8ALZ
Cryo-EM structure of ASCC3 in complex with ASC1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002020 | molecular_function | protease binding |
| A | 0003713 | molecular_function | transcription coactivator activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005813 | cellular_component | centrosome |
| A | 0005829 | cellular_component | cytosol |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016604 | cellular_component | nuclear body |
| A | 0016922 | molecular_function | nuclear receptor binding |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0030331 | molecular_function | nuclear estrogen receptor binding |
| A | 0030520 | biological_process | estrogen receptor signaling pathway |
| A | 0031594 | cellular_component | neuromuscular junction |
| A | 0032790 | biological_process | ribosome disassembly |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0035035 | molecular_function | histone acetyltransferase binding |
| A | 0044389 | molecular_function | ubiquitin-like protein ligase binding |
| A | 0045661 | biological_process | regulation of myoblast differentiation |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0072344 | biological_process | rescue of stalled ribosome |
| A | 0180022 | cellular_component | RQC-trigger complex |
| A | 1990116 | biological_process | ribosome-associated ubiquitin-dependent protein catabolic process |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0005524 | molecular_function | ATP binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 94 |
| Details | Domain: {"description":"ASCH","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Zinc finger: {"description":"C4-type"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 183 |
| Details | Domain: {"description":"Helicase ATP-binding 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 186 |
| Details | Domain: {"description":"Helicase C-terminal 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 309 |
| Details | Domain: {"description":"SEC63 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 175 |
| Details | Domain: {"description":"Helicase ATP-binding 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 195 |
| Details | Domain: {"description":"Helicase C-terminal 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 364 |
| Details | Domain: {"description":"SEC63 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Motif: {"description":"DEVH box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Motif: {"description":"DEIH box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
