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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
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
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
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
B0030032biological_processlamellipodium assembly
B0030055cellular_componentcell-substrate junction
B0030334biological_processregulation of cell migration
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
B0042995cellular_componentcell projection
B0043034cellular_componentcostamere
B0043297biological_processapical junction assembly
B0044291cellular_componentcell-cell contact zone
B0045294molecular_functionalpha-catenin binding
B0045296molecular_functioncadherin binding
B0048675biological_processaxon extension
B0051015molecular_functionactin filament binding
B0051893biological_processregulation of focal adhesion assembly
B0061826cellular_componentpodosome ring
B0070062cellular_componentextracellular exosome
B0070161cellular_componentanchoring junction
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 Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P85972
ChainResidueDetails
AASP98
AILE273
AGLN575
BASP98
BILE273
BGLN575

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AMSE174
AILE497
BMSE174
BILE497

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ALYS261
ALYS276
ALEU580
AASP601
APRO796
AASP810
BLYS261
BLYS276
BLEU580
BASP601
BPRO796
BASP810

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AALA289
BALA289

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
APRO291
BPRO291

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
APRO347
BPRO347

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
ALEU435
BLEU435

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000305
ChainResidueDetails
AARG538
BARG538

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
APRO605
BPRO605

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO673
BPRO673

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ALEU722
BLEU722

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648
ChainResidueDetails
AARG823
BARG823

218500

PDB entries from 2024-04-17

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