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UniProtKB - Q64727 (VINC_MOUSE)

Entry version 175 (18 Sep 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Vinculin

Gene

Vcl

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

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 (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
Biological processCell adhesion

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-114608 Platelet degranulation
R-MMU-445355 Smooth Muscle Contraction
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-6798695 Neutrophil degranulation

<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 14

Organism-specific databases

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

More...MGIi		MGI:98927 Vcl

<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, Cytoplasm, Cytoskeleton, Membrane

<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_00000642531 – 1066VinculinAdd BLAST1066

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-acetyllysineBy similarity1
Modified residuei260PhosphoserineCombined sources1
Modified residuei272PhosphoserineBy similarity1
Modified residuei275PhosphoserineBy similarity1
Modified residuei290PhosphoserineCombined sources1
Modified residuei346PhosphoserineCombined sources1
Modified residuei434PhosphoserineBy similarity1
Modified residuei496N6-acetyllysineBy similarity1
Modified residuei537PhosphotyrosineCurated1
Modified residuei574PhosphoserineBy similarity1
Modified residuei579PhosphoserineCombined sources1
Modified residuei600PhosphoserineCombined sources1
Modified residuei604PhosphothreonineBy similarity1
Modified residuei672PhosphothreonineBy similarity1
Modified residuei721PhosphoserineCombined sources1
Modified residuei795PhosphoserineBy similarity1
Modified residuei809PhosphoserineCombined sources1
Modified residuei822PhosphotyrosineCombined sources1
Modified residuei1065Phosphotyrosine; by SRC-type Tyr-kinasesBy 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

Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1065 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

The CPTAC Assay portal

More...CPTACi		non-CPTAC-3755

Encyclopedia of Proteome Dynamics

More...EPDi		Q64727

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q64727

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q64727

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

More...PaxDbi		Q64727

PeptideAtlas

More...PeptideAtlasi		Q64727

PRoteomics IDEntifications database

More...PRIDEi		Q64727

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		Q64727

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q64727

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

More...PhosphoSitePlusi		Q64727

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		Q64727

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000021823 Expressed in 290 organ(s), highest expression level in urinary bladder

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q64727 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q64727 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_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, NRAP and TLN1.

Interacts with SYNM.

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 SORBS1 (PubMed:10085297).

Interacts with SYNM (By similarity).

Interacts with CTNNA1 (By similarity). Binds to ACTN4; this interaction triggers conformational changes (By similarity).

By similarity2 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		204506, 10 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q64727

Protein interaction database and analysis system

More...IntActi		Q64727, 17 interactors

Molecular INTeraction database

More...MINTi		Q64727

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000022369

<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

11066
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		Q64727

Database of comparative protein structure models

More...ModBasei		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 ‘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 headBy similarityAdd BLAST835
Regioni168 – 208Talin-interactionBy similarityAdd BLAST41
Regioni259 – 5893 X 112 AA tandem repeatsSequence analysisAdd BLAST331
Regioni741 – 764Interaction with ACTN4By similarityAdd BLAST24
Regioni836 – 878Linker (Pro-rich)By similarityAdd BLAST43
Regioni879 – 1066C-terminal tailBy similarityAdd BLAST188
Regioni935 – 978Facilitates phospholipid membrane insertion1 PublicationAdd BLAST44
Regioni1052 – 1066Facilitates phospholipid membrane insertion1 PublicationAdd 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.By similarity
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. 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.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 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

More...GeneTreei		ENSGT00950000182729

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000007828

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q64727

KEGG Orthology (KO)

More...KOi		K05700

Identification of Orthologs from Complete Genome Data

More...OMAi		TPGREQN

Database of Orthologous Groups

More...OrthoDBi		270073at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q64727

TreeFam database of animal gene trees

More...TreeFami		TF313686

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...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		PTHR46180 PTHR46180, 2 hits

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01044 Vinculin, 2 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>. 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.

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

Q64727-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
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 KGWLRDPNAS PGDAGEQAIR 
       310        320        330        340        350
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM 
       360        370        380        390        400
QKAQQVSQGL DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG 
       410        420        430        440        450
GPEGEEQIRG ALAEARKIAE LCDDPKERDD ILRSLGEIAA LTSKLGDLRR 
       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 KDLKAQMQEA MTQEVSDVFS 
       610        620        630        640        650
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV 
       660        670        680        690        700
GTANKSTVEG IQASVKTARE LTPQVISAAR 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 KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC 
       960        970        980        990       1000
AKDIAKASDE VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST 
      1010       1020       1030       1040       1050
VKATMLGRTN ISDEESEQAT EMLVHNAQNL MQSVKETVRE AEAASIKIRT 
      1060 
DAGFTLRWVR KTPWYQ
Length:1,066
Mass (Da):116,717
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:i067F1B16A5285859
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
A0A286YDJ4A0A286YDJ4_MOUSE
Vinculin
Vcl
149Annotation 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 conflicti16V → E in AAB96843 (PubMed:7568093).Curated1
Sequence conflicti215T → S in AAB96843 (PubMed:7568093).Curated1
Sequence conflicti363L → V in AAB96843 (PubMed:7568093).Curated1
Sequence conflicti499Q → K in BAC37033 (PubMed:16141072).Curated1
Sequence conflicti501Q → R in AAB96843 (PubMed:7568093).Curated1
Sequence conflicti799M → K in BAC37033 (PubMed:16141072).Curated1
Sequence conflicti812G → D in AAB96843 (PubMed:7568093).Curated1
Sequence conflicti1044A → T in BAC37033 (PubMed:16141072).Curated1

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
L13300, L13299 Genomic DNA Translation: AAA40557.1
L18880 mRNA Translation: AAB96843.1
AK035184 mRNA Translation: BAC28973.1
AK077850 mRNA Translation: BAC37033.1
BC008520 mRNA Translation: AAH08520.1
BC008554 mRNA Translation: AAH08554.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS26860.1

Protein sequence database of the Protein Information Resource

More...PIRi		A60965
T10108

NCBI Reference Sequences

More...RefSeqi		NP_033528.3, NM_009502.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823

Database of genes from NCBI RefSeq genomes

More...GeneIDi		22330

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:22330

UCSC genome browser

More...UCSCi		uc007skz.1 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
L13300, L13299 Genomic DNA Translation: AAA40557.1
L18880 mRNA Translation: AAB96843.1
AK035184 mRNA Translation: BAC28973.1
AK077850 mRNA Translation: BAC37033.1
BC008520 mRNA Translation: AAH08520.1
BC008554 mRNA Translation: AAH08554.1
CCDSiCCDS26860.1
PIRiA60965
T10108
RefSeqiNP_033528.3, NM_009502.4

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
5Y04X-ray2.85A1-250[»]
SMRiQ64727
ModBaseiSearch...

Protein-protein interaction databases

BioGridi204506, 10 interactors
CORUMiQ64727
IntActiQ64727, 17 interactors
MINTiQ64727
STRINGi10090.ENSMUSP00000022369

PTM databases

iPTMnetiQ64727
PhosphoSitePlusiQ64727

2D gel databases

REPRODUCTION-2DPAGEiQ64727

Proteomic databases

CPTACinon-CPTAC-3755
EPDiQ64727
jPOSTiQ64727
MaxQBiQ64727
PaxDbiQ64727
PeptideAtlasiQ64727
PRIDEiQ64727

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823
GeneIDi22330
KEGGimmu:22330
UCSCiuc007skz.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7414
MGIiMGI:98927 Vcl

Phylogenomic databases

eggNOGiKOG3681 Eukaryota
ENOG410XSRU LUCA
GeneTreeiENSGT00950000182729
HOGENOMiHOG000007828
InParanoidiQ64727
KOiK05700
OMAiTPGREQN
OrthoDBi270073at2759
PhylomeDBiQ64727
TreeFamiTF313686

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-MMU-445355 Smooth Muscle Contraction
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

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

More...ChiTaRSi		Vcl mouse
PMAP-CutDBiQ64727

Protein Ontology

More...PROi		PR:Q64727

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000021823 Expressed in 290 organ(s), highest expression level in urinary bladder
ExpressionAtlasiQ64727 baseline and differential
GenevisibleiQ64727 MM

Family and domain databases

InterProiView protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR017997 Vinculin
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS
PANTHERiPTHR46180 PTHR46180, 2 hits
PfamiView protein in Pfam
PF01044 Vinculin, 2 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...

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 nameiVINC_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: Q64727
Secondary accession number(s): Q8BP32
, Q8BS46, Q922C5, Q922D9
<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: July 15, 1998
Last sequence update: January 23, 2007
Last modified: September 18, 2019
This is version 175 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, 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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