DGAT2_YEAST - dbPTM
DGAT2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DGAT2_YEAST
UniProt AC Q08650
Protein Name Diacylglycerol O-acyltransferase 1
Gene Name DGA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 418
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Lipid droplet.
Protein Description Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis. May be involved in lipid particle synthesis from the endoplasmic reticulum and ergosterol biosynthesis. Also has monoacylglycerol acyltransferase (MGAT) activity, catalyzing the acyl-CoA-dependent esterification of monoacylglycerol to diacylglycerol..
Protein Sequence MSGTFNDIRRRKKEEGSPTAGITERHENKSLSSIDKREQTLKPQLESCCPLATPFERRLQTLAVAWHTSSFVLFSIFTLFAISTPALWVLAIPYMIYFFFDRSPATGEVVNRYSLRFRSLPIWKWYCDYFPISLIKTVNLKPTFTLSKNKRVNEKNYKIRLWPTKYSINLKSNSTIDYRNQECTGPTYLFGYHPHGIGALGAFGAFATEGCNYSKIFPGIPISLMTLVTQFHIPLYRDYLLALGISSVSRKNALRTLSKNQSICIVVGGARESLLSSTNGTQLILNKRKGFIKLAIQTGNINLVPVFAFGEVDCYNVLSTKKDSVLGKMQLWFKENFGFTIPIFYARGLFNYDFGLLPFRAPINVVVGRPIYVEKKITNPPDDVVNHFHDLYIAELKRLYYENREKYGVPDAELKIVG
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
4Phosphorylation----MSGTFNDIRRR
----CCCCHHHHHHH		16.3824961812
12UbiquitinationFNDIRRRKKEEGSPT
HHHHHHHHHHCCCCC		63.8324961812
13UbiquitinationNDIRRRKKEEGSPTA
HHHHHHHHHCCCCCC		60.2224961812
17PhosphorylationRRKKEEGSPTAGITE
HHHHHCCCCCCCCCH		23.5117330950
19PhosphorylationKKEEGSPTAGITERH
HHHCCCCCCCCCHHH		38.9324961812
29UbiquitinationITERHENKSLSSIDK
CCHHHCCCCCCCCCH		50.1924961812
33PhosphorylationHENKSLSSIDKREQT
HCCCCCCCCCHHHHH		39.8530377154
141UbiquitinationLIKTVNLKPTFTLSK
HEEEECCCCCEEECC		36.4924961812
173N-linked_GlycosylationYSINLKSNSTIDYRN
EEEECCCCCEEEECC		41.40-
258PhosphorylationKNALRTLSKNQSICI
HHHHHHHCCCCEEEE		29.0227017623
260N-linked_GlycosylationALRTLSKNQSICIVV
HHHHHCCCCEEEEEE		37.14-
277PhosphorylationARESLLSSTNGTQLI
HHHHHHHCCCCCEEE		26.3427017623
278PhosphorylationRESLLSSTNGTQLIL
HHHHHHCCCCCEEEE		34.0027017623
279N-linked_GlycosylationESLLSSTNGTQLILN
HHHHHCCCCCEEEEC		54.16-
281PhosphorylationLLSSTNGTQLILNKR
HHHCCCCCEEEECCC		23.4427017623
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 DGAT2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DGAT2_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 DGAT2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDAT_YEASTLRO1genetic
11751875
ARE1_YEASTARE1genetic
11741946
ARE2_YEASTARE2genetic
11741946
PDAT_YEASTLRO1genetic
11741946
BFR1_YEASTBFR1genetic
16269340
DOP1_YEASTDOP1genetic
16269340
GET2_YEASTGET2genetic
16269340
DGK1_YEASTDGK1genetic
16269340
TSC3_YEASTTSC3genetic
16269340
RDL1_YEASTRDL1genetic
16269340
ACO1_YEASTOLE1genetic
16269340
ICE2_YEASTICE2genetic
16269340
PMA1_YEASTPMA1genetic
16269340
PDAT_YEASTLRO1genetic
16269340
MTC4_YEASTMTC4genetic
16269340
PDAT_YEASTLRO1genetic
19608739
PDAT_YEASTLRO1genetic
19690167
BFR1_YEASTBFR1genetic
19690167
DOP1_YEASTDOP1genetic
19690167
GET2_YEASTGET2genetic
19690167
DGK1_YEASTDGK1genetic
19690167
TSC3_YEASTTSC3genetic
19690167
RDL1_YEASTRDL1genetic
19690167
ACO1_YEASTOLE1genetic
19690167
ICE2_YEASTICE2genetic
19690167
CHO2_YEASTCHO2genetic
19690167
RLA1_YEASTRPP1Agenetic
20093466
PHO23_YEASTPHO23genetic
20093466
PDAT_YEASTLRO1genetic
20554061
PDAT_YEASTLRO1genetic
20526336
PAH1_YEASTPAH1genetic
21422231
PDAT_YEASTLRO1genetic
21693588
SSB1_YEASTSSB1physical
22940862
SNF2_YEASTSNF2genetic
23613035
TGL5_YEASTTGL5genetic
25461829
TGL3_YEASTTGL3genetic
25461829
ARE1_YEASTARE1genetic
25500271
ARE2_YEASTARE2genetic
25500271
CSN12_YEASTYJR084Wgenetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
VAM7_YEASTVAM7genetic
27708008
ATG32_YEASTATG32genetic
27708008
DAL81_YEASTDAL81genetic
27708008
PCY1_YEASTPCT1genetic
26269581
DGK1_YEASTDGK1genetic
26269581
TOR1_YEASTTOR1genetic
26907989
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DGAT2_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-17, AND MASSSPECTROMETRY.
"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-17, AND MASSSPECTROMETRY.

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