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Protein

Vinculin

Gene

VCL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

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

GO - Biological processi

  • adherens junction assembly Source: BHF-UCL
  • apical junction assembly Source: UniProtKB
  • axon extension Source: Ensembl
  • cell adhesion Source: UniProtKB
  • cell-matrix adhesion Source: BHF-UCL
  • epithelial cell-cell adhesion Source: BHF-UCL
  • lamellipodium assembly Source: UniProtKB
  • morphogenesis of an epithelium Source: BHF-UCL
  • movement of cell or subcellular component Source: UniProtKB
  • muscle contraction Source: Reactome
  • negative regulation of cell migration Source: UniProtKB
  • platelet aggregation Source: UniProtKB
  • platelet degranulation Source: Reactome
  • protein localization to cell surface Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000035403-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SIGNORiP18206.

Names & Taxonomyi

Protein namesi
Recommended name:
Vinculin
Alternative name(s):
Metavinculin
Short name:
MV
Gene namesi
Name:VCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:12665. VCL.

Subcellular locationi

  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cell junctionadherens junction By similarity
  • Cell junctionfocal adhesion By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: 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

GO - Cellular componenti

  • actin cytoskeleton Source: Ensembl
  • adherens junction Source: UniProtKB
  • brush border Source: AgBase
  • cell Source: AgBase
  • cell-cell adherens junction Source: BHF-UCL
  • cell-cell junction Source: UniProtKB
  • cell-substrate junction Source: UniProtKB
  • costamere Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular vesicle Source: UniProtKB
  • fascia adherens Source: Ensembl
  • focal adhesion Source: UniProtKB
  • inner dense plaque of desmosome Source: AgBase
  • membrane raft Source: UniProtKB
  • outer dense plaque of desmosome Source: AgBase
  • plasma membrane Source: AgBase
  • protein complex Source: UniProtKB
  • terminal web Source: AgBase
  • zonula adherens Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Cardiomyopathy, dilated 1W (CMD1W)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:611407
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035104954Missing in CMD1W. 1 Publication1
Natural variantiVAR_035105975R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. 2 PublicationsCorresponds to variant rs121917776dbSNPEnsembl.1
Cardiomyopathy, familial hypertrophic 15 (CMH15)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
See also OMIM:613255
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035101277L → M in CMH15. 1 PublicationCorresponds to variant rs71579353dbSNPEnsembl.1

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

DisGeNETi7414.
MalaCardsiVCL.
MIMi611407. phenotype.
613255. phenotype.
OpenTargetsiENSG00000035403.
Orphaneti154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
PharmGKBiPA37288.

Polymorphism and mutation databases

BioMutaiVCL.
DMDMi21903479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000642522 – 1134VinculinAdd BLAST1133

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei97PhosphoserineBy similarity1
Modified residuei173N6-acetyllysineCombined sources1
Modified residuei260PhosphoserineCombined sources1
Modified residuei272PhosphoserineBy similarity1
Modified residuei275PhosphoserineCombined sources1
Modified residuei288PhosphoserineCombined sources1
Modified residuei290PhosphoserineCombined sources1
Modified residuei346PhosphoserineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei496N6-acetyllysineCombined sources1
Modified residuei537PhosphotyrosineSequence analysis1
Modified residuei574PhosphoserineBy similarity1
Modified residuei579PhosphoserineCombined sources1
Modified residuei600PhosphoserineCombined sources1
Modified residuei604PhosphothreonineCombined sources1
Modified residuei672PhosphothreonineCombined sources1
Modified residuei721PhosphoserineCombined sources1
Modified residuei795PhosphoserineCombined sources1
Modified residuei809PhosphoserineCombined sources1
Modified residuei822PhosphotyrosineCombined sources1
Modified residuei1133Phosphotyrosine; by SRC-type Tyr-kinases1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP18206.
PaxDbiP18206.
PeptideAtlasiP18206.
PRIDEiP18206.

2D gel databases

DOSAC-COBS-2DPAGEP18206.
OGPiP18206.
REPRODUCTION-2DPAGEIPI00291175.
SWISS-2DPAGEP18206.
UCD-2DPAGEP18206.

PTM databases

iPTMnetiP18206.
PhosphoSitePlusiP18206.
SwissPalmiP18206.

Expressioni

Tissue specificityi

Metavinculin is muscle-specific.

Gene expression databases

BgeeiENSG00000035403.
CleanExiHS_VCL.
ExpressionAtlasiP18206. baseline and differential.
GenevisibleiP18206. HS.

Organism-specific databases

HPAiCAB002453.
HPA002131.
HPA063777.

Interactioni

Subunit structurei

Exhibits self-association properties. Interacts with APBB1IP and NRAP (By similarity). Interacts with TLN1. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin (By similarity). Interacts with SYNM. Interacts with SORBS1 (By similarity). Interacts with CTNNA1 (PubMed:26691986).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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.
TEKT1Q969V43EBI-716775,EBI-10180409

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • alpha-catenin binding Source: UniProtKB
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • dystroglycan binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi113257. 109 interactors.
DIPiDIP-35570N.
IntActiP18206. 44 interactors.
MINTiMINT-92846.
STRINGi9606.ENSP00000211998.

Structurei

Secondary structure

11134
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi7 – 13Combined sources7
Helixi16 – 26Combined sources11
Beta strandi28 – 30Combined sources3
Beta strandi33 – 35Combined sources3
Helixi38 – 40Combined sources3
Helixi41 – 64Combined sources24
Helixi68 – 97Combined sources30
Helixi102 – 145Combined sources44
Helixi146 – 150Combined sources5
Helixi154 – 179Combined sources26
Helixi185 – 218Combined sources34
Beta strandi220 – 222Combined sources3
Helixi223 – 248Combined sources26
Helixi253 – 255Combined sources3
Helixi258 – 274Combined sources17
Helixi277 – 284Combined sources8
Helixi294 – 310Combined sources17
Helixi315 – 338Combined sources24
Turni339 – 342Combined sources4
Helixi343 – 345Combined sources3
Helixi347 – 351Combined sources5
Helixi353 – 393Combined sources41
Turni394 – 396Combined sources3
Helixi402 – 420Combined sources19
Helixi425 – 447Combined sources23
Turni448 – 450Combined sources3
Turni455 – 458Combined sources4
Helixi460 – 482Combined sources23
Helixi493 – 505Combined sources13
Helixi514 – 530Combined sources17
Helixi535 – 561Combined sources27
Helixi568 – 577Combined sources10
Helixi579 – 598Combined sources20
Helixi604 – 614Combined sources11
Turni620 – 624Combined sources5
Helixi625 – 650Combined sources26
Helixi655 – 681Combined sources27
Helixi690 – 714Combined sources25
Helixi719 – 743Combined sources25
Helixi746 – 772Combined sources27
Helixi777 – 792Combined sources16
Helixi794 – 806Combined sources13
Turni811 – 813Combined sources3
Helixi814 – 833Combined sources20
Helixi896 – 909Combined sources14
Helixi964 – 977Combined sources14
Helixi986 – 1005Combined sources20
Helixi1009 – 1011Combined sources3
Helixi1012 – 1037Combined sources26
Helixi1043 – 1053Combined sources11
Helixi1056 – 1072Combined sources17
Turni1073 – 1076Combined sources4
Beta strandi1077 – 1079Combined sources3
Helixi1081 – 1113Combined sources33
Beta strandi1114 – 1117Combined sources4
Turni1120 – 1122Combined sources3
Beta strandi1128 – 1130Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP18206.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati259 – 3691Add BLAST111
Repeati370 – 4792Add BLAST110
Repeati480 – 5893Add BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 835N-terminal globular headAdd BLAST834
Regioni168 – 208Talin-interactionBy similarityAdd BLAST41
Regioni259 – 5893 X 112 AA tandem repeatsAdd BLAST331
Regioni836 – 878Linker (Pro-rich)Add BLAST43
Regioni879 – 1134C-terminal tailAdd BLAST256
Regioni1003 – 1046Facilitates phospholipid membrane insertionBy similarityAdd BLAST44
Regioni1120 – 1134Facilitates phospholipid membrane insertionBy similarityAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi837 – 878Pro-richAdd BLAST42

Domaini

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

Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3681. Eukaryota.
ENOG410XSRU. LUCA.
GeneTreeiENSGT00550000074411.
HOGENOMiHOG000007828.
HOVERGENiHBG079758.
InParanoidiP18206.
KOiK05700.
OMAiTPGREQN.
OrthoDBiEOG091G038S.
PhylomeDBiP18206.
TreeFamiTF313686.

Family and domain databases

InterProiIPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 5 hits.
PfamiPF01044. Vinculin. 3 hits.
[Graphical view]
SUPFAMiSSF47220. SSF47220. 6 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

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

« 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 KGWLRDPSAS PGDAGEQAIR
310 320 330 340 350
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGSSPVAM
360 370 380 390 400
QKAQQVSQGL DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG
410 420 430 440 450
GPEGEEQIRG ALAEARKIAE LCDDPKERDD ILRSLGEISA LTSKLADLRR
460 470 480 490 500
QGKGDSPEAR ALAKQVATAL QNLQTKTNRA VANSRPAKAA VHLEGKIEQA
510 520 530 540 550
QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD LLAKCDRVDQ
560 570 580 590 600
LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKARMQEA MTQEVSDVFS
610 620 630 640 650
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGKL GATAEKAAAV
660 670 680 690 700
GTANKSTVEG IQASVKTARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN
710 720 730 740 750
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANIQPQMLV
760 770 780 790 800
AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD
810 820 830 840 850
AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE
860 870 880 890 900
QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM
910 920 930 940 950
AARQLHDEAR KWSSKPGIPA AEVGIGVVAE ADAADAAGFP VPPDMEDDYE
960 970 980 990 1000
PELLLMPSNQ PVNQPILAAA QSLHREATKW SSKGNDIIAA AKRMALLMAE
1010 1020 1030 1040 1050
MSRLVRGGSG TKRALIQCAK DIAKASDEVT RLAKEVAKQC TDKRIRTNLL
1060 1070 1080 1090 1100
QVCERIPTIS TQLKILSTVK ATMLGRTNIS DEESEQATEM LVHNAQNLMQ
1110 1120 1130
SVKETVREAE AASIKIRTDA GFTLRWVRKT PWYQ
Length:1,134
Mass (Da):123,799
Last modified:January 23, 2007 - v4
Checksum:iBFBD687DA836B0FA
GO
Isoform 1 (identifier: P18206-2) [UniParc]FASTAAdd to basket
Also known as: Vinculin

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

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

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

Note: No experimental confirmation available.
Show »
Length:222
Mass (Da):24,904
Checksum:iCBC9C4E86C7B5002
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037667234V → L.1 PublicationCorresponds to variant rs17853882dbSNPEnsembl.1
Natural variantiVAR_035101277L → M in CMH15. 1 PublicationCorresponds to variant rs71579353dbSNPEnsembl.1
Natural variantiVAR_035102934A → V.1 PublicationCorresponds to variant rs16931179dbSNPEnsembl.1
Natural variantiVAR_035103943P → A.1 PublicationCorresponds to variant rs71579375dbSNPEnsembl.1
Natural variantiVAR_035104954Missing in CMD1W. 1 Publication1
Natural variantiVAR_035105975R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. 2 PublicationsCorresponds to variant rs121917776dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0118571 – 73Missing in isoform 3. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_011858262 – 295DTEAM…PGDAG → VRVLSGEISKIPNSPWLGVL IGTCLILYLVIFVA in isoform 3. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_011859296 – 1134Missing in isoform 3. 1 PublicationAdd BLAST839
Alternative sequenceiVSP_006731916 – 983Missing in isoform 1. 2 PublicationsAdd BLAST68

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Vinculin entry

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi113257. 109 interactors.
DIPiDIP-35570N.
IntActiP18206. 44 interactors.
MINTiMINT-92846.
STRINGi9606.ENSP00000211998.

PTM databases

iPTMnetiP18206.
PhosphoSitePlusiP18206.
SwissPalmiP18206.

Polymorphism and mutation databases

BioMutaiVCL.
DMDMi21903479.

2D gel databases

DOSAC-COBS-2DPAGEP18206.
OGPiP18206.
REPRODUCTION-2DPAGEIPI00291175.
SWISS-2DPAGEP18206.
UCD-2DPAGEP18206.

Proteomic databases

EPDiP18206.
PaxDbiP18206.
PeptideAtlasiP18206.
PRIDEiP18206.

Protocols and materials databases

DNASUi7414.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7414.
DisGeNETi7414.
GeneCardsiVCL.
GeneReviewsiVCL.
H-InvDBHIX0170429.
HGNCiHGNC:12665. VCL.
HPAiCAB002453.
HPA002131.
HPA063777.
MalaCardsiVCL.
MIMi193065. gene.
611407. phenotype.
613255. phenotype.
neXtProtiNX_P18206.
OpenTargetsiENSG00000035403.
Orphaneti154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
PharmGKBiPA37288.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3681. Eukaryota.
ENOG410XSRU. LUCA.
GeneTreeiENSGT00550000074411.
HOGENOMiHOG000007828.
HOVERGENiHBG079758.
InParanoidiP18206.
KOiK05700.
OMAiTPGREQN.
OrthoDBiEOG091G038S.
PhylomeDBiP18206.
TreeFamiTF313686.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000035403-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SIGNORiP18206.

Miscellaneous databases

ChiTaRSiVCL. human.
EvolutionaryTraceiP18206.
GeneWikiiVinculin.
GenomeRNAii7414.
PROiP18206.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000035403.
CleanExiHS_VCL.
ExpressionAtlasiP18206. baseline and differential.
GenevisibleiP18206. HS.

Family and domain databases

InterProiIPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 5 hits.
PfamiPF01044. Vinculin. 3 hits.
[Graphical view]
SUPFAMiSSF47220. SSF47220. 6 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVINC_HUMAN
AccessioniPrimary (citable) accession number: P18206
Secondary accession number(s): Q16450
, Q5SWX2, Q7Z3B8, Q8IXU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 193 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.