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Protein

Vinculin

Gene

VCL

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

Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.1 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

  • actin binding Source: BHF-UCL
  • alpha-catenin binding Source: UniProtKB
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • dystroglycan binding Source: UniProtKB
  • structural molecule activity Source: InterPro
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

<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
Biological processCell adhesion

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-114608 Platelet degranulation
R-HSA-445355 Smooth Muscle Contraction
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-6798695 Neutrophil degranulation
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF

SIGNOR Signaling Network Open Resource

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SIGNORi
P18206

<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:
Vinculin
Alternative name(s):
Metavinculin
Short name:
MV
<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:VCL
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 10

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000035403.16

Human Gene Nomenclature Database

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HGNCi
HGNC:12665 VCL

Online Mendelian Inheritance in Man (OMIM)

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MIMi
193065 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P18206

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Cardiomyopathy, dilated 1W (CMD1W)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:611407
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_035104954Missing in CMD1W. 1 Publication1
Natural variantiVAR_035105975R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. 2 PublicationsCorresponds to variant dbSNP:rs121917776EnsemblClinVar.1
Cardiomyopathy, familial hypertrophic 15 (CMH15)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
See also OMIM:613255
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035101277L → M in CMH15. 1 PublicationCorresponds to variant dbSNP:rs71579353EnsemblClinVar.1

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
7414

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
VCL

MalaCards human disease database

More...
MalaCardsi
VCL
MIMi611407 phenotype
613255 phenotype

Open Targets

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OpenTargetsi
ENSG00000035403

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
154 Familial isolated dilated cardiomyopathy
155 NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA37288

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
VCL

Domain mapping of disease mutations (DMDM)

More...
DMDMi
21903479

<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 ‘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_00000642521 – 1134VinculinAdd BLAST1134

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 residuei97PhosphoserineBy similarity1
Modified residuei173N6-acetyllysineCombined sources1
Modified residuei260PhosphoserineCombined sources1
Modified residuei272PhosphoserineBy similarity1
Modified residuei275PhosphoserineCombined sources1
Modified residuei288PhosphoserineCombined sources1
Modified residuei290PhosphoserineCombined sources1
Modified residuei346PhosphoserineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei496N6-acetyllysineCombined sources1
Modified residuei537PhosphotyrosineCurated1
Modified residuei574PhosphoserineBy similarity1
Modified residuei579PhosphoserineCombined sources1
Modified residuei600PhosphoserineCombined sources1
Modified residuei604PhosphothreonineCombined sources1
Modified residuei672PhosphothreonineCombined sources1
Modified residuei721PhosphoserineCombined sources1
Modified residuei795PhosphoserineCombined sources1
Modified residuei809PhosphoserineCombined sources1
Modified residuei822PhosphotyrosineCombined sources1
Modified residuei1133Phosphotyrosine; by SRC-type Tyr-kinases1 Publication1

<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

Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1133 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques (By similarity).By similarity
Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P18206

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P18206

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

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PaxDbi
P18206

PeptideAtlas

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PeptideAtlasi
P18206

PRoteomics IDEntifications database

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PRIDEi
P18206

ProteomicsDB human proteome resource

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ProteomicsDBi
53553
53554 [P18206-2]
53555 [P18206-3]

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P18206

USC-OGP 2-DE database

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OGPi
P18206

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00291175

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P18206

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P18206

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P18206

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

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PhosphoSitePlusi
P18206

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P18206

<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

Metavinculin is muscle-specific.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000035403 Expressed in 244 organ(s), highest expression level in myometrium

CleanEx database of gene expression profiles

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CleanExi
HS_VCL

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P18206 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P18206 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB002453
HPA002131
HPA063777

<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

Exhibits self-association properties. Interacts with APBB1IP and NRAP (By similarity). Interacts with TLN1. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin (By similarity). Interacts with SYNM. Interacts with SORBS1 (By similarity). Interacts with CTNNA1 (PubMed:26691986). Binds to ACTN4; this interaction triggers conformational changes (PubMed:15988023).By similarity5 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113257, 116 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P18206

Database of interacting proteins

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DIPi
DIP-35570N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P18206

Protein interaction database and analysis system

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IntActi
P18206, 50 interactors

Molecular INTeraction database

More...
MINTi
P18206

STRING: functional protein association networks

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STRINGi
9606.ENSP00000211998

<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

11134
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RKCX-ray2.70A1-258[»]
1RKEX-ray2.35A1-258[»]
B882-1134[»]
1SYQX-ray2.42A1-258[»]
1TR2X-ray2.90A/B1-1134[»]
1YDIX-ray1.80A1-258[»]
2GWWX-ray2.72A1-258[»]
2HSQX-ray3.97A1-258[»]
2IBFX-ray3.20A1-258[»]
3H2UX-ray2.75A/C879-1134[»]
3H2VX-ray2.90A/B/C/D879-1134[»]
3JBKelectron microscopy8.20M858-1129[»]
3MYIX-ray2.20A959-1130[»]
3RF3X-ray1.61A/B1-258[»]
3S90X-ray1.97A/B1-252[»]
3TJ5X-ray1.99A1-255[»]
3TJ6X-ray2.76A1-257[»]
3VF0X-ray2.54A856-1134[»]
4DJ9X-ray2.25A1-258[»]
4EHPX-ray2.66A1-252[»]
4LN2X-ray1.00B857-867[»]
4LNPX-ray1.41B870-879[»]
4PR9X-ray3.20A/B/C/D/E/F891-1134[»]
5L0CX-ray3.10A/B/C/D959-1134[»]
5L0DX-ray2.75A/B/C/D959-1130[»]
5L0FX-ray2.76A/B959-1134[»]
5L0GX-ray3.40A/B/C/D959-1134[»]
5L0HX-ray2.90A959-1134[»]
5L0IX-ray2.45A959-1134[»]
5L0JX-ray4.00A/B969-1134[»]
5O2QNMR-A854-870[»]
6FUYX-ray3.00A1-1134[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P18206

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

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SMRi
P18206

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P18206

<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 ‘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>Repeati259 – 3691Sequence analysisAdd BLAST111
Repeati370 – 4792Sequence analysisAdd BLAST110
Repeati480 – 5893Sequence analysisAdd BLAST110

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>Regioni1 – 835N-terminal globular head1 PublicationAdd BLAST835
Regioni168 – 208Talin-interactionBy similarityAdd BLAST41
Regioni259 – 5893 X 112 AA tandem repeatsSequence analysisAdd BLAST331
Regioni741 – 764Interaction with ACTN4Combined sources1 PublicationAdd BLAST24
Regioni836 – 878Linker (Pro-rich)1 PublicationAdd BLAST43
Regioni879 – 1134C-terminal tail1 PublicationAdd BLAST256
Regioni1003 – 1046Facilitates phospholipid membrane insertionBy similarityAdd BLAST44
Regioni1120 – 1134Facilitates phospholipid membrane insertionBy similarityAdd BLAST15

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 biasi837 – 878Pro-richPROSITE-ProRule annotationAdd BLAST42

<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

Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion.1 Publication
The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. In isoform 2 (metavinculin) a 68 residue insertion in the tail domain promotes actin severing instead of bundling. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly.1 Publication

<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 vinculin/alpha-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3681 Eukaryota
ENOG410XSRU LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155700

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007828

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG079758

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P18206

KEGG Orthology (KO)

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KOi
K05700

Identification of Orthologs from Complete Genome Data

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OMAi
TPGREQN

Database of Orthologous Groups

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OrthoDBi
614199at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P18206

TreeFam database of animal gene trees

More...
TreeFami
TF313686

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR017997 Vinculin
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS

The PANTHER Classification System

More...
PANTHERi
PTHR18914 PTHR18914, 3 hits
PTHR18914:SF1 PTHR18914:SF1, 3 hits

Pfam protein domain database

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Pfami
View protein in Pfam
PF01044 Vinculin, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47220 SSF47220, 6 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00663 VINCULIN_1, 1 hit
PS00664 VINCULIN_2, 3 hits

<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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)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.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 2 (identifier: P18206-1) [UniParc]FASTAAdd to basket
Also known as: Metavinculin

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA
60 70 80 90 100
VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY
110 120 130 140 150
SVPARDYLID GSRGILSGTS DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV
160 170 180 190 200
VETMEDLVTY TKNLGPGMTK MAKMIDERQQ ELTHQEHRVM LVNSMNTVKE
210 220 230 240 250
LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE INEIIRVLQL
260 270 280 290 300
TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPSAS PGDAGEQAIR
310 320 330 340 350
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGSSPVAM
360 370 380 390 400
QKAQQVSQGL DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG
410 420 430 440 450
GPEGEEQIRG ALAEARKIAE LCDDPKERDD ILRSLGEISA LTSKLADLRR
460 470 480 490 500
QGKGDSPEAR ALAKQVATAL QNLQTKTNRA VANSRPAKAA VHLEGKIEQA
510 520 530 540 550
QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD LLAKCDRVDQ
560 570 580 590 600
LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKARMQEA MTQEVSDVFS
610 620 630 640 650
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGKL GATAEKAAAV
660 670 680 690 700
GTANKSTVEG IQASVKTARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN
710 720 730 740 750
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANIQPQMLV
760 770 780 790 800
AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD
810 820 830 840 850
AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE
860 870 880 890 900
QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM
910 920 930 940 950
AARQLHDEAR KWSSKPGIPA AEVGIGVVAE ADAADAAGFP VPPDMEDDYE
960 970 980 990 1000
PELLLMPSNQ PVNQPILAAA QSLHREATKW SSKGNDIIAA AKRMALLMAE
1010 1020 1030 1040 1050
MSRLVRGGSG TKRALIQCAK DIAKASDEVT RLAKEVAKQC TDKRIRTNLL
1060 1070 1080 1090 1100
QVCERIPTIS TQLKILSTVK ATMLGRTNIS DEESEQATEM LVHNAQNLMQ
1110 1120 1130
SVKETVREAE AASIKIRTDA GFTLRWVRKT PWYQ
Length:1,134
Mass (Da):123,799
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:iBFBD687DA836B0FA
GO
Isoform 1 (identifier: P18206-2) [UniParc]FASTAAdd to basket
Also known as: Vinculin

The sequence of this isoform differs from the canonical sequence as follows:
     916-983: Missing.

Show »
Length:1,066
Mass (Da):116,722
Checksum:iC9B67AA072009EBD
GO
Isoform 3 (identifier: P18206-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
     262-295: DTEAMKRALASIDSKLNQAKGWLRDPSASPGDAG → VRVLSGEISKIPNSPWLGVLIGTCLILYLVIFVA
     296-1134: Missing.

Note: No experimental confirmation available.
Show »
Length:222
Mass (Da):24,904
Checksum:iCBC9C4E86C7B5002
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A096LPE1A0A096LPE1_HUMAN
Vinculin
VCL
57Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037667234V → L1 PublicationCorresponds to variant dbSNP:rs17853882Ensembl.1
Natural variantiVAR_035101277L → M in CMH15. 1 PublicationCorresponds to variant dbSNP:rs71579353EnsemblClinVar.1
Natural variantiVAR_035102934A → V1 PublicationCorresponds to variant dbSNP:rs16931179EnsemblClinVar.1
Natural variantiVAR_035103943P → A1 PublicationCorresponds to variant dbSNP:rs71579375EnsemblClinVar.1
Natural variantiVAR_035104954Missing in CMD1W. 1 Publication1
Natural variantiVAR_035105975R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. 2 PublicationsCorresponds to variant dbSNP:rs121917776EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0118571 – 73Missing in isoform 3. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_011858262 – 295DTEAM…PGDAG → VRVLSGEISKIPNSPWLGVL IGTCLILYLVIFVA in isoform 3. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_011859296 – 1134Missing in isoform 3. 1 PublicationAdd BLAST839
Alternative sequenceiVSP_006731916 – 983Missing in isoform 1. 2 PublicationsAdd BLAST68

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M33308 mRNA Translation: AAA61283.1
BX537994 mRNA Translation: CAD97952.1
AL596247, AL731576 Genomic DNA Translation: CAI13972.1
AL731576, AL596247 Genomic DNA Translation: CAI39673.1
BC039174 mRNA Translation: AAH39174.1
L04933 Genomic DNA Translation: AAA61271.1
S87180, S87175, S87178 Genomic DNA Translation: AAB21656.1
S87223, S87218 Genomic DNA Translation: AAB21657.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS7340.1 [P18206-2]
CCDS7341.1 [P18206-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A35955

NCBI Reference Sequences

More...
RefSeqi
NP_003364.1, NM_003373.3 [P18206-2]
NP_054706.1, NM_014000.2 [P18206-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.643896

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000211998; ENSP00000211998; ENSG00000035403 [P18206-1]
ENST00000372755; ENSP00000361841; ENSG00000035403 [P18206-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7414

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7414

UCSC genome browser

More...
UCSCi
uc001jwe.4 human [P18206-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Vinculin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33308 mRNA Translation: AAA61283.1
BX537994 mRNA Translation: CAD97952.1
AL596247, AL731576 Genomic DNA Translation: CAI13972.1
AL731576, AL596247 Genomic DNA Translation: CAI39673.1
BC039174 mRNA Translation: AAH39174.1
L04933 Genomic DNA Translation: AAA61271.1
S87180, S87175, S87178 Genomic DNA Translation: AAB21656.1
S87223, S87218 Genomic DNA Translation: AAB21657.1
CCDSiCCDS7340.1 [P18206-2]
CCDS7341.1 [P18206-1]
PIRiA35955
RefSeqiNP_003364.1, NM_003373.3 [P18206-2]
NP_054706.1, NM_014000.2 [P18206-1]
UniGeneiHs.643896

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RKCX-ray2.70A1-258[»]
1RKEX-ray2.35A1-258[»]
B882-1134[»]
1SYQX-ray2.42A1-258[»]
1TR2X-ray2.90A/B1-1134[»]
1YDIX-ray1.80A1-258[»]
2GWWX-ray2.72A1-258[»]
2HSQX-ray3.97A1-258[»]
2IBFX-ray3.20A1-258[»]
3H2UX-ray2.75A/C879-1134[»]
3H2VX-ray2.90A/B/C/D879-1134[»]
3JBKelectron microscopy8.20M858-1129[»]
3MYIX-ray2.20A959-1130[»]
3RF3X-ray1.61A/B1-258[»]
3S90X-ray1.97A/B1-252[»]
3TJ5X-ray1.99A1-255[»]
3TJ6X-ray2.76A1-257[»]
3VF0X-ray2.54A856-1134[»]
4DJ9X-ray2.25A1-258[»]
4EHPX-ray2.66A1-252[»]
4LN2X-ray1.00B857-867[»]
4LNPX-ray1.41B870-879[»]
4PR9X-ray3.20A/B/C/D/E/F891-1134[»]
5L0CX-ray3.10A/B/C/D959-1134[»]
5L0DX-ray2.75A/B/C/D959-1130[»]
5L0FX-ray2.76A/B959-1134[»]
5L0GX-ray3.40A/B/C/D959-1134[»]
5L0HX-ray2.90A959-1134[»]
5L0IX-ray2.45A959-1134[»]
5L0JX-ray4.00A/B969-1134[»]
5O2QNMR-A854-870[»]
6FUYX-ray3.00A1-1134[»]
ProteinModelPortaliP18206
SMRiP18206
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113257, 116 interactors
CORUMiP18206
DIPiDIP-35570N
ELMiP18206
IntActiP18206, 50 interactors
MINTiP18206
STRINGi9606.ENSP00000211998

PTM databases

iPTMnetiP18206
PhosphoSitePlusiP18206
SwissPalmiP18206

Polymorphism and mutation databases

BioMutaiVCL
DMDMi21903479

2D gel databases

DOSAC-COBS-2DPAGEiP18206
OGPiP18206
REPRODUCTION-2DPAGEiIPI00291175
SWISS-2DPAGEiP18206
UCD-2DPAGEiP18206

Proteomic databases

EPDiP18206
jPOSTiP18206
PaxDbiP18206
PeptideAtlasiP18206
PRIDEiP18206
ProteomicsDBi53553
53554 [P18206-2]
53555 [P18206-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7414
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000211998; ENSP00000211998; ENSG00000035403 [P18206-1]
ENST00000372755; ENSP00000361841; ENSG00000035403 [P18206-2]
GeneIDi7414
KEGGihsa:7414
UCSCiuc001jwe.4 human [P18206-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7414
DisGeNETi7414
EuPathDBiHostDB:ENSG00000035403.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
VCL
GeneReviewsiVCL

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0170429
HGNCiHGNC:12665 VCL
HPAiCAB002453
HPA002131
HPA063777
MalaCardsiVCL
MIMi193065 gene
611407 phenotype
613255 phenotype
neXtProtiNX_P18206
OpenTargetsiENSG00000035403
Orphaneti154 Familial isolated dilated cardiomyopathy
155 NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy
PharmGKBiPA37288

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3681 Eukaryota
ENOG410XSRU LUCA
GeneTreeiENSGT00940000155700
HOGENOMiHOG000007828
HOVERGENiHBG079758
InParanoidiP18206
KOiK05700
OMAiTPGREQN
OrthoDBi614199at2759
PhylomeDBiP18206
TreeFamiTF313686

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-445355 Smooth Muscle Contraction
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-6798695 Neutrophil degranulation
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
SIGNORiP18206

Miscellaneous databases

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

More...
ChiTaRSi
VCL human
EvolutionaryTraceiP18206

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Vinculin

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

More...
GenomeRNAii
7414

Protein Ontology

More...
PROi
PR:P18206

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000035403 Expressed in 244 organ(s), highest expression level in myometrium
CleanExiHS_VCL
ExpressionAtlasiP18206 baseline and differential
GenevisibleiP18206 HS

Family and domain databases

InterProiView protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR017997 Vinculin
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS
PANTHERiPTHR18914 PTHR18914, 3 hits
PTHR18914:SF1 PTHR18914:SF1, 3 hits
PfamiView protein in Pfam
PF01044 Vinculin, 3 hits
SUPFAMiSSF47220 SSF47220, 6 hits
PROSITEiView protein in PROSITE
PS00663 VINCULIN_1, 1 hit
PS00664 VINCULIN_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiVINC_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: P18206
Secondary accession number(s): Q16450
, Q5SWX2, Q7Z3B8, Q8IXU7
<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: November 1, 1990
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 212 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
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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
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