8Y1U
Crystal structure of ASB7-Elongin B/C bound to the LZTS1-degron
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000792 | cellular_component | heterochromatin |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005694 | cellular_component | chromosome |
| A | 0005829 | cellular_component | cytosol |
| A | 0016567 | biological_process | protein ubiquitination |
| A | 0031466 | cellular_component | Cul5-RING ubiquitin ligase complex |
| A | 0035556 | biological_process | intracellular signal transduction |
| A | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| A | 0120261 | biological_process | regulation of heterochromatin organization |
| A | 1990756 | molecular_function | ubiquitin-like ligase-substrate adaptor activity |
| C | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| C | 0030891 | cellular_component | VCB complex |
| C | 0070449 | cellular_component | elongin complex |
| D | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 28 |
| Details | Repeat: {"description":"ANK 6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 34 |
| Details | Repeat: {"description":"ANK 8","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Motif: {"description":"PxVxL motif 1","evidences":[{"source":"PubMed","id":"40440427","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Motif: {"description":"PxVxL motif 2","evidences":[{"source":"PubMed","id":"40440427","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Motif: {"description":"PxVxL motif 3","evidences":[{"source":"PubMed","id":"40440427","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"40440427","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
