Wgenetic
20093466
ASI3_YEASTASI3genetic
20093466
CSK2C_YEASTCKB2genetic
20093466
AZF1_YEASTAZF1genetic
20093466
DGK1_YEASTDGK1genetic
20093466
ALG5_YEASTALG5genetic
20093466
ATG13_YEASTATG13genetic
20093466
SSD1_YEASTSSD1genetic
17390123
FLO8_YEASTFLO8genetic
17390123
WSC3_YEASTWSC3genetic
17390123
KPC1_YEASTPKC1genetic
17390123
WSC2_YEASTWSC2genetic
17390123
SMP1_YEASTSMP1physical
21193057
GPP2_YEASTGPP2genetic
21623372
FOLE_YEASTMET7genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
COQ4_YEASTCOQ4genetic
21623372
KCS1_YEASTKCS1genetic
21623372
THRC_YEASTTHR4genetic
21623372
NHP10_YEASTNHP10genetic
27708008
KPR4_YEASTPRS4genetic
27708008
SNF1_YEASTSNF1genetic
27708008
GPP2_YEASTGPP2genetic
27708008
UBP3_YEASTUBP3genetic
27708008
CSK2B_YEASTCKB1genetic
27708008
UBCX_YEASTPEX4genetic
27708008
SNF6_YEASTSNF6genetic
27708008
STE24_YEASTSTE24genetic
27708008
VPS24_YEASTVPS24genetic
27708008
MAC1_YEASTMAC1genetic
27708008
NGL2_YEASTNGL2genetic
27708008
EOS1_YEASTEOS1genetic
27708008
LEU1_YEASTLEU4genetic
27708008
RTG1_YEASTRTG1genetic
27708008
CSK2C_YEASTCKB2genetic
27708008
AZF1_YEASTAZF1genetic
27708008
YME1_YEASTYME1genetic
27708008
ATG13_YEASTATG13genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPP1_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-9, 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 THR-58, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"Global analyses of sumoylated proteins in Saccharomyces cerevisiae.Induction of protein sumoylation by cellular stresses.";
Zhou W., Ryan J.J., Zhou H.;
J. Biol. Chem. 279:32262-32268(2004).
Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND MASS SPECTROMETRY.

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