DDX3_DROME - dbPTM
DDX3_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX3_DROME
UniProt AC Q9VHP0
Protein Name ATP-dependent RNA helicase bel
Gene Name bel {ECO:0000312|EMBL:AAF54262.1}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 798
Subcellular Localization Cytoplasm . In nurse cells, follicle cells, and within the oocyte. Vas and bel colocalize in the perinuclear region of nurse cells.
Protein Description ATP-dependent RNA helicase that is essential and required for cellular function, larval growth, and for male and female fertility. Also required for RNA interference (RNAi), double-stranded RNA induces potent and specific gene silencing, by acting downstream of dsRNA internalization. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger..
Protein Sequence MSNAINQNGTGLEQQVAGLDLNGGSADYSGPITSKTSTNSVTGGVYVPPHLRGGGGNNNAADAESQGQGQGQGQGFDSRSGNPRQETRDPQQSRGGGGEYRRGGGGGGRGFNRQSGDYGYGSGGGGRRGGGGRFEDNYNGGEFDSRRGGDWNRSGGGGGGGRGFGRGPSYRGGGGGSGSNLNEQTAEDGQAQQQQQPRNDRWQEPERPAGFDGSEGGQSAGGNRSYNNRGERGGGGYNSRWKEGGGSNVDYTKLGARDERLEVELFGVGNTGINFDKYEDIPVEATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELGHVPPPQSTRQYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNMPPTGQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILWVYEPDKRSYLLDLLSSIRDGPEYTKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNICSDLLELLIETKQEIPSFMEDMSSDRGHGGAKRAGRGGGGRYGGGFGSRDYRQSSGGGGGGRSGPPPRSGGSGSGGGGGSYRSNGNSYGGNSGGGGYYGGGAGGGSYGGSYGGGSASHSSNAPDWWAQ
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
36PhosphorylationSGPITSKTSTNSVTG
CCCCCCCCCCCCCCC		40.3219429919
37PhosphorylationGPITSKTSTNSVTGG
CCCCCCCCCCCCCCC		29.3619429919
38PhosphorylationPITSKTSTNSVTGGV
CCCCCCCCCCCCCCE		36.4219429919
40PhosphorylationTSKTSTNSVTGGVYV
CCCCCCCCCCCCEEC		22.5719429919
42PhosphorylationKTSTNSVTGGVYVPP
CCCCCCCCCCEECCC		28.2119429919
115PhosphorylationGRGFNRQSGDYGYGS
CCCCCCCCCCCCCCC		30.3219429919
118PhosphorylationFNRQSGDYGYGSGGG
CCCCCCCCCCCCCCC		18.7719429919
120PhosphorylationRQSGDYGYGSGGGGR
CCCCCCCCCCCCCCC		11.2419429919
122PhosphorylationSGDYGYGSGGGGRRG
CCCCCCCCCCCCCCC		26.2719429919
138PhosphorylationGGRFEDNYNGGEFDS
CCCCCCCCCCCCCCC		27.7518281928
169PhosphorylationRGFGRGPSYRGGGGG
CCCCCCCCCCCCCCC		30.2222817900
170PhosphorylationGFGRGPSYRGGGGGS
CCCCCCCCCCCCCCC		19.1918281928
177PhosphorylationYRGGGGGSGSNLNEQ
CCCCCCCCCCCCCHH		42.1819429919
179PhosphorylationGGGGGSGSNLNEQTA
CCCCCCCCCCCHHHH		39.5819429919
185PhosphorylationGSNLNEQTAEDGQAQ
CCCCCHHHHCCHHHH		26.3229892262
214PhosphorylationRPAGFDGSEGGQSAG
CCCCCCCCCCCCCCC		34.6118327897
219PhosphorylationDGSEGGQSAGGNRSY
CCCCCCCCCCCCCCC		31.9622817900
251PhosphorylationGGGSNVDYTKLGARD
CCCCCCCCCCCCCCC		11.0718281928
574PhosphorylationETKKGADSLEEFLYQ
EECCCCCCHHHHHHH		36.8321082442
638PhosphorylationVINFDLPSDVEEYVH
EECCCCCCCHHHHHH		62.6819429919
712PhosphorylationGRGGGGRYGGGFGSR
CCCCCCCCCCCCCCC		24.3218281928
718PhosphorylationRYGGGFGSRDYRQSS
CCCCCCCCCCCCCCC		21.5119429919
721PhosphorylationGGFGSRDYRQSSGGG
CCCCCCCCCCCCCCC		14.9418281928
724PhosphorylationGSRDYRQSSGGGGGG
CCCCCCCCCCCCCCC		23.1925749252
725PhosphorylationSRDYRQSSGGGGGGR
CCCCCCCCCCCCCCC		32.8721082442
739PhosphorylationRSGPPPRSGGSGSGG
CCCCCCCCCCCCCCC		53.9619429919
742PhosphorylationPPPRSGGSGSGGGGG
CCCCCCCCCCCCCCC		33.0519429919
744PhosphorylationPRSGGSGSGGGGGSY
CCCCCCCCCCCCCCC		35.6419429919
750PhosphorylationGSGGGGGSYRSNGNS
CCCCCCCCCCCCCCC		22.2022817900
768PhosphorylationNSGGGGYYGGGAGGG
CCCCCCCCCCCCCCC		16.7518281928
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 DDX3_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX3_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 DDX3_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNB_DROMECycBgenetic
26876306
AGO2_DROMEAGO2physical
21730191
E74EB_DROMEEip74EFphysical
23209440
E74EA_DROMEEip74EFphysical
23209440
BRC1_DROMEbrphysical
23209440
BRC4_DROMEbrphysical
23209440
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDX3_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-177; SER-179; SER-214;SER-219 AND SER-638, AND MASS SPECTROMETRY.

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