Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P50552 (VASP_HUMAN)

Entry version 192 (18 Sep 2019)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Vasodilator-stimulated phosphoprotein

Gene

VASP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.5 Publications

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.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-202433 Generation of second messenger molecules
R-HSA-376176 Signaling by ROBO receptors
R-HSA-446353 Cell-extracellular matrix interactions

SIGNOR Signaling Network Open Resource

More...SIGNORi		P50552

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P50552 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Vasodilator-stimulated phosphoprotein
Short name:
VASP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:VASP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:12652 VASP

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601703 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P50552

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi157S → 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 Publication1
Mutagenesisi239S → 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 Publication1
Mutagenesisi278T → A: Promotes F-actin assembly; when associated with A-157 and A-239. 1 Publication1
Mutagenesisi278T → E: Interferes with F-actin assembly; when associated with A-157 and A-239. 1 Publication1
Mutagenesisi370F → A: Lower stability of tetramerization domain. 1 Publication1
Mutagenesisi370F → I or K: No change in stability of tetramerization domain. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		7408

Open Targets

More...OpenTargetsi		ENSG00000125753

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA37276

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		VASP

Domain mapping of disease mutations (DMDM)

More...DMDMi		1718079

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000657672 – 380Vasodilator-stimulated phosphoproteinAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei39PhosphotyrosineCombined sources1
Modified residuei46PhosphoserineCombined sources1
Modified residuei157Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK14 Publications1
Modified residuei239Phosphoserine; by PKA and PKG/PRKG1Combined sources2 Publications1
Modified residuei278Phosphothreonine; by PKA, PKG/PRKG1 and AMPK2 Publications1
Modified residuei283N6-acetyllysineCombined sources1
Modified residuei284PhosphothreonineCombined sources1
Modified residuei305PhosphoserineCombined sources1
Modified residuei314PhosphoserineCombined sources1
Modified residuei316PhosphothreonineCombined sources1
Modified residuei322Phosphoserine; by AMPKCombined sources1
Modified residuei323PhosphoserineBy similarity1
Modified residuei325PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		P50552

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P50552

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P50552

MaxQB - The MaxQuant DataBase

More...MaxQBi		P50552

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P50552

PeptideAtlas

More...PeptideAtlasi		P50552

PRoteomics IDEntifications database

More...PRIDEi		P50552

ProteomicsDB human proteome resource

More...ProteomicsDBi		56248

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P50552

2D gel databases

USC-OGP 2-DE database

More...OGPi		P50552

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P50552

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P50552

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in platelets.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000125753 Expressed in 209 organ(s), highest expression level in blood

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P50552 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P50552 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004612
HPA005724

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113251, 97 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P50552

Database of interacting proteins

More...DIPi		DIP-44105N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P50552

Protein interaction database and analysis system

More...IntActi		P50552, 52 interactors

Molecular INTeraction database

More...MINTi		P50552

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000245932

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P50552

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P50552

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 113WH1PROSITE-ProRule annotationAdd BLAST112
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati344 – 3581Add BLAST15
Repeati359 – 3732Add BLAST15

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni225 – 377EVH2Add BLAST153
Regioni225 – 245EVH2 block AAdd BLAST21
Regioni259 – 278EVH2 block BAdd BLAST20
Regioni343 – 377EVH2 block CAdd BLAST35
Regioni344 – 3732 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
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili337 – 373Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi234 – 237KLKR4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi118 – 216Pro-richAdd BLAST99
Compositional biasi215 – 222Poly-Gly8
Compositional biasi259 – 262Poly-Gly4
Compositional biasi322 – 325Poly-Ser4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the Ena/VASP family.Curated

Keywords - Domaini

Coiled coil, Repeat, SH3-binding

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4590 Eukaryota
ENOG41101TS LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156765

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000013015

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P50552

KEGG Orthology (KO)

More...KOi		K06274

Identification of Orthologs from Complete Genome Data

More...OMAi		PGPSEHI

Database of Orthologous Groups

More...OrthoDBi		263288at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P50552

TreeFam database of animal gene trees

More...TreeFami		TF321411

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.5.1160, 1 hit
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR042180 IF_rod_dom_coil1B
IPR011993 PH-like_dom_sf
IPR034367 VASP
IPR017354 VASP/EVL
IPR038023 VASP_sf
IPR014885 VASP_tetra
IPR000697 WH1/EVH1_dom

The PANTHER Classification System

More...PANTHERi		PTHR11202:SF12 PTHR11202:SF12, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08776 VASP_tetra, 1 hit
PF00568 WH1, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF038010 Vasodilator_Phospo, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00461 WH1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF118370 SSF118370, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50229 WH1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

P50552-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV 
        60         70         80         90        100
GRKMQPDQQV VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA 
       110        120        130        140        150
QFAAGMASAL EALEGGGPPP PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE 
       160        170        180        190        200
HIERRVSNAG GPPAPPAGGP PPPPGPPPPP GPPPPPGLPP SGVPAAAHGA 
       210        220        230        240        250
GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK QEEASGGPTA 
       260        270        280        290        300
PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP 
       310        320        330        340        350
AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSDLQRVKQE 
       360        370        380
LLEEVKKELQ KVKEEIIEAF VQELRKRGSP
Length:380
Mass (Da):39,830
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i17634B8134DEBF59
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EM16K7EM16_HUMAN
Vasodilator-stimulated phosphoprote...
VASP
183Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ENL7K7ENL7_HUMAN
Vasodilator-stimulated phosphoprote...
VASP
103Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ENR7K7ENR7_HUMAN
Vasodilator-stimulated phosphoprote...
VASP
59Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EIG8K7EIG8_HUMAN
Vasodilator-stimulated phosphoprote...
VASP
46Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EQD0K7EQD0_HUMAN
Vasodilator-stimulated phosphoprote...
VASP
35Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2S → SS in AAH26019 (PubMed:15489334).Curated1
Sequence conflicti241Missing in AAH26019 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_048929104A → T. Corresponds to variant dbSNP:rs10415373Ensembl.1
Natural variantiVAR_048930140Q → H. Corresponds to variant dbSNP:rs34345197Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33051.1

Protein sequence database of the Protein Information Resource

More...PIRi		S51797

NCBI Reference Sequences

More...RefSeqi		NP_003361.1, NM_003370.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000245932; ENSP00000245932; ENSG00000125753

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7408

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7408

UCSC genome browser

More...UCSCi		uc002pcg.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
SMRiP50552
ModBaseiSearch...

Protein-protein interaction databases

BioGridi113251, 97 interactors
CORUMiP50552
DIPiDIP-44105N
ELMiP50552
IntActiP50552, 52 interactors
MINTiP50552
STRINGi9606.ENSP00000245932

Protein family/group databases

MoonDBiP50552 Predicted

PTM databases

iPTMnetiP50552
PhosphoSitePlusiP50552

Polymorphism and mutation databases

BioMutaiVASP
DMDMi1718079

2D gel databases

OGPiP50552

Proteomic databases

EPDiP50552
jPOSTiP50552
MassIVEiP50552
MaxQBiP50552
PaxDbiP50552
PeptideAtlasiP50552
PRIDEiP50552
ProteomicsDBi56248
TopDownProteomicsiP50552

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245932; ENSP00000245932; ENSG00000125753
GeneIDi7408
KEGGihsa:7408
UCSCiuc002pcg.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7408
DisGeNETi7408

GeneCards: human genes, protein and diseases

More...GeneCardsi		VASP
HGNCiHGNC:12652 VASP
HPAiCAB004612
HPA005724
MIMi601703 gene
neXtProtiNX_P50552
OpenTargetsiENSG00000125753
PharmGKBiPA37276

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4590 Eukaryota
ENOG41101TS LUCA
GeneTreeiENSGT00940000156765
HOGENOMiHOG000013015
InParanoidiP50552
KOiK06274
OMAiPGPSEHI
OrthoDBi263288at2759
PhylomeDBiP50552
TreeFamiTF321411

Enzyme and pathway databases

ReactomeiR-HSA-202433 Generation of second messenger molecules
R-HSA-376176 Signaling by ROBO receptors
R-HSA-446353 Cell-extracellular matrix interactions
SIGNORiP50552

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		VASP human
EvolutionaryTraceiP50552

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Vasodilator-stimulated_phosphoprotein

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		7408

Pharos

More...Pharosi		P50552

Protein Ontology

More...PROi		PR:P50552

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000125753 Expressed in 209 organ(s), highest expression level in blood
ExpressionAtlasiP50552 baseline and differential
GenevisibleiP50552 HS

Family and domain databases

Gene3Di1.20.5.1160, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR042180 IF_rod_dom_coil1B
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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVASP_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P50552
Secondary accession number(s): B2RBT9, Q6PIZ1, Q93035
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 18, 2019
This is version 192 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again