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UniProtKB - P18206 (VINC_HUMAN)

Protein

Vinculin

Gene

VCL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • dystroglycan binding Source: UniProtKB
  • structural molecule activity Source: InterPro
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActin-binding
Biological processCell adhesion

Enzyme and pathway databases

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000035403.16
HGNCiHGNC:12665 VCL
MIMi193065 gene
neXtProtiNX_P18206

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 dbSNP:rs121917776EnsemblClinVar.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 dbSNP:rs71579353EnsemblClinVar.1

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

DisGeNETi7414
GeneReviewsiVCL
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
ChainiPRO_00000642521 – 1134VinculinAdd BLAST1134

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 residuei537PhosphotyrosineCurated1
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
ProteomicsDBi53553
53554 [P18206-2]
53555 [P18206-3]

2D gel databases

DOSAC-COBS-2DPAGEiP18206
OGPiP18206
REPRODUCTION-2DPAGEiIPI00291175
SWISS-2DPAGEiP18206
UCD-2DPAGEiP18206

PTM databases

iPTMnetiP18206
PhosphoSitePlusiP18206
SwissPalmiP18206

Expressioni

Tissue specificityi

Metavinculin is muscle-specific.

Gene expression databases

BgeeiENSG00000035403 Expressed in 244 organ(s), highest expression level in myometrium
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). Binds to ACTN4; this interaction triggers conformational changes (PubMed:15988023).By similarity5 Publications

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi113257, 115 interactors
CORUMiP18206
DIPiDIP-35570N
ELMiP18206
IntActiP18206, 50 interactors
MINTiP18206
STRINGi9606.ENSP00000211998

Structurei

Secondary structure

11134
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP18206
SMRiP18206
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18206

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 835N-terminal globular head1 PublicationAdd BLAST835
Regioni168 – 208Talin-interactionBy similarityAdd BLAST41
Regioni259 – 5893 X 112 AA tandem repeatsSequence analysisAdd BLAST331
Regioni741 – 764Interaction with ACTN4Combined sources1 PublicationAdd BLAST24
Regioni836 – 878Linker (Pro-rich)1 PublicationAdd BLAST43
Regioni879 – 1134C-terminal tail1 PublicationAdd 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-richPROSITE-ProRule annotationAdd 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

InterProiView protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR017997 Vinculin
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS
PANTHERiPTHR18914 PTHR18914, 3 hits
PTHR18914:SF1 PTHR18914:SF1, 3 hits
PfamiView protein in Pfam
PF01044 Vinculin, 3 hits
SUPFAMiSSF47220 SSF47220, 6 hits
PROSITEiView protein in PROSITE
PS00663 VINCULIN_1, 1 hit
PS00664 VINCULIN_2, 3 hits

Sequences (3+)i

Sequence statusi: Complete.

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

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A096LPE1A0A096LPE1_HUMAN
Vinculin
VCL
57Annotation score:

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037667234V → L1 PublicationCorresponds to variant dbSNP:rs17853882Ensembl.1
Natural variantiVAR_035101277L → M in CMH15. 1 PublicationCorresponds to variant dbSNP:rs71579353EnsemblClinVar.1
Natural variantiVAR_035102934A → V1 PublicationCorresponds to variant dbSNP:rs16931179EnsemblClinVar.1
Natural variantiVAR_035103943P → A1 PublicationCorresponds to variant dbSNP:rs71579375EnsemblClinVar.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 dbSNP:rs121917776EnsemblClinVar.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

Similar proteinsi

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[»]
5O2QNMR-A854-870[»]
6FUYX-ray3.00A1-1134[»]
ProteinModelPortaliP18206
SMRiP18206
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113257, 115 interactors
CORUMiP18206
DIPiDIP-35570N
ELMiP18206
IntActiP18206, 50 interactors
MINTiP18206
STRINGi9606.ENSP00000211998

PTM databases

iPTMnetiP18206
PhosphoSitePlusiP18206
SwissPalmiP18206

Polymorphism and mutation databases

BioMutaiVCL
DMDMi21903479

2D gel databases

DOSAC-COBS-2DPAGEiP18206
OGPiP18206
REPRODUCTION-2DPAGEiIPI00291175
SWISS-2DPAGEiP18206
UCD-2DPAGEiP18206

Proteomic databases

EPDiP18206
PaxDbiP18206
PeptideAtlasiP18206
PRIDEiP18206
ProteomicsDBi53553
53554 [P18206-2]
53555 [P18206-3]

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
EuPathDBiHostDB:ENSG00000035403.16
GeneCardsiVCL
GeneReviewsiVCL
H-InvDBiHIX0170429
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

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
PROiPR:P18206
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000035403 Expressed in 244 organ(s), highest expression level in myometrium
CleanExiHS_VCL
ExpressionAtlasiP18206 baseline and differential
GenevisibleiP18206 HS

Family and domain databases

InterProiView protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR017997 Vinculin
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS
PANTHERiPTHR18914 PTHR18914, 3 hits
PTHR18914:SF1 PTHR18914:SF1, 3 hits
PfamiView protein in Pfam
PF01044 Vinculin, 3 hits
SUPFAMiSSF47220 SSF47220, 6 hits
PROSITEiView protein in PROSITE
PS00663 VINCULIN_1, 1 hit
PS00664 VINCULIN_2, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiVINC_HUMAN
AccessioniPrimary (citable) accession number: P18206
Secondary accession number(s): Q16450
, Q5SWX2, Q7Z3B8, Q8IXU7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 209 of the entry and version 4 of the sequence. See 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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