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P50552 (VASP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vasodilator-stimulated phosphoprotein

Short name=VASP
Gene names
Name:VASP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2 Ref.11 Ref.16 Ref.20 Ref.21

Subunit structure

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. Ref.2 Ref.10 Ref.12 Ref.13 Ref.14 Ref.19 Ref.25 Ref.34 Ref.35

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cell junctionfocal adhesion. Cell junctiontight junction By similarity. Cell projectionlamellipodium membrane. Cell projectionfilopodium 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). Ref.1 Ref.18 Ref.21 Ref.25

Tissue specificity

Highly expressed in platelets. Ref.1

Domain

The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization. Ref.11

The WH1 domain mediates interaction with XIRP1. Ref.11

Post-translational modification

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. Ref.8 Ref.9 Ref.15 Ref.18 Ref.20 Ref.21

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.

Sequence similarities

Belongs to the Ena/VASP family.

Contains 1 WH1 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Tight junction
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
SH3-binding
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Traceable author statement. Source: Reactome

actin polymerization or depolymerization

Inferred from electronic annotation. Source: InterPro

axon guidance

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

neural tube closure

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from direct assay PubMed 23153535. Source: UniProt

protein homotetramerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

filopodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from direct assay. Source: HPA

lamellipodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

tight junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprofilin binding

Inferred from physical interaction Ref.35. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NR4A1P227362EBI-748201,EBI-721550
NSMAFQ926362EBI-748201,EBI-2947053
RPS6KA1Q154184EBI-748201,EBI-963034
VCLP120032EBI-748201,EBI-1039563From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 380379Vasodilator-stimulated phosphoprotein
PRO_0000065767

Regions

Domain2 – 113112WH1
Repeat344 – 358151
Repeat359 – 373152
Region225 – 377153EVH2
Region225 – 24521EVH2 block A
Region259 – 27820EVH2 block B
Region343 – 37735EVH2 block C
Region344 – 373302 X 15 AA tandem repeats of L-[EQ]-[KR]-[MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-E
Coiled coil337 – 37337 Potential
Motif234 – 2374KLKR
Compositional bias118 – 21699Pro-rich
Compositional bias215 – 2228Poly-Gly
Compositional bias259 – 2624Poly-Gly
Compositional bias322 – 3254Poly-Ser

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.24 Ref.31 Ref.32
Modified residue391Phosphotyrosine Ref.17
Modified residue1571Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK1 Ref.8 Ref.9 Ref.18 Ref.21
Modified residue2391Phosphoserine; by PKA and PKG/PRKG1 Ref.8 Ref.21
Modified residue2781Phosphothreonine; by PKA, PKG/PRKG1 and AMPK Ref.8 Ref.20
Modified residue2831N6-acetyllysine Ref.27
Modified residue3161Phosphothreonine Ref.23 Ref.28
Modified residue3221Phosphoserine; by AMPK Ref.23
Modified residue3231Phosphoserine By similarity

Natural variations

Natural variant1041A → T.
Corresponds to variant rs10415373 [ dbSNP | Ensembl ].
VAR_048929
Natural variant1401Q → H.
Corresponds to variant rs34345197 [ dbSNP | Ensembl ].
VAR_048930

Experimental info

Mutagenesis1571S → 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. Ref.20
Mutagenesis2391S → 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. Ref.20
Mutagenesis2781T → A: Promotes F-actin assembly; when associated with A-157 and A-239. Ref.20
Mutagenesis2781T → E: Interferes with F-actin assembly; when associated with A-157 and A-239. Ref.20
Mutagenesis3701F → A: Lower stability of tetramerization domain. Ref.34
Mutagenesis3701F → I or K: No change in stability of tetramerization domain. Ref.34
Sequence conflict21S → SS in AAH26019. Ref.5
Sequence conflict2411Missing in AAH26019. Ref.5

Secondary structure

........................ 380
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50552 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 17634B8134DEBF59

FASTA38039,830
        10         20         30         40         50         60 
MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV 

        70         80         90        100        110        120 
VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA QFAAGMASAL EALEGGGPPP 

       130        140        150        160        170        180 
PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE HIERRVSNAG GPPAPPAGGP PPPPGPPPPP 

       190        200        210        220        230        240 
GPPPPPGLPP SGVPAAAHGA GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK 

       250        260        270        280        290        300 
QEEASGGPTA PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP 

       310        320        330        340        350        360 
AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSDLQRVKQE LLEEVKKELQ 

       370        380 
KVKEEIIEAF VQELRKRGSP 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP."
Haffner C., Jarchau T., Reinhard M., Hoppe J., Lohmann S.M., Walter U.
EMBO J. 14:19-27(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-32; 87-96; 140-154; 255-282 AND 297-322, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, POSSIBLE FUNCTION.
Tissue: Promyelocyte.
[2]"Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes."
Laurent V., Loisel T.P., Harbeck B., Wehman A., Groebe L., Jockusch B.M., Wehland J., Gertler F.B., Carlier M.-F.
J. Cell Biol. 144:1245-1258(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH L.MONOCYTOGENES ACTA.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Substantia nigra.
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal lung, Fetal spleen and Skin.
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT SER-2.
Tissue: Platelet.
[7]"Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization."
Zimmer M., Fink T., Fischer L., Hauser W., Scherer K., Lichter P., Walter U.
Genomics 36:227-233(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-380.
[8]"cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets."
Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U.
J. Biol. Chem. 269:14509-14517(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 143-164; 235-244 AND 267-285, PHOSPHORYLATION AT SER-157; SER-239 AND THR-278 BY PRKG1.
[9]"Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition."
Horstrup K., Jablonka B., Honig-Liedl P., Just M., Kochsiek K., Walter U.
Eur. J. Biochem. 225:21-27(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-157, FIBRINOGEN RECEPTOR INHIBITION.
[10]"The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins."
Reinhard M., Giehl K., Abel K., Haffner C., Jarchau T., Hoppe V., Jockusch B.M., Walter U.
EMBO J. 14:1583-1589(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACTG1 AND PFN1.
[11]"The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation."
Bachmann C., Fischer L., Walter U., Reinhard M.
J. Biol. Chem. 274:23549-23557(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF EVH2 DOMAIN.
[12]"Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins."
Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C., Golsteyn R.M.
J. Biol. Chem. 275:22503-22511(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZYX.
[13]"LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity."
Petit M.M., Fradelizi J., Golsteyn R.M., Ayoubi T.A., Menichi B., Louvard D., Van de Ven W.J.M., Friederich E.
Mol. Biol. Cell 11:117-129(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LPP.
[14]"Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics."
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.
Dev. Cell 7:571-583(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAPH1.
[15]"Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C."
Chitaley K., Chen L., Galler A., Walter U., Daum G., Clowes A.W.
FEBS Lett. 556:211-215(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PKC.
[16]"Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins."
Barzik M., Kotova T.I., Higgs H.N., Hazelwood L., Hanein D., Gertler F.B., Schafer D.A.
J. Biol. Chem. 280:28653-28662(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, LACK OF ACTIN NUCLEATION ACTIVITY, FUNCTION IN ACTIN FILAMENT ELONGATION.
[17]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser 157 by protein kinase C-dependent and -independent mechanisms in thrombin-stimulated human platelets."
Wentworth J.K., Pula G., Poole A.W.
Biochem. J. 393:555-564(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-157, SUBCELLULAR LOCATION.
[19]"Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP."
van der Ven P.F.M., Ehler E., Vakeel P., Eulitz S., Schenk J.A., Milting H., Micheel B., Fuerst D.O.
Exp. Cell Res. 312:2154-2167(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XIRP1.
[20]"AMP-activated protein kinase impairs endothelial actin cytoskeleton assembly by phosphorylating vasodilator-stimulated phosphoprotein."
Blume C., Benz P.M., Walter U., Ha J., Kemp B.E., Renne T.
J. Biol. Chem. 282:4601-4612(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-278, MUTAGENESIS OF SER-157; SER-239 AND THR-278, FUNCTION.
[21]"Carbon monoxide and nitric oxide mediate cytoskeletal reorganization in microvascular cells via vasodilator-stimulated phosphoprotein phosphorylation: evidence for blunted responsiveness in diabetes."
Li Calzi S., Purich D.L., Chang K.H., Afzal A., Nakagawa T., Busik J.V., Agarwal A., Segal M.S., Grant M.B.
Diabetes 57:2488-2494(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-157 AND SER-239.
[22]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin."
Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B., Hong A., Fox M., Gumucio D.L.
Exp. Biol. Med. (Maywood) 234:40-52(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MEFV.
[26]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity."
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.
EMBO J. 19:4903-4914(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-115.
[34]"The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat."
Kuehnel K., Jarchau T., Wolf E., Schlichting I., Walter U., Wittinghofer A., Strelkov S.V.
Proc. Natl. Acad. Sci. U.S.A. 101:17027-17032(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 336-380, TETRAMERIZATION, MUTAGENESIS OF PHE-370.
[35]"Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP."
Ferron F., Rebowski G., Lee S.H., Dominguez R.
EMBO J. 26:4597-4606(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 203-245 IN COMPLEXES WITH PFN1 AND ACTIN, INTERACTION WITH PFN1 AND MONOMERIC ACTIN.
[36]"Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding."
Baek K., Liu X., Ferron F., Shu S., Korn E.D., Dominguez R.
Proc. Natl. Acad. Sci. U.S.A. 105:11748-11753(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 199-214 IN COMPLEX WITH PFN1 AND ACTIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46389 mRNA. Translation: CAA86523.1.
CH471126 Genomic DNA. Translation: EAW57362.1.
AK314812 mRNA. Translation: BAG37336.1.
BC026019 mRNA. Translation: AAH26019.1.
BC038224 mRNA. Translation: AAH38224.1.
X98534, X98533 Genomic DNA. Translation: CAA67147.2.
PIRS51797.
RefSeqNP_003361.1. NM_003370.3.
UniGeneHs.515469.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGXNMR-A1-115[»]
1JNGmodel-A1-115[»]
1USDX-ray1.70A336-380[»]
1USEX-ray1.30A336-380[»]
2PAVX-ray1.80V199-214[»]
2PBDX-ray1.50V203-245[»]
3CHWX-ray2.30V199-214[»]
ProteinModelPortalP50552.
SMRP50552. Positions 1-115, 338-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113251. 52 interactions.
DIPDIP-44105N.
IntActP50552. 21 interactions.
MINTMINT-1437861.
STRING9606.ENSP00000245932.

PTM databases

PhosphoSiteP50552.

Polymorphism databases

DMDM1718079.

2D gel databases

OGPP50552.

Proteomic databases

PaxDbP50552.
PeptideAtlasP50552.
PRIDEP50552.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245932; ENSP00000245932; ENSG00000125753.
GeneID7408.
KEGGhsa:7408.
UCSCuc002pcg.3. human.

Organism-specific databases

CTD7408.
GeneCardsGC19P046010.
HGNCHGNC:12652. VASP.
HPACAB004612.
HPA005724.
MIM601703. gene.
neXtProtNX_P50552.
PharmGKBPA37276.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265043.
HOGENOMHOG000013015.
HOVERGENHBG006655.
InParanoidP50552.
KOK06274.
PhylomeDBP50552.
TreeFamTF321411.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP50552.
BgeeP50552.
CleanExHS_VASP.
GenevestigatorP50552.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view]
PfamPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTSM00461. WH1. 1 hit.
[Graphical view]
PROSITEPS50229. WH1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVASP. human.
EvolutionaryTraceP50552.
GeneWikiVasodilator-stimulated_phosphoprotein.
GenomeRNAi7408.
NextBio29004.
PROP50552.
SOURCESearch...

Entry information

Entry nameVASP_HUMAN
AccessionPrimary (citable) accession number: P50552
Secondary accession number(s): B2RBT9, Q6PIZ1, Q93035
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM