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Vasodilator-stimulated phosphoprotein (VASP)

 VASP_HUMAN              Reviewed;         380 AA.
P50552; B2RBT9; Q6PIZ1; Q93035;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 186.
RecName: Full=Vasodilator-stimulated phosphoprotein;
Short=VASP;
Name=VASP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-32; 87-96; 140-154;
255-282 AND 297-322, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
POSSIBLE FUNCTION.
TISSUE=Promyelocyte;
PubMed=7828592;
Haffner C., Jarchau T., Reinhard M., Hoppe J., Lohmann S.M.,
Walter U.;
"Molecular cloning, structural analysis and functional expression of
the proline-rich focal adhesion and microfilament-associated protein
VASP.";
EMBO J. 14:19-27(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH
L.MONOCYTOGENES ACTA.
PubMed=10087267; DOI=10.1083/jcb.144.6.1245;
Laurent V., Loisel T.P., Harbeck B., Wehman A., Groebe L.,
Jockusch B.M., Wehland J., Gertler F.B., Carlier M.-F.;
"Role of proteins of the Ena/VASP family in actin-based motility of
Listeria monocytogenes.";
J. Cell Biol. 144:1245-1258(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal lung, Fetal spleen, 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]
PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT SER-2.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-380.
PubMed=8812448; DOI=10.1006/geno.1996.0457;
Zimmer M., Fink T., Fischer L., Hauser W., Scherer K., Lichter P.,
Walter U.;
"Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in
human and mouse: structure, sequence, and chromosomal localization.";
Genomics 36:227-233(1996).
[8]
PROTEIN SEQUENCE OF 143-164; 235-244 AND 267-285, AND PHOSPHORYLATION
AT SER-157; SER-239 AND THR-278 BY PRKG1.
PubMed=8182057;
Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U.;
"cAMP- and cGMP-dependent protein kinase phosphorylation sites of the
focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro
and in intact human platelets.";
J. Biol. Chem. 269:14509-14517(1994).
[9]
PHOSPHORYLATION AT SER-157, AND FIBRINOGEN RECEPTOR INHIBITION.
PubMed=7925440; DOI=10.1111/j.1432-1033.1994.00021.x;
Horstrup K., Jablonka B., Honig-Liedl P., Just M., Kochsiek K.,
Walter U.;
"Phosphorylation of focal adhesion vasodilator-stimulated
phosphoprotein at Ser157 in intact human platelets correlates with
fibrinogen receptor inhibition.";
Eur. J. Biochem. 225:21-27(1994).
[10]
INTERACTION WITH ACTG1 AND PFN1.
PubMed=7737110;
Reinhard M., Giehl K., Abel K., Haffner C., Jarchau T., Hoppe V.,
Jockusch B.M., Walter U.;
"The proline-rich focal adhesion and microfilament protein VASP is a
ligand for profilins.";
EMBO J. 14:1583-1589(1995).
[11]
FUNCTION OF EVH2 DOMAIN.
PubMed=10438535; DOI=10.1074/jbc.274.33.23549;
Bachmann C., Fischer L., Walter U., Reinhard M.;
"The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates
tetramerization, F-actin binding, and actin bundle formation.";
J. Biol. Chem. 274:23549-23557(1999).
[12]
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).
[13]
INTERACTION WITH LPP.
PubMed=10637295; DOI=10.1091/mbc.11.1.117;
Petit M.M., Fradelizi J., Golsteyn R.M., Ayoubi T.A., Menichi B.,
Louvard D., Van de Ven W.J.M., Friederich E.;
"LPP, an actin cytoskeleton protein related to zyxin, harbors a
nuclear export signal and transcriptional activation capacity.";
Mol. Biol. Cell 11:117-129(2000).
[14]
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).
[15]
PHOSPHORYLATION BY PKC.
PubMed=14706852; DOI=10.1016/S0014-5793(03)01435-2;
Chitaley K., Chen L., Galler A., Walter U., Daum G., Clowes A.W.;
"Vasodilator-stimulated phosphoprotein is a substrate for protein
kinase C.";
FEBS Lett. 556:211-215(2004).
[16]
FUNCTION, LACK OF ACTIN NUCLEATION ACTIVITY, AND FUNCTION IN ACTIN
FILAMENT ELONGATION.
PubMed=15939738; DOI=10.1074/jbc.M503957200;
Barzik M., Kotova T.I., Higgs H.N., Hazelwood L., Hanein D.,
Gertler F.B., Schafer D.A.;
"Ena/VASP proteins enhance actin polymerization in the presence of
barbed end capping proteins.";
J. Biol. Chem. 280:28653-28662(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[18]
PHOSPHORYLATION AT SER-157, AND SUBCELLULAR LOCATION.
PubMed=16197368; DOI=10.1042/BJ20050796;
Wentworth J.K., Pula G., Poole A.W.;
"Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser
157 by protein kinase C-dependent and -independent mechanisms in
thrombin-stimulated human platelets.";
Biochem. J. 393:555-564(2006).
[19]
INTERACTION WITH XIRP1.
PubMed=16631741; DOI=10.1016/j.yexcr.2006.03.015;
van der Ven P.F.M., Ehler E., Vakeel P., Eulitz S., Schenk J.A.,
Milting H., Micheel B., Fuerst D.O.;
"Unusual splicing events result in distinct Xin isoforms that
associate differentially with filamin c and Mena/VASP.";
Exp. Cell Res. 312:2154-2167(2006).
[20]
PHOSPHORYLATION AT THR-278, MUTAGENESIS OF SER-157; SER-239 AND
THR-278, AND FUNCTION.
PubMed=17082196; DOI=10.1074/jbc.M608866200;
Blume C., Benz P.M., Walter U., Ha J., Kemp B.E., Renne T.;
"AMP-activated protein kinase impairs endothelial actin cytoskeleton
assembly by phosphorylating vasodilator-stimulated phosphoprotein.";
J. Biol. Chem. 282:4601-4612(2007).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-157 AND
SER-239.
PubMed=18559661; DOI=10.2337/db08-0381;
Li Calzi S., Purich D.L., Chang K.H., Afzal A., Nakagawa T.,
Busik J.V., Agarwal A., Segal M.S., Grant M.B.;
"Carbon monoxide and nitric oxide mediate cytoskeletal reorganization
in microvascular cells via vasodilator-stimulated phosphoprotein
phosphorylation: evidence for blunted responsiveness in diabetes.";
Diabetes 57:2488-2494(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316 AND SER-322, 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).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
SUBCELLULAR LOCATION, AND INTERACTION WITH MEFV.
PubMed=19109554; DOI=10.3181/0806-RM-184;
Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B.,
Hong A., Fox M., Gumucio D.L.;
"Pyrin and ASC co-localize to cellular sites that are rich in
polymerizing actin.";
Exp. Biol. Med. (Maywood) 234:40-52(2009).
[26]
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).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, 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).
[29]
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).
[30]
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).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39; SER-46; SER-239;
THR-284; SER-305 AND SER-314, 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).
[34]
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).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[36]
STRUCTURE BY NMR OF 1-115.
PubMed=10990454; DOI=10.1093/emboj/19.18.4903;
Ball L.J., Kuehne R., Hoffmann B., Haefner A., Schmieder P.,
Volkmer-Engert R., Hof M., Wahl M., Schneider-Mergener J., Walter U.,
Oschkinat H., Jarchau T.;
"Dual epitope recognition by the VASP EVH1 domain modulates
polyproline ligand specificity and binding affinity.";
EMBO J. 19:4903-4914(2000).
[37]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 336-380, TETRAMERIZATION, AND
MUTAGENESIS OF PHE-370.
PubMed=15569942; DOI=10.1073/pnas.0403069101;
Kuehnel K., Jarchau T., Wolf E., Schlichting I., Walter U.,
Wittinghofer A., Strelkov S.V.;
"The VASP tetramerization domain is a right-handed coiled coil based
on a 15-residue repeat.";
Proc. Natl. Acad. Sci. U.S.A. 101:17027-17032(2004).
[38]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 203-245 IN COMPLEXES WITH
PFN1 AND ACTIN, AND INTERACTION WITH PFN1 AND MONOMERIC ACTIN.
PubMed=17914456; DOI=10.1038/sj.emboj.7601874;
Ferron F., Rebowski G., Lee S.H., Dominguez R.;
"Structural basis for the recruitment of profilin-actin complexes
during filament elongation by Ena/VASP.";
EMBO J. 26:4597-4606(2007).
[39]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 199-214 IN COMPLEX WITH PFN1
AND ACTIN.
PubMed=18689676; DOI=10.1073/pnas.0805852105;
Baek K., Liu X., Ferron F., Shu S., Korn E.D., Dominguez R.;
"Modulation of actin structure and function by phosphorylation of Tyr-
53 and profilin binding.";
Proc. Natl. Acad. Sci. U.S.A. 105:11748-11753(2008).
-!- 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, lamellipodial and filopodial
dynamics, platelet activation and cell migration. VASP promotes
actin filament elongation. It protects the barbed end of growing
actin filaments against capping and increases the rate of actin
polymerization in the presence of capping protein. VASP stimulates
actin filament elongation by promoting the transfer of profilin-
bound actin monomers onto the barbed end of growing actin
filaments. Plays a role in actin-based mobility of Listeria
monocytogenes in host cells. Regulates actin dynamics in platelets
and plays an important role in regulating platelet aggregation.
{ECO:0000269|PubMed:10087267, ECO:0000269|PubMed:10438535,
ECO:0000269|PubMed:15939738, ECO:0000269|PubMed:17082196,
ECO:0000269|PubMed:18559661}.
-!- SUBUNIT: Homotetramer. Interacts with PFN1, PFN2, LPP, ACTN1 and
ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions
of ZYX. This interaction is important for targeting to focal
adhesions and the formation of actin-rich structures at the apical
surface of cells. Interacts, via the EVH1 domain, with the Pro-
rich domain of Listeria monocytogenes actA. Interacts with
APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal
SH3 domain of DNMBP (By similarity). Interacts weakly with MEFV.
{ECO:0000250, ECO:0000269|PubMed:10087267,
ECO:0000269|PubMed:10637295, ECO:0000269|PubMed:10801818,
ECO:0000269|PubMed:15469845, ECO:0000269|PubMed:16631741,
ECO:0000269|PubMed:17914456, ECO:0000269|PubMed:18689676,
ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:7737110}.
-!- INTERACTION:
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-748201, EBI-743598;
Q9P2A4:ABI3; NbExp=7; IntAct=EBI-748201, EBI-742038;
Q9UQB8-4:BAIAP2; NbExp=6; IntAct=EBI-748201, EBI-6174091;
O95684:FGFR1OP; NbExp=3; IntAct=EBI-748201, EBI-1266334;
P22736:NR4A1; NbExp=2; IntAct=EBI-748201, EBI-721550;
Q92636:NSMAF; NbExp=2; IntAct=EBI-748201, EBI-2947053;
Q15418:RPS6KA1; NbExp=4; IntAct=EBI-748201, EBI-963034;
Q13296:SCGB2A2; NbExp=3; IntAct=EBI-748201, EBI-9058786;
Q9C026:TRIM9; NbExp=3; IntAct=EBI-748201, EBI-720828;
P12003:VCL (xeno); NbExp=2; IntAct=EBI-748201, EBI-1039563;
Q702N8:XIRP1; NbExp=5; IntAct=EBI-748201, EBI-7851194;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
junction, focal adhesion. Cell junction, tight junction
{ECO:0000250}. Cell projection, lamellipodium membrane. Cell
projection, filopodium membrane. Note=Targeted to stress fibers
and focal adhesions through interaction with a number of proteins
including MRL family members. Localizes to the plasma membrane in
protruding lamellipodia and filopodial tips. Stimulation by
thrombin or PMA, also translocates VASP to focal adhesions.
Localized along the sides of actin filaments throughout the
peripheral cytoplasm under basal conditions. In pre-apoptotic
cells, colocalizes with MEFV in large specks (pyroptosomes).
-!- TISSUE SPECIFICITY: Highly expressed in platelets.
{ECO:0000269|PubMed:7828592}.
-!- 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.
-!- DOMAIN: The WH1 domain mediates interaction with XIRP1.
-!- PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent
protein kinase (PKG) in platelets. The preferred site for PKA is
Ser-157, the preferred site for PKG/PRKG1, Ser-239. In ADP-
activated platelets, phosphorylation by PKA or PKG on Ser-157
leads to fibrinogen receptor inhibition. Phosphorylation on Thr-
278 requires prior phosphorylation on Ser-157 and Ser-239. In
response to phorbol ester (PMA) stimulation, phosphorylated by
PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and
ROCK1. Phosphorylation at Thr-278 by AMPK does not require prior
phosphorylation at Ser-157 or Ser-239. Phosphorylation at Ser-157
by PKA is required for localization to the tight junctions in
epithelial cells. Phosphorylation modulates F-actin binding, actin
filament elongation and platelet activation. Phosphorylation at
Ser-322 by AMPK also alters actin filament binding. Carbon
monoxide (CO) promotes phosphorylation at Ser-157, while nitric
oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-
239. Response to NO and CO is blunted in platelets from diabetic
patients, and VASP is not phosphorylated efficiently at Ser-157
and Ser-239. {ECO:0000269|PubMed:14706852,
ECO:0000269|PubMed:16197368, ECO:0000269|PubMed:17082196,
ECO:0000269|PubMed:18559661, ECO:0000269|PubMed:7925440,
ECO:0000269|PubMed:8182057}.
-!- MISCELLANEOUS: VASP phosphorylation is used to monitor the effect
of so-called antiplatelet drugs that reduce platelet reactivity
and are used to prevent stent thrombosis, strokes and heart
attacks in patients at risk for these problems.
-!- 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; Z46389; CAA86523.1; -; mRNA.
EMBL; CH471126; EAW57362.1; -; Genomic_DNA.
EMBL; AK314812; BAG37336.1; -; mRNA.
EMBL; BC026019; AAH26019.1; -; mRNA.
EMBL; BC038224; AAH38224.1; -; mRNA.
EMBL; X98534; CAA67147.2; -; Genomic_DNA.
EMBL; X98533; CAA67147.2; JOINED; Genomic_DNA.
CCDS; CCDS33051.1; -.
PIR; S51797; S51797.
RefSeq; NP_003361.1; NM_003370.3.
UniGene; Hs.515469; -.
PDB; 1EGX; NMR; -; A=1-115.
PDB; 1JNG; Model; -; A=1-115.
PDB; 1USD; X-ray; 1.70 A; A=336-380.
PDB; 1USE; X-ray; 1.30 A; A=336-380.
PDB; 2PAV; X-ray; 1.80 A; V=199-214.
PDB; 2PBD; X-ray; 1.50 A; V=203-245.
PDB; 3CHW; X-ray; 2.30 A; V=199-214.
PDBsum; 1EGX; -.
PDBsum; 1JNG; -.
PDBsum; 1USD; -.
PDBsum; 1USE; -.
PDBsum; 2PAV; -.
PDBsum; 2PBD; -.
PDBsum; 3CHW; -.
ProteinModelPortal; P50552; -.
SMR; P50552; -.
BioGrid; 113251; 91.
CORUM; P50552; -.
DIP; DIP-44105N; -.
ELM; P50552; -.
IntAct; P50552; 39.
MINT; P50552; -.
STRING; 9606.ENSP00000245932; -.
MoonDB; P50552; Predicted.
iPTMnet; P50552; -.
PhosphoSitePlus; P50552; -.
BioMuta; VASP; -.
DMDM; 1718079; -.
OGP; P50552; -.
EPD; P50552; -.
MaxQB; P50552; -.
PaxDb; P50552; -.
PeptideAtlas; P50552; -.
PRIDE; P50552; -.
ProteomicsDB; 56248; -.
TopDownProteomics; P50552; -.
Ensembl; ENST00000245932; ENSP00000245932; ENSG00000125753.
GeneID; 7408; -.
KEGG; hsa:7408; -.
UCSC; uc002pcg.4; human.
CTD; 7408; -.
DisGeNET; 7408; -.
EuPathDB; HostDB:ENSG00000125753.13; -.
GeneCards; VASP; -.
HGNC; HGNC:12652; VASP.
HPA; CAB004612; -.
HPA; HPA005724; -.
MIM; 601703; gene.
neXtProt; NX_P50552; -.
OpenTargets; ENSG00000125753; -.
PharmGKB; PA37276; -.
eggNOG; KOG4590; Eukaryota.
eggNOG; ENOG41101TS; LUCA.
GeneTree; ENSGT00730000110272; -.
HOGENOM; HOG000013015; -.
HOVERGEN; HBG006655; -.
InParanoid; P50552; -.
KO; K06274; -.
OMA; MSETVIC; -.
OrthoDB; EOG091G0QTE; -.
PhylomeDB; P50552; -.
TreeFam; TF321411; -.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-376176; Signaling by ROBO receptors.
Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
SIGNOR; P50552; -.
ChiTaRS; VASP; human.
EvolutionaryTrace; P50552; -.
GeneWiki; Vasodilator-stimulated_phosphoprotein; -.
GenomeRNAi; 7408; -.
PRO; PR:P50552; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000125753; Expressed in 209 organ(s), highest expression level in blood.
CleanEx; HS_VASP; -.
ExpressionAtlas; P50552; baseline and differential.
Genevisible; P50552; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0005522; F:profilin binding; IPI:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR034367; VASP.
InterPro; IPR017354; VASP/EVL.
InterPro; IPR038023; VASP_sf.
InterPro; IPR014885; VASP_tetra.
InterPro; IPR000697; WH1/EVH1_dom.
PANTHER; PTHR11202:SF12; PTHR11202:SF12; 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;
3D-structure; Acetylation; Actin-binding; Cell junction;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3-binding;
Tight junction.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
CHAIN 2 380 Vasodilator-stimulated phosphoprotein.
/FTId=PRO_0000065767.
DOMAIN 2 113 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REPEAT 344 358 1.
REPEAT 359 373 2.
REGION 225 377 EVH2.
REGION 225 245 EVH2 block A.
REGION 259 278 EVH2 block B.
REGION 343 377 EVH2 block C.
REGION 344 373 2 X 15 AA tandem repeats of L-[EQ]-[KR]-
[MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-
[KRV]-[KQ]-E.
COILED 337 373 {ECO:0000255}.
MOTIF 234 237 KLKR.
COMPBIAS 118 216 Pro-rich.
COMPBIAS 215 222 Poly-Gly.
COMPBIAS 259 262 Poly-Gly.
COMPBIAS 322 325 Poly-Ser.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
MOD_RES 39 39 Phosphotyrosine.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:23186163}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 157 157 Phosphoserine; by PKA, PKC, PKG/PRKG1 and
ROCK1. {ECO:0000269|PubMed:16197368,
ECO:0000269|PubMed:18559661,
ECO:0000269|PubMed:7925440,
ECO:0000269|PubMed:8182057}.
MOD_RES 239 239 Phosphoserine; by PKA and PKG/PRKG1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18559661,
ECO:0000269|PubMed:8182057}.
MOD_RES 278 278 Phosphothreonine; by PKA, PKG/PRKG1 and
AMPK. {ECO:0000269|PubMed:17082196,
ECO:0000269|PubMed:8182057}.
MOD_RES 283 283 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 284 284 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 316 316 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 322 322 Phosphoserine; by AMPK.
{ECO:0000244|PubMed:18669648}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000250|UniProtKB:P70460}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:P70460}.
VARIANT 104 104 A -> T (in dbSNP:rs10415373).
/FTId=VAR_048929.
VARIANT 140 140 Q -> H (in dbSNP:rs34345197).
/FTId=VAR_048930.
MUTAGEN 157 157 S->A: Promotes F-actin assembly; when
associated with A-239 and A-278.
Interferes with F-actin assembly; when
associated with A-239 and E-278.
{ECO:0000269|PubMed:17082196}.
MUTAGEN 239 239 S->A: Promotes F-actin assembly; when
associated with A-157 and A-278.
Interferes with F-actin assembly; when
associated with A-157 and E-278.
{ECO:0000269|PubMed:17082196}.
MUTAGEN 278 278 T->A: Promotes F-actin assembly; when
associated with A-157 and A-239.
{ECO:0000269|PubMed:17082196}.
MUTAGEN 278 278 T->E: Interferes with F-actin assembly;
when associated with A-157 and A-239.
{ECO:0000269|PubMed:17082196}.
MUTAGEN 370 370 F->A: Lower stability of tetramerization
domain. {ECO:0000269|PubMed:15569942}.
MUTAGEN 370 370 F->I,K: No change in stability of
tetramerization domain.
{ECO:0000269|PubMed:15569942}.
CONFLICT 2 2 S -> SS (in Ref. 5; AAH26019).
{ECO:0000305}.
CONFLICT 241 241 Missing (in Ref. 5; AAH26019).
{ECO:0000305}.
STRAND 5 12 {ECO:0000244|PDB:1EGX}.
STRAND 14 16 {ECO:0000244|PDB:1EGX}.
TURN 18 20 {ECO:0000244|PDB:1EGX}.
STRAND 25 27 {ECO:0000244|PDB:1EGX}.
STRAND 34 41 {ECO:0000244|PDB:1EGX}.
TURN 42 45 {ECO:0000244|PDB:1EGX}.
STRAND 46 55 {ECO:0000244|PDB:1EGX}.
STRAND 60 66 {ECO:0000244|PDB:1EGX}.
STRAND 79 86 {ECO:0000244|PDB:1EGX}.
STRAND 88 95 {ECO:0000244|PDB:1EGX}.
HELIX 96 114 {ECO:0000244|PDB:1EGX}.
HELIX 226 231 {ECO:0000244|PDB:2PBD}.
HELIX 341 376 {ECO:0000244|PDB:1USE}.
SEQUENCE 380 AA; 39830 MW; 17634B8134DEBF59 CRC64;
MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV
VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA QFAAGMASAL EALEGGGPPP
PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE HIERRVSNAG GPPAPPAGGP PPPPGPPPPP
GPPPPPGLPP SGVPAAAHGA GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK
QEEASGGPTA PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP
AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSDLQRVKQE LLEEVKKELQ
KVKEEIIEAF VQELRKRGSP


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