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 4  

UniProtKB / Swiss-Prot ID :  EDC4_MOUSE

Gene Name (Synonyms) : 
Edc4  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm, P-body (By similarity). Nucleus (By similarity). 

Protein Function :  In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro) (By similarity). 

Protein Sequence MASCASIDIEDATQHLRDILKLDRPAGGSNAESQRPSSAYNGDLNGLLVPDPLSSGDGNSTNKPGIRTMP...
Predicted Secondary Structure CCCCEEECHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCEEECCCCCCCCCCCCCCCCCCCCC...
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
486PhosphoserineEENDSLGTE
CCCCCCCCC
40.04Phosphositeplus
Link-
489PhosphothreonineDSLGTESSH
CCCCCCCCC
37.68Phosphositeplus
Link-
491PhosphoserineLGTESSHGA
CCCCCCCCC
27.72Phosphositeplus
Link-
676PhosphoserineSSSSSLQAS
CCCCCCCCC
26.84Phosphositeplus
Link-
680PhosphoserineSLQASPRSL
CCCCCCCCC
14.11Phosphositeplus
Link-
683PhosphoserineASPRSLLPG
CCCCCCCCC
37.33Phosphositeplus
Link-
683PhosphoserineASPRSLLPG
CCCCCCCCC
37.33SysPTM
Link-
712PhosphoserineASALSLDLQ
CCCCCCCCC
21.39Phosphositeplus
Link-
727PhosphoserineLPQASPSRT
CCCCCCCCC
20.40Phosphositeplus
Link-
731PhosphothreonineSPSRTRSPD
CCCCCCCCC
39.58Phosphositeplus
Link-
731PhosphothreonineSPSRTRSPD
CCCCCCCCC
39.58SysPTM
Link-
733PhosphoserineSRTRSPDVI
CCCCCCCCC
25.49Phosphositeplus
Link-
733PhosphoserineSRTRSPDVI
CCCCCCCCC
25.49SysPTM
Link-
738PhosphoserinePDVISSAST
CCCCCCCCC
21.50Phosphositeplus
Link-
745PhosphoserineSTALSQDIP
CCCCCCCCC
24.28Phosphositeplus
Link-
814PhosphoserineHSTPSLLEA
CCCCCCCCC
45.75Phosphositeplus
Link-
821PhosphothreonineEAALTQEVA
CCCCCCCCC
20.25Phosphositeplus
Link-
826PhosphothreonineQEVATPDSQ
CCCCCCCCC
32.57Phosphositeplus
Link-
849PhosphoserineTLTESPRNG
CCCCCCCCC
24.75Phosphositeplus
Link-
849PhosphoserineTLTESPRNG
CCCCCCCCC
24.75SysPTM
Link-
876PhosphoserineQQRDSQDTS
CCCCCHHHC
31.95Phosphositeplus
Link-
876PhosphoserineQQRDSQDTS
CCCCCHHHC
31.95SysPTM
Link-
879PhosphothreonineDSQDTSAEQ
CCHHHCCCC
23.38Phosphositeplus
Link-
880PhosphoserineSQDTSAEQS
CHHHCCCCC
37.79PhosphoELM
Link-
880PhosphoserineSQDTSAEQS
CHHHCCCCC
37.79Phosphositeplus
Link-
880PhosphoserineSQDTSAEQS
CHHHCCCCC
37.79SysPTM
Link-
880Phosphoserine.SQDTSAEQS
CHHHCCCCC
37.79UniProtKB
Link-
884PhosphoserineSAEQSDHDD
CCCCCCCCC
28.55PhosphoELM
Link-
884PhosphoserineSAEQSDHDD
CCCCCCCCC
28.55Phosphositeplus
Link-
884PhosphoserineSAEQSDHDD
CCCCCCCCC
28.55SysPTM
Link-
884Phosphoserine.SAEQSDHDD
CCCCCCCCC
28.55UniProtKB
Link-
892PhosphoserineDEVASLASA
CHHHEECCC
29.64PhosphoELM
Link-
892PhosphoserineDEVASLASA
CHHHEECCC
29.64Phosphositeplus
Link-
892PhosphoserineDEVASLASA
CHHHEECCC
29.64SysPTM
Link-
892Phosphoserine.DEVASLASA
CHHHEECCC
29.64UniProtKB
Link-
895PhosphoserineASLASASGG
HEECCCCCC
28.41Phosphositeplus
Link-
897PhosphoserineLASASGGFG
ECCCCCCCC
36.63Phosphositeplus
Link-
906PhosphothreonineSKIPTPRLP
CCCCCCCCC
25.23Phosphositeplus
Link-
930PhosphoserineLKRKSKKDD
CCCCCCCCH
49.31Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-880; SER-884 ANDSER-892, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures