Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Enhancer of mRNA-decapping protein 3  

UniProtKB / Swiss-Prot ID :  EDC3_HUMAN

Gene Name (Synonyms) : 
EDC3, LSM16, YJDC, YJEFN2 PP844  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, P-body. Note=Processing bodies (PB). 

Protein Function :  Binds single-stranded RNA. In the process of mRNA degradation, may play a role in mRNA decapping. May play a role in spermiogenesis and oogenesis. 

Protein Sequence MATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILEIPGP...
Predicted Secondary Structure CCCCCCCCEEEEECCCCCCEECCEEHHHHHCCCEEEECCCCCCCCEEEECEEEEECCCCCEEEEEEECCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
109PhosphoserineKKPASSSSA
CCCCCCCCC
39.00Phosphositeplus
Link-
125PhosphoserineTDVKSQDVA
CCCCCCCCC
31.31HPRD
Link-
125PhosphoserineTDVKSQDVA
CCCCCCCCC
31.31Phosphositeplus
Link-
131PhosphoserineDVAVSPQQQ
CCCCCCCCC
13.78HPRD
Link-
131PhosphoserineDVAVSPQQQ
CCCCCCCCC
13.78PhosphoELM
Link-
131PhosphoserineDVAVSPQQQ
CCCCCCCCC
13.78Phosphositeplus
Link-
131PhosphoserineDVAVSPQQQ
CCCCCCCCC
13.78SysPTM
Link-
131Phosphoserine.DVAVSPQQQ
CCCCCCCCC
13.78UniProtKB
Link-
138PhosphoserineQQQCSKSYV
CCHHHHHHH
21.94Phosphositeplus
Link-
140PhosphoserineQCSKSYVDR
HHHHHHHHH
17.69Phosphositeplus
Link-
150PhosphoserineMESLSQSKS
HHHHHCCCC
41.51HPRD
Link-
150PhosphoserineMESLSQSKS
HHHHHCCCC
41.51Phosphositeplus
Link-
161PhosphoserineRRHNSWSSS
HHHCCCCCC
23.39HPRD
Link-
161PhosphoserineRRHNSWSSS
HHHCCCCCC
23.39PhosphoELM
Link-
161PhosphoserineRRHNSWSSS
HHHCCCCCC
23.39Phosphositeplus
Link-
161PhosphoserineRRHNSWSSS
HHHCCCCCC
23.39SysPTM
Link-
161Phosphoserine.RRHNSWSSS
HHHCCCCCC
23.39UniProtKB
Link-
163PhosphoserineHNSWSSSSR
HCCCCCCCC
21.84Phosphositeplus
Link-
166PhosphoserineWSSSSRHPN
CCCCCCCCC
36.23Phosphositeplus
Link-
173PhosphothreoninePNQATPKKS
CCCCCCCCC
26.36Phosphositeplus
Link-
225PhosphotyrosineEIDTYERRS
HHHHHHCCC
12.04Phosphositeplus
Link-
258PhosphotyrosineEPIVYRRII
CCEEEEEEE
8.56Phosphositeplus
Link-
308PhosphothreonineRLEMTGVCA
HHHHHHHHH
19.65HPRD
Link-
318PhosphothreonineQMALTLLGG
HHHHHHHCC
15.48HPRD
Link-
386PhosphoserineLSLFSKTQG
HHHHHHHCC
39.83HPRD
Link-
386PhosphoserineLSLFSKTQG
HHHHHHHCC
39.83Phosphositeplus
Link-
426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QPWYKAAVA
CHHHHHHHH
26.46Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433B_HUMANphysical interactionMINT-50962MINT15324660
1433Z_HUMANphysical interactionMINT-3320046MINT15161933
DDX6_HUMANphysical interaction
physical interaction
EBI-1162980
EBI-1006852
intact16364915
16364915
EDC4_HUMANphysical interaction
physical interaction
EBI-1006874
EBI-1006852
intact16364915
16364915
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures