ENC_DROME - dbPTM
ENC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENC_DROME
UniProt AC Q8MSX1
Protein Name Protein encore
Gene Name enc
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1818
Subcellular Localization Cytoplasm. Colocalizes with grk.
Protein Description Required for the regulation of germline mitosis, karyosome formation, and establishment of dorsoventral (DS) polarity of the egg and embryo. Involved in proper grk mRNA localization and translation in the oocyte. May control germline mitosis by facilitating the cyclin E (CycE) proteolysis by the SCF-ubiquitin-proteasome complex..
Protein Sequence MSSTKSQVALATNIPTNLSSAASASTAAAAAAVVVVASANAAVASSANSSGVGSGSGPGPGSGAGVSGPVAAGTATAVATGSTVTAATSVAATTSTSVATISTSCSSSSINNINNNCGEECQSAAGSSNLGRQNSFGNRRGNMKGKHLTRSHAMRESTSPPRTPTPRAASEQQQQQLQGEQHEHNNNNNINSSSKAQSAGRGNSPLMETPAVIVTSQQPQQQQQQQQQQQQSVPPKPQQNVPLSNEAEFPKLSPPKKSGGQHNRTNSNGSGMEFNNNNNSSNKKFVVDMKANGLDNKPHNNSSTGVIFNSGMNYKAAERHDRHERHEMSSQNSNLSNNHDEEPYHYEPRGGGGGKKHRANTNAKGNKPRLKNLGGSSSGSIDLGGGGGNGNCNNMSNNGQSNNSSNNTSGFISRENSSEQYTDYGGTDLLVFFRDTLNKNPKDRNILLKIEKDLIDFVQENSRGCEYRFPPASSYNRMLIHRTAAFFGMEHNVDTETQQCVIVAVAKNTRIPEIRFQSLVRDDARKSILKRDTHSFDEVRQSPYLCPLSLDRKAKSFEEREEDYDRARSRIFSRTGGNHDGYSGGGGDEECYGGWEQQQQQQKQSQPPRPKRPNGKMLQMQNSTESRDGMRSGGAVPKSHNFGNYGGPPSSGGPGNNSLPRGDSTNSIKSGRGGFVKQDSTGSTPWRLSPSSSGSIYHYDPSNLPPNQALQHSGNQYQSQNQGNSSSGGYNNYRKSSPHQQQQSQQQQQSQQHHQQQLQQPQQLHQQSSQQYATTELSCSSTESYAEEEAQSPGMECSEGYESYEQQSLPVQQQLSGNGDSASTKGDDCDSLASATACLSITTSTSTKNYDRIEVQKYKNQATSPNIPACCAVGEKLELEAGLPQEQEQEPMAGPSSSGSATSSVGITELPSSQTPLPMVNQVNCDLQSVSPSTTPYSQCEVKTPSQNHAPSAAVEEPKTTTWTYTQSYQAPDGSTVFHTTTTPNGAAPYCATTYQQGPDGSIYAVPQGMVYAAYPQPGVGTAGGASQPLFQLTTSSHPPAQTIFASPEAGAEIPGGTYMIPVFDPAQQPREGLIPAQAIYQTGPGGPGATTVMPMATAAAYPTAQFATAAPNGAPIYQAPLIYSSEPGGGAQLQQLPMAPYPIQYSYPYYHPISYYVPQQAVAAAPMVASQPQVGQAPMQQQAPHTGAGTTTGPPTVVSVSGQQHHQPHQQHHQQQQHSSNGSVVTSSAYGTRVKRTPGGGSIHYNPSYTPSSVAHAGGAHHPSAGSAQIIAAPAASTTTYHALPTLTLAHGGPATGTDLSGAGGAHVYALPAQHALIPTNIFPYAAAAAAAAGGPGGPPTTPQVVQQAPPPPPQSAPHHALITAAPFYPANGGNMDQGASQSAPSTPAAPGRQAPLFSTPPAPNNGSSGSSSAGGGGNSGGYHSNSSTPHYYQGQNSNEGYTSPYEKRNHGGGASGAHSVGVRKPYHPGGYNPRHSVPLGGIPSGAKTPLLNSNNEPTPRASPSSVSLGGASSSGGANSYPHRGPPPHTMGVKRDNKPNQLPLISGPPPSYAANSSPGVSSYESKPPVRLNAGAASFRSQKSMNQDYRRSVSQRNSPSANGGGSGSHESSNNSPNSIVGSQSNSAANTPNAAAPPPPQPQPTLVSHSGGFVVLDQTTGAAMNASPPSLYGGGGGPNAGISGGAGASGAAGSNGGHQPGGGGGARSHIPTAQLHHSAAAAAAAAAGSQQATAAVLSGVAAAAALGGYNPNGASGVYFKYGQTYFAHPSVALPNSRRSPSNDIRPQMAQVAGMYPTMMIQARHPSRHPNPNYKGSRPR
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
135PhosphorylationSNLGRQNSFGNRRGN
CCCCCCCCCCCCCCC		26.6229892262
157PhosphorylationRSHAMRESTSPPRTP
HHHHHCCCCCCCCCC		24.6619429919
158PhosphorylationSHAMRESTSPPRTPT
HHHHCCCCCCCCCCC		40.2619429919
159PhosphorylationHAMRESTSPPRTPTP
HHHCCCCCCCCCCCH		42.0319429919
163PhosphorylationESTSPPRTPTPRAAS
CCCCCCCCCCHHHCC		36.9719429919
165PhosphorylationTSPPRTPTPRAASEQ
CCCCCCCCHHHCCHH		25.4619429919
244PhosphorylationPQQNVPLSNEAEFPK
CCCCCCCCCCCCCCC		26.9319429919
253PhosphorylationEAEFPKLSPPKKSGG
CCCCCCCCCCCCCCC		45.3319429919
265PhosphorylationSGGQHNRTNSNGSGM
CCCCCCCCCCCCCCC		48.6019429919
267PhosphorylationGQHNRTNSNGSGMEF
CCCCCCCCCCCCCCC		41.7919429919
270PhosphorylationNRTNSNGSGMEFNNN
CCCCCCCCCCCCCCC		38.9419429919
314PhosphorylationIFNSGMNYKAAERHD
EECCCCCHHHHHHHH		7.9718281928
329PhosphorylationRHERHEMSSQNSNLS
HHHHHHHHHCCCCCC		26.2821082442
330PhosphorylationHERHEMSSQNSNLSN
HHHHHHHHCCCCCCC		31.8821082442
333PhosphorylationHEMSSQNSNLSNNHD
HHHHHCCCCCCCCCC		31.3521082442
336PhosphorylationSSQNSNLSNNHDEEP
HHCCCCCCCCCCCCC		39.5822817900
533PhosphorylationKSILKRDTHSFDEVR
HHHHHCCCCCHHHHH		24.3721082442
535PhosphorylationILKRDTHSFDEVRQS
HHHCCCCCHHHHHCC		36.1619429919
549PhosphorylationSPYLCPLSLDRKAKS
CCCCCCCCCCCCCCC		17.2321082442
556PhosphorylationSLDRKAKSFEEREED
CCCCCCCCHHHHHHH		42.6319429919
623PhosphorylationKMLQMQNSTESRDGM
CCCCCCCCCCCCCCC		19.3619429919
624PhosphorylationMLQMQNSTESRDGMR
CCCCCCCCCCCCCCC		45.5919429919
626PhosphorylationQMQNSTESRDGMRSG
CCCCCCCCCCCCCCC		35.4419429919
651PhosphorylationNYGGPPSSGGPGNNS
CCCCCCCCCCCCCCC		54.2521082442
658PhosphorylationSGGPGNNSLPRGDST
CCCCCCCCCCCCCCC		43.6921082442
680PhosphorylationGGFVKQDSTGSTPWR
CCCCCCCCCCCCCCE		31.9721082442
850PhosphorylationTSTSTKNYDRIEVQK
CCCCCCCCCEEEEEH		14.2518281928
863PhosphorylationQKYKNQATSPNIPAC
EHHCCCCCCCCCCCC		34.6529892262
864PhosphorylationKYKNQATSPNIPACC
HHCCCCCCCCCCCCH		20.9729892262
944PhosphorylationYSQCEVKTPSQNHAP
CCCCEECCCCCCCCC		33.0919429919
946PhosphorylationQCEVKTPSQNHAPSA
CCEECCCCCCCCCCC		49.1719429919
1457PhosphorylationRNHGGGASGAHSVGV
CCCCCCCCCCCCCCC		39.5221082442
1461PhosphorylationGGASGAHSVGVRKPY
CCCCCCCCCCCCCCC		21.7421082442
1478PhosphorylationGGYNPRHSVPLGGIP
CCCCCCCCCCCCCCC		27.0621082442
1490PhosphorylationGIPSGAKTPLLNSNN
CCCCCCCCCCCCCCC		20.7329892262
1500PhosphorylationLNSNNEPTPRASPSS
CCCCCCCCCCCCCCC		21.1621082442
1578PhosphorylationRLNAGAASFRSQKSM
CCCCCCHHHHHHHHC		22.2121082442
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 ENC_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENC_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 ENC_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED17_DROMEMED17physical
22036573
EBI_DROMEebiphysical
22036573
MED6_DROMEMED6physical
22036573
CPSF6_DROMECG7185physical
22036573
MED18_DROMEMED18physical
22036573
MED11_DROMEMED11physical
22036573
MED7_DROMEMED7physical
22036573
MED14_DROMEMED14physical
22036573
MED20_DROMEMED20physical
22036573
MED27_DROMEMED27physical
22036573
CDK8_DROMECdk8physical
22036573
MED10_DROMEMED10physical
22036573
BAP60_DROMEBap60physical
22036573
MED15_DROMEMED15physical
22036573
CCNE_DROMECycEphysical
14623823
RUX_DROMEruxgenetic
14623823
OTU_DROMEotugenetic
11879639
UBCD2_DROMEUbcD2genetic
14623823
CCNE_DROMECycEgenetic
14623823
CUL1_DROMECul1genetic
14623823
UBCD1_DROMEeffgenetic
14623823
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENC_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-267; SER-270; SER-336AND SER-535, AND MASS SPECTROMETRY.

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