1HCD
STRUCTURE OF HISACTOPHILIN IS SIMILAR TO INTERLEUKIN-1 BETA AND FIBROBLAST GROWTH FACTOR
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003779 | molecular_function | actin binding |
A | 0003785 | molecular_function | actin monomer binding |
A | 0005504 | molecular_function | fatty acid binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006972 | biological_process | hyperosmotic response |
A | 0008289 | molecular_function | lipid binding |
A | 0010447 | biological_process | response to acidic pH |
A | 0015629 | cellular_component | actin cytoskeleton |
A | 0016020 | cellular_component | membrane |
A | 0030041 | biological_process | actin filament polymerization |
A | 0030674 | molecular_function | protein-macromolecule adaptor activity |
A | 0030863 | cellular_component | cortical cytoskeleton |
A | 0045335 | cellular_component | phagocytic vesicle |
A | 0051015 | molecular_function | actin filament binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:7822284 |
Chain | Residue | Details |
A | ASN3 |