Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004402 | molecular_function | histone acetyltransferase activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 53 |
Chain | Residue |
A | CYS22 |
A | VAL24 |
A | CYS25 |
A | HIS40 |
A | HIS42 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 54 |
Chain | Residue |
A | CYS9 |
A | CYS12 |
A | CYS31 |
A | CYS34 |
Functional Information from PROSITE/UniProt
site_id | PS01357 |
Number of Residues | 26 |
Details | ZF_ZZ_1 Zinc finger ZZ-type signature. CneCkhhvet..RWhCtv...CeDYdLCinC |
Chain | Residue | Details |
A | CYS9-CYS34 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 48 |
Details | Zinc finger: {"description":"ZZ-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00228","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00228","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q92793","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |