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 | 0030016 | cellular_component | myofibril |
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 | 0048471 | cellular_component | perinuclear region of cytoplasm |
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 | 110 |
Details | Repeat: {"description":"1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 109 |
Details | Repeat: {"description":"3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | Region: {"description":"Talin-interaction","evidences":[{"source":"UniProtKB","id":"P12003","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 23 |
Details | Region: {"description":"Interaction with ACTN4","evidences":[{"source":"PubMed","id":"15988023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YDI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
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_FI6 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P85972","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Modified 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | Modified 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
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 |