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Q8T4F7

- ENA_DROME

UniProt

Q8T4F7 - ENA_DROME

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Protein

Protein enabled

Gene

ena

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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-KW
  6. cytosol Source: Reactome
  7. filopodium tip Source: FlyBase
  8. lamellipodium Source: UniProtKB
Complete GO annotation...

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 – 4251Phosphotyrosine1 Publication
Modified residuei607 – 6071Phosphotyrosine1 Publication
Modified residuei625 – 6251Phosphotyrosine1 Publication
Modified residuei650 – 6501Phosphotyrosine1 Publication
Modified residuei666 – 6661Phosphotyrosine1 Publication
Modified residuei826 – 8261Phosphotyrosine1 Publication
Modified residuei905 – 9051Phosphoserine1 Publication
Modified residuei914 – 9141Phosphoserine1 Publication
Modified residuei924 – 9241Phosphoserine2 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) [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

        10         20         30         40         50
MAMKKLYAKT SFTSKKPSSA ANSTPILAYH QQQHQQPGNG ICEFQVVAPG
60 70 80 90 100
HSGELMIRRS QSMHHKMSPP VGGLGSKSEY YSIEELQELD LLDYRHPMYH
110 120 130 140 150
HYQQQELRQR YHEHEQLVLQ LPKATSPKAG PIYEAPQRSQ QQQDQMLYVP
160 170 180 190 200
TAAQRDSSSS AAATSIASSS TLTSSPSPSS SSSLIFSTLR KCVSPSNPSV
210 220 230 240 250
NPNQPSKTQP SKLGCSMSFS IRTTTATAAT AAAANAATAT LSTQQQQQQA
260 270 280 290 300
QQQHKQHLYS NIHHYLIRQQ QQKQHYTLQR RHNSVKDKFI GGITTIFAEQ
310 320 330 340 350
SIIGARASVM VYDDNQKKWV PSGSSSGLSK VQIYHHQQNN TFRVVGRKLQ
360 370 380 390 400
DHEVVINCSI LKGLKYNQAT ATFHQWRDSK FVYGLNFSSQ NDAENFARAM
410 420 430 440 450
MHALEVLSGR VANNPGGPPT NGNGYEEDMG YRTMTSEDAA ILRQNNSIGG
460 470 480 490 500
HVTPSAQTPT SQTNQNNIPQ SPPTPQGHHR TSSAPPAPQP QQQQQQQQAQ
510 520 530 540 550
QMGQPGSHYG PTGNGPTSNG LPQQVNSQIP PAPQQQPQQQ QFQQQQQQQQ
560 570 580 590 600
YQQMVQAGYA PSQQYQQPHY VLSNSNPNLT VHQYPTQQAQ QQPPQAPQPP
610 620 630 640 650
LQNGGMYMVG HGHLPSSASA NSVVYASQQQ MLPQAHPQAP QAPTMPGPGY
660 670 680 690 700
GGPPVPPPQQ QAENPYGQVP MPPPMNPSQQ QQPGQVPLNR MSSQGGPGGP
710 720 730 740 750
PAPAPPPPPP SFGGAAGGGP PPPAPPQMFN GAPPPPAMGG GPPPAPPAPP
760 770 780 790 800
AMGGGPPPAP GGPGAPPPPP PPPGLGGAPK KEDPQADLMG SLASQLQQIK
810 820 830 840 850
LKKNKVTTSA PENSGSSTSS GGSGNYGTIG RSSNGMASMM DEMAKTLARR
860 870 880 890 900
RAQAEKKDPD PEAEVKKRPW EKSNTLPHKL SGGAGSGSAG SGHEGANGNS
910 920 930 940 950
GGAGSNTTNS GGESPRPMRK RFGSASEETI LKVNGDGLSL ALSNGDLDTL
960 970 980
KAEIVREMRL EIQKVKNEII DAIKSEFNRR

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_001014536.2. [Q8T4F7-2]
NP_001014537.1. NM_001014537.3. [Q8T4F7-3]
NP_001137709.1. NM_001144237.2. [Q8T4F7-4]
NP_725857.1. NM_166329.2. [Q8T4F7-2]
NP_725858.1. NM_166330.2. [Q8T4F7-2]
NP_725859.2. NM_166331.3. [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_001014536.2. [Q8T4F7-2 ]
NP_001014537.1. NM_001014537.3. [Q8T4F7-3 ]
NP_001137709.1. NM_001144237.2. [Q8T4F7-4 ]
NP_725857.1. NM_166329.2. [Q8T4F7-2 ]
NP_725858.1. NM_166330.2. [Q8T4F7-2 ]
NP_725859.2. NM_166331.3. [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

« Hide 'large scale' publications
  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 29, 2014
This is version 108 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