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6FUY

Crystal structure of human full-length vinculin-T12-A974K (residues 1-1066)

Replaces:  6FMM
Functional Information from GO Data
ChainGOidnamespacecontents
A0002009biological_processmorphogenesis of an epithelium
A0002102cellular_componentpodosome
A0002162molecular_functiondystroglycan binding
A0003779molecular_functionactin binding
A0005198molecular_functionstructural molecule activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005911cellular_componentcell-cell junction
A0005912cellular_componentadherens junction
A0005916cellular_componentfascia adherens
A0005925cellular_componentfocal adhesion
A0007155biological_processcell adhesion
A0007160biological_processcell-matrix adhesion
A0008013molecular_functionbeta-catenin binding
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0030016cellular_componentmyofibril
A0030032biological_processlamellipodium assembly
A0030055cellular_componentcell-substrate junction
A0030334biological_processregulation of cell migration
A0030336biological_processnegative regulation of cell migration
A0031625molecular_functionubiquitin protein ligase binding
A0032991cellular_componentprotein-containing complex
A0034333biological_processadherens junction assembly
A0034394biological_processprotein localization to cell surface
A0034774cellular_componentsecretory granule lumen
A0035580cellular_componentspecific granule lumen
A0035633biological_processmaintenance of blood-brain barrier
A0042383cellular_componentsarcolemma
A0042995cellular_componentcell projection
A0043034cellular_componentcostamere
A0043297biological_processapical junction assembly
A0044291cellular_componentcell-cell contact zone
A0045294molecular_functionalpha-catenin binding
A0045296molecular_functioncadherin binding
A0048471cellular_componentperinuclear region of cytoplasm
A0048675biological_processaxon extension
A0051015molecular_functionactin filament binding
A0051893biological_processregulation of focal adhesion assembly
A0061826cellular_componentpodosome ring
A0070062cellular_componentextracellular exosome
A0070161cellular_componentanchoring junction
A0070527biological_processplatelet aggregation
A0090136biological_processepithelial cell-cell adhesion
A1903140biological_processregulation of establishment of endothelial barrier
A1903561cellular_componentextracellular vesicle
A1904702biological_processregulation of protein localization to adherens junction
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue CA A 1101
ChainResidue
AASP800

Functional Information from PROSITE/UniProt
site_idPS00663
Number of Residues21
DetailsVINCULIN_1 Vinculin family talin-binding region signature. KnLgpgMtkMakmideRQQEL
ChainResidueDetails
ALYS162-LEU182

site_idPS00664
Number of Residues11
DetailsVINCULIN_2 Vinculin repeated domain signature. LnQAkgWLrDP
ChainResidueDetails
ALEU277-PRO287
AILE388-PRO398
AILE497-PRO507

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues110
DetailsRepeat: {"description":"1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues109
DetailsRepeat: {"description":"3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsRegion: {"description":"Talin-interaction","evidences":[{"source":"UniProtKB","id":"P12003","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues23
DetailsRegion: {"description":"Interaction with ACTN4","evidences":[{"source":"PubMed","id":"15988023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YDI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues43
DetailsRegion: {"description":"Facilitates phospholipid membrane insertion","evidences":[{"source":"UniProtKB","id":"Q64727","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P85972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"15229287","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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