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P18206

- VINC_HUMAN

UniProt

P18206 - VINC_HUMAN

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Protein
Vinculin
Gene
VCL
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

GO - Molecular functioni

  1. actin binding Source: BHF-UCL
  2. alpha-catenin binding Source: UniProtKB
  3. beta-catenin binding Source: BHF-UCL
  4. cadherin binding Source: BHF-UCL
  5. dystroglycan binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. structural molecule activity Source: InterPro

GO - Biological processi

  1. adherens junction assembly Source: BHF-UCL
  2. apical junction assembly Source: UniProtKB
  3. blood coagulation Source: Reactome
  4. cell adhesion Source: UniProtKB
  5. cell-matrix adhesion Source: BHF-UCL
  6. cellular component movement Source: UniProtKB
  7. epithelial cell-cell adhesion Source: BHF-UCL
  8. lamellipodium assembly Source: UniProtKB
  9. morphogenesis of an epithelium Source: BHF-UCL
  10. muscle contraction Source: Reactome
  11. negative regulation of cell migration Source: UniProtKB
  12. platelet activation Source: Reactome
  13. platelet degranulation Source: Reactome
  14. protein localization to cell surface Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_20558. Smooth Muscle Contraction.

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
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:12665. VCL.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: InterPro
  2. adherens junction Source: UniProtKB
  3. cell-cell adherens junction Source: BHF-UCL
  4. cell-cell junction Source: UniProtKB
  5. cell-substrate junction Source: UniProtKB
  6. costamere Source: UniProtKB
  7. cytoskeleton Source: UniProtKB
  8. cytosol Source: Reactome
  9. extracellular region Source: Reactome
  10. extracellular vesicular exosome Source: UniProt
  11. fascia adherens Source: Ensembl
  12. focal adhesion Source: UniProtKB
  13. plasma membrane Source: UniProtKB-SubCell
  14. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti954 – 9541Missing in CMD1W. 1 Publication
VAR_035104
Natural varianti975 – 9751R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. 2 Publications
VAR_035105
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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti277 – 2771L → M in CMH15. 1 Publication
VAR_035101

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11341133Vinculin
PRO_0000064252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731N6-acetyllysine1 Publication
Modified residuei288 – 2881Phosphoserine1 Publication
Modified residuei290 – 2901Phosphoserine3 Publications
Modified residuei346 – 3461Phosphoserine1 Publication
Modified residuei434 – 4341Phosphoserine1 Publication
Modified residuei496 – 4961N6-acetyllysine1 Publication
Modified residuei537 – 5371Phosphotyrosine Reviewed prediction
Modified residuei721 – 7211Phosphoserine4 Publications
Modified residuei822 – 8221Phosphotyrosine1 Publication
Modified residuei1133 – 11331Phosphotyrosine; by SRC-type Tyr-kinases1 Publication

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

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP18206.
PaxDbiP18206.
PRIDEiP18206.

2D gel databases

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

PTM databases

PhosphoSiteiP18206.

Expressioni

Tissue specificityi

Metavinculin is muscle-specific.

Gene expression databases

ArrayExpressiP18206.
BgeeiP18206.
CleanExiHS_VCL.
GenevestigatoriP18206.

Organism-specific databases

HPAiCAB002453.
HPA002131.

Interactioni

Subunit structurei

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.1 Publication

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.

Protein-protein interaction databases

BioGridi113257. 83 interactions.
DIPiDIP-35570N.
IntActiP18206. 19 interactions.
MINTiMINT-92846.
STRINGi9606.ENSP00000211998.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63
Helixi7 – 137
Helixi16 – 2611
Beta strandi28 – 303
Beta strandi33 – 353
Helixi38 – 403
Helixi41 – 6424
Helixi68 – 9730
Helixi102 – 14544
Helixi146 – 1505
Helixi154 – 17926
Helixi185 – 21834
Beta strandi220 – 2223
Helixi223 – 24826
Helixi253 – 2553
Helixi258 – 27417
Helixi277 – 2848
Helixi294 – 31017
Helixi315 – 33824
Turni339 – 3424
Helixi343 – 3453
Helixi347 – 3515
Helixi353 – 39341
Turni394 – 3963
Helixi402 – 42019
Helixi425 – 44723
Turni448 – 4503
Turni455 – 4584
Helixi460 – 48223
Helixi493 – 50513
Helixi514 – 53017
Helixi535 – 56127
Helixi568 – 57710
Helixi579 – 59820
Helixi604 – 61411
Turni620 – 6245
Helixi625 – 65026
Helixi655 – 68127
Helixi690 – 71425
Helixi719 – 74325
Helixi746 – 77227
Helixi777 – 79216
Helixi794 – 80613
Turni811 – 8133
Helixi814 – 83320
Helixi896 – 90914
Helixi964 – 97714
Helixi986 – 100520
Helixi1012 – 103726
Helixi1043 – 105311
Helixi1056 – 107217
Turni1073 – 10764
Beta strandi1077 – 10793
Helixi1081 – 111333
Beta strandi1114 – 11174
Beta strandi1119 – 11213
Beta strandi1128 – 11303

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
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[»]
ProteinModelPortaliP18206.
SMRiP18206. Positions 1-258, 957-1134.

Miscellaneous databases

EvolutionaryTraceiP18206.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati259 – 3691111
Add
BLAST
Repeati370 – 4791102
Add
BLAST
Repeati480 – 5891103
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 835834N-terminal globular head
Add
BLAST
Regioni168 – 20841Talin-interaction By similarity
Add
BLAST
Regioni259 – 5893313 X 112 AA tandem repeats
Add
BLAST
Regioni836 – 87843Linker (Pro-rich)
Add
BLAST
Regioni879 – 1134256C-terminal tail
Add
BLAST
Regioni1003 – 104644Facilitates phospholipid membrane insertion By similarity
Add
BLAST
Regioni1120 – 113415Facilitates phospholipid membrane insertion By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi837 – 87842Pro-rich
Add
BLAST

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG329927.
HOGENOMiHOG000007828.
HOVERGENiHBG079758.
InParanoidiP18206.
KOiK05700.
OMAiLTHQVHR.
OrthoDBiEOG73NG2V.
PhylomeDBiP18206.
TreeFamiTF313686.

Family and domain databases

InterProiIPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PfamiPF01044. Vinculin. 3 hits.
[Graphical view]
PRINTSiPR00806. VINCULIN.
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. Align

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

MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA     50
VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY 100
SVPARDYLID GSRGILSGTS DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV 150
VETMEDLVTY TKNLGPGMTK MAKMIDERQQ ELTHQEHRVM LVNSMNTVKE 200
LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE INEIIRVLQL 250
TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPSAS PGDAGEQAIR 300
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGSSPVAM 350
QKAQQVSQGL DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG 400
GPEGEEQIRG ALAEARKIAE LCDDPKERDD ILRSLGEISA LTSKLADLRR 450
QGKGDSPEAR ALAKQVATAL QNLQTKTNRA VANSRPAKAA VHLEGKIEQA 500
QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD LLAKCDRVDQ 550
LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKARMQEA MTQEVSDVFS 600
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGKL GATAEKAAAV 650
GTANKSTVEG IQASVKTARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN 700
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANIQPQMLV 750
AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD 800
AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE 850
QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM 900
AARQLHDEAR KWSSKPGIPA AEVGIGVVAE ADAADAAGFP VPPDMEDDYE 950
PELLLMPSNQ PVNQPILAAA QSLHREATKW SSKGNDIIAA AKRMALLMAE 1000
MSRLVRGGSG TKRALIQCAK DIAKASDEVT RLAKEVAKQC TDKRIRTNLL 1050
QVCERIPTIS TQLKILSTVK ATMLGRTNIS DEESEQATEM LVHNAQNLMQ 1100
SVKETVREAE AASIKIRTDA GFTLRWVRKT PWYQ 1134
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti234 – 2341V → L.1 Publication
Corresponds to variant rs17853882 [ dbSNP | Ensembl ].
VAR_037667
Natural varianti277 – 2771L → M in CMH15. 1 Publication
VAR_035101
Natural varianti934 – 9341A → V.1 Publication
Corresponds to variant rs16931179 [ dbSNP | Ensembl ].
VAR_035102
Natural varianti943 – 9431P → A.1 Publication
VAR_035103
Natural varianti954 – 9541Missing in CMD1W. 1 Publication
VAR_035104
Natural varianti975 – 9751R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. 2 Publications
VAR_035105

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373Missing in isoform 3.
VSP_011857Add
BLAST
Alternative sequencei262 – 29534DTEAM…PGDAG → VRVLSGEISKIPNSPWLGVL IGTCLILYLVIFVA in isoform 3.
VSP_011858Add
BLAST
Alternative sequencei296 – 1134839Missing in isoform 3.
VSP_011859Add
BLAST
Alternative sequencei916 – 98368Missing in isoform 1.
VSP_006731Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc001jwd.3. human. [P18206-1]
uc001jwe.3. human. [P18206-2]

Polymorphism databases

DMDMi21903479.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Vinculin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7340.1. [P18206-2 ]
CCDS7341.1. [P18206-1 ]
PIRi A35955.
RefSeqi NP_003364.1. NM_003373.3. [P18206-2 ]
NP_054706.1. NM_014000.2. [P18206-1 ]
UniGenei Hs.643896.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RKC X-ray 2.70 A 1-258 [» ]
1RKE X-ray 2.35 A 1-258 [» ]
B 882-1134 [» ]
1SYQ X-ray 2.42 A 1-258 [» ]
1TR2 X-ray 2.90 A/B 1-1134 [» ]
1YDI X-ray 1.80 A 1-258 [» ]
2GWW X-ray 2.72 A 1-258 [» ]
2HSQ X-ray 3.97 A 1-258 [» ]
2IBF X-ray 3.20 A 1-258 [» ]
3H2U X-ray 2.75 A/C 879-1134 [» ]
3H2V X-ray 2.90 A/B/C/D 879-1134 [» ]
3MYI X-ray 2.20 A 959-1130 [» ]
3RF3 X-ray 1.61 A/B 1-258 [» ]
3S90 X-ray 1.97 A/B 1-252 [» ]
3TJ5 X-ray 1.99 A 1-255 [» ]
3TJ6 X-ray 2.76 A 1-257 [» ]
3VF0 X-ray 2.54 A 856-1134 [» ]
4DJ9 X-ray 2.25 A 1-258 [» ]
4EHP X-ray 2.66 A 1-252 [» ]
4LN2 X-ray 1.00 B 857-867 [» ]
4LNP X-ray 1.41 B 870-879 [» ]
ProteinModelPortali P18206.
SMRi P18206. Positions 1-258, 957-1134.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113257. 83 interactions.
DIPi DIP-35570N.
IntActi P18206. 19 interactions.
MINTi MINT-92846.
STRINGi 9606.ENSP00000211998.

PTM databases

PhosphoSitei P18206.

Polymorphism databases

DMDMi 21903479.

2D gel databases

DOSAC-COBS-2DPAGE P18206.
OGPi P18206.
REPRODUCTION-2DPAGE IPI00291175.
SWISS-2DPAGE P18206.
UCD-2DPAGE P18206.

Proteomic databases

MaxQBi P18206.
PaxDbi P18206.
PRIDEi P18206.

Protocols and materials databases

DNASUi 7414.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000211998 ; ENSP00000211998 ; ENSG00000035403 . [P18206-1 ]
ENST00000372755 ; ENSP00000361841 ; ENSG00000035403 . [P18206-2 ]
GeneIDi 7414.
KEGGi hsa:7414.
UCSCi uc001jwd.3. human. [P18206-1 ]
uc001jwe.3. human. [P18206-2 ]

Organism-specific databases

CTDi 7414.
GeneCardsi GC10P075757.
GeneReviewsi VCL.
H-InvDB HIX0170429.
HGNCi HGNC:12665. VCL.
HPAi CAB002453.
HPA002131.
MIMi 193065. gene.
611407. phenotype.
613255. phenotype.
neXtProti NX_P18206.
Orphaneti 154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
PharmGKBi PA37288.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG329927.
HOGENOMi HOG000007828.
HOVERGENi HBG079758.
InParanoidi P18206.
KOi K05700.
OMAi LTHQVHR.
OrthoDBi EOG73NG2V.
PhylomeDBi P18206.
TreeFami TF313686.

Enzyme and pathway databases

Reactomei REACT_20558. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSi VCL. human.
EvolutionaryTracei P18206.
GeneWikii Vinculin.
GenomeRNAii 7414.
NextBioi 29028.
PROi P18206.
SOURCEi Search...

Gene expression databases

ArrayExpressi P18206.
Bgeei P18206.
CleanExi HS_VCL.
Genevestigatori P18206.

Family and domain databases

InterProi IPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view ]
PANTHERi PTHR18914. PTHR18914. 1 hit.
Pfami PF01044. Vinculin. 3 hits.
[Graphical view ]
PRINTSi PR00806. VINCULIN.
SUPFAMi SSF47220. SSF47220. 6 hits.
PROSITEi PS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
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Publicationsi

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  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Endothelial cell.
  2. 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.
    , 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. 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. 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.

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: September 3, 2014
This is version 167 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

External Data

Dasty 3

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