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Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)

 EVL_HUMAN               Reviewed;         416 AA.
Q9UI08; A8K105; B7Z3I5; O95884; Q7Z522; Q8TBV1; Q9UF25; Q9UIC2;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-NOV-2002, sequence version 2.
12-SEP-2018, entry version 171.
RecName: Full=Ena/VASP-like protein;
AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
Name=EVL; Synonyms=RNB6;
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).
Ohta S., Mineta T., Kimoto M., Tabuchi K.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wan Y.Z., Yu L., Yue P., Tu Q., Fu S.N., Zhao S.Y.;
"Cloning of a new human cDNA homologous to R.norvegicus RNB6 mRNA.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Substantia nigra;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and Pancreas;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-416.
TISSUE=Brain;
Mei G., Yu W., Gibbs R.A.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-364.
TISSUE=Uterus;
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).
[10]
INTERACTION WITH FYB1.
PubMed=10747096; DOI=10.1083/jcb.149.1.181;
Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B.,
Wehland J.;
"Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP),
Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the
Arp2/3 complex link T cell receptor (TCR) signaling to the actin
cytoskeleton.";
J. Cell Biol. 149:181-194(2000).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-369, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-304; SER-306;
SER-329; SER-331 AND SER-349, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-341 AND
SER-354, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
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).
[15]
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).
[16]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-331 AND
SER-369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-369, 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).
[19]
IDENTIFICATION (ISOFORM 5).
TISSUE=Fetal brain;
Lemonidis K.;
Submitted (NOV-2016) to UniProtKB.
[20]
INTERACTION WITH SEMA6A.
PubMed=10993894; DOI=10.1074/jbc.M006316200;
Klostermann A., Lutz B., Gertler F., Behl C.;
"The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-
1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-
like protein (EVL) via a novel carboxyl-terminal zyxin-like domain.";
J. Biol. Chem. 275:39647-39653(2000).
[21]
INTERACTION WITH RAPH1.
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).
[22]
INTERACTION WITH ZYX.
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]
INTERACTION WITH ZDHHC17.
PubMed=28882895; DOI=10.1074/jbc.M117.799650;
Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
"Peptide array based screening reveals a large number of proteins
interacting with the ankyrin repeat domain of the zDHHC17 S-
acyltransferase.";
J. Biol. Chem. 292:17190-17202(2017).
[24]
VARIANTS [LARGE SCALE ANALYSIS] LEU-188 AND LEU-247.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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. EVL enhances actin
nucleation and polymerization.
-!- SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of
ABL1, LYN and SRC. Also binds to profilin, with preference for
isoform IIa of PFN2, and the WW domain of APBB1/FE65. Binds to
SEMA6A. Interacts, via the Pro-rich region, with the C-terminal
SH3 domain of DNMBP. Interacts with RAPH1. Binds, via the EVH1
domain, the Pro-rich domain of Listeria monocytogenes actA (By
similarity). Binds, via the EVH1 domain, the Pro-rich domain of
ZYX. Interacts with FYB1 (PubMed:10747096). Interacts with ZDHHC17
(PubMed:28882895). {ECO:0000250|UniProtKB:P70429,
ECO:0000269|PubMed:10747096, ECO:0000269|PubMed:10993894,
ECO:0000269|PubMed:15469845, ECO:0000269|PubMed:18158903,
ECO:0000269|PubMed:28882895}.
-!- INTERACTION:
Q9P2A4:ABI3; NbExp=3; IntAct=EBI-346653, EBI-742038;
P42858:HTT; NbExp=2; IntAct=EBI-6448852, EBI-466029;
Q13813:SPTAN1; NbExp=4; IntAct=EBI-346653, EBI-351450;
Q9C026:TRIM9; NbExp=3; IntAct=EBI-346653, EBI-720828;
Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-6448852, EBI-524753;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P70429}. Cytoplasm, cytoskeleton, stress
fiber {ECO:0000250|UniProtKB:P70429}. Cell projection,
lamellipodium {ECO:0000250|UniProtKB:P70429}. Note=Targeted to the
leading edge of lamellipodia and the distal tip of stress fibers
through interaction with a number of proteins. In activated T-
cells, localizes to the F-actin collar and the distal tip of
microspikes. {ECO:0000250|UniProtKB:P70429}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=2; Synonyms=EVL-I;
IsoId=Q9UI08-1; Sequence=Displayed;
Name=1;
IsoId=Q9UI08-2; Sequence=VSP_004044;
Name=3;
IsoId=Q9UI08-3; Sequence=VSP_057322, VSP_057323;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9UI08-4; Sequence=VSP_058779;
Name=5;
IsoId=Q9UI08-5; Sequence=VSP_004044, VSP_058778;
-!- 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: Phosphorylated by PKA; phosphorylation abolishes binding to
SH3 domains of ABL and SRC. {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}.
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EMBL; AF052504; AAF21709.1; -; mRNA.
EMBL; AF087843; AAP97156.1; -; mRNA.
EMBL; AF112209; AAF17197.1; -; mRNA.
EMBL; AK289720; BAF82409.1; -; mRNA.
EMBL; AK295919; BAH12221.1; -; mRNA.
EMBL; AL133368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL157912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF456005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF456007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF456010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81684.1; -; Genomic_DNA.
EMBL; BC023997; AAH23997.1; -; mRNA.
EMBL; BC032358; AAH32358.1; -; mRNA.
EMBL; AF131766; AAD20040.1; -; mRNA.
EMBL; AL133642; CAB63763.2; -; mRNA.
CCDS; CCDS81851.1; -. [Q9UI08-1]
CCDS; CCDS9955.1; -. [Q9UI08-2]
RefSeq; NP_001317150.1; NM_001330221.1. [Q9UI08-1]
RefSeq; NP_057421.1; NM_016337.2. [Q9UI08-2]
UniGene; Hs.125867; -.
ProteinModelPortal; Q9UI08; -.
SMR; Q9UI08; -.
BioGrid; 119556; 45.
ELM; Q9UI08; -.
IntAct; Q9UI08; 17.
MINT; Q9UI08; -.
STRING; 9606.ENSP00000376652; -.
iPTMnet; Q9UI08; -.
PhosphoSitePlus; Q9UI08; -.
BioMuta; EVL; -.
DMDM; 25090276; -.
EPD; Q9UI08; -.
PaxDb; Q9UI08; -.
PeptideAtlas; Q9UI08; -.
PRIDE; Q9UI08; -.
ProteomicsDB; 84445; -.
ProteomicsDB; 84446; -. [Q9UI08-2]
DNASU; 51466; -.
Ensembl; ENST00000392920; ENSP00000376652; ENSG00000196405. [Q9UI08-2]
Ensembl; ENST00000402714; ENSP00000384720; ENSG00000196405. [Q9UI08-1]
Ensembl; ENST00000544450; ENSP00000437904; ENSG00000196405. [Q9UI08-3]
GeneID; 51466; -.
KEGG; hsa:51466; -.
UCSC; uc001ygt.4; human. [Q9UI08-1]
CTD; 51466; -.
DisGeNET; 51466; -.
EuPathDB; HostDB:ENSG00000196405.12; -.
GeneCards; EVL; -.
H-InvDB; HIX0011964; -.
HGNC; HGNC:20234; EVL.
HPA; CAB033987; -.
HPA; HPA018849; -.
HPA; HPA019536; -.
neXtProt; NX_Q9UI08; -.
OpenTargets; ENSG00000196405; -.
PharmGKB; PA134890866; -.
eggNOG; ENOG410IQ1Z; Eukaryota.
eggNOG; ENOG410YM7V; LUCA.
GeneTree; ENSGT00730000110272; -.
HOGENOM; HOG000013015; -.
HOVERGEN; HBG006655; -.
InParanoid; Q9UI08; -.
OMA; STQRQVQ; -.
OrthoDB; EOG091G0QTE; -.
PhylomeDB; Q9UI08; -.
TreeFam; TF321411; -.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-376176; Signaling by ROBO receptors.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
SignaLink; Q9UI08; -.
ChiTaRS; EVL; human.
GeneWiki; Enah/Vasp-like; -.
GenomeRNAi; 51466; -.
PRO; PR:Q9UI08; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000196405; Expressed in 222 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_EVL; -.
ExpressionAtlas; Q9UI08; baseline and differential.
Genevisible; Q9UI08; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005522; F:profilin binding; ISS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
GO; GO:0007015; P:actin filament organization; TAS:ProtInc.
GO; GO:0045010; P:actin nucleation; IEA:InterPro.
GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:1900028; P:negative regulation of ruffle assembly; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR034319; ENA/VASP-like_protein.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR017354; VASP/EVL.
InterPro; IPR038023; VASP_sf.
InterPro; IPR014885; VASP_tetra.
InterPro; IPR000697; WH1/EVH1_dom.
PANTHER; PTHR11202:SF4; PTHR11202:SF4; 1.
Pfam; PF08776; VASP_tetra; 1.
Pfam; PF00568; WH1; 1.
PIRSF; PIRSF038010; Vasodilator_Phospo; 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;
Polymorphism; Reference proteome; SH3-binding.
CHAIN 1 416 Ena/VASP-like protein.
/FTId=PRO_0000087104.
DOMAIN 1 112 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REGION 222 413 EVH2.
REGION 222 242 EVH2 block A.
REGION 265 282 EVH2 block B.
REGION 342 362 Required for interaction with ZDHHC17.
{ECO:0000269|PubMed:28882895}.
REGION 379 413 EVH2 block C.
MOTIF 231 234 KLKR.
COMPBIAS 162 206 Pro-rich.
MOD_RES 130 130 Phosphoserine.
{ECO:0000250|UniProtKB:O08719}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000250|UniProtKB:O08719}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:24275569}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 1 M -> MAT (in isoform 1 and isoform 5).
{ECO:0000303|PubMed:10931946,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.19, ECO:0000303|Ref.2}.
/FTId=VSP_004044.
VAR_SEQ 1 1 M -> MFAFEEF (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057322.
VAR_SEQ 342 362 Missing (in isoform 5).
{ECO:0000303|Ref.19}.
/FTId=VSP_058778.
VAR_SEQ 364 416 MKPAGSVNDMALDAFDLDRMKQEILEEVVRELHKVKEEIID
AIRQELSGISTT -> YRTTLLLTCPPGFGAPLSPVP (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057323.
VAR_SEQ 368 397 Missing (in isoform 4).
/FTId=VSP_058779.
VARIANT 188 188 P -> L (in a colorectal cancer sample;
somatic mutation; dbSNP:rs367737727).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036464.
VARIANT 247 247 P -> L (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036465.
CONFLICT 201 201 P -> S (in Ref. 3; AAF17197).
{ECO:0000305}.
CONFLICT 329 329 S -> N (in Ref. 2; AAP97156).
{ECO:0000305}.
CONFLICT 364 364 M -> Y (in Ref. 9; CAB63763).
{ECO:0000305}.
SEQUENCE 416 AA; 44620 MW; AD5B67458755D659 CRC64;
MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASNTFRVV GVKLQDQQVV
INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT FSNAMLFALN IMNSQEGGPS
SQRQVQNGPS PDEMDIQRRQ VMEQHQQQRQ ESLERRTSAT GPILPPGHPS SAASAPVSCS
GPPPPPPPPV PPPPTGATPP PPPPLPAGGA QGSSHDESSM SGLAAAIAGA KLRRVQRPED
ASGGSSPSGT SKSDANRASS GGGGGGLMEE MNKLLAKRRK AASQSDKPAE KKEDESQMED
PSTSPSPGTR AASQPPNSSE AGRKPWERSN SVEKPVSSIL SRTPSVAKSP EAKSPLQSQP
HSRMKPAGSV NDMALDAFDL DRMKQEILEE VVRELHKVKE EIIDAIRQEL SGISTT


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