EDC4_DROME - dbPTM
EDC4_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDC4_DROME
UniProt AC Q9VKK1
Protein Name Enhancer of mRNA-decapping protein 4 homolog
Gene Name Ge-1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1354
Subcellular Localization Cytoplasm, P-body .
Protein Description In the process of mRNA degradation, seems to play a role in mRNA decapping. Required for silencing a subset of endogenous miRNA targets..
Protein Sequence MLIALFALAHLPIFRKTPLSASSSPPPSVHRSPRCGKASTAYHPPPADACISITASAIDAASGMSNSAEQDKPIAANGNAAEPQEIEVIHFQAQEKQCCRVIRSNKTKVLTSGGVHTRGSSKVKLKNIVDYKWERKYYYPGHLVAVHRDGKHLAYAINVNNKATGMEGMVRVCNIATSMRALIKGMSGEVLDLQFAHTDCERILAVIDVSSLFVYKVDQIEGNLLCNLVLKVEDPIANYVPEYDMVSWCPYVCSSSATVPINDDDDENQLLIWSRSSQFQCFQVKMIVSEHGRGKIQPAALESGYLKIEEDSLITCAALSPDGTTVAAACADGLVRFYQIYLFDVRNHRCLHEWKPHDGKKVCSLFFLDNINKPVEESYWQHVITTSDANTEIKLWNCSLWKCLQTINVVASPSSLQPRNFIAGIDRSANYLVLSCLDSLAVYVMQIGSTGGADSENRSSDSEGEGCDTSKRIQNVAEFKLSSGILSFSIVNASMRRVKNSIESYYPIEEPDDFDDDSNSTSALVLHMFVVQAKSLQECQIIYQPCVAEKTERSSLNSKRSQTPEDNLLIKEEPESPNSGTVGAVQLDALFAKSAKRASTGSSSAMVAVAAAAAAAPSAILQDATKEAAKSESPQLSSAYTQQVNLMTPDAFSASGTAAAAAVFVSTSTTTSIGTDSSTTTSGQDRSIDSAVLQTIRMLATVTSKTSENPNAEVLLNLMNNTLIEDREQQKLKEKLDARKKFIAIDRNPERNVAENLASGSSSPSREVQEIMATQDDADAYEAELENLDDDDDDEEEELANSSPLPEAVDGTWPIVKLSSHSAELQNAAQIMSQAVQNTNNGNVPPTLGGGHNNNTSVGSNSNNNTATTLSTSNTSSSNNAGGTCVDSSGTGELNAKMELLIDLVKAQSKQINKLENEVNKLQKQQEAAAALHSKQDTSLEPKNLSQLAYKIEMQLSKLMEQYLKRYENEHKKKLTEFLAARESQNRELRDSVLQVLNQYVMNHFTDIIGNVLNMELQRQLLPRVNANMDQLQAQMQVEIVQKLSVFDKTVKENIAQVCKSKQFLDTFGKSVLIGVQTSLQTAFIESMSSTLIPAYEKSSQNMFKQLHDAFSVGIKDFMVQFNTYLQHMPQPQAGSGNTEEINNKLSMLKQLVESSLHKHRTELTDAMLETQREVKSLEILLARQVQETIRAELRKHMEAQNVAMRSQAATPAPPYDLRDSIKQLLMAGQINKAFHQALLANDLGLVEFTLRHTDSNQAFAPEGCRLEQKVLLSLIQQISADMTNHNELKQRYLNEALLAINMADPITREHAPKVLTELYRNCQQFIKNSPKNSQFSNVRLLMKAIITYRDQLK
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
24PhosphorylationTPLSASSSPPPSVHR
CCCCCCCCCCCCCCC		38.6421082442
32PhosphorylationPPPSVHRSPRCGKAS
CCCCCCCCCCCCCCC		11.2118327897
120PhosphorylationGGVHTRGSSKVKLKN
CCCCCCCCCCEEEEC		24.5627794539
449PhosphorylationVYVMQIGSTGGADSE
HHEHHCCCCCCCCCC		26.0522668510
460PhosphorylationADSENRSSDSEGEGC
CCCCCCCCCCCCCCC		41.7529892262
462PhosphorylationSENRSSDSEGEGCDT
CCCCCCCCCCCCCCH		49.8329892262
470PhosphorylationEGEGCDTSKRIQNVA
CCCCCCHHHHHHHHH		13.4922668510
554PhosphorylationVAEKTERSSLNSKRS
CCHHHHHHHCCCCCC		32.7119429919
555PhosphorylationAEKTERSSLNSKRSQ
CHHHHHHHCCCCCCC		37.4819429919
561PhosphorylationSSLNSKRSQTPEDNL
HHCCCCCCCCCCCCC		41.9919429919
563PhosphorylationLNSKRSQTPEDNLLI
CCCCCCCCCCCCCEE		29.8619429919
576PhosphorylationLIKEEPESPNSGTVG
EECCCCCCCCCCCCC		39.8519429919
579PhosphorylationEEPESPNSGTVGAVQ
CCCCCCCCCCCCHHH		38.9419429919
581PhosphorylationPESPNSGTVGAVQLD
CCCCCCCCCCHHHHH		18.6519429919
687PhosphorylationTTSGQDRSIDSAVLQ
CCCCCCCCHHHHHHH		38.7519429919
690PhosphorylationGQDRSIDSAVLQTIR
CCCCCHHHHHHHHHH		20.7119429919
703PhosphorylationIRMLATVTSKTSENP
HHHHHHHCCCCCCCC		21.8319429919
704PhosphorylationRMLATVTSKTSENPN
HHHHHHCCCCCCCCC		29.6019429919
759PhosphorylationNVAENLASGSSSPSR
CHHHHHHCCCCCCCH		42.2319429919
761PhosphorylationAENLASGSSSPSREV
HHHHHCCCCCCCHHH		25.7519429919
762PhosphorylationENLASGSSSPSREVQ
HHHHCCCCCCCHHHH		50.2019429919
763PhosphorylationNLASGSSSPSREVQE
HHHCCCCCCCHHHHH		28.7019429919
765PhosphorylationASGSSSPSREVQEIM
HCCCCCCCHHHHHHH		42.9219429919
965AcetylationKLMEQYLKRYENEHK
HHHHHHHHHHHHHHH		48.2621791702
1207PhosphorylationAQNVAMRSQAATPAP
HHHHHHHHCCCCCCC		15.8719429919
1211PhosphorylationAMRSQAATPAPPYDL
HHHHCCCCCCCCCCH		24.0119429919
1216PhosphorylationAATPAPPYDLRDSIK
CCCCCCCCCHHHHHH		26.9325749252
1317PhosphorylationEHAPKVLTELYRNCQ
HHHHHHHHHHHHHHH		27.2522817900
1320PhosphorylationPKVLTELYRNCQQFI
HHHHHHHHHHHHHHH		8.1122817900
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_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDC4_DROME !!
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_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UFD1_DROMEUfd1-likephysical
14605208
LCP2_DROMELcp2physical
14605208
STAU_DROMEstaugenetic
21655181
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EDC4_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-561; THR-563;SER-576; SER-759; SER-762; SER-763; SER-1207; THR-1211; THR-1317 ANDTYR-1320, AND MASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576 AND THR-581, ANDMASS SPECTROMETRY.

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