EDC3_YEAST - dbPTM
EDC3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDC3_YEAST
UniProt AC P39998
Protein Name Enhancer of mRNA-decapping protein 3
Gene Name EDC3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 551
Subcellular Localization Cytoplasm, P-body . Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay.
Protein Description Stimulates decapping of both stable and unstable mRNA during mRNA decay. Does not affect nonsense-mediated mRNA decay. Required for normal P-body assembly..
Protein Sequence MSQFVGFGVQVELKDGKLIQGKIAKATSKGLTLNDVQFGDGGKSQAFKVRASRLKDLKVLTVASQSGKRKQQRQQQQQNDYNQNRGEHIDWQDDDVSKIKQQEDFDFQRNLGMFNKKDVFAQLKQNDDILPENRLQGHNRKQTQLQQNNYQNDELVIPDAKKDSWNKISSRNEQSTHQSQPQQDAQDDLVLEDDEHEYDVDDIDDPKYLPITQSLNITHLIHSATNSPSINDKTKGTVINDKDQVLAKLGQMIISQSRSNSTSLPAANKQTTIRSKNTKQNIPMATPVQLLEMESITSEFFSINSAGLLENFAVNASFFLKQKLGGRARLRLQNSNPEPLVVILASDSNRSGAKALALGRHLCQTGHIRVITLFTCSQNELQDSMVKKQTDIYKKCGGKIVNSVSSLESAMETLNSPVEIVIDAMQGYDCTLSDLAGTSEVIESRIKSMISWCNKQRGSTKVWSLDIPNGFDAGSGMPDIFFSDRIEATGIICSGWPLIAINNLIANLPSLEDAVLIDIGIPQGAYSQRTSLRKFQNCDLFVTDGSLLLDL
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
43AcetylationVQFGDGGKSQAFKVR
EECCCCCCCHHEEEE		44.9424489116
143PhosphorylationQGHNRKQTQLQQNNY
CCCCHHHHHHHHHCC		33.9923749301
175PhosphorylationISSRNEQSTHQSQPQ
CCCCCCCCCCCCCCC		22.9819779198
179PhosphorylationNEQSTHQSQPQQDAQ
CCCCCCCCCCCCCHH		35.9021551504
223PhosphorylationNITHLIHSATNSPSI
EEHHEEECCCCCCCC		29.7820377248
225PhosphorylationTHLIHSATNSPSIND
HHEEECCCCCCCCCC		38.9621440633
227PhosphorylationLIHSATNSPSINDKT
EEECCCCCCCCCCCC		18.7020377248
229PhosphorylationHSATNSPSINDKTKG
ECCCCCCCCCCCCCC		33.5719779198
233AcetylationNSPSINDKTKGTVIN
CCCCCCCCCCCEEEC		47.8824489116
242AcetylationKGTVINDKDQVLAKL
CCEEECCHHHHHHHH		45.6424489116
255PhosphorylationKLGQMIISQSRSNST
HHHHHHHHCCCCCCC		15.9222369663
257PhosphorylationGQMIISQSRSNSTSL
HHHHHHCCCCCCCCC		30.7722369663
259PhosphorylationMIISQSRSNSTSLPA
HHHHCCCCCCCCCCC		40.1422369663
261PhosphorylationISQSRSNSTSLPAAN
HHCCCCCCCCCCCCC		22.1825521595
262PhosphorylationSQSRSNSTSLPAANK
HCCCCCCCCCCCCCC		38.2322369663
263PhosphorylationQSRSNSTSLPAANKQ
CCCCCCCCCCCCCCC		31.9822890988
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 EDC3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDC3_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 EDC3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCP2_YEASTDCP2physical
10900456
FIR1_YEASTFIR1physical
10900456
HIR3_YEASTHIR3physical
10900456
SEF1_YEASTSEF1physical
10900456
SKT5_YEASTSKT5physical
10900456
SPT6_YEASTSPT6physical
10900456
SRL2_YEASTSRL2physical
10900456
XRN1_YEASTXRN1physical
10900456
EDC3_YEASTEDC3physical
10900456
DSE1_YEASTDSE1physical
10900456
EDC3_YEASTEDC3physical
11967834
SKI3_YEASTSKI3genetic
15020463
SKI8_YEASTSKI8genetic
15020463
DCP2_YEASTDCP2physical
16554755
DCP1_YEASTDCP1physical
16429126
DCP2_YEASTDCP2physical
16429126
XRN1_YEASTXRN1physical
16429126
TTL_YEASTPBY1physical
16429126
EDC3_YEASTEDC3physical
11283351
RS28B_YEASTRPS28Bphysical
11283351
DCP1_YEASTDCP1physical
11283351
EDC3_YEASTEDC3physical
17984320
DCP1_YEASTDCP1physical
17984320
DHH1_YEASTDHH1physical
17984320
DCP2_YEASTDCP2physical
17984320
DCP2_YEASTDCP2physical
18467557
LSM4_YEASTLSM4physical
18467557
SCD6_YEASTSCD6genetic
18408161
EDC1_YEASTEDC1genetic
18408161
PBP4_YEASTPBP4genetic
18408161
PBP1_YEASTPBP1genetic
18408161
LSM12_YEASTLSM12genetic
18408161
TTL_YEASTPBY1physical
18408161
DHH1_YEASTDHH1physical
18408161
DCP2_YEASTDCP2physical
18408161
DCP1_YEASTDCP1physical
18408161
EF1A_YEASTTEF2physical
18408161
RL4A_YEASTRPL4Aphysical
18408161
RLA0_YEASTRPP0physical
18408161
EFGM_YEASTMEF1genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
BRR1_YEASTBRR1genetic
19061648
SYNC_YEASTDED81genetic
19061648
IF2G_YEASTGCD11genetic
19061648
LSM4_YEASTLSM4genetic
19061648
LCP5_YEASTLCP5genetic
19061648
CHD1_YEASTCHD1genetic
19061648
PABP_YEASTPAB1genetic
19061648
CAK1_YEASTCAK1genetic
19061648
LSM7_YEASTLSM7genetic
19061648
DCP2_YEASTDCP2physical
20832728
EDC3_YEASTEDC3physical
22940862
RS28A_YEASTRPS28Aphysical
23956223
DCP2_YEASTDCP2physical
23956223
DHH1_YEASTDHH1physical
23956223
PAT1_YEASTPAT1physical
24830408
DHH1_YEASTDHH1physical
23851565
LSM4_YEASTLSM4genetic
27543059
SNF5_YEASTSNF5genetic
27708008
CHO2_YEASTCHO2genetic
27708008
DAL81_YEASTDAL81genetic
27708008
SAC1_YEASTSAC1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
DIA2_YEASTDIA2genetic
27708008
SCD6_YEASTSCD6genetic
27708008
HRR25_YEASTHRR25physical
27182950
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EDC3_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-257 AND SER-261, ANDMASS SPECTROMETRY.
"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 SER-257 AND SER-261, ANDMASS 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-257, AND MASSSPECTROMETRY.

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