VASP

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]

Description

Vasodilator stimulated phosphoprotein

Tissue specificity

Low tissue specificity

Subcell location

Plasma membrane, Cell Junctions, Focal adhesion sites

Predicted location

Intracellular

Protein family

Mapped to neXtProt
Mapped to UniProt SWISS-PROT
Plasma proteins
Predicted intracellular proteins
Protein evidence (Ezkurdia et al 2014)
Protein evidence (Kim et al 2014)

Chromosome

19 (45506579 - 45526983)

Ensembl ID

ENSG00000125753  (ver. 103.38)

Orthologs

Mouse Vasp: ENSMUSG00000030403

UniProt

P50552

neXtProt

NX_P50552

Human splice variants
Mouse splice variants

Protein structure