Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P18206 (VINC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vinculin
Alternative name(s):
Metavinculin
Short name=MV
Gene names
Name:VCL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1134 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15 Ref.19

Subunit structure

Exhibits self-association properties. Interacts with APBB1IP, NRAP and SORBS1 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. Ref.11

Subcellular location

Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionfocal adhesion. Note: Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions By similarity. Colocalizes with LIMD1 in the focal adhesions. Ref.12

Tissue specificity

Metavinculin is muscle-specific.

Domain

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. Ref.15

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. Ref.15

Post-translational modification

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. Ref.9

Acetylated; mainly by myristic acid but also by a small amount of palmitic acid By similarity.

Involvement in disease

Cardiomyopathy, dilated 1W (CMD1W) [MIM:611407]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23

Cardiomyopathy, familial hypertrophic 15 (CMH15) [MIM:613255]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

Sequence similarities

Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCardiomyopathy
Disease mutation
   DomainRepeat
   LigandActin-binding
   PTMAcetylation
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadherens junction assembly

Inferred from mutant phenotype PubMed 20086044. Source: BHF-UCL

apical junction assembly

Inferred from mutant phenotype PubMed 9700171. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement PubMed 15501673. Source: UniProtKB

cell-matrix adhesion

Traceable author statement PubMed 20086044. Source: BHF-UCL

cellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

epithelial cell-cell adhesion

Inferred from mutant phenotype PubMed 20086044. Source: BHF-UCL

lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

morphogenesis of an epithelium

Inferred from mutant phenotype PubMed 20086044. Source: BHF-UCL

muscle contraction

Traceable author statement. Source: Reactome

negative regulation of cell migration

Traceable author statement PubMed 15494027. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

protein localization to cell surface

Inferred from mutant phenotype PubMed 20086044. Source: BHF-UCL

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: InterPro

adherens junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell adherens junction

Inferred from direct assay PubMed 20086044. Source: BHF-UCL

cell-cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell-substrate junction

Non-traceable author statement Ref.1. Source: UniProtKB

costamere

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

fascia adherens

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 9700171. Source: UniProtKB

   Molecular_functionactin binding

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

alpha-catenin binding

Inferred from physical interaction PubMed 9700171. Source: UniProtKB

beta-catenin binding

Inferred from sequence or structural similarity PubMed 20086044. Source: BHF-UCL

cadherin binding

Inferred from sequence or structural similarity PubMed 20086044. Source: BHF-UCL

dystroglycan binding

Inferred from physical interaction PubMed 18341635. Source: UniProtKB

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARPC2O151442EBI-716775,EBI-352356
ipaAP180103EBI-716775,EBI-7640410From a different organism.
ipaAQ6XVZ24EBI-716775,EBI-7255868From a different organism.
Sorbs1Q62417-23EBI-716775,EBI-7072893From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P18206-1)

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.
Isoform 1 (identifier: P18206-2)

Also known as: Vinculin;

The sequence of this isoform differs from the canonical sequence as follows:
     916-983: Missing.
Isoform 3 (identifier: P18206-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 11341133Vinculin
PRO_0000064252

Regions

Repeat259 – 3691111
Repeat370 – 4791102
Repeat480 – 5891103
Region2 – 835834N-terminal globular head
Region168 – 20841Talin-interaction By similarity
Region259 – 5893313 X 112 AA tandem repeats
Region836 – 87843Linker (Pro-rich)
Region879 – 1134256C-terminal tail
Region1003 – 104644Facilitates phospholipid membrane insertion By similarity
Region1120 – 113415Facilitates phospholipid membrane insertion By similarity
Compositional bias837 – 87842Pro-rich

Amino acid modifications

Modified residue1731N6-acetyllysine Ref.14
Modified residue2881Phosphoserine Ref.16
Modified residue2901Phosphoserine Ref.13 Ref.16 Ref.18
Modified residue3461Phosphoserine Ref.18
Modified residue4341Phosphoserine Ref.18
Modified residue4961N6-acetyllysine Ref.14
Modified residue5371Phosphotyrosine Potential
Modified residue7211Phosphoserine Ref.10 Ref.13 Ref.16 Ref.18
Modified residue8221Phosphotyrosine Ref.13
Modified residue11331Phosphotyrosine; by SRC-type Tyr-kinases Ref.9

Natural variations

Alternative sequence1 – 7373Missing in isoform 3.
VSP_011857
Alternative sequence262 – 29534DTEAM…PGDAG → VRVLSGEISKIPNSPWLGVL IGTCLILYLVIFVA in isoform 3.
VSP_011858
Alternative sequence296 – 1134839Missing in isoform 3.
VSP_011859
Alternative sequence916 – 98368Missing in isoform 1.
VSP_006731
Natural variant2341V → L. Ref.4
Corresponds to variant rs17853882 [ dbSNP | Ensembl ].
VAR_037667
Natural variant2771L → M in CMH15. Ref.24
VAR_035101
Natural variant9341A → V. Ref.23
Corresponds to variant rs16931179 [ dbSNP | Ensembl ].
VAR_035102
Natural variant9431P → A. Ref.23
VAR_035103
Natural variant9541Missing in CMD1W. Ref.22
VAR_035104
Natural variant9751R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. Ref.22 Ref.23
VAR_035105

Secondary structure

...................................................................................................... 1134
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (Metavinculin) [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: BFBD687DA836B0FA

FASTA1,134123,799
        10         20         30         40         50         60 
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE 

        70         80         90        100        110        120 
TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS 

       130        140        150        160        170        180 
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ 

       190        200        210        220        230        240 
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE 

       250        260        270        280        290        300 
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPSAS PGDAGEQAIR 

       310        320        330        340        350        360 
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGSSPVAM QKAQQVSQGL 

       370        380        390        400        410        420 
DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE 

       430        440        450        460        470        480 
LCDDPKERDD ILRSLGEISA LTSKLADLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA 

       490        500        510        520        530        540 
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD 

       550        560        570        580        590        600 
LLAKCDRVDQ LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKARMQEA MTQEVSDVFS 

       610        620        630        640        650        660 
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGKL GATAEKAAAV GTANKSTVEG 

       670        680        690        700        710        720 
IQASVKTARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK 

       730        740        750        760        770        780 
SLLDASEEAI KKDLDKCKVA MANIQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR 

       790        800        810        820        830        840 
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP 

       850        860        870        880        890        900 
DFPPPPPDLE QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM 

       910        920        930        940        950        960 
AARQLHDEAR KWSSKPGIPA AEVGIGVVAE ADAADAAGFP VPPDMEDDYE PELLLMPSNQ 

       970        980        990       1000       1010       1020 
PVNQPILAAA QSLHREATKW SSKGNDIIAA AKRMALLMAE MSRLVRGGSG TKRALIQCAK 

      1030       1040       1050       1060       1070       1080 
DIAKASDEVT RLAKEVAKQC TDKRIRTNLL QVCERIPTIS TQLKILSTVK ATMLGRTNIS 

      1090       1100       1110       1120       1130 
DEESEQATEM LVHNAQNLMQ SVKETVREAE AASIKIRTDA GFTLRWVRKT PWYQ 

« Hide

Isoform 1 (Vinculin) [UniParc].

Checksum: C9B67AA072009EBD
Show »

FASTA1,066116,722
Isoform 3 [UniParc].

Checksum: CBC9C4E86C7B5002
Show »

FASTA22224,904

References

« Hide 'large scale' references
[1]"Complete sequence of human vinculin and assignment of the gene to chromosome 10."
Weller P.A., Ogryzko E.P., Corben E.B., Zhidkova N.I., Patel B., Price G.J., Spurr N.K., Koteliansky V.E., Critchley D.R.
Proc. Natl. Acad. Sci. U.S.A. 87:5667-5671(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Endothelial cell.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Retina.
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-234.
Tissue: Prostate.
[5]"Organization of the human gene encoding the cytoskeletal protein vinculin and the sequence of the vinculin promoter."
Moiseyeva E.P., Weller P.A., Zhidkova N.I., Corben E.B., Patel B., Jasinska I., Koteliansky V.E., Critchley D.R.
J. Biol. Chem. 268:4318-4325(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
[6]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 114-132; 247-261; 327-339; 353-366; 465-476 AND 548-561, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[7]"An additional exon in the human vinculin gene specifically encodes meta-vinculin-specific difference peptide. Cross-species comparison reveals variable and conserved motifs in the meta-vinculin insert."
Koteliansky V.E., Ogryzko E.P., Zhidkova N.I., Weller P.A., Critchley D.R., Vancompernolle K., Vandekerckhove J., Strasser P., Way M., Gimona M., Small J.V.
Eur. J. Biochem. 204:767-772(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 854-1051, ALTERNATIVE SPLICING (ISOFORM 2).
Tissue: Uterus.
[8]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-7 (ISOFORMS 1/2).
Tissue: Platelet.
[9]"The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading."
Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E., Haimovich B.
Mol. Biol. Cell 15:4234-4247(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-1133, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Human alpha-synemin interacts directly with vinculin and metavinculin."
Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.
Biochem. J. 409:657-667(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYNM.
[12]"Cell cycle regulated phosphorylation of LIMD1 in cell lines and expression in human breast cancers."
Huggins C.J., Andrulis I.L.
Cancer Lett. 267:55-66(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-721 AND TYR-822, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173 AND LYS-496, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein."
Le Clainche C., Dwivedi S.P., Didry D., Carlier M.F.
J. Biol. Chem. 285:23420-23432(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-290 AND SER-721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-346; SER-434 AND SER-721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"The C-terminal tail domain of metavinculin, vinculin's splice variant, severs actin filaments."
Janssen M.E., Liu H., Volkmann N., Hanein D.
J. Cell Biol. 197:585-593(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 2).
[20]"Structural basis for amplifying vinculin activation by talin."
Izard T., Vonrhein C.
J. Biol. Chem. 279:27667-27678(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 1-258 IN COMPLEX WITH TLN1.
[21]"Vinculin activation by talin through helical bundle conversion."
Izard T., Evans G., Borgon R.A., Rush C.L., Bricogne G., Bois P.R.J.
Nature 427:171-175(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-258 IN COMPLEX WITH TLN1.
[22]"Metavinculin mutations alter actin interaction in dilated cardiomyopathy."
Olson T.M., Illenberger S., Kishimoto N.Y., Huttelmaier S., Keating M.T., Jockusch B.M.
Circulation 105:431-437(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1W LEU-954 DEL AND TRP-975, CHARACTERIZATION OF VARIANT CMD1W TRP-975.
[23]"Identification of a metavinculin missense mutation, R975W, associated with both hypertrophic and dilated cardiomyopathy."
Vasile V.C., Will M.L., Ommen S.R., Edwards W.D., Olson T.M., Ackerman M.J.
Mol. Genet. Metab. 87:169-174(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1W TRP-975, VARIANTS VAL-934 AND ALA-943.
[24]"A missense mutation in a ubiquitously expressed protein, vinculin, confers susceptibility to hypertrophic cardiomyopathy."
Vasile V.C., Ommen S.R., Edwards W.D., Ackerman M.J.
Biochem. Biophys. Res. Commun. 345:998-1003(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMH15 MET-277.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA35955.
RefSeqNP_003364.1. NM_003373.3.
NP_054706.1. NM_014000.2.
UniGeneHs.643896.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray2.72A1-257[»]
2HSQX-ray3.97A2-257[»]
2IBFX-ray3.20A1-258[»]
3H2UX-ray2.75A/C879-1134[»]
3H2VX-ray2.90A/B/C/D879-1134[»]
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[»]
ProteinModelPortalP18206.
SMRP18206. Positions 1-258, 957-1134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113257. 82 interactions.
DIPDIP-35570N.
IntActP18206. 19 interactions.
MINTMINT-92846.
STRING9606.ENSP00000211998.

PTM databases

PhosphoSiteP18206.

Polymorphism databases

DMDM21903479.

2D gel databases

DOSAC-COBS-2DPAGEP18206.
OGPP18206.
REPRODUCTION-2DPAGEIPI00291175.
SWISS-2DPAGEP18206.
UCD-2DPAGEP18206.

Proteomic databases

PaxDbP18206.
PRIDEP18206.

Protocols and materials databases

DNASU7414.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000211998; ENSP00000211998; ENSG00000035403. [P18206-1]
ENST00000372755; ENSP00000361841; ENSG00000035403. [P18206-2]
GeneID7414.
KEGGhsa:7414.
UCSCuc001jwd.3. human. [P18206-1]
uc001jwe.3. human. [P18206-2]

Organism-specific databases

CTD7414.
GeneCardsGC10P075757.
H-InvDBHIX0170429.
HGNCHGNC:12665. VCL.
HPACAB002453.
HPA002131.
MIM193065. gene.
611407. phenotype.
613255. phenotype.
neXtProtNX_P18206.
Orphanet154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
PharmGKBPA37288.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG329927.
HOGENOMHOG000007828.
HOVERGENHBG079758.
InParanoidP18206.
KOK05700.
OMAPILICSM.
OrthoDBEOG73NG2V.
PhylomeDBP18206.
TreeFamTF313686.

Enzyme and pathway databases

ReactomeREACT_17044. Muscle contraction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP18206.
BgeeP18206.
CleanExHS_VCL.
GenevestigatorP18206.

Family and domain databases

InterProIPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERPTHR18914. PTHR18914. 1 hit.
PfamPF01044. Vinculin. 3 hits.
[Graphical view]
PRINTSPR00806. VINCULIN.
SUPFAMSSF47220. SSF47220. 6 hits.
PROSITEPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVCL. human.
EvolutionaryTraceP18206.
GeneWikiVinculin.
GenomeRNAi7414.
NextBio29028.
PROP18206.
SOURCESearch...

Entry information

Entry nameVINC_HUMAN
AccessionPrimary (citable) accession number: P18206
Secondary accession number(s): Q16450 expand/collapse secondary AC list , Q5SWX2, Q7Z3B8, Q8IXU7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM