BICC_DROME - dbPTM
BICC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BICC_DROME
UniProt AC Q24009
Protein Name Protein bicaudal C
Gene Name BicC
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 905
Subcellular Localization
Protein Description RNA-binding protein that is involved in oogenesis. Required for correct targeting of the migrating anterior follicle cells and the establishment of anterior-posterior polarity in the oocyte. May act as translational repressor of oskar during oogenesis. Function seems to be sensitive to small changes in expression..
Protein Sequence MLSCASFNKLMYPSAADVAKPPMVGLEVEAGSIGSLSSLHALPSTTSVGSGAPSETQSEISSVDSDWSDIRAIAMKLGVQNPDDLHTERFKVDRQKLEQLIKAESSIEGMNGAEYFFHDIMNTTDTYVSWPCRLKIGAKSKKDPHVRIVGKVDQVQRAKERILSSLDSRGTRVIMKMDVSYTDHSYIIGRGGNNIKRIMDDTHTHIHFPDSNRSNPTEKSNQVSLCGSLEGVERARALVRLSTPLLISFEMPVMGPNKPQPDHETPYIKMIETKFNVQVIFSTRPKLHTSLVLVKGSEKESAQVRDATQLLINFACESIASQILVNVQMEISPQHHEIVKGKNNVNLLSIMERTQTKIIFPDLSDMNVKPLKKSQVTISGRIDDVYLARQQLLGNLPVALIFDFPDNHNDASEIMSLNTKYGVYITLRQKQRQSTLAIVVKGVEKFIDKIYEARQEILRLATPFVKPEIPDYYFMPKDKDLNLAYRTQLTALLAGYVDSPKTPSLLPPSLAGQLTPYANNNHLLLNANGLATPTGVCAPTQKYMQLHNSFQQAQNRSMVAGGQSNNGNYLQVPGAVAPPLKPPTVSPRNSCSQNTSGYQSFSSSTTSLEQSYPPYAQLPGTVSSTSSSTAGSQNRAHYSPDSTYGSEGGGVGGGGGGGARLGRRLSDGVLLGLSNSNGGGGNSGGAHLLPGSAESYRSLHYDLGGNKHSGHRAFDFDMKRALGYKAMERTPVAGELRTPTTAWMGMGLSSTSPAPAPLENGENGAAGGGASSGWRLPPGLGSPYGLSATTGLLDATPVNRRMQLAKHKDIQTLLTSLGLEHYIKIFVLNEIDLEVFTTLTEENLMELGIAAFGARKKLLTAIHTLLANEAACSTMPSSSSSQNSSSPRFSGSAAPGAERRPSNQW
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
549PhosphorylationKYMQLHNSFQQAQNR
HHHHHHHHHHHHHHH
17.4322817900
557PhosphorylationFQQAQNRSMVAGGQS
HHHHHHHHHCCCCCC
25.7622817900
584PhosphorylationAPPLKPPTVSPRNSC
CCCCCCCCCCCCCCC
41.9930478224
586PhosphorylationPLKPPTVSPRNSCSQ
CCCCCCCCCCCCCCC
22.1822817900
639PhosphorylationSQNRAHYSPDSTYGS
CCCCCCCCCCCCCCC
16.6222817900
642PhosphorylationRAHYSPDSTYGSEGG
CCCCCCCCCCCCCCC
27.2330478224
643PhosphorylationAHYSPDSTYGSEGGG
CCCCCCCCCCCCCCC
39.0018327897
644PhosphorylationHYSPDSTYGSEGGGV
CCCCCCCCCCCCCCC
23.7018327897
646PhosphorylationSPDSTYGSEGGGVGG
CCCCCCCCCCCCCCC
23.7418327897
666PhosphorylationARLGRRLSDGVLLGL
CCCCCCCCCCEEEEC
30.4322817900
692PhosphorylationGAHLLPGSAESYRSL
CCCCCCCCHHHHHCE
27.2422817900
695PhosphorylationLLPGSAESYRSLHYD
CCCCCHHHHHCEEEE
26.0922817900
696PhosphorylationLPGSAESYRSLHYDL
CCCCHHHHHCEEEEC
8.849671494
782PhosphorylationRLPPGLGSPYGLSAT
CCCCCCCCCCCCCCC
21.7130478224
796PhosphorylationTTGLLDATPVNRRMQ
CCCCCCCCCCCHHHH
27.6930478224

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 BICC_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BICC_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 BICC_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VND_DROMEvndphysical
14605208
DDX6_DROMEme31Bgenetic
19217894
EXU_DROMEexugenetic
19217894
GRK_DROMEgrkphysical
23213441
BICC_DROMEBicCphysical
17981137

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BICC_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-557; SER-586; SER-639;SER-642; THR-643; TYR-644; SER-646; SER-666; SER-692; SER-695 ANDTYR-696, AND MASS SPECTROMETRY.

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