Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002009 | biological_process | morphogenesis of an epithelium |
| A | 0002102 | cellular_component | podosome |
| A | 0002162 | molecular_function | dystroglycan binding |
| A | 0003779 | molecular_function | actin binding |
| A | 0005198 | molecular_function | structural molecule activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005911 | cellular_component | cell-cell junction |
| A | 0005912 | cellular_component | adherens junction |
| A | 0005916 | cellular_component | fascia adherens |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0007155 | biological_process | cell adhesion |
| A | 0007160 | biological_process | cell-matrix adhesion |
| A | 0008013 | molecular_function | beta-catenin binding |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0016020 | cellular_component | membrane |
| A | 0030032 | biological_process | lamellipodium assembly |
| A | 0030055 | cellular_component | cell-substrate junction |
| A | 0030334 | biological_process | regulation of cell migration |
| A | 0030336 | biological_process | negative regulation of cell migration |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0034333 | biological_process | adherens junction assembly |
| A | 0034394 | biological_process | protein localization to cell surface |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0035580 | cellular_component | specific granule lumen |
| A | 0035633 | biological_process | maintenance of blood-brain barrier |
| A | 0042383 | cellular_component | sarcolemma |
| A | 0042995 | cellular_component | cell projection |
| A | 0043034 | cellular_component | costamere |
| A | 0043297 | biological_process | apical junction assembly |
| A | 0044291 | cellular_component | cell-cell contact zone |
| A | 0045294 | molecular_function | alpha-catenin binding |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0048675 | biological_process | axon extension |
| A | 0051015 | molecular_function | actin filament binding |
| A | 0051893 | biological_process | regulation of focal adhesion assembly |
| A | 0061826 | cellular_component | podosome ring |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070161 | cellular_component | anchoring junction |
| A | 0070527 | biological_process | platelet aggregation |
| A | 0090136 | biological_process | epithelial cell-cell adhesion |
| A | 1903140 | biological_process | regulation of establishment of endothelial barrier |
| A | 1903561 | cellular_component | extracellular vesicle |
| A | 1904702 | biological_process | regulation of protein localization to adherens junction |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue CA A 1101 |
| Chain | Residue |
| A | ASP800 |
Functional Information from PROSITE/UniProt
| site_id | PS00663 |
| Number of Residues | 21 |
| Details | VINCULIN_1 Vinculin family talin-binding region signature. KnLgpgMtkMakmideRQQEL |
| Chain | Residue | Details |
| A | LYS162-LEU182 |
| site_id | PS00664 |
| Number of Residues | 11 |
| Details | VINCULIN_2 Vinculin repeated domain signature. LnQAkgWLrDP |
| Chain | Residue | Details |
| A | LEU277-PRO287 | |
| A | ILE388-PRO398 | |
| A | ILE497-PRO507 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P85972 |
| Chain | Residue | Details |
| A | SER97 | |
| A | SER272 | |
| A | SER574 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS173 | |
| A | LYS496 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER260 | |
| A | SER275 | |
| A | SER579 | |
| A | SER600 | |
| A | SER795 | |
| A | SER809 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER288 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER290 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER346 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER434 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000305 |
| Chain | Residue | Details |
| A | TYR537 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR604 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR672 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_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 |
| Chain | Residue | Details |
| A | SER721 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | TYR822 |
