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P12003

- VINC_CHICK

UniProt

P12003 - VINC_CHICK

Protein

Vinculin

Gene

VCL

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (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.3 Publications

    GO - Molecular functioni

    1. alpha-catenin binding Source: BHF-UCL
    2. beta-catenin binding Source: BHF-UCL
    3. cadherin binding Source: BHF-UCL
    4. protein binding Source: IntAct
    5. structural molecule activity Source: InterPro

    GO - Biological processi

    1. adherens junction assembly Source: BHF-UCL
    2. apical junction assembly Source: Ensembl
    3. epithelial cell-cell adhesion Source: BHF-UCL
    4. lamellipodium assembly Source: UniProtKB
    5. morphogenesis of an epithelium Source: BHF-UCL
    6. protein localization to cell surface Source: Ensembl
    7. regulation of cell migration Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vinculin
    Alternative name(s):
    Metavinculin
    Gene namesi
    Name:VCL
    Synonyms:VINC1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side
    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.

    GO - Cellular componenti

    1. actin cytoskeleton Source: InterPro
    2. adherens junction Source: UniProtKB
    3. cell-cell junction Source: UniProtKB
    4. costamere Source: UniProtKB
    5. fascia adherens Source: Ensembl
    6. focal adhesion Source: UniProtKB
    7. mitochondrial inner membrane Source: UniProtKB
    8. plasma membrane Source: UniProtKB-SubCell
    9. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1001Y → F: Some reduction of phosphorylation levels in platelets. Little change in cell spreading. Complete loss of phosphorylation. No change in subcellular location nor on in vitro actin binding. 40% decrease in cell spreading; when associated with F-1134. 1 Publication
    Mutagenesisi160 – 1601Y → F: No change of phosphorylation levels in platelets. 1 Publication
    Mutagenesisi537 – 5371Y → F: No change of phosphorylation levels in platelets. 1 Publication
    Mutagenesisi692 – 6921Y → F: No change of phosphorylation levels in platelets. 1 Publication
    Mutagenesisi822 – 8221Y → F: No change of phosphorylation levels in platelets. 1 Publication
    Mutagenesisi1134 – 11341Y → F: Greatly reduced phosphorylation levels in platelets. Little change in cell spreading. Complete loss of phosphorylation. No change in subcellular location nor on in vitro actin binding. 40% decrease in cell spreading; when associated with F-100. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 11351134VinculinPRO_0000064255Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei100 – 1001Phosphotyrosine1 Publication
    Modified residuei537 – 5371PhosphotyrosineSequence Analysis
    Modified residuei822 – 8221PhosphotyrosineSequence Analysis
    Modified residuei1134 – 11341Phosphotyrosine; by SRC-type Tyr-kinases1 Publication

    Post-translational modificationi

    Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1134 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques.1 Publication
    Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP12003.
    PRIDEiP12003.

    Expressioni

    Tissue specificityi

    Isoform Metavinculin is muscle-specific.

    Interactioni

    Subunit structurei

    Exhibits self-association properties. Interacts with APBB1IP, NRAP and 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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTN1P05094-25EBI-1039563,EBI-6049246
    PXNP490245EBI-1039563,EBI-2896280
    Tln1P260393EBI-1039563,EBI-1039593From a different organism.
    VASPP505522EBI-1039563,EBI-748201From a different organism.

    Protein-protein interaction databases

    BioGridi676671. 2 interactions.
    DIPiDIP-35191N.
    IntActiP12003. 12 interactions.
    STRINGi9031.ENSGALP00000008131.

    Structurei

    Secondary structure

    1
    1135
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2822
    Turni29 – 324
    Beta strandi33 – 353
    Helixi41 – 6323
    Helixi68 – 736
    Helixi75 – 9723
    Helixi102 – 14645
    Helixi148 – 1503
    Helixi154 – 18128
    Helixi185 – 21531
    Beta strandi218 – 2214
    Helixi222 – 24928
    Helixi253 – 2553
    Helixi256 – 27520
    Helixi277 – 2859
    Turni292 – 2954
    Helixi296 – 31116
    Helixi318 – 33821
    Turni339 – 3424
    Helixi347 – 39549
    Helixi405 – 42117
    Helixi428 – 45124
    Helixi457 – 48226
    Helixi493 – 50513
    Helixi516 – 53116
    Helixi535 – 55622
    Helixi567 – 59832
    Helixi604 – 61411
    Helixi622 – 65029
    Helixi654 – 68128
    Turni682 – 6843
    Helixi689 – 71426
    Helixi719 – 73921
    Beta strandi742 – 7443
    Turni746 – 7483
    Helixi752 – 77221
    Helixi777 – 80226
    Beta strandi803 – 8064
    Turni809 – 8135
    Helixi814 – 8174
    Turni818 – 8236
    Helixi824 – 83512
    Beta strandi887 – 8904
    Helixi892 – 8954
    Helixi897 – 90913
    Helixi987 – 100519
    Helixi1010 – 10123
    Helixi1013 – 104028
    Helixi1044 – 105411
    Helixi1057 – 107418
    Beta strandi1075 – 10773
    Helixi1082 – 111332
    Helixi1121 – 11233

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QKRX-ray1.80A/B879-1135[»]
    1ST6X-ray3.10A1-1135[»]
    1T01X-ray2.06A1-254[»]
    1U6HX-ray2.38A1-259[»]
    1XWJX-ray2.60A2-259[»]
    1ZVZX-ray1.80A2-259[»]
    1ZW2X-ray2.10A2-259[»]
    1ZW3X-ray3.30A2-259[»]
    2GDCX-ray2.74A1-266[»]
    3ZDLX-ray2.30A1-259[»]
    4E17X-ray2.30A1-259[»]
    4E18X-ray2.40A1-259[»]
    DisProtiDP00556.
    ProteinModelPortaliP12003.
    SMRiP12003. Positions 1-254.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12003.

    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 headBy similarityAdd
    BLAST
    Regioni168 – 20841Talin-interactionAdd
    BLAST
    Regioni259 – 5893313 X 112 AA tandem repeatsAdd
    BLAST
    Regioni836 – 87843Linker (Pro-rich)By similarityAdd
    BLAST
    Regioni879 – 1135257C-terminal tailBy similarityAdd
    BLAST
    Regioni1004 – 104744Facilitates phospholipid membrane insertionBy similarityAdd
    BLAST
    Regioni1121 – 113515Facilitates 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 By similarity.By similarity
    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. 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 By similarity.By similarity

    Sequence similaritiesi

    Belongs to the vinculin/alpha-catenin family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG329927.
    HOGENOMiHOG000007828.
    HOVERGENiHBG079758.
    InParanoidiP12003.
    KOiK05700.
    PhylomeDBiP12003.

    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. 8 hits.
    PROSITEiPS00663. VINCULIN_1. 1 hit.
    PS00664. VINCULIN_2. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: P12003-2) [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 TAPVSAVQAA     50
    VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY 100
    SVPARDYLID GSRGILSGTS DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV 150
    VETMEDLVTY TKNLGPGMTK MAKMIDERQQ ELTHQEHRVM LVNSMNTVKE 200
    LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE INEIIRVLQL 250
    TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR 300
    QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM 350
    QKAQQVSQGL DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG 400
    GSEGEEHIRG IMSEARKVAE LCEEPKERDD ILRSLGEISA LTAKLSDLRR 450
    HGKGDSPEAR ALAKQIATSL QNLQSKTNRA VANTRPVKAA VHLEGKIEQA 500
    QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD LLAKCDRVDQ 550
    LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS 600
    DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV 650
    GTANKTTVEG IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN 700
    QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANMQPQMLV 750
    AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD 800
    AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE 850
    HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM 900
    AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY 950
    EPELLLMPTN QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA 1000
    EMSRLVRGGS GNKRALIQCA KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL 1050
    LQVCERIPTI STQLKILSTV KATMLGRTNI SDEESEQATE MLVHNAQNLM 1100
    QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ 1135
    Length:1,135
    Mass (Da):124,560
    Last modified:January 23, 2007 - v4
    Checksum:i28CC2699C9511058
    GO
    Isoform 1 (identifier: P12003-1) [UniParc]FASTAAdd to Basket

    Also known as: Vinculin

    The sequence of this isoform differs from the canonical sequence as follows:
         916-984: Missing.

    Show »
    Length:1,066
    Mass (Da):116,999
    Checksum:i6F585201260BA47F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti442 – 4476TAKLSD → QLSCQI(PubMed:2497736)Curated
    Sequence conflicti442 – 4476TAKLSD → QLSCQI in CAA68412. (PubMed:3117046)Curated
    Sequence conflicti701 – 7011Q → H(PubMed:2497736)Curated
    Sequence conflicti701 – 7011Q → H in CAA68412. (PubMed:3117046)Curated
    Sequence conflicti880 – 8801E → K in CAA68412. (PubMed:3117046)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei916 – 98469Missing in isoform 1. 2 PublicationsVSP_010772Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04126 mRNA. Translation: AAA49136.1.
    M87837 Genomic DNA. Translation: AAA49135.1.
    Y00312 mRNA. Translation: CAA68412.1.
    PIRiA31346. A29997.
    RefSeqiNP_990772.1. NM_205441.1. [P12003-1]
    UniGeneiGga.698.

    Genome annotation databases

    GeneIDi396422.
    KEGGigga:396422.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04126 mRNA. Translation: AAA49136.1 .
    M87837 Genomic DNA. Translation: AAA49135.1 .
    Y00312 mRNA. Translation: CAA68412.1 .
    PIRi A31346. A29997.
    RefSeqi NP_990772.1. NM_205441.1. [P12003-1 ]
    UniGenei Gga.698.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QKR X-ray 1.80 A/B 879-1135 [» ]
    1ST6 X-ray 3.10 A 1-1135 [» ]
    1T01 X-ray 2.06 A 1-254 [» ]
    1U6H X-ray 2.38 A 1-259 [» ]
    1XWJ X-ray 2.60 A 2-259 [» ]
    1ZVZ X-ray 1.80 A 2-259 [» ]
    1ZW2 X-ray 2.10 A 2-259 [» ]
    1ZW3 X-ray 3.30 A 2-259 [» ]
    2GDC X-ray 2.74 A 1-266 [» ]
    3ZDL X-ray 2.30 A 1-259 [» ]
    4E17 X-ray 2.30 A 1-259 [» ]
    4E18 X-ray 2.40 A 1-259 [» ]
    DisProti DP00556.
    ProteinModelPortali P12003.
    SMRi P12003. Positions 1-254.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676671. 2 interactions.
    DIPi DIP-35191N.
    IntActi P12003. 12 interactions.
    STRINGi 9031.ENSGALP00000008131.

    Proteomic databases

    PaxDbi P12003.
    PRIDEi P12003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396422.
    KEGGi gga:396422.

    Organism-specific databases

    CTDi 7414.

    Phylogenomic databases

    eggNOGi NOG329927.
    HOGENOMi HOG000007828.
    HOVERGENi HBG079758.
    InParanoidi P12003.
    KOi K05700.
    PhylomeDBi P12003.

    Miscellaneous databases

    EvolutionaryTracei P12003.
    NextBioi 20816463.
    PROi P12003.

    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. 8 hits.
    PROSITEi PS00663. VINCULIN_1. 1 hit.
    PS00664. VINCULIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA-derived sequence of chicken embryo vinculin."
      Coutu M.D., Craig S.W.
      Proc. Natl. Acad. Sci. U.S.A. 85:8535-8539(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryo.
    2. "Primary sequence and domain structure of chicken vinculin."
      Price G.J., Jones P., Davison M.D., Patel B., Bendori R., Geiger B., Critchley D.R.
      Biochem. J. 259:453-461(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryo.
    3. "Chicken vinculin and meta-vinculin are derived from a single gene by alternative splicing of a 207-base pair exon unique to meta-vinculin."
      Byrne B.J., Kaczorowski Y.J., Coutu M.D., Craig S.W.
      J. Biol. Chem. 267:12845-12850(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
    4. "Isolation and characterization of a vinculin cDNA from chick-embryo fibroblasts."
      Price G.J., Jones P., Davison M.D., Patel B., Eperon I.C., Critchley D.R.
      Biochem. J. 245:595-603(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-881.
      Tissue: Embryo.
    5. "The cytoskeletal protein vinculin is acylated by myristic acid."
      Kellie S., Wigglesworth N.M.
      FEBS Lett. 213:428-432(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION.
    6. "Identification of a talin binding site in the cytoskeletal protein vinculin."
      Jones P., Jackson P., Price G.J., Patel B., Ohanion V., Lear A.L., Critchley D.R.
      J. Cell Biol. 109:2917-2927(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: TALIN INTERACTION DOMAIN.
    7. "Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks."
      Luo G., Herrera A.H., Horowits R.
      Biochemistry 38:6135-6143(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NRAP.
    8. "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-100 AND TYR-1134, FUNCTION, MUTAGENESIS OF TYR-100; TYR-160; TYR-537; TYR-692; TYR-822 AND TYR-1134.
    9. "Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner."
      le Duc Q., Shi Q., Blonk I., Sonnenberg A., Wang N., Leckband D., de Rooij J.
      J. Cell Biol. 189:1107-1115(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin."
      Peng X., Cuff L.E., Lawton C.D., DeMali K.A.
      J. Cell Sci. 123:567-577(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1.
    11. "Crystal structure of the vinculin tail suggests a pathway for activation."
      Bakolitsa C., de Pereda J.M., Bagshaw C.R., Critchley D.R., Liddington R.C.
      Cell 99:603-613(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 881-1135 OF ISOFORM 1.
    12. "RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover."
      Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R., Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.
      J. Biol. Chem. 288:8238-8249(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-259 IN COMPLEX WITH APBB1IP, INTERACTION WITH TLN1 AND APBB1IP.

    Entry informationi

    Entry nameiVINC_CHICK
    AccessioniPrimary (citable) accession number: P12003
    Secondary accession number(s): Q91024
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3