GPD1_YEAST - dbPTM
GPD1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPD1_YEAST
UniProt AC Q00055
Protein Name Glycerol-3-phosphate dehydrogenase [NAD(+)] 1
Gene Name GPD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 391
Subcellular Localization Cytoplasm. Peroxisome.
Protein Description Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells..
Protein Sequence MSAAADRLNLTSGHLNAGRKRSSSSVSLKAAEKPFKVTVIGSGNWGTTIAKVVAENCKGYPEVFAPIVQMWVFEEEINGEKLTEIINTRHQNVKYLPGITLPDNLVANPDLIDSVKDVDIIVFNIPHQFLPRICSQLKGHVDSHVRAISCLKGFEVGAKGVQLLSSYITEELGIQCGALSGANIATEVAQEHWSETTVAYHIPKDFRGEGKDVDHKVLKALFHRPYFHVSVIEDVAGISICGALKNVVALGCGFVEGLGWGNNASAAIQRVGLGEIIRFGQMFFPESREETYYQESAGVADLITTCAGGRNVKVARLMATSGKDAWECEKELLNGQSAQGLITCKEVHEWLETCGSVEDFPLFEAVYQIVYNNYPMKNLPDMIEELDLHED
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
2Acetylation------MSAAADRLN
------CCHHHHHHH		26.98-
2Phosphorylation------MSAAADRLN
------CCHHHHHHH		26.9822369663
11PhosphorylationAADRLNLTSGHLNAG
HHHHHHCCCCCCCCC		31.4329136822
12PhosphorylationADRLNLTSGHLNAGR
HHHHHCCCCCCCCCC		27.6429136822
20UbiquitinationGHLNAGRKRSSSSVS
CCCCCCCCCCCCCCC		56.5717644757
22PhosphorylationLNAGRKRSSSSVSLK
CCCCCCCCCCCCCEE		37.2922369663
23PhosphorylationNAGRKRSSSSVSLKA
CCCCCCCCCCCCEEE		30.5722369663
24PhosphorylationAGRKRSSSSVSLKAA
CCCCCCCCCCCEEEC		35.6922369663
25PhosphorylationGRKRSSSSVSLKAAE
CCCCCCCCCCEEECC		20.0622369663
27PhosphorylationKRSSSSVSLKAAEKP
CCCCCCCCEEECCCC		26.5422369663
332-HydroxyisobutyrylationVSLKAAEKPFKVTVI
CCEEECCCCEEEEEE		51.53-
36UbiquitinationKAAEKPFKVTVIGSG
EECCCCEEEEEEECC		45.5917644757
51UbiquitinationNWGTTIAKVVAENCK
CCHHHHHHHHHHHCC		33.1317644757
94UbiquitinationNTRHQNVKYLPGITL
HCCCCCCCCCCCCCC		48.9317644757
94AcetylationNTRHQNVKYLPGITL
HCCCCCCCCCCCCCC		48.9324489116
116UbiquitinationPDLIDSVKDVDIIVF
HHHHHHCCCCCEEEE		56.8617644757
138AcetylationPRICSQLKGHVDSHV
HHHHHHHCCCHHHHH		39.0622865919
152UbiquitinationVRAISCLKGFEVGAK
HHHHHHHCCCCCCHH		66.9224961812
152AcetylationVRAISCLKGFEVGAK
HHHHHHHCCCCCCHH		66.9224489116
211AcetylationKDFRGEGKDVDHKVL
CCCCCCCCCCCHHHH		50.7222865919
219AcetylationDVDHKVLKALFHRPY
CCCHHHHHHHHCCCC		46.1324489116
245UbiquitinationISICGALKNVVALGC
HHHHHHHHHHHHCCC		47.3517644757
323AcetylationRLMATSGKDAWECEK
EHHHCCCCCHHHHHH		44.0025381059
330AcetylationKDAWECEKELLNGQS
CCHHHHHHHHHCCCC		66.3824489116
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 GPD1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPD1_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 GPD1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPD2_YEASTGPD2genetic
15611083
GPD2_YEASTGPD2genetic
15127164
GPDM_YEASTGUT2genetic
9559543
MIG1_YEASTMIG1genetic
7729414
FPS1_YEASTFPS1genetic
15611083
GPD2_YEASTGPD2genetic
18032102
GPD2_YEASTGPD2genetic
20430884
AYR1_YEASTAYR1genetic
21623372
GDE_YEASTGDB1genetic
21623372
DHAS_YEASTHOM2genetic
21623372
GPD2_YEASTGPD2genetic
21623372
FAT1_YEASTFAT1genetic
21623372
ACEB_YEASTICL2genetic
21623372
6PGD1_YEASTGND1genetic
21623372
PPT2_YEASTPPT2genetic
21623372
ERG2_YEASTERG2genetic
21623372
GCSH_YEASTGCV3genetic
21623372
DHSO1_YEASTSOR1genetic
21720823
GRE3_YEASTGRE3genetic
21720823
GPD2_YEASTGPD2genetic
21724879
DHE4_YEASTGDH1genetic
21909679
GPD2_YEASTGPD2genetic
21944208
GPD2_YEASTGPD2genetic
23801122
STL1_YEASTSTL1genetic
23801122
GPD2_YEASTGPD2genetic
23891562
AYR1_YEASTAYR1genetic
23891562
GPD2_YEASTGPD2genetic
25401080
PNC1_YEASTPNC1physical
26516056
HOG1_YEASTHOG1genetic
26140985
ACT_YEASTACT1genetic
27708008
MED14_YEASTRGR1genetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
MOB2_YEASTMOB2genetic
27708008
SWC4_YEASTSWC4genetic
27708008
NTR2_YEASTNTR2genetic
27708008
SEC22_YEASTSEC22genetic
27708008
CAP_YEASTSRV2genetic
27708008
AIM11_YEASTAIM11genetic
27708008
TFS2_YEASTDST1genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
AYR1_YEASTAYR1genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
PRR1_YEASTPRR1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
GPT2_YEASTGPT2genetic
27708008
SRL3_YEASTSRL3genetic
27708008
MLP1_YEASTMLP1genetic
27708008
POM33_YEASTPOM33genetic
27708008
PUR91_YEASTADE16genetic
27708008
YL224_YEASTYLR224Wgenetic
27708008
SEI1_YEASTFLD1genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
TDA1_YEASTTDA1genetic
27708008
GAS1_YEASTGAS1genetic
27708008
PET8_YEASTPET8genetic
27708008
ERFD_YEASTSHR5genetic
27708008
PMP1_YEASTPMP1physical
26404137
GPD2_YEASTGPD2genetic
26156706
PNC1_YEASTPNC1physical
26276932
PEX3_YEASTPEX3genetic
28928432
PEX5_YEASTPEX5genetic
28928432
LYS1_YEASTLYS1genetic
28928432
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPD1_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-12; SER-24; SER-25 ANDSER-27, 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-23; SER-25 AND SER-27,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-24 AND SER-27, 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-24 AND SER-27, AND MASSSPECTROMETRY.

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