1ST6
Crystal structure of a cytoskeletal protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001725 | cellular_component | stress fiber |
| 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 | 0005623 | cellular_component | obsolete cell |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005903 | cellular_component | brush border |
| A | 0005911 | cellular_component | cell-cell junction |
| A | 0005912 | cellular_component | adherens junction |
| A | 0005915 | cellular_component | zonula adherens |
| A | 0005916 | cellular_component | fascia adherens |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0005927 | cellular_component | muscle tendon junction |
| A | 0007155 | biological_process | cell adhesion |
| A | 0008013 | molecular_function | beta-catenin binding |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0016020 | cellular_component | membrane |
| A | 0017166 | molecular_function | vinculin binding |
| A | 0030016 | cellular_component | myofibril |
| A | 0030018 | cellular_component | Z disc |
| A | 0030032 | biological_process | lamellipodium assembly |
| A | 0030334 | biological_process | regulation of cell migration |
| A | 0030486 | cellular_component | smooth muscle dense body |
| A | 0031594 | cellular_component | neuromuscular junction |
| 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 | 0042383 | cellular_component | sarcolemma |
| A | 0042803 | molecular_function | protein homodimerization activity |
| 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 | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0051015 | molecular_function | actin filament binding |
| A | 0051371 | molecular_function | muscle alpha-actinin binding |
| A | 0051393 | molecular_function | alpha-actinin binding |
| A | 0051893 | biological_process | regulation of focal adhesion assembly |
| A | 0061826 | cellular_component | podosome ring |
| A | 0090136 | biological_process | epithelial cell-cell adhesion |
| A | 0090636 | cellular_component | outer dense plaque of desmosome |
| A | 0090637 | cellular_component | inner dense plaque of desmosome |
| A | 0097110 | molecular_function | scaffold protein binding |
| A | 0098723 | cellular_component | skeletal muscle myofibril |
| A | 1903140 | biological_process | regulation of establishment of endothelial barrier |
| A | 1904702 | biological_process | regulation of protein localization to adherens junction |
| A | 1990357 | cellular_component | terminal web |
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. MnQAkgWLrDP |
| Chain | Residue | Details |
| A | MET277-PRO287 | |
| A | ILE388-PRO398 | |
| A | ILE497-PRO507 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 110 |
| Details | Repeat: {"description":"1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 109 |
| Details | Repeat: {"description":"2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 109 |
| Details | Repeat: {"description":"3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 833 |
| Details | Region: {"description":"N-terminal globular head","evidences":[{"source":"UniProtKB","id":"P18206","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | Region: {"description":"Talin-interaction","evidences":[{"source":"PubMed","id":"2512301","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 330 |
| Details | Region: {"description":"3 X 112 AA tandem repeats","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 43 |
| Details | Region: {"description":"Facilitates phospholipid membrane insertion","evidences":[{"source":"UniProtKB","id":"Q64727","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15229287","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P18206","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"15229287","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
