Vasodilator-stimulated phosphoprotein (VASP)

The protein contains 380 amino acids for an estimated molecular weight of 39830 Da.

 

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. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 100%
Model score: 0

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VariantDescription
dbSNP:rs10415373
dbSNP:rs34345197

The reference OMIM entry for this protein is 601703

Vasodilator-stimulated phosphoprotein; vasp

DESCRIPTION

Human platelet activation is inhibited by agents such as prostaglandins and NO donors, which elevate cAMP or cGMP levels. The vasodilator-stimulated phosphoprotein (VASP) is phosphorylated in human platelets in response to both cAMP- and cGMP-elevating agents, and its phosphorylation correlates with platelet inhibition (summary by Haffner et al., 1995).

CLONING

Haffner et al. (1995) cloned the VASP gene from human and canine cells and showed that VASP is a 380-amino acid protein with a predicted molecular mass of 39.8 kD. Zimmer et al. (1996) cloned human and mouse VASP from genomic cosmid libraries. They determined that the human and mouse VASP genes are 89% identical at the amino acid level.

GENE FUNCTION

Brindle et al. (1996) showed that VASP binds to the proline-rich domain of vinculin (193065). They suggested that this interaction is important for actin-filament assembly and focal adhesion stability. Kanchanawong et al. (2010) used 3-dimensional super-resolution fluorescence microscopy to map nanoscale protein organization in focal adhesions. Their results revealed that integrins and actin are vertically separated by an approximately 40-nm focal adhesion core region consisting of multiple protein-specific strata: a membrane-apposed integrin signaling layer containing integrin cytoplasmic tails (see 193210), focal adhesion kinase (600758), and paxillin (602505); an intermediate force-transduction layer containing talin (186745) and vinculin; and an uppermost actin-regulatory layer containing zyxin (602002), VASP, and alpha-actinin (102575). By localizing amino- and carboxy-terminally tagged talins, Kanchanawong et al. (2010) revealed talin's polarized orientation, indicative of a role in organizing the focal adhesion strata. Kanchanawong et al. (2010) concluded that their composite multilaminar protein architecture provided a molecular blueprint for understanding focal adhesion functions.

GENE STRUCTURE

Zimmer et al. (1996) determined that human and mouse VASP consist of 13 exons and span a genomic DNA region of approximately 20 kb.

MAPPING

Zimmer et al. (1996) mapped human VASP to chromosome 19q13.2-q13.3 using fluorescence in situ hybridization. They noted that VASP is located about 92 kb distal to ERCC1 (126380) and about 300 kb proximal to the myotonic dystrophy protein kinase gene (160900). ... More on the omim web site

Subscribe to this protein entry history

May 13, 2019: Protein entry updated
Automatic update: model status changed

Nov. 17, 2018: Protein entry updated
Automatic update: model status changed

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Oct. 27, 2017: Protein entry updated
Automatic update: model status changed

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 601703 was added.

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed