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P50552

- VASP_HUMAN

UniProt

P50552 - VASP_HUMAN

Protein

Vasodilator-stimulated phosphoprotein

Gene

VASP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.5 Publications

    GO - Molecular functioni

    1. profilin binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin polymerization or depolymerization Source: InterPro
    2. axon guidance Source: Reactome
    3. cell junction assembly Source: Reactome
    4. neural tube closure Source: Ensembl
    5. positive regulation of actin filament polymerization Source: UniProt
    6. protein homotetramerization Source: InterPro
    7. T cell receptor signaling pathway Source: Reactome

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_12623. Generation of second messenger molecules.
    REACT_19351. Signaling by Robo receptor.
    REACT_20649. Cell-extracellular matrix interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vasodilator-stimulated phosphoprotein
    Short name:
    VASP
    Gene namesi
    Name:VASP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:12652. VASP.

    Subcellular locationi

    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).

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. filopodium membrane Source: UniProtKB-SubCell
    6. focal adhesion Source: HPA
    7. lamellipodium membrane Source: UniProtKB-SubCell
    8. plasma membrane Source: HPA
    9. tight junction Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571S → 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. 1 Publication
    Mutagenesisi239 – 2391S → 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. 1 Publication
    Mutagenesisi278 – 2781T → A: Promotes F-actin assembly; when associated with A-157 and A-239. 1 Publication
    Mutagenesisi278 – 2781T → E: Interferes with F-actin assembly; when associated with A-157 and A-239. 1 Publication
    Mutagenesisi370 – 3701F → A: Lower stability of tetramerization domain. 1 Publication
    Mutagenesisi370 – 3701F → I or K: No change in stability of tetramerization domain. 1 Publication

    Organism-specific databases

    PharmGKBiPA37276.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 380379Vasodilator-stimulated phosphoproteinPRO_0000065767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei39 – 391Phosphotyrosine2 Publications
    Modified residuei157 – 1571Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK15 Publications
    Modified residuei239 – 2391Phosphoserine; by PKA and PKG/PRKG13 Publications
    Modified residuei278 – 2781Phosphothreonine; by PKA, PKG/PRKG1 and AMPK3 Publications
    Modified residuei283 – 2831N6-acetyllysine1 Publication
    Modified residuei316 – 3161Phosphothreonine3 Publications
    Modified residuei322 – 3221Phosphoserine; by AMPK2 Publications
    Modified residuei323 – 3231PhosphoserineBy similarity

    Post-translational modificationi

    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-239.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP50552.
    PaxDbiP50552.
    PeptideAtlasiP50552.
    PRIDEiP50552.

    2D gel databases

    OGPiP50552.

    PTM databases

    PhosphoSiteiP50552.

    Expressioni

    Tissue specificityi

    Highly expressed in platelets.1 Publication

    Gene expression databases

    ArrayExpressiP50552.
    BgeeiP50552.
    CleanExiHS_VASP.
    GenevestigatoriP50552.

    Organism-specific databases

    HPAiCAB004612.
    HPA005724.

    Interactioni

    Subunit structurei

    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.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BAIAP2Q9UQB8-46EBI-748201,EBI-6174091
    NR4A1P227362EBI-748201,EBI-721550
    NSMAFQ926362EBI-748201,EBI-2947053
    RPS6KA1Q154184EBI-748201,EBI-963034
    VCLP120032EBI-748201,EBI-1039563From a different organism.
    XIRP1Q702N85EBI-748201,EBI-7851194

    Protein-protein interaction databases

    BioGridi113251. 52 interactions.
    DIPiDIP-44105N.
    IntActiP50552. 25 interactions.
    MINTiMINT-1437861.
    STRINGi9606.ENSP00000245932.

    Structurei

    Secondary structure

    1
    380
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 128
    Beta strandi14 – 163
    Turni18 – 203
    Beta strandi25 – 273
    Beta strandi34 – 418
    Turni42 – 454
    Beta strandi46 – 5510
    Beta strandi60 – 667
    Beta strandi79 – 868
    Beta strandi88 – 958
    Helixi96 – 11419
    Helixi226 – 2316
    Helixi341 – 37636

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP50552.
    SMRiP50552. Positions 1-115, 338-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50552.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 113112WH1PROSITE-ProRule annotationAdd
    BLAST
    Repeati344 – 358151Add
    BLAST
    Repeati359 – 373152Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni225 – 377153EVH2Add
    BLAST
    Regioni225 – 24521EVH2 block AAdd
    BLAST
    Regioni259 – 27820EVH2 block BAdd
    BLAST
    Regioni343 – 37735EVH2 block CAdd
    BLAST
    Regioni344 – 373302 X 15 AA tandem repeats of L-[EQ]-[KR]-[MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-EAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili337 – 37337Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi234 – 2374KLKR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi118 – 21699Pro-richAdd
    BLAST
    Compositional biasi215 – 2228Poly-Gly
    Compositional biasi259 – 2624Poly-Gly
    Compositional biasi322 – 3254Poly-Ser

    Domaini

    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.
    The WH1 domain mediates interaction with XIRP1.

    Sequence similaritiesi

    Belongs to the Ena/VASP family.Curated
    Contains 1 WH1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, SH3-binding

    Phylogenomic databases

    eggNOGiNOG265043.
    HOGENOMiHOG000013015.
    HOVERGENiHBG006655.
    InParanoidiP50552.
    KOiK06274.
    PhylomeDBiP50552.
    TreeFamiTF321411.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR017354. Vasodilator_phosphoprotein.
    IPR014885. VASP_tetra.
    IPR000697. WH1/EVH1.
    [Graphical view]
    PfamiPF08776. VASP_tetra. 1 hit.
    PF00568. WH1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
    SMARTiSM00461. WH1. 1 hit.
    [Graphical view]
    PROSITEiPS50229. WH1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P50552-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV    50
    GRKMQPDQQV VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA 100
    QFAAGMASAL EALEGGGPPP PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE 150
    HIERRVSNAG GPPAPPAGGP PPPPGPPPPP GPPPPPGLPP SGVPAAAHGA 200
    GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK QEEASGGPTA 250
    PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP 300
    AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSDLQRVKQE 350
    LLEEVKKELQ KVKEEIIEAF VQELRKRGSP 380
    Length:380
    Mass (Da):39,830
    Last modified:January 23, 2007 - v3
    Checksum:i17634B8134DEBF59
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21S → SS in AAH26019. (PubMed:15489334)Curated
    Sequence conflicti241 – 2411Missing in AAH26019. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti104 – 1041A → T.
    Corresponds to variant rs10415373 [ dbSNP | Ensembl ].
    VAR_048929
    Natural varianti140 – 1401Q → H.
    Corresponds to variant rs34345197 [ dbSNP | Ensembl ].
    VAR_048930

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS33051.1.
    PIRiS51797.
    RefSeqiNP_003361.1. NM_003370.3.
    UniGeneiHs.515469.

    Genome annotation databases

    EnsembliENST00000245932; ENSP00000245932; ENSG00000125753.
    GeneIDi7408.
    KEGGihsa:7408.
    UCSCiuc002pcg.3. human.

    Polymorphism databases

    DMDMi1718079.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS33051.1.
    PIRi S51797.
    RefSeqi NP_003361.1. NM_003370.3.
    UniGenei Hs.515469.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EGX NMR - A 1-115 [» ]
    1JNG model - A 1-115 [» ]
    1USD X-ray 1.70 A 336-380 [» ]
    1USE X-ray 1.30 A 336-380 [» ]
    2PAV X-ray 1.80 V 199-214 [» ]
    2PBD X-ray 1.50 V 203-245 [» ]
    3CHW X-ray 2.30 V 199-214 [» ]
    ProteinModelPortali P50552.
    SMRi P50552. Positions 1-115, 338-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113251. 52 interactions.
    DIPi DIP-44105N.
    IntActi P50552. 25 interactions.
    MINTi MINT-1437861.
    STRINGi 9606.ENSP00000245932.

    PTM databases

    PhosphoSitei P50552.

    Polymorphism databases

    DMDMi 1718079.

    2D gel databases

    OGPi P50552.

    Proteomic databases

    MaxQBi P50552.
    PaxDbi P50552.
    PeptideAtlasi P50552.
    PRIDEi P50552.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000245932 ; ENSP00000245932 ; ENSG00000125753 .
    GeneIDi 7408.
    KEGGi hsa:7408.
    UCSCi uc002pcg.3. human.

    Organism-specific databases

    CTDi 7408.
    GeneCardsi GC19P046010.
    HGNCi HGNC:12652. VASP.
    HPAi CAB004612.
    HPA005724.
    MIMi 601703. gene.
    neXtProti NX_P50552.
    PharmGKBi PA37276.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265043.
    HOGENOMi HOG000013015.
    HOVERGENi HBG006655.
    InParanoidi P50552.
    KOi K06274.
    PhylomeDBi P50552.
    TreeFami TF321411.

    Enzyme and pathway databases

    Reactomei REACT_12623. Generation of second messenger molecules.
    REACT_19351. Signaling by Robo receptor.
    REACT_20649. Cell-extracellular matrix interactions.

    Miscellaneous databases

    ChiTaRSi VASP. human.
    EvolutionaryTracei P50552.
    GeneWikii Vasodilator-stimulated_phosphoprotein.
    GenomeRNAii 7408.
    NextBioi 29004.
    PROi P50552.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50552.
    Bgeei P50552.
    CleanExi HS_VASP.
    Genevestigatori P50552.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR017354. Vasodilator_phosphoprotein.
    IPR014885. VASP_tetra.
    IPR000697. WH1/EVH1.
    [Graphical view ]
    Pfami PF08776. VASP_tetra. 1 hit.
    PF00568. WH1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038010. Vasodilator_Phospo. 1 hit.
    SMARTi SM00461. WH1. 1 hit.
    [Graphical view ]
    PROSITEi PS50229. WH1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    23. 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. 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. 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.

    Entry informationi

    Entry nameiVASP_HUMAN
    AccessioniPrimary (citable) accession number: P50552
    Secondary accession number(s): B2RBT9, Q6PIZ1, Q93035
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3