Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein enabled

 ENA_DROME               Reviewed;         980 AA.
Q8T4F7; A4UZP3; B7YZL0; Q24035; Q86NN6; Q8MMB3; Q9V8R3;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 4.
18-JUL-2018, entry version 142.
RecName: Full=Protein enabled;
Name=ena; Synonyms=enb; ORFNames=CG15112;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2),
INTERACTION WITH ABL AND SRC, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
TISSUE=Embryo;
PubMed=7535279; DOI=10.1101/gad.9.5.521;
Gertler F.B., Comer A.R., Juang J.-L., Ahern S.M., Clark M.J.,
Liebl E.C., Hoffmann F.M.;
"Enabled, a dosage-sensitive suppressor of mutations in the Drosophila
Abl tyrosine kinase, encodes an Abl substrate with SH3 domain-binding
properties.";
Genes Dev. 9:521-533(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=Berkeley; TISSUE=Embryo;
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.
[6]
FUNCTION.
PubMed=15790972; DOI=10.1242/dev.01736;
Forsthoefel D.J., Liebl E.C., Kolodziej P.A., Seeger M.A.;
"The Abelson tyrosine kinase, the Trio GEF and Enabled interact with
the Netrin receptor Frazzled in Drosophila.";
Development 132:1983-1994(2005).
[7]
PHOSPHORYLATION AT TYR-425; TYR-607; TYR-625; TYR-650; TYR-666 AND
TYR-826.
PubMed=9418863; DOI=10.1128/MCB.18.1.152;
Comer A.R., Ahern-Djamali S.M., Juang J.-L., Jackson P.D.,
Hoffmann F.M.;
"Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase
regulates the in vivo function and protein-protein interactions of
Enabled.";
Mol. Cell. Biol. 18:152-160(1998).
[8]
INTERACTION WITH CHIC.
PubMed=10220404; DOI=10.1073/pnas.96.9.4977;
Ahern-Djamali S.M., Bachmann C., Hua P., Reddy S.K., Kastenmeier A.S.,
Walter U., Hoffmann F.M.;
"Identification of profilin and src homology 3 domains as binding
partners for Drosophila enabled.";
Proc. Natl. Acad. Sci. U.S.A. 96:4977-4982(1999).
[9]
INTERACTION WITH ROBO.
PubMed=10892742; DOI=10.1016/S0092-8674(00)80883-1;
Bashaw G.J., Kidd T., Murray D., Pawson T., Goodman C.S.;
"Repulsive axon guidance: Abelson and Enabled play opposing roles
downstream of the roundabout receptor.";
Cell 101:703-715(2000).
[10]
INTERACTION WITH ZYX102EF.
PubMed=12594038; DOI=10.1016/S0378-1119(02)01173-3;
Renfranz P.J., Siegrist S.E., Stronach B.E., Macalma T.,
Beckerle M.C.;
"Molecular and phylogenetic characterization of Zyx102, a Drosophila
orthologue of the zyxin family that interacts with Drosophila
Enabled.";
Gene 305:13-26(2003).
[11]
SUBCELLULAR LOCATION.
PubMed=14762109; DOI=10.1242/jcs.00921;
Biyasheva A., Svitkina T., Kunda P., Baum B., Borisy G.;
"Cascade pathway of filopodia formation downstream of SCAR.";
J. Cell Sci. 117:837-848(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905; SER-914 AND
SER-924, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- 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. {ECO:0000269|PubMed:15790972}.
-!- SUBUNIT: Interacts with Abl and Src SH3 domains. Binds, in vitro
and in vivo, the cytoplasmic domain of robo. Interacts with
Zyx102EF and chic. {ECO:0000269|PubMed:10220404,
ECO:0000269|PubMed:10892742, ECO:0000269|PubMed:12594038,
ECO:0000269|PubMed:7535279}.
-!- INTERACTION:
P00522:Abl; NbExp=3; IntAct=EBI-466810, EBI-534090;
P25843:chic; NbExp=3; IntAct=EBI-466810, EBI-156199;
P16621:Lar; NbExp=2; IntAct=EBI-466810, EBI-668630;
P05480:Src (xeno); NbExp=2; IntAct=EBI-466810, EBI-298680;
-!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
{ECO:0000269|PubMed:14762109}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:14762109}. Note=Expressed at the leading edge
of lamellipodia. Colocalizes with chic at the periphery of cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=4; Synonyms=F;
IsoId=Q8T4F7-4; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=1; Synonyms=B;
IsoId=Q8T4F7-1; Sequence=VSP_037651, VSP_037652, VSP_019865,
VSP_037653;
Note=No experimental confirmation available.;
Name=2; Synonyms=A, C, E;
IsoId=Q8T4F7-2; Sequence=VSP_017574, VSP_017575;
Name=3; Synonyms=D;
IsoId=Q8T4F7-3; Sequence=VSP_017574, VSP_017575, VSP_019865,
VSP_019866;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in axons of the embryonic nervous
system. {ECO:0000269|PubMed:7535279}.
-!- 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.
-!- PTM: Tyrosine phosphorylated on multiple sites by Abl kinase. In
vitro, phosphorylation on specific tyrosine residues inhibits
interaction with Abl and Src SH3 domains.
{ECO:0000269|PubMed:17372656, ECO:0000269|PubMed:18327897,
ECO:0000269|PubMed:7535279, ECO:0000269|PubMed:9418863}.
-!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U21123; AAA85120.1; -; Genomic_DNA.
EMBL; AE013599; AAF57598.2; -; Genomic_DNA.
EMBL; AE013599; AAM68438.2; -; Genomic_DNA.
EMBL; AE013599; AAM68439.2; -; Genomic_DNA.
EMBL; AE013599; AAX52696.1; -; Genomic_DNA.
EMBL; AE013599; AAX52697.1; -; Genomic_DNA.
EMBL; AE013599; ACL83163.1; -; Genomic_DNA.
EMBL; AY084210; AAL89948.1; -; mRNA.
EMBL; BT004488; AAO42652.1; -; mRNA.
PIR; A56154; A56154.
RefSeq; NP_001014536.1; NM_001014536.2. [Q8T4F7-2]
RefSeq; NP_001014537.1; NM_001014537.3. [Q8T4F7-3]
RefSeq; NP_001137709.1; NM_001144237.2. [Q8T4F7-4]
RefSeq; NP_725857.1; NM_166329.2. [Q8T4F7-2]
RefSeq; NP_725858.1; NM_166330.2. [Q8T4F7-2]
RefSeq; NP_725859.2; NM_166331.3. [Q8T4F7-1]
UniGene; Dm.14700; -.
ProteinModelPortal; Q8T4F7; -.
SMR; Q8T4F7; -.
BioGrid; 62866; 64.
IntAct; Q8T4F7; 41.
STRING; 7227.FBpp0113115; -.
iPTMnet; Q8T4F7; -.
PaxDb; Q8T4F7; -.
PRIDE; Q8T4F7; -.
EnsemblMetazoa; FBtr0086582; FBpp0085766; FBgn0000578. [Q8T4F7-2]
EnsemblMetazoa; FBtr0086583; FBpp0085767; FBgn0000578. [Q8T4F7-2]
EnsemblMetazoa; FBtr0086584; FBpp0085768; FBgn0000578. [Q8T4F7-1]
EnsemblMetazoa; FBtr0100174; FBpp0099530; FBgn0000578. [Q8T4F7-3]
EnsemblMetazoa; FBtr0100176; FBpp0099532; FBgn0000578. [Q8T4F7-2]
EnsemblMetazoa; FBtr0114623; FBpp0113115; FBgn0000578. [Q8T4F7-4]
EnsemblMetazoa; FBtr0340450; FBpp0309392; FBgn0000578.
GeneID; 37201; -.
KEGG; dme:Dmel_CG15112; -.
UCSC; CG15112-RA; d. melanogaster.
CTD; 37201; -.
FlyBase; FBgn0000578; ena.
eggNOG; KOG4590; Eukaryota.
eggNOG; ENOG41101TS; LUCA.
GeneTree; ENSGT00730000110272; -.
InParanoid; Q8T4F7; -.
OrthoDB; EOG091G0QTE; -.
PhylomeDB; Q8T4F7; -.
ChiTaRS; ena; fly.
GenomeRNAi; 37201; -.
PRO; PR:Q8T4F7; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0000578; -.
ExpressionAtlas; Q8T4F7; baseline and differential.
Genevisible; Q8T4F7; DM.
GO; GO:0005912; C:adherens junction; IDA:FlyBase.
GO; GO:0030424; C:axon; IDA:FlyBase.
GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
GO; GO:0005911; C:cell-cell junction; IDA:FlyBase.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IDA:FlyBase.
GO; GO:0032433; C:filopodium tip; IDA:FlyBase.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0071212; C:subsynaptic reticulum; IDA:FlyBase.
GO; GO:0003779; F:actin binding; ISS:FlyBase.
GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0048749; P:compound eye development; IGI:FlyBase.
GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:FlyBase.
GO; GO:0007010; P:cytoskeleton organization; TAS:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0007391; P:dorsal closure; IGI:FlyBase.
GO; GO:0003382; P:epithelial cell morphogenesis; IGI:FlyBase.
GO; GO:0046847; P:filopodium assembly; IMP:FlyBase.
GO; GO:0060288; P:formation of a compartment boundary; IMP:FlyBase.
GO; GO:0007390; P:germ-band shortening; IMP:FlyBase.
GO; GO:0035262; P:gonad morphogenesis; IMP:FlyBase.
GO; GO:0008258; P:head involution; IMP:FlyBase.
GO; GO:0045886; P:negative regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0030335; P:positive regulation of cell migration; IMP:FlyBase.
GO; GO:0031346; P:positive regulation of cell projection organization; IDA:FlyBase.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IPI:FlyBase.
GO; GO:0008064; P:regulation of actin polymerization or depolymerization; TAS:FlyBase.
GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:FlyBase.
GO; GO:1990255; P:subsynaptic reticulum organization; IMP:FlyBase.
GO; GO:0007396; P:suture of dorsal opening; IMP:FlyBase.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR038023; VASP_sf.
InterPro; IPR014885; VASP_tetra.
InterPro; IPR000697; WH1/EVH1_dom.
Pfam; PF08776; VASP_tetra; 1.
Pfam; PF00568; WH1; 1.
SMART; SM00461; WH1; 1.
SUPFAM; SSF118370; SSF118370; 1.
PROSITE; PS50229; WH1; 1.
1: Evidence at protein level;
Actin-binding; Alternative splicing; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein;
Reference proteome; SH3-binding.
CHAIN 1 980 Protein enabled.
/FTId=PRO_0000227757.
DOMAIN 146 407 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REGION 791 980 EVH2.
REGION 791 810 EVH2 block A.
REGION 837 854 EVH2 block B.
REGION 947 980 EVH2 block C.
MOTIF 800 803 KLKR.
COMPBIAS 157 220 Ser-rich.
COMPBIAS 244 279 Gln-rich.
COMPBIAS 457 685 Gln-rich.
COMPBIAS 633 784 Pro-rich.
MOD_RES 425 425 Phosphotyrosine.
{ECO:0000269|PubMed:9418863}.
MOD_RES 607 607 Phosphotyrosine.
{ECO:0000269|PubMed:9418863}.
MOD_RES 625 625 Phosphotyrosine.
{ECO:0000269|PubMed:9418863}.
MOD_RES 650 650 Phosphotyrosine.
{ECO:0000269|PubMed:9418863}.
MOD_RES 666 666 Phosphotyrosine.
{ECO:0000269|PubMed:9418863}.
MOD_RES 826 826 Phosphotyrosine.
{ECO:0000269|PubMed:9418863}.
MOD_RES 905 905 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 914 914 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 924 924 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
VAR_SEQ 2 297 Missing (in isoform 2 and isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_017574.
VAR_SEQ 147 147 L -> F (in isoform 1).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_037651.
VAR_SEQ 148 298 Missing (in isoform 1).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_037652.
VAR_SEQ 298 298 A -> T (in isoform 2 and isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_017575.
VAR_SEQ 482 482 S -> SRNSL (in isoform 1 and isoform 3).
{ECO:0000303|PubMed:12537569,
ECO:0000303|Ref.5}.
/FTId=VSP_019865.
VAR_SEQ 563 563 Missing (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_019866.
VAR_SEQ 932 932 K -> KQ (in isoform 1).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_037653.
CONFLICT 120 120 Q -> H (in Ref. 4; AAL89948).
{ECO:0000305}.
CONFLICT 491 493 Missing (in Ref. 4; AAL89948).
{ECO:0000305}.
CONFLICT 612 612 G -> S (in Ref. 1; AAA85120).
{ECO:0000305}.
CONFLICT 799 799 I -> F (in Ref. 1; AAA85120 and 4;
AAL89948). {ECO:0000305}.
SEQUENCE 980 AA; 104824 MW; 7B084A0AEC098297 CRC64;
MAMKKLYAKT SFTSKKPSSA ANSTPILAYH QQQHQQPGNG ICEFQVVAPG HSGELMIRRS
QSMHHKMSPP VGGLGSKSEY YSIEELQELD LLDYRHPMYH HYQQQELRQR YHEHEQLVLQ
LPKATSPKAG PIYEAPQRSQ QQQDQMLYVP TAAQRDSSSS AAATSIASSS TLTSSPSPSS
SSSLIFSTLR KCVSPSNPSV NPNQPSKTQP SKLGCSMSFS IRTTTATAAT AAAANAATAT
LSTQQQQQQA QQQHKQHLYS NIHHYLIRQQ QQKQHYTLQR RHNSVKDKFI GGITTIFAEQ
SIIGARASVM VYDDNQKKWV PSGSSSGLSK VQIYHHQQNN TFRVVGRKLQ DHEVVINCSI
LKGLKYNQAT ATFHQWRDSK FVYGLNFSSQ NDAENFARAM MHALEVLSGR VANNPGGPPT
NGNGYEEDMG YRTMTSEDAA ILRQNNSIGG HVTPSAQTPT SQTNQNNIPQ SPPTPQGHHR
TSSAPPAPQP QQQQQQQQAQ QMGQPGSHYG PTGNGPTSNG LPQQVNSQIP PAPQQQPQQQ
QFQQQQQQQQ YQQMVQAGYA PSQQYQQPHY VLSNSNPNLT VHQYPTQQAQ QQPPQAPQPP
LQNGGMYMVG HGHLPSSASA NSVVYASQQQ MLPQAHPQAP QAPTMPGPGY GGPPVPPPQQ
QAENPYGQVP MPPPMNPSQQ QQPGQVPLNR MSSQGGPGGP PAPAPPPPPP SFGGAAGGGP
PPPAPPQMFN GAPPPPAMGG GPPPAPPAPP AMGGGPPPAP GGPGAPPPPP PPPGLGGAPK
KEDPQADLMG SLASQLQQIK LKKNKVTTSA PENSGSSTSS GGSGNYGTIG RSSNGMASMM
DEMAKTLARR RAQAEKKDPD PEAEVKKRPW EKSNTLPHKL SGGAGSGSAG SGHEGANGNS
GGAGSNTTNS GGESPRPMRK RFGSASEETI LKVNGDGLSL ALSNGDLDTL KAEIVREMRL
EIQKVKNEII DAIKSEFNRR


Related products :

Catalog number Product name Quantity
CSB-EL007661MO Mouse Protein enabled homolog(ENAH) ELISA kit 96T
G2750 Protein enabled homolog (ENAH), Mouse, ELISA Kit 96T
G2749 Protein enabled homolog (ENAH), Human, ELISA Kit 96T
CSB-EL007661HU Human Protein enabled homolog(ENAH) ELISA kit 96T
EIAAB12935 Enah,Mena,Mouse,Mus musculus,Ndpp1,NDPP-1,NPC-derived proline-rich protein 1,Protein enabled homolog
CSB-EL007661HU Human Protein enabled homolog(ENAH) ELISA kit SpeciesHuman 96T
CSB-EL007661MO Mouse Protein enabled homolog(ENAH) ELISA kit SpeciesMouse 96T
ENAH_HUMAN ELISA Kit FOR Protein enabled homolog; organism: Human; gene name: ENAH 96T
EIAAB12936 ENAH,Homo sapiens,Human,MENA,Protein enabled homolog
ENAH_MOUSE ELISA Kit FOR Protein enabled homolog; organism: Mouse; gene name: Enah 96T
Y090238 Anti-enabled Monoclonal Antibody 100ul
ENC1 ENAH Gene enabled homolog (Drosophila)
CSB-EL007661MO Mouse enabled homolog (Drosophila) (ENAH) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL007661HU Human enabled homolog (Drosophila) (ENAH) ELISA kit, Species Human, Sample Type serum, plasma 96T
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
29-850 The protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions.The protein encoded by this 0.1 mg
EIAAB44668 Dap12,DNAX-activation protein 12,Karap,KAR-associated protein,Killer-activating receptor-associated protein,Mouse,Mus musculus,TYRO protein tyrosine kinase-binding protein,Tyrobp
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB44667 DAP12,DNAX-activation protein 12,Homo sapiens,Human,KARAP,KAR-associated protein,Killer-activating receptor-associated protein,TYRO protein tyrosine kinase-binding protein,TYROBP
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
EIAAB32247 ADP-ribosylation factor-like protein 6-interacting protein 5,Aip-5,ARL-6-interacting protein 5,ARL6IP5,Cytoskeleton-related vitamin A-responsive protein,Dermal papilla-derived protein 11,DERP11,Glutam


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur