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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1TR2

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

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
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
A0043034cellular_componentcostamere
A0043297biological_processapical junction assembly
A0044291cellular_componentcell-cell contact zone
A0045294molecular_functionalpha-catenin binding
A0045296molecular_functioncadherin binding
A0048471cellular_componentperinuclear region of cytoplasm
A0051015molecular_functionactin filament binding
A0051893biological_processregulation of focal adhesion assembly
A0061826cellular_componentpodosome ring
A0070062cellular_componentextracellular exosome
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
B0002009biological_processmorphogenesis of an epithelium
B0002102cellular_componentpodosome
B0002162molecular_functiondystroglycan binding
B0003779molecular_functionactin binding
B0005198molecular_functionstructural molecule activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005911cellular_componentcell-cell junction
B0005912cellular_componentadherens junction
B0005916cellular_componentfascia adherens
B0005925cellular_componentfocal adhesion
B0007155biological_processcell adhesion
B0007160biological_processcell-matrix adhesion
B0008013molecular_functionbeta-catenin binding
B0015629cellular_componentactin cytoskeleton
B0016020cellular_componentmembrane
B0030016cellular_componentmyofibril
B0030032biological_processlamellipodium assembly
B0030055cellular_componentcell-substrate junction
B0030336biological_processnegative regulation of cell migration
B0031625molecular_functionubiquitin protein ligase binding
B0032991cellular_componentprotein-containing complex
B0034333biological_processadherens junction assembly
B0034394biological_processprotein localization to cell surface
B0034774cellular_componentsecretory granule lumen
B0035580cellular_componentspecific granule lumen
B0035633biological_processmaintenance of blood-brain barrier
B0042383cellular_componentsarcolemma
B0043034cellular_componentcostamere
B0043297biological_processapical junction assembly
B0044291cellular_componentcell-cell contact zone
B0045294molecular_functionalpha-catenin binding
B0045296molecular_functioncadherin binding
B0048471cellular_componentperinuclear region of cytoplasm
B0051015molecular_functionactin filament binding
B0051893biological_processregulation of focal adhesion assembly
B0061826cellular_componentpodosome ring
B0070062cellular_componentextracellular exosome
B0070527biological_processplatelet aggregation
B0090136biological_processepithelial cell-cell adhesion
B1903140biological_processregulation of establishment of endothelial barrier
B1903561cellular_componentextracellular vesicle
B1904702biological_processregulation of protein localization to adherens junction
B1904813cellular_componentficolin-1-rich granule lumen
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 Residues84
DetailsRegion: {"description":"Linker (Pro-rich)","evidences":[{"source":"PubMed","id":"20484056","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues60
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues32
DetailsCompositional bias: {"description":"Pro residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P85972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
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_FI8
Number of Residues2
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_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
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_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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