Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000281 | biological_process | mitotic cytokinesis |
| C | 0000902 | biological_process | cell morphogenesis |
| C | 0001778 | biological_process | plasma membrane repair |
| C | 0001891 | cellular_component | phagocytic cup |
| C | 0005200 | molecular_function | structural constituent of cytoskeleton |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005811 | cellular_component | lipid droplet |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005884 | cellular_component | actin filament |
| C | 0005911 | cellular_component | cell-cell junction |
| C | 0005938 | cellular_component | cell cortex |
| C | 0006897 | biological_process | endocytosis |
| C | 0006909 | biological_process | phagocytosis |
| C | 0006935 | biological_process | chemotaxis |
| C | 0006972 | biological_process | hyperosmotic response |
| C | 0007010 | biological_process | cytoskeleton organization |
| C | 0015629 | cellular_component | actin cytoskeleton |
| C | 0016192 | biological_process | vesicle-mediated transport |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017022 | molecular_function | myosin binding |
| C | 0030027 | cellular_component | lamellipodium |
| C | 0030139 | cellular_component | endocytic vesicle |
| C | 0030864 | cellular_component | cortical actin cytoskeleton |
| C | 0031143 | cellular_component | pseudopodium |
| C | 0031252 | cellular_component | cell leading edge |
| C | 0032009 | cellular_component | early phagosome |
| C | 0032010 | cellular_component | phagolysosome |
| C | 0042331 | biological_process | phototaxis |
| C | 0045335 | cellular_component | phagocytic vesicle |
| C | 0051591 | biological_process | response to cAMP |
| C | 0060187 | cellular_component | cell pole |
| C | 0061836 | cellular_component | intranuclear rod |
| C | 0061851 | cellular_component | leading edge of lamellipodium |
| C | 0070685 | cellular_component | macropinocytic cup |
| S | 0051015 | molecular_function | actin filament binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA S 128 |
| Chain | Residue |
| S | GLY43 |
| S | ASP44 |
| S | GLU75 |
| S | VAL123 |
| S | HOH1031 |
| S | HOH1117 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA S 129 |
| Chain | Residue |
| S | ALA94 |
| S | HOH1004 |
| S | HOH1082 |
| S | HOH1223 |
| C | GLU167 |
| S | ASP87 |
| S | GLY92 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 377 |
| Chain | Residue |
| C | ATP376 |
| C | HOH1001 |
| C | HOH1008 |
| C | HOH1050 |
| C | HOH1065 |
| C | HOH1108 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ATP C 376 |
| Chain | Residue |
| C | GLY13 |
| C | SER14 |
| C | GLY15 |
| C | MET16 |
| C | LYS18 |
| C | GLY156 |
| C | ASP157 |
| C | GLY158 |
| C | VAL159 |
| C | GLY182 |
| C | ARG210 |
| C | LYS213 |
| C | GLU214 |
| C | GLY301 |
| C | GLY302 |
| C | THR303 |
| C | MET305 |
| C | PHE306 |
| C | CA377 |
| C | HOH1009 |
| C | HOH1065 |
| C | HOH1108 |
| C | HOH1134 |
| C | HOH1164 |
| C | HOH1222 |
| C | HOH1243 |
| C | HOH1294 |
| C | HOH1305 |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| C | TYR53-GLY63 | |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WISKeEYDE |
| Chain | Residue | Details |
| C | TRP356-GLU364 | |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEAaLNPkaNR |
| Chain | Residue | Details |
| C | LEU104-ARG116 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 82 |
| Details | Repeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Region: {"description":"Actin-actin interfilament contact point"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"7498488","evidenceCode":"ECO:0000269"}]} |