Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0008285 | biological_process | negative regulation of cell population proliferation |
A | 0016573 | biological_process | histone acetylation |
A | 0070776 | cellular_component | MOZ/MORF histone acetyltransferase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | CYS199 |
A | CYS201 |
A | TYR206 |
A | HIS223 |
A | CYS226 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 302 |
Chain | Residue |
A | CYS242 |
A | CYS212 |
A | CYS217 |
A | PHE222 |
A | CYS239 |
Functional Information from PROSITE/UniProt
site_id | PS01359 |
Number of Residues | 44 |
Details | ZF_PHD_1 Zinc finger PHD-type signature. Cl.Chqvsygem.....................................IgCddpdCsiewFHfaCvglttkprgk...................................WfCprC |
Chain | Residue | Details |
A | CYS199-CYS242 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 49 |
Details | Zinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9UK53","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Site: {"description":"Histone H3K4me3 binding","evidences":[{"source":"UniProtKB","id":"Q9UK53","evidenceCode":"ECO:0000250"}]} |