EDC4_MOUSE - dbPTM
EDC4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDC4_MOUSE
UniProt AC Q3UJB9
Protein Name Enhancer of mRNA-decapping protein 4 {ECO:0000305}
Gene Name Edc4 {ECO:0000312|MGI:MGI:2446249}
Organism Mus musculus (Mouse).
Sequence Length 1406
Subcellular Localization Cytoplasm, P-body . Nucleus .
Protein Description 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)..
Protein Sequence MASCASIDIEDATQHLRDILKLDRPAGGSNAESQRPSSAYNGDLNGLLVPDPLSSGDGNSTNKPGIRTMPPINLQEKQVICLSGDDSSTCIGILAKEVEIVASSDSSISSKARGSNKVKIQPVAKYDWEQKYYYGNLIAVSNSFLAYAIRAANNGSAMVRVISVSTSERTLLKGFTGSVADLAFAHLNSPQLACLDEAGNLFVWRLALVKGKIQEEILVHIRQPEGTALNHFRRIIWCPFIPEESEDCCEESSPTVALLHEDRAEVWDLDMLRSSHNTWPVDVSQIKQGFIVVKGHSTCLSEGALSPDGTVLATASHDGFVKFWQIYIEGQDEPRCLHEWKPHDGRPLSCLLFCDNHKKQDPEVPFWRFLITGADQNRELKMWCTVSWTCLQTIRFSPDIFSSVSVPPSLKVCLDLSAEYLILSDVQRKVLYVMELLQNQDEGRACFSSISEFLLTHPVLSFGIQVVSRCRLRHTEVLPAEEENDSLGTESSHGAGALESAAGVLIKLFCVHTKALQDVQIRFQPQLNPDVVAPLSTHTAHEDFTFGESRPELGSEGLASAAHGSQPDLRRIVELPAPADFLSLSSETKPELMTPDAFMTPTASLQQISASPSSSSSSSSSSSSSSSSSSSSLTAVSAVSSSSAMDPSLPRPPEELTLSPKLQLDGSLTLNSSSSSLQASPRSLLPGLLPGPADKLISKGPGQVSTAASALSLDLQEVEPLGLPQASPSRTRSPDVISSASTALSQDIPEIASEALSRGFGSSVPEGLIEPNSMASAASALHLLSPRPRQGPELGSQLGLDGGPGDGDRHSTPSLLEAALTQEVATPDSQVWPTAPDITRETCSTLTESPRNGLQEKHKSLAFHRPPYHLLQQRDSQDTSAEQSDHDDEVASLASASGGFGSKIPTPRLPSKDWKTKGSPRTSPKLKRKSKKDDGDSAVGSRLTEHQVAEPPEDWPALIWQQQRELAELWHNQEELLQRLCAQLEGLQSTVTDHVERALETRHEQEQRRLERALAEGQQRGGQLQEQLTQQLSQALSSAVAGRLERSVRDEIKKTVPPCVSRSLEPVAGQLSNSVATKLTAVEGSMKENISKLLKSKNLTDAIARAAADTLQGPMQAAYREAFQSVVLPAFEKSCQAMFQQINDSFRLGTQEYLQQLESHMKSRKAREQEAREPVLAQLRGLVSTLQSATEQMAATVSSSVRAEVQHQLHVAVGSLQESILAQVQRIVKGEVSVALKEQQATVTSSIMQAMRSAAGTPVPSAHLDCQAQQAHILQLLQQGHLNQAFQQALTAADLNLVLYVCETVDPAQVFGQPPCPLSQPVLLSLIQQLASDLGTRSDLKLSYLEEAVMHLDHSDPITRDHMGSVMAQVRQKLFQFLQADPHNSLSKAARRLSLMLHGLVTPSLP
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
2Acetylation------MASCASIDI
------CCCCCCCCH		25.31-
3Phosphorylation-----MASCASIDIE
-----CCCCCCCCHH		23.2929472430
6Phosphorylation--MASCASIDIEDAT
--CCCCCCCCHHHHH		25.7226824392
125AcetylationVKIQPVAKYDWEQKY
CEEEECEECCHHHCE		43.93-
134PhosphorylationDWEQKYYYGNLIAVS
CHHHCEEECCEEEEC		9.1022418434
141PhosphorylationYGNLIAVSNSFLAYA
ECCEEEECHHHHHHH		20.1022418434
143PhosphorylationNLIAVSNSFLAYAIR
CEEEECHHHHHHHHH		17.7122418434
147PhosphorylationVSNSFLAYAIRAANN
ECHHHHHHHHHHHHC		12.5222418434
390S-palmitoylationWCTVSWTCLQTIRFS
HHEEEHHHHHHHCCC		1.8428680068
475PhosphorylationSRCRLRHTEVLPAEE
HCCCCCCCEEECCCH		22.7325159016
486PhosphorylationPAEEENDSLGTESSH
CCCHHCCCCCCCCCC		40.0426824392
489PhosphorylationEENDSLGTESSHGAG
HHCCCCCCCCCCCHH		37.6830387612
491PhosphorylationNDSLGTESSHGAGAL
CCCCCCCCCCCHHHH		27.7221659605
492PhosphorylationDSLGTESSHGAGALE
CCCCCCCCCCHHHHH		21.5125159016
500PhosphorylationHGAGALESAAGVLIK
CCHHHHHHHHHHHHH		25.0330635358
555PhosphorylationESRPELGSEGLASAA
CCCCCCCHHHHHHHH		40.9129233185
560PhosphorylationLGSEGLASAAHGSQP
CCHHHHHHHHCCCCC		30.9125338131
565PhosphorylationLASAAHGSQPDLRRI
HHHHHCCCCCCHHHH		28.7728066266
583PhosphorylationPAPADFLSLSSETKP
CCCCCHHCCCCCCCC		26.63-
585PhosphorylationPADFLSLSSETKPEL
CCCHHCCCCCCCCCC		23.81-
588PhosphorylationFLSLSSETKPELMTP
HHCCCCCCCCCCCCC		54.57-
620PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
621PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
622PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
623PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
624PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
625PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
657PhosphorylationPRPPEELTLSPKLQL
CCCCHHCCCCCCEEE		28.5925338131
659PhosphorylationPPEELTLSPKLQLDG
CCHHCCCCCCEEECC		18.1126824392
667PhosphorylationPKLQLDGSLTLNSSS
CCEEECCCEEECCCC		20.1825619855
669PhosphorylationLQLDGSLTLNSSSSS
EEECCCEEECCCCCC		26.1225619855
672PhosphorylationDGSLTLNSSSSSLQA
CCCEEECCCCCCCCC		34.4125619855
673PhosphorylationGSLTLNSSSSSLQAS
CCEEECCCCCCCCCC		32.9225619855
674PhosphorylationSLTLNSSSSSLQASP
CEEECCCCCCCCCCH		24.6225619855
675PhosphorylationLTLNSSSSSLQASPR
EEECCCCCCCCCCHH		36.7025619855
676PhosphorylationTLNSSSSSLQASPRS
EECCCCCCCCCCHHH		26.8425619855
680PhosphorylationSSSSLQASPRSLLPG
CCCCCCCCHHHHCCC		14.1127087446
683PhosphorylationSLQASPRSLLPGLLP
CCCCCHHHHCCCCCC		37.3321082442
705PhosphorylationSKGPGQVSTAASALS
CCCCCHHHHHHHHHC		12.3925619855
706PhosphorylationKGPGQVSTAASALSL
CCCCHHHHHHHHHCC		27.6425619855
709PhosphorylationGQVSTAASALSLDLQ
CHHHHHHHHHCCCCC		27.5525619855
712PhosphorylationSTAASALSLDLQEVE
HHHHHHHCCCCCCCC		21.3928973931
727PhosphorylationPLGLPQASPSRTRSP
CCCCCCCCCCCCCCH		20.4027087446
729PhosphorylationGLPQASPSRTRSPDV
CCCCCCCCCCCCHHH		43.7327087446
731PhosphorylationPQASPSRTRSPDVIS
CCCCCCCCCCHHHHH		39.5827087446
733PhosphorylationASPSRTRSPDVISSA
CCCCCCCCHHHHHHH		25.4927087446
738PhosphorylationTRSPDVISSASTALS
CCCHHHHHHHHHHHH		21.5025177544
739PhosphorylationRSPDVISSASTALSQ
CCHHHHHHHHHHHHC		18.3425177544
741PhosphorylationPDVISSASTALSQDI
HHHHHHHHHHHHCCH		19.0325177544
742PhosphorylationDVISSASTALSQDIP
HHHHHHHHHHHCCHH		31.1927087446
745PhosphorylationSSASTALSQDIPEIA
HHHHHHHHCCHHHHH		24.2827087446
753PhosphorylationQDIPEIASEALSRGF
CCHHHHHHHHHHCCC		29.1225619855
757PhosphorylationEIASEALSRGFGSSV
HHHHHHHHCCCCCCC		37.0925619855
762PhosphorylationALSRGFGSSVPEGLI
HHHCCCCCCCCCCCC		26.3821183079
779PhosphorylationNSMASAASALHLLSP
CCHHHHHHHHHHHCC		30.9521183079
785PhosphorylationASALHLLSPRPRQGP
HHHHHHHCCCCCCCC		25.8119060867
796PhosphorylationRQGPELGSQLGLDGG
CCCCCCHHCCCCCCC		34.5524899341
811PhosphorylationPGDGDRHSTPSLLEA
CCCCCCCCCHHHHHH		42.7919060867
812PhosphorylationGDGDRHSTPSLLEAA
CCCCCCCCHHHHHHH		15.6925293948
814PhosphorylationGDRHSTPSLLEAALT
CCCCCCHHHHHHHHH		45.7519060867
821PhosphorylationSLLEAALTQEVATPD
HHHHHHHHCCCCCCC		20.2522817900
826PhosphorylationALTQEVATPDSQVWP
HHHCCCCCCCHHCCC		32.5725293948
842PhosphorylationAPDITRETCSTLTES
CCCCCHHHHHHCCCC		14.4125266776
844PhosphorylationDITRETCSTLTESPR
CCCHHHHHHCCCCCC		33.5925777480
845PhosphorylationITRETCSTLTESPRN
CCHHHHHHCCCCCCC		39.5925777480
847PhosphorylationRETCSTLTESPRNGL
HHHHHHCCCCCCCCC		34.2128066266
849PhosphorylationTCSTLTESPRNGLQE
HHHHCCCCCCCCCHH		24.7526824392
868PhosphorylationLAFHRPPYHLLQQRD
HHHCCCCHHHHCCCC		14.0524719451
876PhosphorylationHLLQQRDSQDTSAEQ
HHHCCCCCCCCCHHH		31.9524925903
879PhosphorylationQQRDSQDTSAEQSDH
CCCCCCCCCHHHCCC		23.3824925903
880PhosphorylationQRDSQDTSAEQSDHD
CCCCCCCCHHHCCCH		37.7925521595
884PhosphorylationQDTSAEQSDHDDEVA
CCCCHHHCCCHHHHH		28.5524925903
892PhosphorylationDHDDEVASLASASGG
CCHHHHHHHHHHCCC		29.6424925903
895PhosphorylationDEVASLASASGGFGS
HHHHHHHHHCCCCCC		28.4124925903
897PhosphorylationVASLASASGGFGSKI
HHHHHHHCCCCCCCC		36.6324925903
902PhosphorylationSASGGFGSKIPTPRL
HHCCCCCCCCCCCCC		25.7525619855
906PhosphorylationGFGSKIPTPRLPSKD
CCCCCCCCCCCCCCC		25.2325619855
911PhosphorylationIPTPRLPSKDWKTKG
CCCCCCCCCCCCCCC		48.0828059163
916PhosphorylationLPSKDWKTKGSPRTS
CCCCCCCCCCCCCCC		36.0623737553
919PhosphorylationKDWKTKGSPRTSPKL
CCCCCCCCCCCCHHH		16.8630352176
922PhosphorylationKTKGSPRTSPKLKRK
CCCCCCCCCHHHCCC		53.4122324799
923PhosphorylationTKGSPRTSPKLKRKS
CCCCCCCCHHHCCCC		22.7130352176
930PhosphorylationSPKLKRKSKKDDGDS
CHHHCCCCCCCCCCC		49.3125266776
981S-palmitoylationEELLQRLCAQLEGLQ
HHHHHHHHHHHHCHH		2.1828680068
1080PhosphorylationNSVATKLTAVEGSMK
HHHHHHHHHCCCHHH		30.1627742792
1085PhosphorylationKLTAVEGSMKENISK
HHHHCCCHHHHHHHH		17.1127742792
1162UbiquitinationQQLESHMKSRKAREQ
HHHHHHHHHHHHHHH		41.50-
1233PhosphorylationRIVKGEVSVALKEQQ
HHHCCCHHHHHHHHH		9.4323140645
1257PhosphorylationAMRSAAGTPVPSAHL
HHHHHCCCCCCCHHH		19.1821082442
1385PhosphorylationLQADPHNSLSKAARR
HHHCCCCHHHHHHHH		30.8726824392
1387PhosphorylationADPHNSLSKAARRLS
HCCCCHHHHHHHHHH		21.7725168779
1394PhosphorylationSKAARRLSLMLHGLV
HHHHHHHHHHHCCCC		15.21-
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 EDC4_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDC4_MOUSE !!
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 EDC4_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECHA_HUMANHADHAphysical
20360068
AP2B1_HUMANAP2B1physical
20360068
AP2M1_HUMANAP2M1physical
20360068
DCP2_HUMANDCP2physical
20360068
ECHB_HUMANHADHBphysical
20360068
AP2A1_HUMANAP2A1physical
20360068
EDC4_HUMANEDC4physical
20360068
EDC3_HUMANEDC3physical
20360068
PATL1_HUMANPATL1physical
20360068
KC1E_HUMANCSNK1Ephysical
20360068
SGF29_HUMANCCDC101physical
20360068
C4BPA_HUMANC4BPAphysical
26496610
DDX6_HUMANDDX6physical
26496610
SRP09_HUMANSRP9physical
26496610
ZN33A_HUMANZNF33Aphysical
26496610
MARF1_HUMANKIAA0430physical
26496610
PNRC1_HUMANPNRC1physical
26496610
CP131_HUMANCEP131physical
26496610
DCP1A_HUMANDCP1Aphysical
26496610
EDC3_HUMANEDC3physical
26496610
SGF29_HUMANCCDC101physical
26496610
DCP2_HUMANDCP2physical
26496610
PATL1_HUMANPATL1physical
26496610
E2AK4_HUMANEIF2AK4physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EDC4_MOUSE

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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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