ENA_DROME - dbPTM
ENA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENA_DROME
UniProt AC Q8T4F7
Protein Name Protein enabled
Gene Name ena
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 980
Subcellular Localization Cell projection, lamellipodium . Cytoplasm, cytoskeleton . Expressed at the leading edge of lamellipodia. Colocalizes with chic at the periphery of cells.
Protein Description Functions, together with Abl, trio and fra, in a complex signaling network that regulates axon guidance at the CNS midline. Required in part for robo-mediated repulsive axon guidance. May be involved in lamellipodial dynamics..
Protein Sequence MAMKKLYAKTSFTSKKPSSAANSTPILAYHQQQHQQPGNGICEFQVVAPGHSGELMIRRSQSMHHKMSPPVGGLGSKSEYYSIEELQELDLLDYRHPMYHHYQQQELRQRYHEHEQLVLQLPKATSPKAGPIYEAPQRSQQQQDQMLYVPTAAQRDSSSSAAATSIASSSTLTSSPSPSSSSSLIFSTLRKCVSPSNPSVNPNQPSKTQPSKLGCSMSFSIRTTTATAATAAAANAATATLSTQQQQQQAQQQHKQHLYSNIHHYLIRQQQQKQHYTLQRRHNSVKDKFIGGITTIFAEQSIIGARASVMVYDDNQKKWVPSGSSSGLSKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWRDSKFVYGLNFSSQNDAENFARAMMHALEVLSGRVANNPGGPPTNGNGYEEDMGYRTMTSEDAAILRQNNSIGGHVTPSAQTPTSQTNQNNIPQSPPTPQGHHRTSSAPPAPQPQQQQQQQQAQQMGQPGSHYGPTGNGPTSNGLPQQVNSQIPPAPQQQPQQQQFQQQQQQQQYQQMVQAGYAPSQQYQQPHYVLSNSNPNLTVHQYPTQQAQQQPPQAPQPPLQNGGMYMVGHGHLPSSASANSVVYASQQQMLPQAHPQAPQAPTMPGPGYGGPPVPPPQQQAENPYGQVPMPPPMNPSQQQQPGQVPLNRMSSQGGPGGPPAPAPPPPPPSFGGAAGGGPPPPAPPQMFNGAPPPPAMGGGPPPAPPAPPAMGGGPPPAPGGPGAPPPPPPPPGLGGAPKKEDPQADLMGSLASQLQQIKLKKNKVTTSAPENSGSSTSSGGSGNYGTIGRSSNGMASMMDEMAKTLARRRAQAEKKDPDPEAEVKKRPWEKSNTLPHKLSGGAGSGSAGSGHEGANGNSGGAGSNTTNSGGESPRPMRKRFGSASEETILKVNGDGLSLALSNGDLDTLKAEIVREMRLEIQKVKNEIIDAIKSEFNRR
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
68PhosphorylationQSMHHKMSPPVGGLG
HHCCCCCCCCCCCCC		30.7519429919
80PhosphorylationGLGSKSEYYSIEELQ
CCCCCCCEECHHHHH		15.0318281928
94PhosphorylationQELDLLDYRHPMYHH
HHCCCCCCCCCCHHH		15.7018281928
99PhosphorylationLDYRHPMYHHYQQQE
CCCCCCCHHHHHHHH		7.0118281928
126PhosphorylationLQLPKATSPKAGPIY
HCCCCCCCCCCCCCC		29.3018281928
133 (in isoform 1)Phosphorylation-14.7918281928
133PhosphorylationSPKAGPIYEAPQRSQ
CCCCCCCCCCCCCCH		14.7927626673
274PhosphorylationIRQQQQKQHYTLQRR
HHHHHHHHHHHHHHH		30.409418863
425PhosphorylationPPTNGNGYEEDMGYR
CCCCCCCCCCCCCCC		21.839418863
431PhosphorylationGYEEDMGYRTMTSED
CCCCCCCCCCCCHHH		9.0418281928
447PhosphorylationAILRQNNSIGGHVTP
HHHHHCCCCCCCCCC		30.1121082442
453PhosphorylationNSIGGHVTPSAQTPT
CCCCCCCCCCCCCCC		13.0721082442
456PhosphorylationGGHVTPSAQTPTSQT
CCCCCCCCCCCCCCC		20.619418863
460PhosphorylationTPSAQTPTSQTNQNN
CCCCCCCCCCCCCCC		36.5321082442
463PhosphorylationAQTPTSQTNQNNIPQ
CCCCCCCCCCCCCCC		38.2421082442
471PhosphorylationNQNNIPQSPPTPQGH
CCCCCCCCCCCCCCC		27.7421082442
474PhosphorylationNIPQSPPTPQGHHRT
CCCCCCCCCCCCCCC		31.469418863
499PhosphorylationQQQQQQQAQQMGQPG
HHHHHHHHHHHCCCC		9.389418863
515PhosphorylationHYGPTGNGPTSNGLP
CCCCCCCCCCCCCCC		28.369418863
607PhosphorylationPLQNGGMYMVGHGHL
CCCCCCEEEEECCCC		7.609418863
625PhosphorylationASANSVVYASQQQML
CCCCHHHHHHHHHCC		9.819418863
650PhosphorylationPTMPGPGYGGPPVPP
CCCCCCCCCCCCCCC		23.269418863
666PhosphorylationQQQAENPYGQVPMPP
HHHCCCCCCCCCCCC		31.609418863
675PhosphorylationQVPMPPPMNPSQQQQ
CCCCCCCCCHHHCCC		16.569418863
754PhosphorylationPAPPAMGGGPPPAPG
CCCCCCCCCCCCCCC		32.1418327897
763PhosphorylationPPPAPGGPGAPPPPP
CCCCCCCCCCCCCCC		41.5118327897
773PhosphorylationPPPPPPPPGLGGAPK
CCCCCCCCCCCCCCC		57.3118327897
826PhosphorylationSSGGSGNYGTIGRSS
CCCCCCCCCCCCCCC		21.129418863
828PhosphorylationGGSGNYGTIGRSSNG
CCCCCCCCCCCCCCH		15.1923607784
881PhosphorylationNTLPHKLSGGAGSGS
CCCCCCCCCCCCCCC		39.7329892262
900PhosphorylationHEGANGNSGGAGSNT
CCCCCCCCCCCCCCC		39.7522668510
905PhosphorylationGNSGGAGSNTTNSGG
CCCCCCCCCCCCCCC		30.3919060867
907PhosphorylationSGGAGSNTTNSGGES
CCCCCCCCCCCCCCC		29.1123607784
910PhosphorylationAGSNTTNSGGESPRP
CCCCCCCCCCCCCCC		46.1923607784
914PhosphorylationTTNSGGESPRPMRKR
CCCCCCCCCCCCHHH		29.5023607784
924PhosphorylationPMRKRFGSASEETIL
CCHHHCCCCCCCEEE		26.3821082442
926PhosphorylationRKRFGSASEETILKV
HHHCCCCCCCEEEEE		37.3519429919
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
274YPhosphorylationKinaseABL1-PhosphoELM
425YPhosphorylationKinaseABL-FAMILY-GPS
456YPhosphorylationKinaseABL1-PhosphoELM
474YPhosphorylationKinaseABL1-PhosphoELM
499YPhosphorylationKinaseABL1-PhosphoELM
515YPhosphorylationKinaseABL1-PhosphoELM
607YPhosphorylationKinaseABL-FAMILY-GPS
625YPhosphorylationKinaseABL-FAMILY-GPS
650YPhosphorylationKinaseABL-FAMILY-GPS
666YPhosphorylationKinaseABL-FAMILY-GPS
675YPhosphorylationKinaseABL1-PhosphoELM
826YPhosphorylationKinaseABL-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENA_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 ENA_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP1B_DROMEflwphysical
14605208
ROP_DROMERopphysical
22036573
NOTCH_DROMENgenetic
12781136
DIA_DROMEdiaphysical
19846663
ENA_DROMEenaphysical
9693373
ABL_DROMEAblphysical
7535279
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENA_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-905; SER-914 ANDSER-924, 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-924, AND MASSSPECTROMETRY.
"Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinaseregulates the in vivo function and protein-protein interactions ofEnabled.";
Comer A.R., Ahern-Djamali S.M., Juang J.-L., Jackson P.D.,Hoffmann F.M.;
Mol. Cell. Biol. 18:152-160(1998).
Cited for: PHOSPHORYLATION AT TYR-425; TYR-607; TYR-625; TYR-650; TYR-666 ANDTYR-826.

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