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Q8T4F7 (ENA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein enabled
Gene names
Name:ena
Synonyms:enb
ORF Names:CG15112
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length980 AA.
Sequence statusComplete.
Protein existenceEvidence 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 projectionlamellipodium. Cytoplasmcytoskeleton. Note: Expressed at the leading edge of lamellipodia. Colocalizes 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 componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainSH3-binding
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype PubMed 19675132. Source: FlyBase

actin filament organization

Inferred from mutant phenotype PubMed 14527345PubMed 19000833PubMed 19576200. Source: FlyBase

axon guidance

Inferred from mutant phenotype PubMed 10069336. Source: FlyBase

axonogenesis

Inferred from mutant phenotype Ref.9. 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

cytoskeleton organization

Traceable author statement PubMed 12147138. Source: FlyBase

dendrite morphogenesis

Inferred from mutant phenotype PubMed 10521399PubMed 18817767. Source: FlyBase

dorsal closure

Inferred from genetic interaction PubMed 11756472. 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 cell migration

Inferred from mutant phenotype PubMed 21045209. Source: FlyBase

positive regulation of cell projection organization

Inferred from direct assay PubMed 21045209. 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 filopodium assembly

Inferred from mutant phenotype PubMed 19846663. 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_componentadherens junction

Inferred from direct assay PubMed 11756472PubMed 17507404. Source: FlyBase

axon

Inferred from direct assay PubMed 11756472. Source: FlyBase

cell leading edge

Inferred from direct assay PubMed 17507404. 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 17507404PubMed 21045209. Source: FlyBase

lamellipodium

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionSH3 domain binding

Inferred from direct assay Ref.8. Source: UniProtKB

actin binding

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

protein binding

Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 980980Protein enabled
PRO_0000227757

Regions

Domain146 – 407262WH1
Region791 – 980190EVH2
Region791 – 81020EVH2 block A
Region837 – 85418EVH2 block B
Region947 – 98034EVH2 block C
Motif800 – 8034KLKR
Compositional bias157 – 22064Ser-rich
Compositional bias244 – 27936Gln-rich
Compositional bias457 – 685229Gln-rich
Compositional bias633 – 784152Pro-rich

Amino acid modifications

Modified residue4251Phosphotyrosine Ref.7
Modified residue6071Phosphotyrosine Ref.7
Modified residue6251Phosphotyrosine Ref.7
Modified residue6501Phosphotyrosine Ref.7
Modified residue6661Phosphotyrosine Ref.7
Modified residue8261Phosphotyrosine Ref.7
Modified residue9051Phosphoserine Ref.13
Modified residue9141Phosphoserine Ref.13
Modified residue9241Phosphoserine Ref.12 Ref.13

Natural variations

Alternative sequence2 – 297296Missing in isoform 2 and isoform 3.
VSP_017574
Alternative sequence1471L → F in isoform 1.
VSP_037651
Alternative sequence148 – 298151Missing in isoform 1.
VSP_037652
Alternative sequence2981A → T in isoform 2 and isoform 3.
VSP_017575
Alternative sequence4821S → SRNSL in isoform 1 and isoform 3.
VSP_019865
Alternative sequence5631Missing in isoform 3.
VSP_019866
Alternative sequence9321K → KQ in isoform 1.
VSP_037653

Experimental info

Sequence conflict1201Q → H in AAL89948. Ref.4
Sequence conflict491 – 4933Missing in AAL89948. Ref.4
Sequence conflict6121G → S in AAA85120. Ref.1
Sequence conflict7991I → F in AAA85120. Ref.1
Sequence conflict7991I → F in AAL89948. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 (F) [UniParc].

Last modified July 7, 2009. Version 4.
Checksum: 7B084A0AEC098297

FASTA980104,824
        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 

« Hide

Isoform 1 (B) [UniParc].

Checksum: 7E0CD375D351C674
Show »

FASTA83489,280
Isoform 2 (A) (C) (E) [UniParc].

Checksum: E1FFB5A8091FA77E
Show »

FASTA68471,985
Isoform 3 (D) [UniParc].

Checksum: F480275EB4CC79A8
Show »

FASTA68772,327

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, 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.
+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.
PIRA56154.
RefSeqNP_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]
UniGeneDm.14700.

3D structure databases

ProteinModelPortalQ8T4F7.
SMRQ8T4F7. Positions 298-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62866. 44 interactions.
IntActQ8T4F7. 32 interactions.
MINTMINT-817415.

Proteomic databases

PaxDbQ8T4F7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0114623; FBpp0113115; FBgn0000578. [Q8T4F7-4]
GeneID37201.
KEGGdme:Dmel_CG15112.
UCSCCG15112-RA. d. melanogaster.

Organism-specific databases

CTD37201.
FlyBaseFBgn0000578. ena.

Phylogenomic databases

eggNOGNOG289321.
GeneTreeENSGT00730000110272.
InParanoidQ8T4F7.
OMAINCSILK.
OrthoDBEOG72JWGQ.
PhylomeDBQ8T4F7.

Enzyme and pathway databases

ReactomeREACT_227403. Developmental Biology.

Gene expression databases

BgeeQ8T4F7.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view]
PfamPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
SMARTSM00160. RanBD. 1 hit.
SM00461. WH1. 1 hit.
[Graphical view]
PROSITEPS50229. WH1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSena. drosophila.
GenomeRNAi37201.
NextBio802467.
PROQ8T4F7.

Entry information

Entry nameENA_DROME
AccessionPrimary (citable) accession number: Q8T4F7
Secondary accession number(s): A4UZP3 expand/collapse secondary AC list , B7YZL0, Q24035, Q86NN6, Q8MMB3, Q9V8R3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 105 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase