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UniProtKB - P70460 (VASP_MOUSE)

Protein

Vasodilator-stimulated phosphoprotein

Gene

Vasp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity1 Publication

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

ReactomeiR-MMU-376176 Signaling by ROBO receptors
R-MMU-446353 Cell-extracellular matrix interactions

Names & Taxonomyi

Protein namesi
Recommended name:
Vasodilator-stimulated phosphoprotein
Short name:
VASP
Gene namesi
Name:Vasp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:109268 Vasp

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi153S → D: Reduces actin polymerization to a lesser extent than wild-type. Greater effect on actin polymerization; when associated with D-235 and E-274. 1 Publication1
Mutagenesisi232 – 233RK → GE or EE: Reduced binding to monomeric actin. No VASP-induced actin polymerization. 1 Publication2
Mutagenesisi235S → D: Reduces actin polymerization to a lesser extent than wild-type. 1 Publication1
Mutagenesisi274T → E: Reduces actin polymerization to a lesser extent than wild-type. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000657682 – 375Vasodilator-stimulated phosphoproteinAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei39PhosphotyrosineBy similarity1
Modified residuei46PhosphoserineBy similarity1
Modified residuei153Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK11 Publication1
Modified residuei235Phosphoserine; by PKA and PKGCombined sources1 Publication1
Modified residuei274Phosphothreonine; by PKA, PKG/PRKG1 and AMPKBy similarity1
Modified residuei279N6-acetyllysineBy similarity1
Modified residuei309PhosphoserineBy similarity1
Modified residuei311PhosphothreonineBy similarity1
Modified residuei317PhosphoserineCombined sources1
Modified residuei318Phosphoserine; by AMPK1 Publication1
Modified residuei320PhosphoserineCombined sources1

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

EPDiP70460
MaxQBiP70460
PaxDbiP70460
PeptideAtlasiP70460
PRIDEiP70460

PTM databases

iPTMnetiP70460
PhosphoSitePlusiP70460
SwissPalmiP70460

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

BgeeiENSMUSG00000030403 Expressed in 272 organ(s), highest expression level in intestine
CleanExiMM_VASP
GenevisibleiP70460 MM

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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi204499, 4 interactors
DIPiDIP-29360N
IntActiP70460, 5 interactors
MINTiP70460
STRINGi10090.ENSMUSP00000032561

Structurei

3D structure databases

ProteinModelPortaliP70460
SMRiP70460
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 113WH1PROSITE-ProRule annotationAdd BLAST112
Repeati340 – 3541Add BLAST15
Repeati355 – 3692Add BLAST15

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni221 – 373EVH2Add BLAST153
Regioni221 – 241EVH2 block AAdd BLAST21
Regioni257 – 274EVH2 block BAdd BLAST18
Regioni338 – 372EVH2 block CAdd BLAST35
Regioni339 – 3682 X 15 AA tandem repeats of L-[EQ]-[KR] [MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-EAdd BLAST30

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili337 – 367Sequence analysisAdd BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi230 – 233KLKR4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi166 – 182Poly-ProAdd BLAST17
Compositional biasi317 – 320Poly-Ser4

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

Keywords - Domaini

Coiled coil, Repeat, SH3-binding

Phylogenomic databases

eggNOGiKOG4590 Eukaryota
ENOG41101TS LUCA
GeneTreeiENSGT00730000110272
HOVERGENiHBG006655
InParanoidiP70460
KOiK06274
OMAiMSETVIC
OrthoDBiEOG091G0QTE
PhylomeDBiP70460
TreeFamiTF321411

Family and domain databases

Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR011993 PH-like_dom_sf
IPR034367 VASP
IPR017354 VASP/EVL
IPR038023 VASP_sf
IPR014885 VASP_tetra
IPR000697 WH1/EVH1_dom
PANTHERiPTHR11202:SF12 PTHR11202:SF12, 1 hit
PfamiView protein in Pfam
PF08776 VASP_tetra, 1 hit
PF00568 WH1, 1 hit
PIRSFiPIRSF038010 Vasodilator_Phospo, 1 hit
SMARTiView protein in SMART
SM00461 WH1, 1 hit
SUPFAMiSSF118370 SSF118370, 1 hit
PROSITEiView protein in PROSITE
PS50229 WH1, 1 hit

Sequencei

Sequence statusi: Complete.

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

P70460-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSETVICSSR ATVMLYDDSN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV 
        60         70         80         90        100
GRKMQPDQQV VINCAIIRGV KYNQATPIFH QWRDARQVWG LNFGSKEDAI 
       110        120        130        140        150
QFATGMANAL EALEGGGPPP APAPPAWSAQ NGPSPEELEQ QKRQPEHMER 
       160        170        180        190        200
RVSNAGGPPA PPAGGPPPPP GPPPPPGPPP PPGLPSSGVS GAGHGAGAAP 
       210        220        230        240        250
PPAPPLPTAQ GPNSGGSGAP GLAAAIAGAK LRKVSKQEEA SGGPLAPKAE 
       260        270        280        290        300
NSRSTGGGLM EEMNAMLARR RKATQVGEKP PKDESASEES EARLPAQSEP 
       310        320        330        340        350
VRRPWEKNST TLPRMKSSSS VTTSEAHPST PCSSDDSDLE RVKQELLEEV 
       360        370 
RKELQKMKEE IIEVFVQELR KRGSP
Length:375
Mass (Da):39,667
Last modified:January 23, 2007 - v4
Checksum:i19369286CF4276C7
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti106 – 115Missing in BAE42025 (PubMed:16141072).Curated10
Sequence conflicti237Missing in BAE33933 (PubMed:16141072).Curated1
Sequence conflicti337S → Y in BAE29310 (PubMed:16141072).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti209A → T2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V8CX-ray1.98C165-184[»]
ProteinModelPortaliP70460
SMRiP70460
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204499, 4 interactors
DIPiDIP-29360N
IntActiP70460, 5 interactors
MINTiP70460
STRINGi10090.ENSMUSP00000032561

PTM databases

iPTMnetiP70460
PhosphoSitePlusiP70460
SwissPalmiP70460

Proteomic databases

EPDiP70460
MaxQBiP70460
PaxDbiP70460
PeptideAtlasiP70460
PRIDEiP70460

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7408
MGIiMGI:109268 Vasp

Phylogenomic databases

eggNOGiKOG4590 Eukaryota
ENOG41101TS LUCA
GeneTreeiENSGT00730000110272
HOVERGENiHBG006655
InParanoidiP70460
KOiK06274
OMAiMSETVIC
OrthoDBiEOG091G0QTE
PhylomeDBiP70460
TreeFamiTF321411

Enzyme and pathway databases

ReactomeiR-MMU-376176 Signaling by ROBO receptors
R-MMU-446353 Cell-extracellular matrix interactions

Miscellaneous databases

PROiPR:P70460
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030403 Expressed in 272 organ(s), highest expression level in intestine
CleanExiMM_VASP
GenevisibleiP70460 MM

Family and domain databases

Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR011993 PH-like_dom_sf
IPR034367 VASP
IPR017354 VASP/EVL
IPR038023 VASP_sf
IPR014885 VASP_tetra
IPR000697 WH1/EVH1_dom
PANTHERiPTHR11202:SF12 PTHR11202:SF12, 1 hit
PfamiView protein in Pfam
PF08776 VASP_tetra, 1 hit
PF00568 WH1, 1 hit
PIRSFiPIRSF038010 Vasodilator_Phospo, 1 hit
SMARTiView protein in SMART
SM00461 WH1, 1 hit
SUPFAMiSSF118370 SSF118370, 1 hit
PROSITEiView protein in PROSITE
PS50229 WH1, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiVASP_MOUSE
AccessioniPrimary (citable) accession number: P70460
Secondary accession number(s): Q3TAP0
, Q3TCD2, Q3U0C2, Q3UDF1, Q91VD2, Q9R214
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 158 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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