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6NR7

Rerefinement of chicken vinculin

Functional Information from GO Data
ChainGOidnamespacecontents
A0001725cellular_componentstress fiber
A0002009biological_processmorphogenesis of an epithelium
A0002102cellular_componentpodosome
A0002162molecular_functiondystroglycan binding
A0003779molecular_functionactin binding
A0005198molecular_functionstructural molecule activity
A0005515molecular_functionprotein binding
A0005623cellular_componentobsolete cell
A0005737cellular_componentcytoplasm
A0005743cellular_componentmitochondrial inner membrane
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005903cellular_componentbrush border
A0005911cellular_componentcell-cell junction
A0005912cellular_componentadherens junction
A0005915cellular_componentzonula adherens
A0005916cellular_componentfascia adherens
A0005925cellular_componentfocal adhesion
A0005927cellular_componentmuscle tendon junction
A0007155biological_processcell adhesion
A0008013molecular_functionbeta-catenin binding
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0017166molecular_functionvinculin binding
A0030016cellular_componentmyofibril
A0030018cellular_componentZ disc
A0030032biological_processlamellipodium assembly
A0030334biological_processregulation of cell migration
A0030486cellular_componentsmooth muscle dense body
A0031594cellular_componentneuromuscular junction
A0031625molecular_functionubiquitin protein ligase binding
A0032991cellular_componentprotein-containing complex
A0034333biological_processadherens junction assembly
A0034394biological_processprotein localization to cell surface
A0042383cellular_componentsarcolemma
A0042803molecular_functionprotein homodimerization activity
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
A0051371molecular_functionmuscle alpha-actinin binding
A0051393molecular_functionalpha-actinin binding
A0051893biological_processregulation of focal adhesion assembly
A0061826cellular_componentpodosome ring
A0070161cellular_componentanchoring junction
A0090136biological_processepithelial cell-cell adhesion
A0090636cellular_componentouter dense plaque of desmosome
A0090637cellular_componentinner dense plaque of desmosome
A0097110molecular_functionscaffold protein binding
A0098723cellular_componentskeletal muscle myofibril
A1903140biological_processregulation of establishment of endothelial barrier
A1904702biological_processregulation of protein localization to adherens junction
A1990357cellular_componentterminal web
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 1101
ChainResidue
ALYS911
AARG1060

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 1102
ChainResidue
AGLU186
AHIS187
ATRP253
AASP254

site_idAC3
Number of Residues3
Detailsbinding site for residue KYG A 1103
ChainResidue
AGLN18
AHIS22
ALYS952

site_idAC4
Number of Residues1
Detailsbinding site for residue PO4 A 1104
ChainResidue
AASP953

site_idAC5
Number of Residues3
Detailsbinding site for residue PO4 A 1105
ChainResidue
AGLN550
AARG780
ALYS784

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. MnQAkgWLrDP
ChainResidueDetails
AMET277-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":"2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues109
DetailsRepeat: {"description":"3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues833
DetailsRegion: {"description":"N-terminal globular head","evidences":[{"source":"UniProtKB","id":"P18206","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsRegion: {"description":"Talin-interaction","evidences":[{"source":"PubMed","id":"2512301","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues330
DetailsRegion: {"description":"3 X 112 AA tandem repeats","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues42
DetailsRegion: {"description":"Linker (Pro-rich)","evidences":[{"source":"UniProtKB","id":"P18206","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues51
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues57
DetailsRegion: {"description":"Facilitates phospholipid membrane insertion","evidences":[{"source":"UniProtKB","id":"Q64727","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues16
DetailsCompositional bias: {"description":"Pro residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15229287","evidenceCode":"ECO:0000269"}]}
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":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P18206","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"15229287","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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