Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001725 | cellular_component | stress fiber |
| A | 0003785 | molecular_function | actin monomer binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005523 | molecular_function | tropomyosin binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005865 | cellular_component | striated muscle thin filament |
| A | 0005884 | cellular_component | actin filament |
| A | 0010628 | biological_process | positive regulation of gene expression |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0030027 | cellular_component | lamellipodium |
| A | 0030041 | biological_process | actin filament polymerization |
| A | 0030175 | cellular_component | filopodium |
| A | 0030240 | biological_process | skeletal muscle thin filament assembly |
| A | 0031013 | molecular_function | troponin I binding |
| A | 0031432 | molecular_function | titin binding |
| A | 0031941 | cellular_component | filamentous actin |
| A | 0032036 | molecular_function | myosin heavy chain binding |
| A | 0032432 | cellular_component | actin filament bundle |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044297 | cellular_component | cell body |
| A | 0048306 | molecular_function | calcium-dependent protein binding |
| A | 0048741 | biological_process | skeletal muscle fiber development |
| A | 0051017 | biological_process | actin filament bundle assembly |
| A | 0090131 | biological_process | mesenchyme migration |
| A | 0098723 | cellular_component | skeletal muscle myofibril |
| A | 0140660 | molecular_function | cytoskeletal motor activator activity |
| G | 0051015 | molecular_function | actin filament binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A1376 |
| Chain | Residue |
| A | GLN137 |
| A | ATP1377 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA G1743 |
| Chain | Residue |
| A | GLU167 |
| A | HOH2087 |
| G | ASP487 |
| G | GLY492 |
| G | PRO494 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA G1744 |
| Chain | Residue |
| G | GLU475 |
| G | THR524 |
| G | GLY444 |
| G | ASP445 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA G1745 |
| Chain | Residue |
| G | ASN564 |
| G | ASP565 |
| G | GLU587 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA G1746 |
| Chain | Residue |
| G | ASP669 |
| G | ASP670 |
| G | GLU692 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP A1377 |
| Chain | Residue |
| A | GLY13 |
| A | SER14 |
| A | GLY15 |
| A | LEU16 |
| A | LYS18 |
| A | GLY156 |
| A | ASP157 |
| A | GLY158 |
| A | VAL159 |
| A | GLY182 |
| A | LYS213 |
| A | GLU214 |
| A | GLY302 |
| A | THR303 |
| A | MET305 |
| A | TYR306 |
| A | LYS336 |
| A | CA1376 |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| A | TYR53-GLY63 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WITKqEYDE |
| Chain | Residue | Details |
| A | TRP356-GLU364 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
| Chain | Residue | Details |
| A | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12460571, ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, ECO:0007744|PDB:2FH2, ECO:0007744|PDB:2FH3 |
| Chain | Residue | Details |
| G | GLY444 | |
| G | GLU587 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12460571, ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, ECO:0007744|PDB:2FH3 |
| Chain | Residue | Details |
| G | ASP445 | |
| G | GLU475 | |
| G | THR524 | |
| G | ASN564 | |
| G | ASP565 | |
| G | ASP669 | |
| G | GLU692 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12460571, ECO:0007744|PDB:1H1V |
| Chain | Residue | Details |
| G | ASP487 | |
| G | GLY492 | |
| G | PRO494 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12460571, ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, ECO:0007744|PDB:2FH3 |
| Chain | Residue | Details |
| G | ASP670 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:10210201 |
| Chain | Residue | Details |
| G | TYR438 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13020 |
| Chain | Residue | Details |
| G | LYS557 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201 |
| Chain | Residue | Details |
| G | TYR576 | |
| G | TYR624 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| G | THR715 |
