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P70460

- VASP_MOUSE

UniProt

P70460 - VASP_MOUSE

Protein

Vasodilator-stimulated phosphoprotein

Gene

Vasp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 4 (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 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. actin cytoskeleton organization Source: MGI
    2. actin polymerization or depolymerization Source: InterPro
    3. axon guidance Source: MGI
    4. neural tube closure Source: MGI
    5. protein homotetramerization Source: InterPro

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_221567. Signaling by Robo receptor.
    REACT_225768. Generation of second messenger molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vasodilator-stimulated phosphoprotein
    Short name:
    VASP
    Gene namesi
    Name:Vasp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:109268. Vasp.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cell junctionfocal adhesion 1 Publication. Cell junctiontight junction By similarity. Cell projectionlamellipodium membrane 1 Publication. Cell projectionfilopodium membrane 1 Publication
    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 By similarity. In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) By similarity.By similarity

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. filopodium Source: MGI
    4. filopodium membrane Source: UniProtKB-SubCell
    5. focal adhesion Source: MGI
    6. lamellipodium Source: MGI
    7. lamellipodium membrane Source: UniProtKB-SubCell
    8. 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
    Mutagenesisi153 – 1531S → D: Reduces actin polymerization to a lesser extent than wild-type. Greater effect on actin polymerization; when associated with D-235 and E-274. 2 Publications
    Mutagenesisi232 – 2332RK → GE or EE: Reduced binding to monomeric actin. No VASP-induced actin polymerization. 1 Publication
    Mutagenesisi235 – 2351S → D: Reduces actin polymerization to a lesser extent than wild-type. 2 Publications
    Mutagenesisi274 – 2741T → E: Reduces actin polymerization to a lesser extent than wild-type. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 375374Vasodilator-stimulated phosphoproteinPRO_0000065768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei39 – 391PhosphotyrosineBy similarity
    Modified residuei153 – 1531Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK11 Publication
    Modified residuei235 – 2351Phosphoserine; by PKA and PKG1 Publication
    Modified residuei274 – 2741Phosphothreonine; by PKA, PKG/PRKG1 and AMPKBy similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity
    Modified residuei311 – 3111PhosphothreonineBy similarity
    Modified residuei317 – 3171PhosphoserineBy similarity
    Modified residuei318 – 3181Phosphoserine; by AMPK1 Publication

    Post-translational modificationi

    Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-153, the preferred site for PKG, Ser-235. In ADP-activated platelets, phosphorylation by PKA or PKG/PRKG1 on Ser-153 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-274 requires prior phosphorylation on Ser-153 and Ser-235. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-274 by AMPK does not require prior phosphorylation at Ser-153 or Ser-235. Phosphorylation at Ser-153 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-318 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-153, while nitric oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-235.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP70460.
    PaxDbiP70460.
    PRIDEiP70460.

    PTM databases

    PhosphoSiteiP70460.

    Expressioni

    Tissue specificityi

    Highly expressed in thymus and spleen. Lower levels in lung, ovary, placenta and fat.1 Publication

    Developmental stagei

    Expressed constantly throughout brain development, with lower levels in adulthood.1 Publication

    Gene expression databases

    BgeeiP70460.
    CleanExiMM_VASP.
    GenevestigatoriP70460.

    Interactioni

    Subunit structurei

    Homotetramer By similarity. 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. Interacts weakly with MEFV By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204499. 2 interactions.
    IntActiP70460. 3 interactions.
    MINTiMINT-1215713.

    Structurei

    3D structure databases

    ProteinModelPortaliP70460.
    SMRiP70460. Positions 1-115, 333-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 113112WH1PROSITE-ProRule annotationAdd
    BLAST
    Repeati340 – 354151Add
    BLAST
    Repeati355 – 369152Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 373153EVH2Add
    BLAST
    Regioni221 – 24121EVH2 block AAdd
    BLAST
    Regioni257 – 27418EVH2 block BAdd
    BLAST
    Regioni338 – 37235EVH2 block CAdd
    BLAST
    Regioni339 – 368302 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 – 36731Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi230 – 2334KLKR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi166 – 18217Poly-ProAdd
    BLAST
    Compositional biasi317 – 3204Poly-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.By similarity

    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.
    GeneTreeiENSGT00730000110272.
    HOVERGENiHBG006655.
    InParanoidiP70460.
    KOiK06274.
    OMAiQPEHMER.
    OrthoDBiEOG72JWGQ.
    PhylomeDBiP70460.
    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.

    P70460-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSETVICSSR ATVMLYDDSN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV    50
    GRKMQPDQQV VINCAIIRGV KYNQATPIFH QWRDARQVWG LNFGSKEDAI 100
    QFATGMANAL EALEGGGPPP APAPPAWSAQ NGPSPEELEQ QKRQPEHMER 150
    RVSNAGGPPA PPAGGPPPPP GPPPPPGPPP PPGLPSSGVS GAGHGAGAAP 200
    PPAPPLPTAQ GPNSGGSGAP GLAAAIAGAK LRKVSKQEEA SGGPLAPKAE 250
    NSRSTGGGLM EEMNAMLARR RKATQVGEKP PKDESASEES EARLPAQSEP 300
    VRRPWEKNST TLPRMKSSSS VTTSEAHPST PCSSDDSDLE RVKQELLEEV 350
    RKELQKMKEE IIEVFVQELR KRGSP 375
    Length:375
    Mass (Da):39,667
    Last modified:January 23, 2007 - v4
    Checksum:i19369286CF4276C7
    GO

    Sequence cautioni

    The sequence CAA67108.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 11510Missing in BAE42025. (PubMed:16141072)Curated
    Sequence conflicti237 – 2371Missing in BAE33933. (PubMed:16141072)Curated
    Sequence conflicti337 – 3371S → Y in BAE29310. (PubMed:16141072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti209 – 2091A → T.2 Publications

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98475 Genomic DNA. Translation: CAA67108.1. Sequence problems.
    AF084548 mRNA. Translation: AAD16045.1.
    AK140329 mRNA. Translation: BAE24338.1.
    AK150103 mRNA. Translation: BAE29310.1.
    AK157021 mRNA. Translation: BAE33933.1.
    AK170780 mRNA. Translation: BAE42025.1.
    AK171715 mRNA. Translation: BAE42628.1.
    BC010223 mRNA. Translation: AAH10223.1.
    BC015289 mRNA. Translation: AAH15289.1.
    CCDSiCCDS52056.1.
    RefSeqiNP_001268950.1. NM_001282021.1.
    NP_001268951.1. NM_001282022.1.
    NP_033525.2. NM_009499.3.
    UniGeneiMm.9684.

    Genome annotation databases

    EnsembliENSMUST00000032561; ENSMUSP00000032561; ENSMUSG00000030403.
    GeneIDi22323.
    KEGGimmu:22323.
    UCSCiuc009fle.2. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98475 Genomic DNA. Translation: CAA67108.1 . Sequence problems.
    AF084548 mRNA. Translation: AAD16045.1 .
    AK140329 mRNA. Translation: BAE24338.1 .
    AK150103 mRNA. Translation: BAE29310.1 .
    AK157021 mRNA. Translation: BAE33933.1 .
    AK170780 mRNA. Translation: BAE42025.1 .
    AK171715 mRNA. Translation: BAE42628.1 .
    BC010223 mRNA. Translation: AAH10223.1 .
    BC015289 mRNA. Translation: AAH15289.1 .
    CCDSi CCDS52056.1.
    RefSeqi NP_001268950.1. NM_001282021.1.
    NP_001268951.1. NM_001282022.1.
    NP_033525.2. NM_009499.3.
    UniGenei Mm.9684.

    3D structure databases

    ProteinModelPortali P70460.
    SMRi P70460. Positions 1-115, 333-372.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204499. 2 interactions.
    IntActi P70460. 3 interactions.
    MINTi MINT-1215713.

    PTM databases

    PhosphoSitei P70460.

    Proteomic databases

    MaxQBi P70460.
    PaxDbi P70460.
    PRIDEi P70460.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032561 ; ENSMUSP00000032561 ; ENSMUSG00000030403 .
    GeneIDi 22323.
    KEGGi mmu:22323.
    UCSCi uc009fle.2. mouse.

    Organism-specific databases

    CTDi 7408.
    MGIi MGI:109268. Vasp.

    Phylogenomic databases

    eggNOGi NOG265043.
    GeneTreei ENSGT00730000110272.
    HOVERGENi HBG006655.
    InParanoidi P70460.
    KOi K06274.
    OMAi QPEHMER.
    OrthoDBi EOG72JWGQ.
    PhylomeDBi P70460.
    TreeFami TF321411.

    Enzyme and pathway databases

    Reactomei REACT_221567. Signaling by Robo receptor.
    REACT_225768. Generation of second messenger molecules.

    Miscellaneous databases

    ChiTaRSi VASP. mouse.
    NextBioi 302545.
    PROi P70460.
    SOURCEi Search...

    Gene expression databases

    Bgeei P70460.
    CleanExi MM_VASP.
    Genevestigatori P70460.

    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. "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], VARIANT THR-209.
      Strain: 129.
    2. "Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their regulation of cyclic AMP response element-dependent gene transcription."
      Collins S.P., Uhler M.D.
      J. Biol. Chem. 274:8391-8404(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION.
      Strain: C57BL/6J.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-209.
      Strain: C57BL/6J and NOD.
      Tissue: Adipose tissue, Bone marrow, Dendritic cell and Spleen.
    4. "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].
      Strain: FVB/N.
      Tissue: Kidney and Mammary tumor.
    5. Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    6. "Directed actin polymerization is the driving force for epithelial cell-cell adhesion."
      Vasioukhin V., Bauer C., Yin M., Fuchs E.
      Cell 100:209-219(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin."
      Harbeck B., Huttelmaier S., Schlueter K., Jockusch B.M., Illenberger S.
      J. Biol. Chem. 275:30817-30825(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACTN1; PFN1; PFN2; VCL AND ZYX, PHOSPHORYLATION AT SER-153 AND SER-235, MUTAGENESIS OF SER-153; SER-235 AND THR-274.
    8. "The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin."
      Walders-Harbeck B., Khaitlina S.Y., Hinssen H., Jockusch B.M., Illenberger S.
      FEBS Lett. 529:275-280(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACTG1, PHOSPHORYLATION, MUTAGENESIS OF 232-ARG-LYS-233.
    9. "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton."
      Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H., Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.
      J. Biol. Chem. 278:49031-49043(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNMBP.
    10. "PREL1 provides a link from Ras signalling to the actin cytoskeleton via Ena/VASP proteins."
      Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.
      FEBS Lett. 579:455-463(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APBB1IP.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Phosphorylation of VASP by AMPK alters actin binding and occurs at a novel site."
      Thomson D.M., Ascione M.P., Grange J., Nelson C., Hansen M.D.
      Biochem. Biophys. Res. Commun. 414:215-219(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-318.

    Entry informationi

    Entry nameiVASP_MOUSE
    AccessioniPrimary (citable) accession number: P70460
    Secondary accession number(s): Q3TAP0
    , Q3TCD2, Q3U0C2, Q3UDF1, Q91VD2, Q9R214
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 123 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3