Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004322 | molecular_function | ferroxidase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005764 | cellular_component | lysosome |
A | 0005776 | cellular_component | autophagosome |
A | 0005829 | cellular_component | cytosol |
A | 0006826 | biological_process | iron ion transport |
A | 0006879 | biological_process | intracellular iron ion homeostasis |
A | 0006880 | biological_process | intracellular sequestering of iron ion |
A | 0006955 | biological_process | immune response |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0008199 | molecular_function | ferric iron binding |
A | 0008285 | biological_process | negative regulation of cell population proliferation |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0031410 | cellular_component | cytoplasmic vesicle |
A | 0042802 | molecular_function | identical protein binding |
A | 0044754 | cellular_component | autolysosome |
A | 0046872 | molecular_function | metal ion binding |
A | 0048147 | biological_process | negative regulation of fibroblast proliferation |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070288 | cellular_component | ferritin complex |
A | 0110076 | biological_process | negative regulation of ferroptosis |
A | 0140315 | molecular_function | iron ion sequestering activity |
A | 1904724 | cellular_component | tertiary granule lumen |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue TRS A 201 |
Chain | Residue |
A | HIS128 |
A | HOH309 |
A | HOH335 |
A | HOH357 |
A | HOH366 |
A | HOH542 |
A | ASP131 |
A | PHE132 |
A | THR135 |
A | HIS136 |
A | ASN139 |
A | CL218 |
A | MG223 |
A | HOH304 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue BCN A 202 |
Chain | Residue |
A | LEU28 |
A | LEU28 |
A | SER31 |
A | SER31 |
A | TYR32 |
A | LEU35 |
A | ARG63 |
A | ARG63 |
A | ILE85 |
A | ILE85 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue FE A 203 |
Chain | Residue |
A | GLU27 |
A | GLU62 |
A | HIS65 |
A | FE204 |
A | HOH445 |
A | HOH601 |
A | HOH611 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue FE A 204 |
Chain | Residue |
A | GLU62 |
A | GLU107 |
A | GLN141 |
A | FE203 |
A | HOH445 |
A | HOH489 |
A | HOH611 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue FE A 205 |
Chain | Residue |
A | GLN58 |
A | GLU61 |
A | HOH494 |
A | HOH599 |
A | HOH605 |
A | HOH613 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue FE A 206 |
Chain | Residue |
A | HIS57 |
A | GLU61 |
A | HOH597 |
A | HOH603 |
A | HOH606 |
A | HOH612 |
site_id | AC7 |
Number of Residues | 12 |
Details | binding site for residue FE A 207 |
Chain | Residue |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | CL210 |
A | CL210 |
A | CL210 |
A | CL210 |
A | HOH386 |
A | HOH386 |
A | HOH386 |
A | HOH386 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue FE A 208 |
Chain | Residue |
A | HOH319 |
A | HOH319 |
A | HOH319 |
A | HOH405 |
A | HOH405 |
A | HOH405 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue FE A 209 |
Chain | Residue |
A | ASP131 |
A | ASP131 |
A | ASP131 |
A | HOH315 |
A | HOH315 |
A | HOH315 |
A | HOH324 |
A | HOH324 |
A | HOH324 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue CL A 210 |
Chain | Residue |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | FE207 |
A | FE207 |
A | FE207 |
A | FE207 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue CL A 211 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue CL A 212 |
Chain | Residue |
A | GLN83 |
A | ASP84 |
A | LYS86 |
A | CL221 |
A | HOH420 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue CL A 213 |
Chain | Residue |
A | ASN125 |
A | HOH314 |
A | HOH352 |
A | HOH425 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue CL A 214 |
Chain | Residue |
A | ASN21 |
A | HOH471 |
A | HOH518 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue CL A 215 |
Chain | Residue |
A | ARG9 |
A | ASN11 |
A | TYR12 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue CL A 216 |
Chain | Residue |
A | GLN75 |
A | HOH332 |
A | HOH383 |
A | HOH584 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue CL A 217 |
Chain | Residue |
A | ASP150 |
A | HIS151 |
A | ASN154 |
A | HOH308 |
A | HOH432 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue CL A 218 |
Chain | Residue |
A | GLN75 |
A | ASN139 |
A | TRS201 |
site_id | AE1 |
Number of Residues | 1 |
Details | binding site for residue CL A 219 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue CL A 220 |
Chain | Residue |
A | GLU134 |
A | THR135 |
A | HIS136 |
A | TYR137 |
A | ASN139 |
A | GLU140 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue CL A 221 |
Chain | Residue |
A | LYS86 |
A | CL212 |
A | HOH343 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue CL A 222 |
Chain | Residue |
A | ASN25 |
A | HOH563 |
A | HOH564 |
A | HOH602 |
site_id | AE5 |
Number of Residues | 6 |
Details | binding site for residue MG A 223 |
Chain | Residue |
A | TRS201 |
A | HOH335 |
A | HOH357 |
A | HOH366 |
A | HOH370 |
A | HOH553 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue MG A 224 |
Chain | Residue |
A | HOH446 |
A | HOH456 |
A | HOH543 |
A | HOH544 |
A | HOH602 |
A | HOH607 |
site_id | AE7 |
Number of Residues | 8 |
Details | binding site for residue MG A 225 |
Chain | Residue |
A | HOH305 |
A | HOH305 |
A | HOH313 |
A | HOH313 |
A | HOH420 |
A | HOH420 |
A | HOH437 |
A | HOH437 |
Functional Information from PROSITE/UniProt
site_id | PS00204 |
Number of Residues | 21 |
Details | FERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEthYLneqvkaIK |
Chain | Residue | Details |
A | ASP126-LYS146 | |
site_id | PS00540 |
Number of Residues | 19 |
Details | FERRITIN_1 Ferritin iron-binding regions signature 1. EeREhaEKLMklQNqRgGR |
Chain | Residue | Details |
A | GLU61-ARG79 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU27 | |
A | HIS65 | |
Chain | Residue | Details |
A | GLU62 | |
A | GLU107 | |
A | GLN141 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Essential for association with cargo receptor NCOA4 => ECO:0000269|PubMed:26436293 |
Chain | Residue | Details |
A | ARG22 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | SER178 | |
Chain | Residue | Details |
A | SER182 | |