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P50552

- VASP_HUMAN

UniProt

P50552 - VASP_HUMAN

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Protein

Vasodilator-stimulated phosphoprotein

Gene
VASP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.6 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
Complete GO annotation...

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).4 Publications

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
Complete GO annotation...

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 – 11Removed1 Publication
Chaini2 – 380379Vasodilator-stimulated phosphoproteinPRO_0000065767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei39 – 391Phosphotyrosine1 Publication
Modified residuei157 – 1571Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK14 Publications
Modified residuei239 – 2391Phosphoserine; by PKA and PKG/PRKG12 Publications
Modified residuei278 – 2781Phosphothreonine; by PKA, PKG/PRKG1 and AMPK2 Publications
Modified residuei283 – 2831N6-acetyllysine1 Publication
Modified residuei316 – 3161Phosphothreonine2 Publications
Modified residuei322 – 3221Phosphoserine; by AMPK1 Publication
Modified residuei323 – 3231Phosphoserine By 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-239.6 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.9 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.

Protein-protein interaction databases

BioGridi113251. 52 interactions.
DIPiDIP-44105N.
IntActiP50552. 23 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.

Miscellaneous databases

EvolutionaryTraceiP50552.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 113112WH1Add
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 – 37337 Reviewed predictionAdd
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.1 Publication
The WH1 domain mediates interaction with XIRP1.1 Publication

Sequence similaritiesi

Belongs to the Ena/VASP family.
Contains 1 WH1 domain.

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

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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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → SS in AAH26019. 1 Publication
Sequence conflicti241 – 2411Missing in AAH26019. 1 Publication

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. 23 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 146 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

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