Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000785 | cellular_component | chromatin |
A | 0000786 | cellular_component | nucleosome |
A | 0003682 | molecular_function | chromatin binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005694 | cellular_component | chromosome |
A | 0006325 | biological_process | chromatin organization |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0032452 | molecular_function | histone demethylase activity |
A | 0032453 | molecular_function | histone H3K4 demethylase activity |
A | 0040029 | biological_process | epigenetic regulation of gene expression |
A | 0042393 | molecular_function | histone binding |
A | 0044726 | biological_process | epigenetic programing of female pronucleus |
A | 0046872 | molecular_function | metal ion binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071514 | biological_process | genomic imprinting |
A | 0071949 | molecular_function | FAD binding |
A | 0140682 | molecular_function | FAD-dependent H3K4me/H3K4me3 demethylase activity |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD A 901 |
Chain | Residue |
A | ILE388 |
A | GLY419 |
A | ARG420 |
A | ARG434 |
A | GLY435 |
A | ALA436 |
A | ILE438 |
A | VAL598 |
A | VAL627 |
A | PRO628 |
A | TRP757 |
A | GLY389 |
A | TRP762 |
A | ALA766 |
A | GLY794 |
A | GLU795 |
A | GLN803 |
A | THR804 |
A | VAL805 |
A | ALA808 |
A | HOH1108 |
A | HOH1125 |
A | GLY391 |
A | HOH1127 |
A | HOH1148 |
A | HOH1188 |
A | PRO392 |
A | ALA393 |
A | LEU411 |
A | GLU412 |
A | ALA413 |
A | LYS414 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 902 |
Chain | Residue |
A | CYS53 |
A | CYS58 |
A | HIS84 |
A | HIS90 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 903 |
Chain | Residue |
A | CYS65 |
A | CYS73 |
A | CYS92 |
A | CYS95 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 904 |
Chain | Residue |
A | CYS142 |
A | CYS147 |
A | CYS169 |
A | CYS185 |
Functional Information from PROSITE/UniProt
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
C | LYS14-LEU20 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | PRO168-ASP180 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Required to promote KDM1B demethylase activity toward histone H3K4me1 and H3K4me2 => ECO:0000269|PubMed:23260659 |
Chain | Residue | Details |
B | PHE217 | |
A | GLN803 | |
A | CYS58 | |
A | CYS65 | |
A | CYS73 | |
A | HIS84 | |
A | HIS90 | |
A | CYS92 | |
A | CYS95 | |
A | VAL598 | |
Chain | Residue | Details |
B | SER167 | |
A | CYS147 | |
A | CYS169 | |
A | CYS185 | |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS176 | |
B | LYS179 | |
B | LYS201 | |
B | LYS211 | |
B | LYS240 | |
Chain | Residue | Details |
B | LYS227 | |
B | LYS237 | |
Chain | Residue | Details |
A | SER247 | |