EXU_DROME - dbPTM
EXU_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXU_DROME
UniProt AC P28750
Protein Name Maternal protein exuperantia
Gene Name exu
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 532
Subcellular Localization
Protein Description Ensures the proper localization of the mRNA of the bicoid gene to the anterior regions of the oocyte thus playing a fundamental role in the establishment of the polarity of the oocyte. May bind the bcd mRNA..
Protein Sequence MVADNIDAGVAIAVADQSSSPVGDKVELPAGNYILVGVDIDTTGRRLMDEIVQLAAYTPTDHFEQYIMPYMNLNPAARQRHQVRVISIGFYRMLKSMQTYKIIKSKSEIAALKDFLNWLEQLKTKAGPSSDGIVLIYHEERKFIPYMILESLKKYGLLERFTASVKSFANSINLAKASIGDANIKNYSLRKLSKILSTTKEEDAACSASTSGSGSGLGSGSSMVSDSVSISPRDSTVTNGDDKQSSKNAVQGKRELFDGNASVRAKLAFDVALQLSNSDGKPEPKSSEALENMFNAIRPFAKLVVSDVLELDIQIENLERQNSFRPVFLNYFKTTLYHRVRAVKFRIVLAENGFDLNTLSAIWAEKNIEGLDIALQSIGRLKSKDKAELLELLDSYFDPKKTTVKPVVKGNSNNNNNYRRRNRRGGRQSVKDARPSSSPSASTEFGAGGDKSRSVSSLPDSTTKTPSPNKPRMHRKRNSRQSLGATPNGLKVAAEISSSGVSELNNSAPPAVTISPVVAQPSPTPVAITASN
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
235PhosphorylationVSISPRDSTVTNGDD
EEECCCCCCCCCCCC
26.5119429919
236PhosphorylationSISPRDSTVTNGDDK
EECCCCCCCCCCCCC
35.3219429919
436PhosphorylationSVKDARPSSSPSAST
CHHHCCCCCCCCCCC
37.5819429919
437PhosphorylationVKDARPSSSPSASTE
HHHCCCCCCCCCCCC
49.2919429919
438PhosphorylationKDARPSSSPSASTEF
HHCCCCCCCCCCCCC
27.4919429919
440PhosphorylationARPSSSPSASTEFGA
CCCCCCCCCCCCCCC
36.4819429919
442PhosphorylationPSSSPSASTEFGAGG
CCCCCCCCCCCCCCC
32.5719429919
443PhosphorylationSSSPSASTEFGAGGD
CCCCCCCCCCCCCCC
34.7428490779
452PhosphorylationFGAGGDKSRSVSSLP
CCCCCCCCCCCCCCC
34.2319429919
454PhosphorylationAGGDKSRSVSSLPDS
CCCCCCCCCCCCCCC
33.1819429919
456PhosphorylationGDKSRSVSSLPDSTT
CCCCCCCCCCCCCCC
27.6619429919
457PhosphorylationDKSRSVSSLPDSTTK
CCCCCCCCCCCCCCC
41.5919429919
461PhosphorylationSVSSLPDSTTKTPSP
CCCCCCCCCCCCCCC
35.7219429919
465PhosphorylationLPDSTTKTPSPNKPR
CCCCCCCCCCCCCCC
27.2322817900
467PhosphorylationDSTTKTPSPNKPRMH
CCCCCCCCCCCCCCC
46.461756733
482PhosphorylationRKRNSRQSLGATPNG
CCCCCCHHCCCCCCH
27.8821082442

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 EXU_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXU_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 EXU_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JMJD6_DROMEPSRphysical
22036573
NCBP1_DROMECbp80physical
22036573
CUP_DROMEcupphysical
14691132
GRK_DROMEgrkphysical
23213441
BCD_DROMEbcdphysical
27376588
BCD_DROMEbcdphysical
7479884
IF4E_DROMEeIF-4Ephysical
14691132

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EXU_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-467, AND MASSSPECTROMETRY.

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