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Q8T4F7

- ENA_DROME

UniProt

Q8T4F7 - ENA_DROME

Protein

Protein enabled

Gene

ena

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 4 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. actin binding Source: FlyBase
    2. protein binding Source: UniProtKB
    3. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: FlyBase
    2. actin filament organization Source: FlyBase
    3. axon guidance Source: FlyBase
    4. axonogenesis Source: FlyBase
    5. border follicle cell migration Source: FlyBase
    6. compound eye development Source: FlyBase
    7. cytoplasmic transport, nurse cell to oocyte Source: FlyBase
    8. cytoskeleton organization Source: FlyBase
    9. dendrite morphogenesis Source: FlyBase
    10. dorsal closure Source: FlyBase
    11. epithelial cell morphogenesis Source: FlyBase
    12. formation of a compartment boundary Source: FlyBase
    13. germ-band shortening Source: FlyBase
    14. gonad morphogenesis Source: FlyBase
    15. head involution Source: FlyBase
    16. positive regulation of cell migration Source: FlyBase
    17. positive regulation of cell projection organization Source: FlyBase
    18. positive regulation of filopodium assembly Source: FlyBase
    19. regulation of actin polymerization or depolymerization Source: FlyBase
    20. regulation of cell shape Source: FlyBase
    21. regulation of filopodium assembly Source: FlyBase
    22. regulation of lamellipodium assembly Source: FlyBase
    23. suture of dorsal opening Source: FlyBase

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein enabled
    Gene namesi
    Name:ena
    Synonyms:enb
    ORF Names:CG15112
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0000578. ena.

    Subcellular locationi

    Cell projectionlamellipodium 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Expressed at the leading edge of lamellipodia. Colocalizes with chic at the periphery of cells.

    GO - Cellular componenti

    1. adherens junction Source: FlyBase
    2. axon Source: FlyBase
    3. cell-cell junction Source: FlyBase
    4. cell leading edge Source: FlyBase
    5. cytoskeleton Source: UniProtKB-SubCell
    6. cytosol Source: Reactome
    7. filopodium tip Source: FlyBase
    8. lamellipodium Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 980980Protein enabledPRO_0000227757Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei425 – 4251Phosphotyrosine2 Publications
    Modified residuei607 – 6071Phosphotyrosine2 Publications
    Modified residuei625 – 6251Phosphotyrosine2 Publications
    Modified residuei650 – 6501Phosphotyrosine2 Publications
    Modified residuei666 – 6661Phosphotyrosine2 Publications
    Modified residuei826 – 8261Phosphotyrosine2 Publications
    Modified residuei905 – 9051Phosphoserine2 Publications
    Modified residuei914 – 9141Phosphoserine2 Publications
    Modified residuei924 – 9241Phosphoserine3 Publications

    Post-translational modificationi

    Tyrosine phosphorylated on multiple sites by Abl kinase. In vitro, phosphorylation on specific tyrosine residues inhibits interaction with Abl and Src SH3 domains.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8T4F7.

    Expressioni

    Tissue specificityi

    Expressed in axons of the embryonic nervous system.1 Publication

    Gene expression databases

    BgeeiQ8T4F7.

    Interactioni

    Subunit structurei

    Interacts with Abl and Src SH3 domains. Binds, in vitro and in vivo, the cytoplasmic domain of robo. Interacts with Zyx102EF and chic.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AblP005222EBI-466810,EBI-534090
    chicP258433EBI-466810,EBI-156199
    LarP166212EBI-466810,EBI-668630
    SrcP054802EBI-466810,EBI-298680From a different organism.

    Protein-protein interaction databases

    BioGridi62866. 44 interactions.
    IntActiQ8T4F7. 32 interactions.
    MINTiMINT-817415.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8T4F7.
    SMRiQ8T4F7. Positions 298-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini146 – 407262WH1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni791 – 980190EVH2Add
    BLAST
    Regioni791 – 81020EVH2 block AAdd
    BLAST
    Regioni837 – 85418EVH2 block BAdd
    BLAST
    Regioni947 – 98034EVH2 block CAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi800 – 8034KLKR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi157 – 22064Ser-richAdd
    BLAST
    Compositional biasi244 – 27936Gln-richAdd
    BLAST
    Compositional biasi457 – 685229Gln-richAdd
    BLAST
    Compositional biasi633 – 784152Pro-richAdd
    BLAST

    Domaini

    The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.

    Sequence similaritiesi

    Belongs to the Ena/VASP family.Curated
    Contains 1 WH1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiNOG289321.
    GeneTreeiENSGT00730000110272.
    InParanoidiQ8T4F7.
    OMAiINCSILK.
    OrthoDBiEOG72JWGQ.
    PhylomeDBiQ8T4F7.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    IPR014885. VASP_tetra.
    IPR000697. WH1/EVH1.
    [Graphical view]
    PfamiPF08776. VASP_tetra. 1 hit.
    PF00568. WH1. 1 hit.
    [Graphical view]
    SMARTiSM00160. RanBD. 1 hit.
    SM00461. WH1. 1 hit.
    [Graphical view]
    PROSITEiPS50229. WH1. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 4 (identifier: Q8T4F7-4) [UniParc]FASTAAdd to Basket

    Also known as: F

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAMKKLYAKT SFTSKKPSSA ANSTPILAYH QQQHQQPGNG ICEFQVVAPG    50
    HSGELMIRRS QSMHHKMSPP VGGLGSKSEY YSIEELQELD LLDYRHPMYH 100
    HYQQQELRQR YHEHEQLVLQ LPKATSPKAG PIYEAPQRSQ QQQDQMLYVP 150
    TAAQRDSSSS AAATSIASSS TLTSSPSPSS SSSLIFSTLR KCVSPSNPSV 200
    NPNQPSKTQP SKLGCSMSFS IRTTTATAAT AAAANAATAT LSTQQQQQQA 250
    QQQHKQHLYS NIHHYLIRQQ QQKQHYTLQR RHNSVKDKFI GGITTIFAEQ 300
    SIIGARASVM VYDDNQKKWV PSGSSSGLSK VQIYHHQQNN TFRVVGRKLQ 350
    DHEVVINCSI LKGLKYNQAT ATFHQWRDSK FVYGLNFSSQ NDAENFARAM 400
    MHALEVLSGR VANNPGGPPT NGNGYEEDMG YRTMTSEDAA ILRQNNSIGG 450
    HVTPSAQTPT SQTNQNNIPQ SPPTPQGHHR TSSAPPAPQP QQQQQQQQAQ 500
    QMGQPGSHYG PTGNGPTSNG LPQQVNSQIP PAPQQQPQQQ QFQQQQQQQQ 550
    YQQMVQAGYA PSQQYQQPHY VLSNSNPNLT VHQYPTQQAQ QQPPQAPQPP 600
    LQNGGMYMVG HGHLPSSASA NSVVYASQQQ MLPQAHPQAP QAPTMPGPGY 650
    GGPPVPPPQQ QAENPYGQVP MPPPMNPSQQ QQPGQVPLNR MSSQGGPGGP 700
    PAPAPPPPPP SFGGAAGGGP PPPAPPQMFN GAPPPPAMGG GPPPAPPAPP 750
    AMGGGPPPAP GGPGAPPPPP PPPGLGGAPK KEDPQADLMG SLASQLQQIK 800
    LKKNKVTTSA PENSGSSTSS GGSGNYGTIG RSSNGMASMM DEMAKTLARR 850
    RAQAEKKDPD PEAEVKKRPW EKSNTLPHKL SGGAGSGSAG SGHEGANGNS 900
    GGAGSNTTNS GGESPRPMRK RFGSASEETI LKVNGDGLSL ALSNGDLDTL 950
    KAEIVREMRL EIQKVKNEII DAIKSEFNRR 980

    Note: No experimental confirmation available.

    Length:980
    Mass (Da):104,824
    Last modified:July 7, 2009 - v4
    Checksum:i7B084A0AEC098297
    GO
    Isoform 1 (identifier: Q8T4F7-1) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         147-147: L → F
         148-298: Missing.
         482-482: S → SRNSL
         932-932: K → KQ

    Note: No experimental confirmation available.

    Show »
    Length:834
    Mass (Da):89,280
    Checksum:i7E0CD375D351C674
    GO
    Isoform 2 (identifier: Q8T4F7-2) [UniParc]FASTAAdd to Basket

    Also known as: A, C, E

    The sequence of this isoform differs from the canonical sequence as follows:
         2-297: Missing.
         298-298: A → T

    Show »
    Length:684
    Mass (Da):71,985
    Checksum:iE1FFB5A8091FA77E
    GO
    Isoform 3 (identifier: Q8T4F7-3) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         2-297: Missing.
         298-298: A → T
         482-482: S → SRNSL
         563-563: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:687
    Mass (Da):72,327
    Checksum:iF480275EB4CC79A8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201Q → H in AAL89948. (PubMed:12537569)Curated
    Sequence conflicti491 – 4933Missing in AAL89948. (PubMed:12537569)Curated
    Sequence conflicti612 – 6121G → S in AAA85120. (PubMed:7535279)Curated
    Sequence conflicti799 – 7991I → F in AAA85120. (PubMed:7535279)Curated
    Sequence conflicti799 – 7991I → F in AAL89948. (PubMed:12537569)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 297296Missing in isoform 2 and isoform 3. 1 PublicationVSP_017574Add
    BLAST
    Alternative sequencei147 – 1471L → F in isoform 1. 1 PublicationVSP_037651
    Alternative sequencei148 – 298151Missing in isoform 1. 1 PublicationVSP_037652Add
    BLAST
    Alternative sequencei298 – 2981A → T in isoform 2 and isoform 3. 1 PublicationVSP_017575
    Alternative sequencei482 – 4821S → SRNSL in isoform 1 and isoform 3. 2 PublicationsVSP_019865
    Alternative sequencei563 – 5631Missing in isoform 3. 1 PublicationVSP_019866
    Alternative sequencei932 – 9321K → KQ in isoform 1. 1 PublicationVSP_037653

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21123 Genomic DNA. Translation: AAA85120.1.
    AE013599 Genomic DNA. Translation: AAF57598.2.
    AE013599 Genomic DNA. Translation: AAM68438.2.
    AE013599 Genomic DNA. Translation: AAM68439.2.
    AE013599 Genomic DNA. Translation: AAX52696.1.
    AE013599 Genomic DNA. Translation: AAX52697.1.
    AE013599 Genomic DNA. Translation: ACL83163.1.
    AY084210 mRNA. Translation: AAL89948.1.
    BT004488 mRNA. Translation: AAO42652.1.
    PIRiA56154.
    RefSeqiNP_001014536.1. NM_001014536.1. [Q8T4F7-2]
    NP_001014537.1. NM_001014537.2. [Q8T4F7-3]
    NP_001137709.1. NM_001144237.1. [Q8T4F7-4]
    NP_725857.1. NM_166329.1. [Q8T4F7-2]
    NP_725858.1. NM_166330.1. [Q8T4F7-2]
    NP_725859.2. NM_166331.2. [Q8T4F7-1]
    UniGeneiDm.14700.

    Genome annotation databases

    EnsemblMetazoaiFBtr0114623; FBpp0113115; FBgn0000578. [Q8T4F7-4]
    GeneIDi37201.
    KEGGidme:Dmel_CG15112.
    UCSCiCG15112-RA. d. melanogaster.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21123 Genomic DNA. Translation: AAA85120.1 .
    AE013599 Genomic DNA. Translation: AAF57598.2 .
    AE013599 Genomic DNA. Translation: AAM68438.2 .
    AE013599 Genomic DNA. Translation: AAM68439.2 .
    AE013599 Genomic DNA. Translation: AAX52696.1 .
    AE013599 Genomic DNA. Translation: AAX52697.1 .
    AE013599 Genomic DNA. Translation: ACL83163.1 .
    AY084210 mRNA. Translation: AAL89948.1 .
    BT004488 mRNA. Translation: AAO42652.1 .
    PIRi A56154.
    RefSeqi NP_001014536.1. NM_001014536.1. [Q8T4F7-2 ]
    NP_001014537.1. NM_001014537.2. [Q8T4F7-3 ]
    NP_001137709.1. NM_001144237.1. [Q8T4F7-4 ]
    NP_725857.1. NM_166329.1. [Q8T4F7-2 ]
    NP_725858.1. NM_166330.1. [Q8T4F7-2 ]
    NP_725859.2. NM_166331.2. [Q8T4F7-1 ]
    UniGenei Dm.14700.

    3D structure databases

    ProteinModelPortali Q8T4F7.
    SMRi Q8T4F7. Positions 298-408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62866. 44 interactions.
    IntActi Q8T4F7. 32 interactions.
    MINTi MINT-817415.

    Proteomic databases

    PaxDbi Q8T4F7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0114623 ; FBpp0113115 ; FBgn0000578 . [Q8T4F7-4 ]
    GeneIDi 37201.
    KEGGi dme:Dmel_CG15112.
    UCSCi CG15112-RA. d. melanogaster.

    Organism-specific databases

    CTDi 37201.
    FlyBasei FBgn0000578. ena.

    Phylogenomic databases

    eggNOGi NOG289321.
    GeneTreei ENSGT00730000110272.
    InParanoidi Q8T4F7.
    OMAi INCSILK.
    OrthoDBi EOG72JWGQ.
    PhylomeDBi Q8T4F7.

    Miscellaneous databases

    ChiTaRSi ena. drosophila.
    GenomeRNAii 37201.
    NextBioi 802467.
    PROi Q8T4F7.

    Gene expression databases

    Bgeei Q8T4F7.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    IPR014885. VASP_tetra.
    IPR000697. WH1/EVH1.
    [Graphical view ]
    Pfami PF08776. VASP_tetra. 1 hit.
    PF00568. WH1. 1 hit.
    [Graphical view ]
    SMARTi SM00160. RanBD. 1 hit.
    SM00461. WH1. 1 hit.
    [Graphical view ]
    PROSITEi PS50229. WH1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Enabled, a dosage-sensitive suppressor of mutations in the Drosophila Abl tyrosine kinase, encodes an Abl substrate with SH3 domain-binding properties."
      Gertler F.B., Comer A.R., Juang J.-L., Ahern S.M., Clark M.J., Liebl E.C., Hoffmann F.M.
      Genes Dev. 9:521-533(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), INTERACTION WITH ABL AND SRC, PHOSPHORYLATION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: Berkeley.
      Tissue: Embryo.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Strain: Berkeley.
      Tissue: Embryo.
    6. "The Abelson tyrosine kinase, the Trio GEF and Enabled interact with the Netrin receptor Frazzled in Drosophila."
      Forsthoefel D.J., Liebl E.C., Kolodziej P.A., Seeger M.A.
      Development 132:1983-1994(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled."
      Comer A.R., Ahern-Djamali S.M., Juang J.-L., Jackson P.D., Hoffmann F.M.
      Mol. Cell. Biol. 18:152-160(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-425; TYR-607; TYR-625; TYR-650; TYR-666 AND TYR-826.
    8. "Identification of profilin and src homology 3 domains as binding partners for Drosophila enabled."
      Ahern-Djamali S.M., Bachmann C., Hua P., Reddy S.K., Kastenmeier A.S., Walter U., Hoffmann F.M.
      Proc. Natl. Acad. Sci. U.S.A. 96:4977-4982(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHIC.
    9. "Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor."
      Bashaw G.J., Kidd T., Murray D., Pawson T., Goodman C.S.
      Cell 101:703-715(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROBO.
    10. "Molecular and phylogenetic characterization of Zyx102, a Drosophila orthologue of the zyxin family that interacts with Drosophila Enabled."
      Renfranz P.J., Siegrist S.E., Stronach B.E., Macalma T., Beckerle M.C.
      Gene 305:13-26(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZYX102EF.
    11. "Cascade pathway of filopodia formation downstream of SCAR."
      Biyasheva A., Svitkina T., Kunda P., Baum B., Borisy G.
      J. Cell Sci. 117:837-848(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905; SER-914 AND SER-924, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiENA_DROME
    AccessioniPrimary (citable) accession number: Q8T4F7
    Secondary accession number(s): A4UZP3
    , B7YZL0, Q24035, Q86NN6, Q8MMB3, Q9V8R3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 107 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3