8J1R
cryo-EM structures of Ufd4 in complex with Ubc4-Ub
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000209 | biological_process | protein polyubiquitination |
| A | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| A | 0010994 | biological_process | free ubiquitin chain polymerization |
| A | 0035519 | biological_process | protein K29-linked ubiquitination |
| A | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| A | 0061630 | molecular_function | ubiquitin protein ligase activity |
| A | 1904855 | molecular_function | proteasome regulatory particle binding |
| C | 0000209 | biological_process | protein polyubiquitination |
| C | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| C | 0016567 | biological_process | protein ubiquitination |
| C | 0030674 | molecular_function | protein-macromolecule adaptor activity |
| C | 0034605 | biological_process | cellular response to heat |
| C | 0043130 | molecular_function | ubiquitin binding |
| C | 0043162 | biological_process | ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway |
| C | 0061631 | molecular_function | ubiquitin conjugating enzyme activity |
| C | 0070628 | molecular_function | proteasome binding |
| C | 0071629 | biological_process | cytoplasm protein quality control by the ubiquitin-proteasome system |
| C | 0072344 | biological_process | rescue of stalled cytosolic ribosome |
| C | 0072671 | biological_process | mitochondria-associated ubiquitin-dependent protein catabolic process |
| C | 1990116 | biological_process | ribosome-associated ubiquitin-dependent protein catabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00183 |
| Number of Residues | 16 |
| Details | UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInan.GnICLdiL |
| Chain | Residue | Details |
| C | TYR75-LEU90 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 74 |
| Details | Region: {"description":"K-box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00104","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 11 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






