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P18206

- VINC_HUMAN

UniProt

P18206 - VINC_HUMAN

Protein

Vinculin

Gene

VCL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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 1 Publication. Cell junctionadherens junction 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell junctionfocal adhesion 1 Publication
    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.By similarity

    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

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 11Removed
    Chaini2 – 11341133VinculinPRO_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 – 5371PhosphotyrosineSequence Analysis
    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.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

    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.By similarity3 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.

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    1134
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18206.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 835834N-terminal globular headAdd
    BLAST
    Regioni168 – 20841Talin-interactionBy similarityAdd
    BLAST
    Regioni259 – 5893313 X 112 AA tandem repeatsAdd
    BLAST
    Regioni836 – 87843Linker (Pro-rich)Add
    BLAST
    Regioni879 – 1134256C-terminal tailAdd
    BLAST
    Regioni1003 – 104644Facilitates phospholipid membrane insertionBy similarityAdd
    BLAST
    Regioni1120 – 113415Facilitates phospholipid membrane insertionBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi837 – 87842Pro-richAdd
    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

    Belongs to the vinculin/alpha-catenin family.Curated

    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. 1 PublicationVSP_011857Add
    BLAST
    Alternative sequencei262 – 29534DTEAM…PGDAG → VRVLSGEISKIPNSPWLGVL IGTCLILYLVIFVA in isoform 3. 1 PublicationVSP_011858Add
    BLAST
    Alternative sequencei296 – 1134839Missing in isoform 3. 1 PublicationVSP_011859Add
    BLAST
    Alternative sequencei916 – 98368Missing in isoform 1. 2 PublicationsVSP_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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 168 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