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UniProtKB - P70460 (VASP_MOUSE)

Entry version 174 (02 Jun 2021)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
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Protein

Vasodilator-stimulated phosphoprotein

Gene

Vasp

Organism
Mus musculus (Mouse)
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 (By similarity).

By similarity1 Publication

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

<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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:109268, Vasp

<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

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%5Fand%5Fbiotech%5Fsection">'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>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

<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%5Fprocessing%5Fsection">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 methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000657682 – 375Vasodilator-stimulated phosphoproteinAdd BLAST374

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-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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-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

Encyclopedia of Proteome Dynamics

More...EPDi		P70460

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P70460

MaxQB - The MaxQuant DataBase

More...MaxQBi		P70460

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

More...PaxDbi		P70460

PeptideAtlas

More...PeptideAtlasi		P70460

PRoteomics IDEntifications database

More...PRIDEi		P70460

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		300166

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P70460

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

More...PhosphoSitePlusi		P70460

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P70460

<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 thymus and spleen. Lower levels in lung, ovary, placenta and fat.1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed constantly throughout brain development, with lower levels in adulthood.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000030403, Expressed in granulocyte and 298 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P70460, MM

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		204499, 6 interactors

Database of interacting proteins

More...DIPi		DIP-29360N

Protein interaction database and analysis system

More...IntActi		P70460, 5 interactors

Molecular INTeraction database

More...MINTi		P70460

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000032561

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P70460, protein

<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

3D structure databases

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

More...SMRi		P70460

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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%5Fand%5Fdomains%5Fsection">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>Repeati340 – 3541Add BLAST15
Repeati355 – 3692Add 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>Regioni111 – 340DisorderedSequence analysisAdd BLAST230
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
<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 – 367Sequence analysisAdd BLAST31

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>Motifi230 – 233KLKR4

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi159 – 186Pro residuesSequence analysisAdd BLAST28
Compositional biasi265 – 290Basic and acidic residuesSequence analysisAdd BLAST26
Compositional biasi310 – 333Polar residuesSequence analysisAdd BLAST24

<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.By similarity

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156765

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_017790_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P70460

Identification of Orthologs from Complete Genome Data

More...OMAi		IRGVKYN

Database of Orthologous Groups

More...OrthoDBi		972128at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P70460

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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

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
<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:i19369286CF4276C7
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

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 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
<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 varianti209A → T2 Publications1

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
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS52056.1

NCBI Reference Sequences

More...RefSeqi		NP_001268950.1, NM_001282021.1
NP_001268951.1, NM_001282022.1
NP_033525.2, NM_009499.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000032561; ENSMUSP00000032561; ENSMUSG00000030403

Database of genes from NCBI RefSeq genomes

More...GeneIDi		22323

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:22323

UCSC genome browser

More...UCSCi		uc009fle.2, mouse

<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
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

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
2V8CX-ray1.98C165-184[»]
SMRiP70460
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi204499, 6 interactors
DIPiDIP-29360N
IntActiP70460, 5 interactors
MINTiP70460
STRINGi10090.ENSMUSP00000032561

PTM databases

iPTMnetiP70460
PhosphoSitePlusiP70460
SwissPalmiP70460

Proteomic databases

EPDiP70460
jPOSTiP70460
MaxQBiP70460
PaxDbiP70460
PeptideAtlasiP70460
PRIDEiP70460
ProteomicsDBi300166

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1491, 1089 antibodies

The DNASU plasmid repository

More...DNASUi		22323

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7408
MGIiMGI:109268, Vasp

Phylogenomic databases

eggNOGiKOG4590, Eukaryota
GeneTreeiENSGT00940000156765
HOGENOMiCLU_017790_0_0_1
InParanoidiP70460
OMAiIRGVKYN
OrthoDBi972128at2759
PhylomeDBiP70460
TreeFamiTF321411

Enzyme and pathway databases

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

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		22323, 1 hit in 52 CRISPR screens

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

More...ChiTaRSi		Vasp, mouse

Protein Ontology

More...PROi		PR:P70460
RNActiP70460, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000030403, Expressed in granulocyte and 298 other tissues
GenevisibleiP70460, MM

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

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_MOUSE
<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: P70460
Secondary accession number(s): Q3TAP0
, Q3TCD2, Q3U0C2, Q3UDF1, Q91VD2, Q9R214
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 174 of the entry and version 4 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

<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, Reference proteome

Documents

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