Q8T4F7 (ENA_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein enabled

Gene names

Name:	ena
Synonyms:	enb
ORF Names:	CG15112

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	980 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6
Subunit structure	Interacts with Abl and Src SH3 domains. Binds, in vitro and in vivo, the cytoplasmic domain of robo. Interacts with Zyx102EF and chic. Ref.1 Ref.8 Ref.9 Ref.10
Subcellular location	Cell projection › lamellipodium. Cytoplasm › cytoskeleton. Note: Expressed at the leading edge of lamellipodia. Co-localizes with chic at the periphery of cells. Ref.11
Tissue specificity	Expressed in axons of the embryonic nervous system. Ref.1
Domain	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.
Post-translational modification	Tyrosine phosphorylated on multiple sites by Abl kinase. In vitro, phosphorylation on specific tyrosine residues inhibits interaction with Abl and Src SH3 domains. Ref.1 Ref.7
Sequence similarities	Belongs to the Ena/VASP family. Contains 1 WH1 domain.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	SH3-binding
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from mutant phenotype PubMed 14527345PubMed 19000833PubMed 19576200. Source: FlyBase axon guidance Inferred from mutant phenotype PubMed 10069336. Source: FlyBase border follicle cell migration Inferred from mutant phenotype PubMed 19576200. Source: FlyBase compound eye development Inferred from genetic interaction PubMed 19753121. Source: FlyBase cytoplasmic transport, nurse cell to oocyte Inferred from mutant phenotype PubMed 19576200. Source: FlyBase dendrite morphogenesis Inferred from mutant phenotype PubMed 10521399PubMed 18817767. Source: FlyBase epithelial cell morphogenesis Inferred from genetic interaction PubMed 11756472. Source: FlyBase formation of a compartment boundary Inferred from mutant phenotype PubMed 21795284. Source: FlyBase germ-band shortening Inferred from mutant phenotype PubMed 17507404. Source: FlyBase gonad morphogenesis Inferred from mutant phenotype PubMed 23300733. Source: FlyBase head involution Inferred from mutant phenotype PubMed 17507404. Source: FlyBase positive regulation of filopodium assembly Inferred from mutant phenotype PubMed 17507404PubMed 21464901. Source: FlyBase regulation of actin polymerization or depolymerization Traceable author statement PubMed 12231351. Source: FlyBase regulation of cell shape Inferred from mutant phenotype PubMed 14527345. Source: FlyBase regulation of lamellipodium assembly Inferred from mutant phenotype PubMed 19846663. Source: FlyBase suture of dorsal opening Inferred from mutant phenotype PubMed 17507404. Source: FlyBase
Cellular_component	adherens junction Inferred from direct assay PubMed 11756472PubMed 17507404. Source: FlyBase axon Inferred from direct assay PubMed 11756472. Source: FlyBase cell-cell junction Inferred from direct assay Ref.10. Source: FlyBase cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome filopodium tip Inferred from direct assay PubMed 17507404. Source: FlyBase lamellipodium Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	SH3 domain binding Inferred from direct assay Ref.8. Source: UniProtKB actin binding Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Abl	P00522	2	EBI-466810,EBI-534090
chic	P25843	3	EBI-466810,EBI-156199
Lar	P16621	2	EBI-466810,EBI-668630
Src	P05480	2	EBI-466810,EBI-298680	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 4 (identifier: Q8T4F7-4)

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.

Note: No experimental confirmation available.

Isoform 1 (identifier: Q8T4F7-1)

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.

Isoform 2 (identifier: Q8T4F7-2)

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

Isoform 3 (identifier: Q8T4F7-3)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 980	980	Protein enabled		PRO_0000227757
Regions
	Domain	146 – 407	262	WH1
	Region	791 – 980	190	EVH2
	Region	791 – 810	20	EVH2 block A
	Region	837 – 854	18	EVH2 block B
	Region	947 – 980	34	EVH2 block C
	Motif	800 – 803	4	KLKR
	Compositional bias	157 – 220	64	Ser-rich
	Compositional bias	244 – 279	36	Gln-rich
	Compositional bias	457 – 685	229	Gln-rich
	Compositional bias	633 – 784	152	Pro-rich
Amino acid modifications
	Modified residue	425	1	Phosphotyrosine Ref.7
	Modified residue	607	1	Phosphotyrosine Ref.7
	Modified residue	625	1	Phosphotyrosine Ref.7
	Modified residue	650	1	Phosphotyrosine Ref.7
	Modified residue	666	1	Phosphotyrosine Ref.7
	Modified residue	826	1	Phosphotyrosine Ref.7
	Modified residue	905	1	Phosphoserine Ref.13
	Modified residue	914	1	Phosphoserine Ref.13
	Modified residue	924	1	Phosphoserine Ref.12 Ref.13
Natural variations
	Alternative sequence	2 – 297	296	Missing in isoform 2 and isoform 3.		VSP_017574
	Alternative sequence	147	1	L → F in isoform 1.		VSP_037651
	Alternative sequence	148 – 298	151	Missing in isoform 1.		VSP_037652
	Alternative sequence	298	1	A → T in isoform 2 and isoform 3.		VSP_017575
	Alternative sequence	482	1	S → SRNSL in isoform 1 and isoform 3.		VSP_019865
	Alternative sequence	563	1	Missing in isoform 3.		VSP_019866
	Alternative sequence	932	1	K → KQ in isoform 1.		VSP_037653
Experimental info
	Sequence conflict	120	1	Q → H in AAL89948. Ref.4
	Sequence conflict	491 – 493	3	Missing in AAL89948. Ref.4
	Sequence conflict	612	1	G → S in AAA85120. Ref.1
	Sequence conflict	799	1	I → F in AAA85120. Ref.1
	Sequence conflict	799	1	I → F in AAL89948. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 4 (F) [UniParc]. Last modified July 7, 2009. Version 4. Checksum: 7B084A0AEC098297	FASTA	980	104,824
	10 20 30 40 50 60 MAMKKLYAKT SFTSKKPSSA ANSTPILAYH QQQHQQPGNG ICEFQVVAPG HSGELMIRRS 70 80 90 100 110 120 QSMHHKMSPP VGGLGSKSEY YSIEELQELD LLDYRHPMYH HYQQQELRQR YHEHEQLVLQ 130 140 150 160 170 180 LPKATSPKAG PIYEAPQRSQ QQQDQMLYVP TAAQRDSSSS AAATSIASSS TLTSSPSPSS 190 200 210 220 230 240 SSSLIFSTLR KCVSPSNPSV NPNQPSKTQP SKLGCSMSFS IRTTTATAAT AAAANAATAT 250 260 270 280 290 300 LSTQQQQQQA QQQHKQHLYS NIHHYLIRQQ QQKQHYTLQR RHNSVKDKFI GGITTIFAEQ 310 320 330 340 350 360 SIIGARASVM VYDDNQKKWV PSGSSSGLSK VQIYHHQQNN TFRVVGRKLQ DHEVVINCSI 370 380 390 400 410 420 LKGLKYNQAT ATFHQWRDSK FVYGLNFSSQ NDAENFARAM MHALEVLSGR VANNPGGPPT 430 440 450 460 470 480 NGNGYEEDMG YRTMTSEDAA ILRQNNSIGG HVTPSAQTPT SQTNQNNIPQ SPPTPQGHHR 490 500 510 520 530 540 TSSAPPAPQP QQQQQQQQAQ QMGQPGSHYG PTGNGPTSNG LPQQVNSQIP PAPQQQPQQQ 550 560 570 580 590 600 QFQQQQQQQQ YQQMVQAGYA PSQQYQQPHY VLSNSNPNLT VHQYPTQQAQ QQPPQAPQPP 610 620 630 640 650 660 LQNGGMYMVG HGHLPSSASA NSVVYASQQQ MLPQAHPQAP QAPTMPGPGY GGPPVPPPQQ 670 680 690 700 710 720 QAENPYGQVP MPPPMNPSQQ QQPGQVPLNR MSSQGGPGGP PAPAPPPPPP SFGGAAGGGP 730 740 750 760 770 780 PPPAPPQMFN GAPPPPAMGG GPPPAPPAPP AMGGGPPPAP GGPGAPPPPP PPPGLGGAPK 790 800 810 820 830 840 KEDPQADLMG SLASQLQQIK LKKNKVTTSA PENSGSSTSS GGSGNYGTIG RSSNGMASMM 850 860 870 880 890 900 DEMAKTLARR RAQAEKKDPD PEAEVKKRPW EKSNTLPHKL SGGAGSGSAG SGHEGANGNS 910 920 930 940 950 960 GGAGSNTTNS GGESPRPMRK RFGSASEETI LKVNGDGLSL ALSNGDLDTL KAEIVREMRL 970 980 EIQKVKNEII DAIKSEFNRR
	Isoform 1 (B) [UniParc]. Checksum: 7E0CD375D351C674	FASTA	834	89,280
	10 20 30 40 50 60 MAMKKLYAKT SFTSKKPSSA ANSTPILAYH QQQHQQPGNG ICEFQVVAPG HSGELMIRRS 70 80 90 100 110 120 QSMHHKMSPP VGGLGSKSEY YSIEELQELD LLDYRHPMYH HYQQQELRQR YHEHEQLVLQ 130 140 150 160 170 180 LPKATSPKAG PIYEAPQRSQ QQQDQMFEQS IIGARASVMV YDDNQKKWVP SGSSSGLSKV 190 200 210 220 230 240 QIYHHQQNNT FRVVGRKLQD HEVVINCSIL KGLKYNQATA TFHQWRDSKF VYGLNFSSQN 250 260 270 280 290 300 DAENFARAMM HALEVLSGRV ANNPGGPPTN GNGYEEDMGY RTMTSEDAAI LRQNNSIGGH 310 320 330 340 350 360 VTPSAQTPTS QTNQNNIPQS PPTPQGHHRT SRNSLSAPPA PQPQQQQQQQ QAQQMGQPGS 370 380 390 400 410 420 HYGPTGNGPT SNGLPQQVNS QIPPAPQQQP QQQQFQQQQQ QQQYQQMVQA GYAPSQQYQQ 430 440 450 460 470 480 PHYVLSNSNP NLTVHQYPTQ QAQQQPPQAP QPPLQNGGMY MVGHGHLPSS ASANSVVYAS 490 500 510 520 530 540 QQQMLPQAHP QAPQAPTMPG PGYGGPPVPP PQQQAENPYG QVPMPPPMNP SQQQQPGQVP 550 560 570 580 590 600 LNRMSSQGGP GGPPAPAPPP PPPSFGGAAG GGPPPPAPPQ MFNGAPPPPA MGGGPPPAPP 610 620 630 640 650 660 APPAMGGGPP PAPGGPGAPP PPPPPPGLGG APKKEDPQAD LMGSLASQLQ QIKLKKNKVT 670 680 690 700 710 720 TSAPENSGSS TSSGGSGNYG TIGRSSNGMA SMMDEMAKTL ARRRAQAEKK DPDPEAEVKK 730 740 750 760 770 780 RPWEKSNTLP HKLSGGAGSG SAGSGHEGAN GNSGGAGSNT TNSGGESPRP MRKRFGSASE 790 800 810 820 830 ETILKQVNGD GLSLALSNGD LDTLKAEIVR EMRLEIQKVK NEIIDAIKSE FNRR
	Isoform 2 (A) (C) (E) [UniParc]. Checksum: E1FFB5A8091FA77E	FASTA	684	71,985
	10 20 30 40 50 60 MTEQSIIGAR ASVMVYDDNQ KKWVPSGSSS GLSKVQIYHH QQNNTFRVVG RKLQDHEVVI 70 80 90 100 110 120 NCSILKGLKY NQATATFHQW RDSKFVYGLN FSSQNDAENF ARAMMHALEV LSGRVANNPG 130 140 150 160 170 180 GPPTNGNGYE EDMGYRTMTS EDAAILRQNN SIGGHVTPSA QTPTSQTNQN NIPQSPPTPQ 190 200 210 220 230 240 GHHRTSSAPP APQPQQQQQQ QQAQQMGQPG SHYGPTGNGP TSNGLPQQVN SQIPPAPQQQ 250 260 270 280 290 300 PQQQQFQQQQ QQQQYQQMVQ AGYAPSQQYQ QPHYVLSNSN PNLTVHQYPT QQAQQQPPQA 310 320 330 340 350 360 PQPPLQNGGM YMVGHGHLPS SASANSVVYA SQQQMLPQAH PQAPQAPTMP GPGYGGPPVP 370 380 390 400 410 420 PPQQQAENPY GQVPMPPPMN PSQQQQPGQV PLNRMSSQGG PGGPPAPAPP PPPPSFGGAA 430 440 450 460 470 480 GGGPPPPAPP QMFNGAPPPP AMGGGPPPAP PAPPAMGGGP PPAPGGPGAP PPPPPPPGLG 490 500 510 520 530 540 GAPKKEDPQA DLMGSLASQL QQIKLKKNKV TTSAPENSGS STSSGGSGNY GTIGRSSNGM 550 560 570 580 590 600 ASMMDEMAKT LARRRAQAEK KDPDPEAEVK KRPWEKSNTL PHKLSGGAGS GSAGSGHEGA 610 620 630 640 650 660 NGNSGGAGSN TTNSGGESPR PMRKRFGSAS EETILKVNGD GLSLALSNGD LDTLKAEIVR 670 680 EMRLEIQKVK NEIIDAIKSE FNRR
	Isoform 3 (D) [UniParc]. Checksum: F480275EB4CC79A8	FASTA	687	72,327
	10 20 30 40 50 60 MTEQSIIGAR ASVMVYDDNQ KKWVPSGSSS GLSKVQIYHH QQNNTFRVVG RKLQDHEVVI 70 80 90 100 110 120 NCSILKGLKY NQATATFHQW RDSKFVYGLN FSSQNDAENF ARAMMHALEV LSGRVANNPG 130 140 150 160 170 180 GPPTNGNGYE EDMGYRTMTS EDAAILRQNN SIGGHVTPSA QTPTSQTNQN NIPQSPPTPQ 190 200 210 220 230 240 GHHRTSRNSL SAPPAPQPQQ QQQQQQAQQM GQPGSHYGPT GNGPTSNGLP QQVNSQIPPA 250 260 270 280 290 300 PQQQPQQQQF QQQQQQQQYQ QMVQAGYAPS QYQQPHYVLS NSNPNLTVHQ YPTQQAQQQP 310 320 330 340 350 360 PQAPQPPLQN GGMYMVGHGH LPSSASANSV VYASQQQMLP QAHPQAPQAP TMPGPGYGGP 370 380 390 400 410 420 PVPPPQQQAE NPYGQVPMPP PMNPSQQQQP GQVPLNRMSS QGGPGGPPAP APPPPPPSFG 430 440 450 460 470 480 GAAGGGPPPP APPQMFNGAP PPPAMGGGPP PAPPAPPAMG GGPPPAPGGP GAPPPPPPPP 490 500 510 520 530 540 GLGGAPKKED PQADLMGSLA SQLQQIKLKK NKVTTSAPEN SGSSTSSGGS GNYGTIGRSS 550 560 570 580 590 600 NGMASMMDEM AKTLARRRAQ AEKKDPDPEA EVKKRPWEKS NTLPHKLSGG AGSGSAGSGH 610 620 630 640 650 660 EGANGNSGGA GSNTTNSGGE SPRPMRKRFG SASEETILKV NGDGLSLALS NGDLDTLKAE 670 680 IVREMRLEIQ KVKNEIIDAI KSEFNRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: Berkeley. Tissue: Embryo.
[5]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases 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, 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, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	A56154.
RefSeq	NP_001014536.1. NM_001014536.1. NP_001014537.1. NM_001014537.2. NP_001137709.1. NM_001144237.1. NP_725857.1. NM_166329.1. NP_725858.1. NM_166330.1. NP_725859.2. NM_166331.2.
UniGene	Dm.14700.
3D structure databases
ProteinModelPortal	Q8T4F7.
SMR	Q8T4F7. Positions 298-408.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8T4F7. 32 interactions.
MINT	MINT-817415.
Proteomic databases
PaxDb	Q8T4F7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0114623; FBpp0113115; FBgn0000578.
GeneID	37201.
KEGG	dme:Dmel_CG15112.
UCSC	CG15112-RA. d. melanogaster.
Organism-specific databases
CTD	37201.
FlyBase	FBgn0000578. ena.
Phylogenomic databases
eggNOG	NOG289321.
GeneTree	ENSGT00440000039080.
InParanoid	Q8T4F7.
OMA	INCSILK.
OrthoDB	EOG47SQX6.
PhylomeDB	Q8T4F7.
Enzyme and pathway databases
Reactome	REACT_113552. Developmental Biology.
Gene expression databases
Bgee	Q8T4F7.
GermOnline	CG15112. Drosophila melanogaster.
Family and domain databases
Gene3D	2.30.29.30. 1 hit.
InterPro	IPR000697. EVH1. IPR011993. PH_like_dom. IPR000156. Ran_bind_dom. IPR014885. VASP_tetra. [Graphical view]
Pfam	PF08776. VASP_tetra. 1 hit. PF00568. WH1. 1 hit. [Graphical view]
SMART	SM00160. RanBD. 1 hit. SM00461. WH1. 1 hit. [Graphical view]
PROSITE	PS50229. WH1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ena. drosophila.
GenomeRNAi	37201.
NextBio	802467.

Entry information

Entry name

ENA_DROME

Accession

Primary (citable) accession number: Q8T4F7
Secondary accession number(s): A4UZP3 , B7YZL0, Q24035, Q86NN6, Q8MMB3, Q9V8R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	July 7, 2009
Last modified:	May 1, 2013
This is version 95 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project