PGPS1_YEAST - dbPTM
PGPS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGPS1_YEAST
UniProt AC P25578
Protein Name CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
Gene Name PGS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 521
Subcellular Localization Mitochondrion .
Protein Description Essential for the viability of mitochondrial petite mutant. Catalyzes the committed step to the synthesis of the acidic phospholipids..
Protein Sequence MTTRLLQLTRPHYRLLSLPLQKPFNIKRQMSAANPSPFGNYLNTITKSLQQNLQTCFHFQAKEIDIIESPSQFYDLLKTKILNSQNRIFIASLYLGKSETELVDCISQALTKNPKLKVSFLLDGLRGTRELPSACSATLLSSLVAKYGSERVDCRLYKTPAYHGWKKVLVPKRFNEGLGLQHMKIYGFDNEVILSGANLSNDYFTNRQDRYYLFKSRNFSNYYFKLHQLISSFSYQIIKPMVDGSINIIWPDSNPTVEPTKNKRLFLREASQLLDGFLKSSKQSLPITAVGQFSTLVYPISQFTPLFPKYNDKSTEKRTILSLLSTITSNAISWTFTAGYFNILPDIKAKLLATPVAEANVITASPFANGFYQSKGVSSNLPGAYLYLSKKFLQDVCRYRQDHAITLREWQRGVVNKPNGWSYHAKGIWLSARDKNDANNWKPFITVIGSSNYTRRAYSLDLESNALIITRDEELRKKMKAELDNLLQYTKPVTLEDFQSDPERHVGTGVKIATSILGKKL
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
159PhosphorylationVDCRLYKTPAYHGWK
EEEEEEECCCCCCCE
10.2928889911
508PhosphorylationDPERHVGTGVKIATS
CHHHCCCCCHHHHHH
37.4022890988
514PhosphorylationGTGVKIATSILGKKL
CCCHHHHHHHHCCCC
21.5522890988
515PhosphorylationTGVKIATSILGKKL-
CCHHHHHHHHCCCC-
13.5422890988

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 PGPS1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGPS1_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 PGPS1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRE5_YEASTKRE5genetic
15563612
ATH1_YEASTATH1genetic
19401462
GAC1_YEASTGAC1genetic
19401462
GPP2_YEASTGPP2genetic
19401462
HSP12_YEASTHSP12genetic
19401462
IML3_YEASTIML3genetic
19401462
MRK1_YEASTMRK1genetic
19401462
MSN2_YEASTMSN2genetic
19401462
PBS2_YEASTPBS2genetic
19401462
PIL1_YEASTPIL1genetic
19401462
PSR1_YEASTPSR1genetic
19401462
ROM2_YEASTROM2genetic
19401462
SHO1_YEASTSHO1genetic
19401462
SKN7_YEASTSKN7genetic
19401462
HSP72_YEASTSSA2genetic
19401462
SSK2_YEASTSSK2genetic
19401462
SSK22_YEASTSSK22genetic
19401462
STE50_YEASTSTE50genetic
19401462
WSC3_YEASTWSC3genetic
19401462
WSC4_YEASTWSC4genetic
19401462
AP1_YEASTYAP1genetic
19401462
KRE5_YEASTKRE5genetic
19401462
VPS41_YEASTVPS41genetic
20093466
SDHX_YEASTYJL045Wgenetic
20093466
YJ24_YEASTKCH1genetic
20093466
COX12_YEASTCOX12genetic
20093466
VRP1_YEASTVRP1genetic
20093466
YM30_YEASTYMR155Wgenetic
20093466
YNJ5_YEASTYNL095Cgenetic
20093466
TPM1_YEASTTPM1genetic
20093466
INO4_YEASTINO4genetic
20093466
VPH1_YEASTVPH1genetic
20093466
COX10_YEASTCOX10genetic
20093466
RL21B_YEASTRPL21Bgenetic
20093466
TAM41_YEASTTAM41genetic
20485265
ADT2_YEASTPET9genetic
16408847
UPS1_YEASTUPS1genetic
23042293

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGPS1_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-159, AND MASSSPECTROMETRY.

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