Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000281 | biological_process | mitotic cytokinesis |
A | 0000902 | biological_process | cell morphogenesis |
A | 0001778 | biological_process | plasma membrane repair |
A | 0001891 | cellular_component | phagocytic cup |
A | 0005200 | molecular_function | structural constituent of cytoskeleton |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005811 | cellular_component | lipid droplet |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005884 | cellular_component | actin filament |
A | 0005911 | cellular_component | cell-cell junction |
A | 0005938 | cellular_component | cell cortex |
A | 0006897 | biological_process | endocytosis |
A | 0006909 | biological_process | phagocytosis |
A | 0006935 | biological_process | chemotaxis |
A | 0006972 | biological_process | hyperosmotic response |
A | 0007010 | biological_process | cytoskeleton organization |
A | 0015629 | cellular_component | actin cytoskeleton |
A | 0016192 | biological_process | vesicle-mediated transport |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017022 | molecular_function | myosin binding |
A | 0030027 | cellular_component | lamellipodium |
A | 0030139 | cellular_component | endocytic vesicle |
A | 0030864 | cellular_component | cortical actin cytoskeleton |
A | 0031143 | cellular_component | pseudopodium |
A | 0031252 | cellular_component | cell leading edge |
A | 0032009 | cellular_component | early phagosome |
A | 0032010 | cellular_component | phagolysosome |
A | 0042331 | biological_process | phototaxis |
A | 0045335 | cellular_component | phagocytic vesicle |
A | 0051591 | biological_process | response to cAMP |
A | 0060187 | cellular_component | cell pole |
A | 0061836 | cellular_component | intranuclear rod |
A | 0061851 | cellular_component | leading edge of lamellipodium |
A | 0070685 | cellular_component | macropinocytic cup |
G | 0051015 | molecular_function | actin filament binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 402 |
Chain | Residue |
A | ATP401 |
A | HOH460 |
A | HOH466 |
A | HOH651 |
A | HOH665 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | LYS238 |
A | ARG254 |
A | HOH690 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 404 |
Chain | Residue |
A | GLU270 |
A | SER271 |
A | MET269 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 405 |
Chain | Residue |
A | GLY308 |
A | ILE309 |
A | ALA310 |
A | ASP311 |
A | HOH438 |
A | HOH486 |
A | HOH542 |
A | HOH625 |
G | LYS13 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 406 |
Chain | Residue |
A | ASP157 |
A | GLY182 |
A | ARG183 |
A | THR186 |
A | ARG206 |
A | ARG210 |
A | LYS213 |
A | ATP401 |
A | HOH695 |
A | HOH699 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 407 |
Chain | Residue |
A | ARG147 |
A | LYS328 |
A | ILE330 |
A | HOH524 |
A | HOH537 |
G | ARG96 |
G | GOL404 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 408 |
Chain | Residue |
A | ARG62 |
A | ARG62 |
A | THR202 |
A | THR203 |
A | THR203 |
A | ALA204 |
A | ALA204 |
A | HOH570 |
A | HOH573 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 409 |
Chain | Residue |
A | PRO112 |
A | LYS113 |
A | HOH692 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 410 |
Chain | Residue |
A | ASN78 |
A | TRP79 |
A | ASP80 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 411 |
Chain | Residue |
A | THR66 |
A | THR66 |
A | LEU67 |
A | LEU67 |
A | HOH575 |
A | HOH575 |
A | HOH578 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 G 126 |
Chain | Residue |
G | ASN56 |
G | SER70 |
G | GLN71 |
G | ARG91 |
G | HOH483 |
G | HOH518 |
G | HOH533 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA G 401 |
Chain | Residue |
G | GLY41 |
G | ASP42 |
G | GLU73 |
G | VAL121 |
G | HOH418 |
G | HOH430 |
site_id | BC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE ATP A 401 |
Chain | Residue |
A | HOH637 |
A | HOH665 |
A | GLY13 |
A | SER14 |
A | GLY15 |
A | MET16 |
A | LYS18 |
A | GLY156 |
A | ASP157 |
A | GLY182 |
A | ARG210 |
A | LYS213 |
A | GLU214 |
A | GLY301 |
A | GLY302 |
A | THR303 |
A | MET305 |
A | PHE306 |
A | LYS336 |
A | MG402 |
A | SO4406 |
A | HOH416 |
A | HOH435 |
A | HOH442 |
A | HOH460 |
A | HOH466 |
A | HOH467 |
A | HOH485 |
A | HOH508 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 412 |
Chain | Residue |
A | ASP24 |
A | ARG28 |
A | HOH693 |
A | HOH707 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 413 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL G 402 |
Chain | Residue |
G | SER103 |
G | ALA104 |
G | THR105 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL G 403 |
Chain | Residue |
A | ASN296 |
A | HOH420 |
A | HOH537 |
G | ARG96 |
G | HOH413 |
G | HOH433 |
G | HOH443 |
G | HOH510 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL G 404 |
Chain | Residue |
A | SO4407 |
A | HOH453 |
G | LEU65 |
G | GLY66 |
G | ASN67 |
G | CYS69 |
G | VAL98 |
G | HOH415 |
Functional Information from PROSITE/UniProt
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
A | PTR53-GLY63 | |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WISKeEYDE |
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
Chain | Residue | Details |
G | GLY41 | |
G | ASP42 | |
G | GLU73 | |
G | ASP85 | |
G | GLY90 | |
G | ALA92 | |
G | VAL121 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
G | LYS111 | |
Chain | Residue | Details |
G | TYR35 | |