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Reviewed, UniProtKB/Swiss-Prot P18206 (VINC_HUMAN)

Last modified February 9, 2010. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Vinculin
Alternative name(s):
    Metavinculin
Gene names
Name: VCL
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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General annotation (Comments)

Function

Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane. May also play important roles in cell morphology and locomotion.

Subunit structure

Exhibits self-association properties. Interacts with NRAP and SORBS1 By similarity. Interacts with TLN1. Interacts with SYNM. Ref.13

Subcellular location

Cytoplasm › cytoskeleton. Cell junction › adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic face of adhesion plaques.

Tissue specificity

Metavinculin is muscle-specific.

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 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16

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

Involvement in disease

Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:611407]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Ref.20 Ref.21 Ref.22

Sequence similarities

Belongs to the vinculin/alpha-catenin family.

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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
Myristate
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processapical junction assembly

Inferred from mutant phenotype. Source: UniProtKB

cell adhesion

Traceable author statement. Source: UniProtKB

cellular component movement

Traceable author statement. Source: UniProtKB

lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

muscle contraction

Inferred from Experiment. Source: Reactome

negative regulation of cell migration

Traceable author statement. Source: UniProtKB

   Cellular componentactin cytoskeleton

Inferred from electronic annotation. Source: InterPro

costamere

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from Experiment. Source: Reactome

extracellular region

Inferred from Experiment. Source: Reactome

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from direct assay. Source: UniProtKB

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

alpha-catenin binding

Inferred from physical interaction. Source: UniProtKB

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

TLN1P549391EBI-716775,EBI-1035421From a different organism.

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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.

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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
Region168 – 20841Talin-interaction By similarity
Region259 – 5893313 X 112 AA tandem repeats
Compositional bias837 – 87842Pro-rich

Amino acid modifications

Modified residue1001Phosphotyrosine By similarity
Modified residue1731N6-acetyllysine Ref.17
Modified residue2901Phosphoserine Ref.11 Ref.14
Modified residue3241Phosphothreonine By similarity
Modified residue4961N6-acetyllysine Ref.17
Modified residue5081Phosphothreonine Ref.10
Modified residue5371Phosphotyrosine Potential
Modified residue6041Phosphothreonine Ref.11
Modified residue6921Phosphotyrosine Ref.12
Modified residue7211Phosphoserine Ref.11 Ref.14
Modified residue7741Phosphoserine By similarity
Modified residue8221Phosphotyrosine Ref.12 Ref.14 Ref.16
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: dbSNP rs17853882. Ref.4
VAR_037667
Natural variant2771L → M in CMD1W. Ref.22
VAR_035101
Natural variant9341A → V: dbSNP rs16931179. Ref.21
VAR_035102
Natural variant9431P → A
VAR_035103
Natural variant9541Missing in CMD1W.
VAR_035104
Natural variant9751R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. Ref.20 Ref.21
VAR_035105

Secondary structure

1 ........................................................................................ 1134
Helix Strand Turn

Details...

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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).

Checksum: C9B67AA072009EBD
Show »

FASTA1,066116,722
Isoform 3.

Checksum: CBC9C4E86C7B5002
Show »

FASTA22224,904

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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: 2116004] [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: 17974005] [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: 15164054] [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: 15489334] [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: 8440716] [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, 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: 1339348] [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: 12665801] [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: 15229287] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-1133, MASS SPECTROMETRY.
[10]"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.
Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-508, MASS SPECTROMETRY.
Tissue: Hepatocyte.
[11]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; THR-604 AND SER-721, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-692 AND TYR-822, MASS SPECTROMETRY.
[13]"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: 18028034] [Abstract]
Cited for: INTERACTION WITH SYNM.
[14]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-721 AND TYR-822, MASS SPECTROMETRY.
[15]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173 AND LYS-496, MASS SPECTROMETRY.
[18]"Structural basis for amplifying vinculin activation by talin."
Izard T., Vonrhein C.
J. Biol. Chem. 279:27667-27678(2004) [PubMed: 15070891] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 1-258 IN COMPLEX WITH TLN1.
[19]"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: 14702644] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-258 IN COMPLEX WITH TLN1.
[20]"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: 11815424] [Abstract]
Cited for: VARIANTS CMD1W LEU-954 DEL AND TRP-975, CHARACTERIZATION OF VARIANT CMD1W TRP-975.
[21]"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: 16236538] [Abstract]
Cited for: VARIANT CMD1W TRP-975, VARIANTS VAL-934 AND ALA-943.
[22]"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: 16712796] [Abstract]
Cited for: VARIANT CMD1W MET-277.
+Additional computationally mapped references.

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Web resources

GeneReviews
Wikipedia

Vinculin entry

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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.
IPIIPI00291175.
IPI00307162.
IPI00384973.
PIRA35955.
RefSeqNP_003364.1.
NP_054706.1.
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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP18206. 5 interactions.
STRINGP18206.

PTM databases

PhosphoSiteP18206.

2-D gel databases

SWISS-2DPAGEP18206.
Aarhus/Ghent-2DPAGE3708. IEF.
DOSAC-COBS-2DPAGEP18206.
HSC-2DPAGEP18206.
OGPP18206.
REPRODUCTION-2DPAGEIPI00291175.

Proteomic databases

PRIDEP18206.

Genome annotation databases

EnsemblENST00000211998; ENSP00000211998; ENSG00000035403; Homo sapiens. [Genome view]
GeneID7414.
KEGGhsa:7414.
UCSCuc001jwd.1. human.
uc001jwe.1. human.

Organism-specific databases

CTD7414.
GeneCardsGC10P075427.
H-InvDBHIX0008938.
HGNCHGNC:12665. VCL.
HPACAB002453.
HPA002131.
MIM193065. gene.
611407. phenotype.
Orphanet154. Cardiomyopathy, familial dilated.
PharmGKBPA37288.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17973.
HOGENOMHBG358349.
HOVERGENP18206.
InParanoidP18206.
OMAVILHEEA.
OrthoDBEOG90VZ86.
PhylomeDBP18206.

Enzyme and pathway databases

Pathway_Interaction_DBavb3_integrin_pathway. Integrins in angiogenesis.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ReactomeREACT_17044. Muscle contraction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP18206.
BgeeP18206.
CleanExHS_VCL.
GenevestigatorP18206.
GermOnlineENSG00000035403. Homo sapiens.

Family and domain databases

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

Other Resources

NextBio29028.
SOURCESearch...

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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: February 9, 2010
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents