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UniProtKB - P85972 (VINC_RAT)

Entry version 86 (25 May 2022)
Sequence version 1 (02 Sep 2008)
Previous versions | rss
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Protein

Vinculin

Gene

Vcl

Organism
Rattus norvegicus (Rat)
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

<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-RNO-114608, Platelet degranulation
R-RNO-445355, Smooth Muscle Contraction
R-RNO-5674135, MAP2K and MAPK activation
R-RNO-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%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:
VinculinBy similarity
Alternative name(s):
MetavinculinBy similarity
<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:VclBy similarity
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Rattus
<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
  • UP000002494 <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: Unplaced
  • UP000234681 Componenti: Chromosome 15

Organism-specific databases

Rat genome database

More...RGDi		1311217, 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

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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003491171 – 1066VinculinBy similarityAdd 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 residuei97PhosphoserineCombined sources1
Modified residuei173N6-acetyllysineBy similarity1
Modified residuei260PhosphoserineCombined sources1
Modified residuei272PhosphoserineCombined sources1
Modified residuei275PhosphoserineCombined sources1
Modified residuei290PhosphoserineCombined sources1
Modified residuei346PhosphoserineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei496N6-acetyllysineBy similarity1
Modified residuei537PhosphotyrosineCurated1
Modified residuei574PhosphoserineCombined sources1
Modified residuei579PhosphoserineCombined sources1
Modified residuei600PhosphoserineBy similarity1
Modified residuei604PhosphothreonineBy similarity1
Modified residuei672PhosphothreonineBy similarity1
Modified residuei721PhosphoserineCombined sources1
Modified residuei795PhosphoserineCombined sources1
Modified residuei809PhosphoserineBy similarity1
Modified residuei822PhosphotyrosineCombined sources1
Modified residuei1065Phosphotyrosine; by SRC-type Tyr-kinasesBy similarity1

<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

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

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P85972

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

More...PaxDbi		P85972

PRoteomics IDEntifications database

More...PRIDEi		P85972

2D gel databases

The World-2DPAGE database

More...World-2DPAGEi		0004:P85972

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P85972

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

More...PhosphoSitePlusi		P85972

<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

Exhibits self-association properties.

Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL (By similarity).

Interacts with APBB1IP, NRAP and 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 SORBS1 (By similarity).

Interacts with SYNM (By similarity).

Interacts with CTNNA1 (By similarity). Binds to ACTN4; this interaction triggers conformational changes (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		258242, 3 interactors

Protein interaction database and analysis system

More...IntActi		P85972, 4 interactors

Molecular INTeraction database

More...MINTi		P85972

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000015179

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P85972

Biological Magnetic Resonance Data Bank

More...BMRBi		P85972

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

More...SMRi		P85972

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
Regioni857 – 887DisorderedSequence analysisAdd BLAST31
Regioni879 – 1066C-terminal tailBy similarityAdd BLAST188
Regioni935 – 978Facilitates phospholipid membrane insertionBy similarityAdd BLAST44
Regioni1052 – 1066Facilitates 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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi859 – 873Pro residuesSequence analysisAdd BLAST15

<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.Sequence analysis

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3681, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P85972

Database for complete collections of gene phylogenies

More...PhylomeDBi		P85972

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, 1 hit

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%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>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P85972-1 [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 NFTVGKMSAE 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
LAAQLADLAA RGEGESPQAR ALASQLQDSL KDLKTQMQEA MTQEVSDVFS 
       610        620        630        640        650
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV 
       660        670        680        690        700
GAANKSTVEG 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):116,615
Last modified:September 2, 2008 - v1
<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:iE0669F208E4E8A86
GO

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

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K8V2A0A0G2K8V2_RAT
Vinculin
Vcl Vcl_predicted, rCG_41845
1,134Annotation score:

Annotation score:4 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>
R9PXU6R9PXU6_RAT
Vinculin
Vcl
1,066Annotation score:

Annotation score:3 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>

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
CH474061 Genomic DNA Translation: EDL86258.1

NCBI Reference Sequences

More...RefSeqi		NP_001100718.1, NM_001107248.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000015179; ENSRNOP00000015179; ENSRNOG00000010765

Database of genes from NCBI RefSeq genomes

More...GeneIDi		305679

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:305679

UCSC genome browser

More...UCSCi		RGD:1311217, rat

<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
CH474061 Genomic DNA Translation: EDL86258.1
RefSeqiNP_001100718.1, NM_001107248.1

3D structure databases

AlphaFoldDBiP85972
BMRBiP85972
SMRiP85972
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi258242, 3 interactors
IntActiP85972, 4 interactors
MINTiP85972
STRINGi10116.ENSRNOP00000015179

PTM databases

iPTMnetiP85972
PhosphoSitePlusiP85972

2D gel databases

World-2DPAGEi0004:P85972

Proteomic databases

jPOSTiP85972
PaxDbiP85972
PRIDEiP85972

Genome annotation databases

EnsembliENSRNOT00000015179; ENSRNOP00000015179; ENSRNOG00000010765
GeneIDi305679
KEGGirno:305679
UCSCiRGD:1311217, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7414
RGDi1311217, Vcl

Phylogenomic databases

eggNOGiKOG3681, Eukaryota
InParanoidiP85972
PhylomeDBiP85972
TreeFamiTF313686

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...PROi		PR:P85972

Family and domain databases

InterProiView protein in InterPro
IPR036723, Alpha-catenin/vinculin-like_sf
IPR017997, Vinculin
IPR006077, Vinculin/catenin
IPR000633, Vinculin_CS
PANTHERiPTHR46180, PTHR46180, 1 hit
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

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_RAT
<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: P85972
Secondary accession number(s): A6KKR4
<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: September 2, 2008
Last sequence update: September 2, 2008
Last modified: May 25, 2022
This is version 86 of the entry and version 1 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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