|Institutional Source||Beutler Lab|
|Gene Name||vasodilator-stimulated phosphoprotein|
|Essential gene?||Possibly non essential (E-score: 0.413)|
|Stock #||R9264 (G1)|
|Chromosomal Location||19256929-19271817 bp(-) (GRCm38)|
|Type of Mutation||missense|
|DNA Base Change (assembly)||C to T at 19259451 bp (GRCm38)|
|Amino Acid Change||Valine to Isoleucine at position 276 (V276I)|
|Ref Sequence||ENSEMBL: ENSMUSP00000032561 (fasta)|
|Gene Model||predicted gene model for transcript(s): [ENSMUST00000032561] [ENSMUST00000161711]|
AA Change: V276I
AA Change: V276I
|Meta Mutation Damage Score||0.0579|
|Coding Region Coverage||
|Validation Efficiency||100% (58/58)|
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG. [provided by RefSeq, Jul 2008]
PHENOTYPE: Homozygous null mutants exhibit hyperplasia of megakaryocytes, and mutant platelets activated by thrombin display two-fold higher surface expression of P-selectin and fibrinogen binding. [provided by MGI curators]
|Allele List at MGI|
|Other mutations in this stock||
|Other mutations in Vasp||
(F):5'- GTTGGCGGTAAATACAAGTATCAT -3'
(R):5'- TGTAATACATTCTGTCCCATGTTGT -3'
(F):5'- GTATCATAAACTACCCTTTCTATGCC -3'
(R):5'- TAAGCTGCAGGACTCAGTTC -3'