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Protein enabled homolog

 ENAH_HUMAN              Reviewed;         591 AA.
Q8N8S7; D0PQI2; Q502W5; Q5T5M7; Q5VTQ9; Q5VTR0; Q9NVF3; Q9UFB8;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
12-SEP-2018, entry version 160.
RecName: Full=Protein enabled homolog;
Name=ENAH; Synonyms=MENA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Urbanelli L.;
"Human Mena: cDNA cloning, expression and promoter characterization.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Mammary tumor;
PubMed=15027125; DOI=10.1002/ijc.20094;
Di Modugno F., Bronzi G., Scanlan M.J., Del Bello D., Cascioli S.,
Venturo I., Botti C., Nicotra M.R., Mottolese M., Natali P.G.,
Santoni A., Jager E., Nistico P.;
"Human Mena protein, a serex-defined antigen overexpressed in breast
cancer eliciting both humoral and CD8+ T-cell immune response.";
Int. J. Cancer 109:909-918(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=23129656; DOI=10.1073/pnas.1214394109;
Di Modugno F., Iapicca P., Boudreau A., Mottolese M., Terrenato I.,
Perracchio L., Carstens R.P., Santoni A., Bissell M.J., Nistico P.;
"Splicing program of human MENA produces a previously undescribed
isoform associated with invasive, mesenchymal-like breast tumors.";
Proc. Natl. Acad. Sci. U.S.A. 109:19280-19285(2012).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 44-591 (ISOFORM 2).
TISSUE=Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-591 (ISOFORM 2).
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-591 (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
PROTEIN SEQUENCE OF 23-47; 70-81; 123-145; 403-427; 484-499 AND
573-587, FUNCTION, AND INTERACTION WITH BAIAP2.
PubMed=11696321; DOI=10.1016/S0960-9822(01)00506-1;
Krugmann S., Jordens I., Gevaert K., Driessens M., Vandekerckhove J.,
Hall A.;
"Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena
complex.";
Curr. Biol. 11:1645-1655(2001).
[9]
INTERACTION WITH VCL; ZYX AND L.MONOCYTOGENES ACTA.
PubMed=9312002; DOI=10.1093/emboj/16.17.5433;
Niebuhr K., Ebel F., Frank R., Reinhard M., Domann E., Carl U.D.,
Walter U., Gertler F.B., Wehland J., Chakraborty T.;
"A novel proline-rich motif present in ActA of Listeria monocytogenes
and cytoskeletal proteins is the ligand for the EVH1 domain, a protein
module present in the Ena/VASP family.";
EMBO J. 16:5433-5444(1997).
[10]
INTERACTION WITH ZYX.
PubMed=10801818; DOI=10.1074/jbc.M001698200;
Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C.,
Golsteyn R.M.;
"Characterization of the interaction between zyxin and members of the
Ena/vasodilator-stimulated phosphoprotein family of proteins.";
J. Biol. Chem. 275:22503-22511(2000).
[11]
INTERACTION WITH ROBO4.
PubMed=12941633; DOI=10.1016/S0012-1606(03)00258-6;
Park K.W., Morrison C.M., Sorensen L.K., Jones C.A., Rao Y.,
Chien C.-B., Wu J.Y., Urness L.D., Li D.Y.;
"Robo4 is a vascular-specific receptor that inhibits endothelial
migration.";
Dev. Biol. 261:251-267(2003).
[12]
INTERACTION WITH APBB1IP.
TISSUE=T-cell;
PubMed=15469846; DOI=10.1016/j.devcel.2004.07.021;
Lafuente E.M., van Puijenbroek A.A., Krause M., Carman C.V.,
Freeman G.J., Berezovskaya A., Constantine E., Springer T.A.,
Gertler F.B., Boussiotis V.A.;
"RIAM, an Ena/VASP and profilin ligand, interacts with Rap1-GTP and
mediates Rap1-induced adhesion.";
Dev. Cell 7:585-595(2004).
[13]
SUBCELLULAR LOCATION.
PubMed=15469845; DOI=10.1016/j.devcel.2004.07.024;
Krause M., Leslie J.D., Stewart M., Lafuente E.M., Valderrama F.,
Jagannathan R., Strasser G.A., Rubinson D.A., Liu H., Way M.,
Yaffe M.B., Boussiotis V.A., Gertler F.B.;
"Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of
lamellipodial dynamics.";
Dev. Cell 7:571-583(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-506 AND
SER-508, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-502 (ISOFORM
2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-465 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-506 AND
SER-508, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 347-356 IN COMPLEX WITH
APBB1.
PubMed=17686488; DOI=10.1016/j.jmb.2007.06.064;
Meiyappan M., Birrane G., Ladias J.A.A.;
"Structural basis for polyproline recognition by the FE65 WW domain.";
J. Mol. Biol. 372:970-980(2007).
[22]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-113 IN COMPLEX WITH TES,
INTERACTION WITH ZYX, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033;
Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J.,
McDonald N.Q., Way M.;
"Tes, a specific Mena interacting partner, breaks the rules for EVH1
binding.";
Mol. Cell 28:1071-1082(2007).
[23]
X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 1-116 IN COMPLEX WITH TES
AND ACTL7A.
PubMed=21278383; DOI=10.1074/jbc.M110.171264;
Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E.,
Garvalov B.K., McDonald N.Q., Way M.;
"Molecular recognition of the Tes LIM2-3 domains by the actin-related
protein Arp7A.";
J. Biol. Chem. 286:11543-11554(2011).
-!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved
in a range of processes dependent on cytoskeleton remodeling and
cell polarity such as axon guidance and lamellipodial and
filopodial dynamics in migrating cells. ENAH induces the formation
of F-actin rich outgrowths in fibroblasts. Acts synergistically
with BAIAP2-alpha and downstream of NTN1 to promote filipodia
formation (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11696321, ECO:0000269|PubMed:18158903}.
-!- SUBUNIT: Homotetramer (By similarity). Interacts with APBB1IP,
APBB1, PFN1 and ROBO4. Isoforms, containing the polyproline-rich
regions with PPLP motifs, bind the WW domain of APBB1IP. Isoforms,
containing the PPSY motif, bind, in vitro, to the WW2 and WW3
domains of NEDD4 and to the WW1 domain of YAP1. Binds the SH3
domain of BAIAP2-alpha but only after the autoinhibitory region of
BAIAP2-alpha has been blocked by interaction with CDC42.
Interacts, via the EVH1/WH1 domain, with the Pro-rich domains from
VCL, ZYX and Listeria monocytogenes actA and with TES (via LIM
domains). The TES LIM domain and the Pro-rich domains from VCL or
ZYX compete for the same binding site. Interaction with ZYX is
important for targeting ENAH to focal adhesions and enhances
production of actin-rich structures at the apical surface of
cells. Interacts, through the Pro-rich region, with the C-terminal
SH3 domain of DNMPB. Binds GPHN (By similarity). Interacts with
FAT1 (via EVH1 domains) (By similarity). Heterotrimer with TES and
ACTL7A. {ECO:0000250, ECO:0000269|PubMed:10801818,
ECO:0000269|PubMed:11696321, ECO:0000269|PubMed:12941633,
ECO:0000269|PubMed:15469846, ECO:0000269|PubMed:17686488,
ECO:0000269|PubMed:18158903, ECO:0000269|PubMed:21278383,
ECO:0000269|PubMed:9312002}.
-!- INTERACTION:
Q14517:FAT1; NbExp=2; IntAct=EBI-2834410, EBI-1171918;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-2834410, EBI-750109;
Q9UGI8:TES; NbExp=2; IntAct=EBI-2834410, EBI-2561654;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton
{ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell
projection, filopodium {ECO:0000250}. Cell junction, synapse
{ECO:0000250}. Cell junction, focal adhesion. Note=Targeted to the
leading edge of lamellipodia and filopodia by MRL family members.
Colocalizes at filopodial tips with a number of other proteins
including vinculin and zyxlin. Colocalizes with N-WASP at the
leading edge. Colocalizes with GPHN and PFN at synapses (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N8S7-1; Sequence=Displayed;
Name=2;
IsoId=Q8N8S7-2; Sequence=VSP_010564;
Note=Contains a phosphothreonine at position 502. Contains a
phosphoserine at position 512. Contains a phosphoserine at
position 508. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569};
Name=3; Synonyms=Deltav6;
IsoId=Q8N8S7-3; Sequence=VSP_053772, VSP_053773;
Note=Expression restricted to invasive cancer cells. Contains a
phosphothreonine at position 465. Contains a phosphoserine at
position 475. Contains a phosphoserine at position 471.
{ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569};
-!- TISSUE SPECIFICITY: Expressed in myoepithelia of parotid, breast,
bronchial glands and sweat glands. Expressed in colon-rectum
muscolaris mucosae epithelium, pancreas acinar ductal epithelium,
endometrium epithelium, prostate fibromuscolar stroma and placenta
vascular media. Overexpressed in a majority of breast cancer cell
lines and primary breast tumor lesions.
{ECO:0000269|PubMed:15027125}.
-!- 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: NTN1-induced PKA phosphorylation on Ser-265 directly
parallels the formation of filopodial protrusions. {ECO:0000250}.
-!- MISCELLANEOUS: Required to transform actin polymerization into
active movement for the propulsive force of Listeria
monocytogenes. {ECO:0000250}.
-!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91799.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC04736.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ENAHID44148ch1q42.html";
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EMBL; AY345143; AAR04685.1; -; mRNA.
EMBL; AF519769; AAQ08487.1; -; mRNA.
EMBL; EU255274; ABY78022.1; -; mRNA.
EMBL; AC092811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL591380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC065238; AAH65238.1; -; mRNA.
EMBL; BC095481; AAH95481.1; -; mRNA.
EMBL; AK001635; BAA91799.1; ALT_INIT; mRNA.
EMBL; AK096246; BAC04736.1; ALT_INIT; mRNA.
EMBL; AL133059; CAB61384.1; -; mRNA.
CCDS; CCDS31040.1; -. [Q8N8S7-2]
CCDS; CCDS31041.1; -. [Q8N8S7-1]
PIR; T42661; T42661.
RefSeq; NP_001008493.1; NM_001008493.2. [Q8N8S7-1]
RefSeq; NP_060682.2; NM_018212.5. [Q8N8S7-2]
UniGene; Hs.497893; -.
PDB; 2HO2; X-ray; 1.33 A; B=347-356.
PDB; 2IYB; X-ray; 2.35 A; A/B/C/D=1-113.
PDB; 2XQN; X-ray; 2.62 A; M=1-116.
PDB; 4MY6; X-ray; 1.70 A; A/B=1-111.
PDB; 5N91; X-ray; 1.49 A; A/B=1-111.
PDB; 5N9C; X-ray; 1.16 A; A/B=1-111.
PDB; 5N9P; X-ray; 1.80 A; A/B=1-111.
PDB; 5NAJ; X-ray; 1.46 A; A/B/C/D=1-111.
PDB; 5NBF; X-ray; 1.15 A; A=1-111.
PDB; 5NBX; X-ray; 1.65 A; A/B=1-111.
PDB; 5NC2; X-ray; 1.58 A; A/B=1-111.
PDB; 5NC7; X-ray; 2.70 A; A/B/C/D=1-111.
PDB; 5NCF; X-ray; 1.40 A; A/B=1-111.
PDB; 5NCG; X-ray; 1.02 A; A/B=1-111.
PDB; 5NCP; X-ray; 1.65 A; A=1-111.
PDB; 5ND0; X-ray; 1.45 A; A/B=1-111.
PDB; 5NDU; X-ray; 1.42 A; A/B=1-111.
PDB; 5NEG; X-ray; 1.29 A; A/B=1-111.
PDBsum; 2HO2; -.
PDBsum; 2IYB; -.
PDBsum; 2XQN; -.
PDBsum; 4MY6; -.
PDBsum; 5N91; -.
PDBsum; 5N9C; -.
PDBsum; 5N9P; -.
PDBsum; 5NAJ; -.
PDBsum; 5NBF; -.
PDBsum; 5NBX; -.
PDBsum; 5NC2; -.
PDBsum; 5NC7; -.
PDBsum; 5NCF; -.
PDBsum; 5NCG; -.
PDBsum; 5NCP; -.
PDBsum; 5ND0; -.
PDBsum; 5NDU; -.
PDBsum; 5NEG; -.
ProteinModelPortal; Q8N8S7; -.
SMR; Q8N8S7; -.
BioGrid; 120858; 51.
ELM; Q8N8S7; -.
IntAct; Q8N8S7; 23.
MINT; Q8N8S7; -.
STRING; 9606.ENSP00000355809; -.
CarbonylDB; Q8N8S7; -.
iPTMnet; Q8N8S7; -.
PhosphoSitePlus; Q8N8S7; -.
BioMuta; ENAH; -.
DMDM; 48428086; -.
EPD; Q8N8S7; -.
MaxQB; Q8N8S7; -.
PaxDb; Q8N8S7; -.
PeptideAtlas; Q8N8S7; -.
PRIDE; Q8N8S7; -.
ProteomicsDB; 72457; -.
ProteomicsDB; 72458; -. [Q8N8S7-2]
Ensembl; ENST00000366843; ENSP00000355808; ENSG00000154380. [Q8N8S7-2]
Ensembl; ENST00000366844; ENSP00000355809; ENSG00000154380. [Q8N8S7-1]
GeneID; 55740; -.
KEGG; hsa:55740; -.
UCSC; uc001hpc.2; human. [Q8N8S7-1]
CTD; 55740; -.
DisGeNET; 55740; -.
EuPathDB; HostDB:ENSG00000154380.17; -.
GeneCards; ENAH; -.
HGNC; HGNC:18271; ENAH.
HPA; HPA028448; -.
HPA; HPA028696; -.
MIM; 609061; gene.
neXtProt; NX_Q8N8S7; -.
OpenTargets; ENSG00000154380; -.
PharmGKB; PA38517; -.
eggNOG; KOG4590; Eukaryota.
eggNOG; ENOG41101TS; LUCA.
GeneTree; ENSGT00730000110272; -.
HOVERGEN; HBG006655; -.
InParanoid; Q8N8S7; -.
KO; K05746; -.
OrthoDB; EOG091G0QTE; -.
PhylomeDB; Q8N8S7; -.
TreeFam; TF321411; -.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-376176; Signaling by ROBO receptors.
ChiTaRS; ENAH; human.
EvolutionaryTrace; Q8N8S7; -.
GeneWiki; ENAH_(gene); -.
GenomeRNAi; 55740; -.
PRO; PR:Q8N8S7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000154380; Expressed in 231 organ(s), highest expression level in saphenous vein.
CleanEx; HS_ENAH; -.
ExpressionAtlas; Q8N8S7; baseline and differential.
Genevisible; Q8N8S7; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
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;
3D-structure; Actin-binding; Alternative splicing; Cell junction;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Phosphoprotein;
Reference proteome; Repeat; SH3-binding; Synapse.
CHAIN 1 591 Protein enabled homolog.
/FTId=PRO_0000086971.
DOMAIN 1 111 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REPEAT 156 160 1.
REPEAT 161 165 2.
REPEAT 166 170 3.
REPEAT 171 175 4.
REPEAT 176 180 5.
REPEAT 181 185 6.
REPEAT 186 190 7.
REPEAT 191 195 8.
REPEAT 196 200 9.
REGION 156 200 9 X 5 AA tandem repeats of [LMQ]-E-[QR]-
E-[QR].
REGION 391 588 EVH2.
REGION 391 411 EVH2 block A.
REGION 442 459 EVH2 block B.
REGION 554 588 EVH2 block C.
COILED 135 265 {ECO:0000255}.
COILED 557 587 {ECO:0000255}.
MOTIF 400 403 KLKR.
COMPBIAS 310 373 Pro-rich.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 265 265 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q03173}.
MOD_RES 506 506 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 268 304 Missing (in isoform 3).
{ECO:0000303|PubMed:23129656}.
/FTId=VSP_053772.
VAR_SEQ 513 533 Missing (in isoform 3).
{ECO:0000303|PubMed:23129656}.
/FTId=VSP_053773.
VAR_SEQ 514 534 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.1}.
/FTId=VSP_010564.
CONFLICT 493 493 T -> I (in Ref. 5; AAH95481).
{ECO:0000305}.
STRAND 3 17 {ECO:0000244|PDB:5NCG}.
TURN 18 21 {ECO:0000244|PDB:5NCG}.
STRAND 22 25 {ECO:0000244|PDB:5NCG}.
HELIX 26 28 {ECO:0000244|PDB:5NCG}.
STRAND 32 40 {ECO:0000244|PDB:5NCG}.
TURN 41 44 {ECO:0000244|PDB:5NCG}.
STRAND 45 52 {ECO:0000244|PDB:5NCG}.
TURN 53 55 {ECO:0000244|PDB:5NCG}.
STRAND 58 64 {ECO:0000244|PDB:5NCG}.
STRAND 70 72 {ECO:0000244|PDB:5NCG}.
STRAND 74 81 {ECO:0000244|PDB:5NCG}.
STRAND 86 93 {ECO:0000244|PDB:5NCG}.
HELIX 94 110 {ECO:0000244|PDB:5NCG}.
SEQUENCE 591 AA; 66510 MW; BF3252F6FCD1988B CRC64;
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQETGPTL
PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER LERERMERER LERERLERER
LERERLEQEQ LERERQERER QERLERQERL ERQERLERQE RLDRERQERQ ERERLERLER
ERQERERQEQ LEREQLEWER ERRISSAAAP ASVETPLNSV LGDSSASEPG LQAASQPAET
PSQQGIVLGP LAPPPPPPLP PGPAQASVAL PPPPGPPPPP PLPSTGPPPP PPPPPLPNQV
PPPPPPPPAP PLPASGFFLA SMSEDNRPLT GLAAAIAGAK LRKVSRMEDT SFPSGGNAIG
VNSASSKTDT GRGNGPLPLG GSGLMEEMSA LLARRRRIAE KGSTIETEQK EDKGEDSEPV
TSKASSTSTP EPTRKPWERT NTMNGSKSPV ISRRDSPRKN QIVFDNRSYD SLHRPKSTPL
SQPSANGVQT EGLDYDRLKQ DILDEMRKEL TKLKEELIDA IRQELSKSNT A


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