EDC4_RAT - dbPTM
EDC4_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDC4_RAT
UniProt AC Q3ZAV8
Protein Name Enhancer of mRNA-decapping protein 4
Gene Name Edc4
Organism Rattus norvegicus (Rat).
Sequence Length 1407
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 MASCASIDIEDATQHLRDILKLDRPAGGSNVESQRPSSAYNGDLNGLLVPDPLSSGDGNSTSKPGIRTMPPINLQEKQVICLSGDDSSTCIGILAKEVEIVASSDSSISSKARGSNKVKIQPVAKYDWEQKYYYGNLIAVSNSFLAYAIRAANNGSAMVRVISVSTSERTLLKGFTGSVADLAFAHLNSPQLACLDEAGDLFVWRLALVKGKIQEEILVHIRQPEGTPLNHFRRIIWCPFIPEESEDCCEESSPTVALLHEDRAEVWDLDMLRSSHSTWPVDVSQIKQGFIVVKGHSTCLSEGALSPDGTVLATASHDGFVKFWQIYIEGQDEPRCLHEWKPHDGRPLSCLLFCDNHKKQDPEVPFWRFLITGADQNRELKMWCTVSWTCLQTIRFSPDIFSSVSVPPSLKVCLDLSAEYLILSDVQRKVLYVMELLQNQDEGRACFSSISEFLLTHPVLSFGIQVVSRCRLRHTEVLPAEEESDSLGTESSHGAGTLESAAGVLIKLFCVHTKALQDVQIRFQPQLNPDVVAPLSTHTAHEDFTFGESRPELGSEGLASAPHGSQPDLRRIVELPAPADFLSLSSETKPKLMTPDAFMTPTASLQQISASPSSSSSSSSSSSSSSSSSSSSSLTAVSAVSSSSAMDPSLPSRPPEELTLSPKLQLDGSLTISSSSSLQASPRSLLPGLLPGPADKLIPKGPGQVSSGTSALSLDLQEVEPLGLPQASPSRTRSPDVISSASTALSQDIPEIASEALSRGFGSSVPEGLIEPDSMASAASALHLLSPRPRQGPELSSQLGLDGGPGDGDRHSTPSLLEAALTQEVATSDSQVWPTAPDITRETCSTLTESPRNGLQEKHKSLAFHRPPYHLLQQHDSQDTSAEQSDHDDEVASLASASGGFGSKIPTPRLPAKDWKTKGSPRTSPKLKRKSKKDDGDSAVGSRLTEHQVVEPPEDWPALIWQQQRELAELWHNQEELLQRLCAQLEGLQSTVTDHVERALETRHEQEQRRLERALAEGQQRGGQLQEQLTQQLSQALSSAVAGRLERSIRDEIKKTVPPCVSRSLEPVAGQLSNSVATKLTAVEGSMKENISKLLKSKNLTDAIARAAADTLQGPMQAAYREAFQSVVLPAFEKSCQAMFQQINDSFRLGTQEYLQQLDSHMKSRKAREQEAREPVLAQLRGLVSTLQNATEQMAATVSSSVRAEVQHQLHVAVGSLQESILAQVQRIVKGEVSVALKEQQATVTSSIMQAMRSAAGTPVPSAHLDCQAQQAHILQLLQQGHLNQAFQQALTAADLNLVLYVCETVDPAQVFGQPPCPLSQPVLLSLIQQLASDLGTRSDLKLSYLEEAVMHLDHSDPITRDHMGSVMAQVRQKLFQFLQADPHNSLGKAARRLSLMLHGLVTPSLP
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
23.2927097102
6Phosphorylation--MASCASIDIEDAT
--CCCCCCCCHHHHH
25.7227097102
125AcetylationVKIQPVAKYDWEQKY
CEEEECEECCHHHCE
43.93-
475PhosphorylationSRCRLRHTEVLPAEE
HCCCCCCCEEEECHH
22.7327097102
484PhosphorylationVLPAEEESDSLGTES
EEECHHHCCCCCCCC
35.4627097102
486PhosphorylationPAEEESDSLGTESSH
ECHHHCCCCCCCCCC
37.6727097102
489PhosphorylationEESDSLGTESSHGAG
HHCCCCCCCCCCCCC
37.6827097102
491PhosphorylationSDSLGTESSHGAGTL
CCCCCCCCCCCCCHH
27.7227097102
492PhosphorylationDSLGTESSHGAGTLE
CCCCCCCCCCCCHHH
21.5127097102
497PhosphorylationESSHGAGTLESAAGV
CCCCCCCHHHHHHHH
27.1527097102
560PhosphorylationLGSEGLASAPHGSQP
CCCCCCCCCCCCCCC
47.5827097102
565PhosphorylationLASAPHGSQPDLRRI
CCCCCCCCCCCHHHH
35.1927097102
583PhosphorylationPAPADFLSLSSETKP
CCCCHHHCCCCCCCC
26.6323984901
585PhosphorylationPADFLSLSSETKPKL
CCHHHCCCCCCCCCC
23.8123984901
586PhosphorylationADFLSLSSETKPKLM
CHHHCCCCCCCCCCC
55.3623984901
588PhosphorylationFLSLSSETKPKLMTP
HHCCCCCCCCCCCCC
55.3723984901
623PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
649PhosphorylationSSSAMDPSLPSRPPE
CCCCCCCCCCCCCCH
48.9630181290
652PhosphorylationAMDPSLPSRPPEELT
CCCCCCCCCCCHHCC
63.8130181290
681PhosphorylationSSSSLQASPRSLLPG
CCCCCCCCCCHHCCC
14.1127097102
706PhosphorylationPKGPGQVSSGTSALS
CCCCCCCCCCCCEEE
18.3727097102
707PhosphorylationKGPGQVSSGTSALSL
CCCCCCCCCCCEEEC
47.4327097102
709PhosphorylationPGQVSSGTSALSLDL
CCCCCCCCCEEECCC
16.8727097102
710PhosphorylationGQVSSGTSALSLDLQ
CCCCCCCCEEECCCH
30.6427097102
713PhosphorylationSSGTSALSLDLQEVE
CCCCCEEECCCHHCC
21.3927097102
728PhosphorylationPLGLPQASPSRTRSP
CCCCCCCCCCCCCCH
20.4027097102
730PhosphorylationGLPQASPSRTRSPDV
CCCCCCCCCCCCHHH
43.7327097102
732PhosphorylationPQASPSRTRSPDVIS
CCCCCCCCCCHHHHH
39.5821738781
734PhosphorylationASPSRTRSPDVISSA
CCCCCCCCHHHHHHH
25.4923712012
739PhosphorylationTRSPDVISSASTALS
CCCHHHHHHHHHHHH
21.5027097102
740PhosphorylationRSPDVISSASTALSQ
CCHHHHHHHHHHHHC
18.3427097102
742PhosphorylationPDVISSASTALSQDI
HHHHHHHHHHHHCCH
19.0327097102
743PhosphorylationDVISSASTALSQDIP
HHHHHHHHHHHCCHH
31.1927097102
746PhosphorylationSSASTALSQDIPEIA
HHHHHHHHCCHHHHH
24.2827097102
754PhosphorylationQDIPEIASEALSRGF
CCHHHHHHHHHHCCC
29.1228551015
763PhosphorylationALSRGFGSSVPEGLI
HHHCCCCCCCCCCCC
26.3827097102
764PhosphorylationLSRGFGSSVPEGLIE
HHCCCCCCCCCCCCC
41.9127097102
774PhosphorylationEGLIEPDSMASAASA
CCCCCCCHHHHHHHH
27.2827097102
777PhosphorylationIEPDSMASAASALHL
CCCCHHHHHHHHHHH
18.7428432305
780PhosphorylationDSMASAASALHLLSP
CHHHHHHHHHHHHCC
30.9528432305
786PhosphorylationASALHLLSPRPRQGP
HHHHHHHCCCCCCCC
25.8127097102
827PhosphorylationALTQEVATSDSQVWP
HHHHHHCCCCCCCCC
37.94-
843PhosphorylationAPDITRETCSTLTES
CCCCCHHHHHHCCCC
14.4125575281
845PhosphorylationDITRETCSTLTESPR
CCCHHHHHHCCCCCC
33.5925575281
846PhosphorylationITRETCSTLTESPRN
CCHHHHHHCCCCCCC
39.5925575281
848PhosphorylationRETCSTLTESPRNGL
HHHHHHCCCCCCCCC
34.2122108457
850PhosphorylationTCSTLTESPRNGLQE
HHHHCCCCCCCCCHH
24.7527097102
877PhosphorylationHLLQQHDSQDTSAEQ
HHHHHCCCCCCCHHH
28.0328432305
880PhosphorylationQQHDSQDTSAEQSDH
HHCCCCCCCHHHCCC
23.3828432305
881PhosphorylationQHDSQDTSAEQSDHD
HCCCCCCCHHHCCCH
37.7928432305
885PhosphorylationQDTSAEQSDHDDEVA
CCCCHHHCCCHHHHH
28.5522668510
893PhosphorylationDHDDEVASLASASGG
CCHHHHHHHHHHCCC
29.6428432305
896PhosphorylationDEVASLASASGGFGS
HHHHHHHHHCCCCCC
28.41-
898PhosphorylationVASLASASGGFGSKI
HHHHHHHCCCCCCCC
36.63-
907PhosphorylationGFGSKIPTPRLPAKD
CCCCCCCCCCCCCCC
25.23-
1034PhosphorylationEQLTQQLSQALSSAV
HHHHHHHHHHHHHHH
14.7427097102
1038PhosphorylationQQLSQALSSAVAGRL
HHHHHHHHHHHHHHH
21.1927097102
1386PhosphorylationLQADPHNSLGKAARR
HHHCCCCHHHHHHHH
35.1523984901
1395PhosphorylationGKAARRLSLMLHGLV
HHHHHHHHHHHCCCC
15.2123984901

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDC4_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EDC4_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EDC4_RAT

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Related Literatures of Post-Translational Modification

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