GPP2_YEAST - dbPTM
GPP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPP2_YEAST
UniProt AC P40106
Protein Name Glycerol-1-phosphate phosphohydrolase 2 {ECO:0000305}
Gene Name GPP2 {ECO:0000303|PubMed:8662716}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 250
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Glycerol-1-phosphate phosphohydrolase involved in glycerol biosynthesis. Plays a role in osmoadaptation..
Protein Sequence MGLTTKPLSLKVNAALFDVDGTIIISQPAIAAFWRDFGKDKPYFDAEHVIQVSHGWRTFDAIAKFAPDFANEEYVNKLEAEIPVKYGEKSIEVPGAVKLCNALNALPKEKWAVATSGTRDMAQKWFEHLGIRRPKYFITANDVKQGKPHPEPYLKGRNGLGYPINEQDPSKSKVVVFEDAPAGIAAGKAAGCKIIGIATTFDLDFLKEKGCDIIVKNHESIRVGGYNAETDEVEFIFDDYLYAKDDLLKW
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
39AcetylationAFWRDFGKDKPYFDA
HHHHHHCCCCCCCCH		63.6724489116
41AcetylationWRDFGKDKPYFDAEH
HHHHCCCCCCCCHHH		45.1424489116
64AcetylationRTFDAIAKFAPDFAN
CCHHHHHHHCCCCCC		35.6324489116
64UbiquitinationRTFDAIAKFAPDFAN
CCHHHHHHHCCCCCC		35.6324961812
77AcetylationANEEYVNKLEAEIPV
CCHHHHHHHEEECCC		37.3524489116
85AcetylationLEAEIPVKYGEKSIE
HEEECCCCCCCCEEE		42.0322865919
89AcetylationIPVKYGEKSIEVPGA
CCCCCCCCEEECCHH		52.9824489116
90PhosphorylationPVKYGEKSIEVPGAV
CCCCCCCEEECCHHH		21.49-
98AcetylationIEVPGAVKLCNALNA
EECCHHHHHHHHHHC		46.9524489116
108SuccinylationNALNALPKEKWAVAT
HHHHCCCHHHHEEEC		73.1623954790
108AcetylationNALNALPKEKWAVAT
HHHHCCCHHHHEEEC		73.1624489116
1102-HydroxyisobutyrylationLNALPKEKWAVATSG
HHCCCHHHHEEECCC		46.72-
110AcetylationLNALPKEKWAVATSG
HHCCCHHHHEEECCC		46.7222865919
115PhosphorylationKEKWAVATSGTRDMA
HHHHEEECCCCHHHH		22.5322369663
116PhosphorylationEKWAVATSGTRDMAQ
HHHEEECCCCHHHHH		28.5622369663
118PhosphorylationWAVATSGTRDMAQKW
HEEECCCCHHHHHHH		24.2222369663
124AcetylationGTRDMAQKWFEHLGI
CCHHHHHHHHHHCCC		44.2924489116
135AcetylationHLGIRRPKYFITAND
HCCCCCCCEEEEHHH		51.4824489116
144AcetylationFITANDVKQGKPHPE
EEEHHHHCCCCCCCC		57.0824489116
155AcetylationPHPEPYLKGRNGLGY
CCCCCCCCCCCCCCC		50.4022865919
155UbiquitinationPHPEPYLKGRNGLGY
CCCCCCCCCCCCCCC		50.4022817900
171AcetylationINEQDPSKSKVVVFE
CCCCCCCCCEEEEEE		60.7324489116
171UbiquitinationINEQDPSKSKVVVFE
CCCCCCCCCEEEEEE		60.7322817900
172PhosphorylationNEQDPSKSKVVVFED
CCCCCCCCEEEEEEC		34.7121440633
173AcetylationEQDPSKSKVVVFEDA
CCCCCCCEEEEEECC		42.6724489116
1732-HydroxyisobutyrylationEQDPSKSKVVVFEDA
CCCCCCCEEEEEECC		42.67-
173UbiquitinationEQDPSKSKVVVFEDA
CCCCCCCEEEEEECC		42.6723749301
188UbiquitinationPAGIAAGKAAGCKII
CCCHHCHHHCCCEEE		30.2723749301
207AcetylationTFDLDFLKEKGCDII
ECCHHHHHHCCCCEE		58.3225381059
209AcetylationDLDFLKEKGCDIIVK
CHHHHHHCCCCEEEE		64.3525381059
216UbiquitinationKGCDIIVKNHESIRV
CCCCEEEECCCCEEE		42.0223749301
216AcetylationKGCDIIVKNHESIRV
CCCCEEEECCCCEEE		42.0224489116
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 GPP2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPP2_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 GPP2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YIG1_YEASTYIG1physical
10688190
IES5_YEASTIES5genetic
19269370
CAX4_YEASTCAX4genetic
19269370
RIC1_YEASTRIC1genetic
19269370
CTK3_YEASTCTK3genetic
19269370
SGF29_YEASTSGF29genetic
20093466
RS27B_YEASTRPS27Bgenetic
20093466
GPP1_YEASTGPP1genetic
20093466
YPT7_YEASTYPT7genetic
20093466
PHO23_YEASTPHO23genetic
20093466
HSP7F_YEASTSSE1genetic
20093466
SSD1_YEASTSSD1genetic
17390123
FLO8_YEASTFLO8genetic
17390123
WSC3_YEASTWSC3genetic
17390123
WSC2_YEASTWSC2genetic
17390123
KPC1_YEASTPKC1genetic
17390123
SMP1_YEASTSMP1physical
21193057
GPP1_YEASTGPP1genetic
21623372
DHOM_YEASTHOM6genetic
21623372
GPP1_YEASTGPP1genetic
23891562
BCK1_YEASTBCK1genetic
23891562
SGF29_YEASTSGF29genetic
27708008
RV161_YEASTRVS161genetic
27708008
PEX19_YEASTPEX19genetic
27708008
AAKG_YEASTSNF4genetic
27708008
GPP1_YEASTGPP1genetic
27708008
SNX4_YEASTSNX4genetic
27708008
VPS24_YEASTVPS24genetic
27708008
YPT7_YEASTYPT7genetic
27708008
EOS1_YEASTEOS1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPP2_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 THR-115; SER-116 ANDTHR-118, AND MASS SPECTROMETRY.

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