9D1Y
Structure of G75R Ubiquitin bound to KLHDC3-EloB/C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000785 | cellular_component | chromatin |
| A | 0003682 | molecular_function | chromatin binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0007131 | biological_process | reciprocal meiotic recombination |
| A | 0016567 | biological_process | protein ubiquitination |
| A | 0031462 | cellular_component | Cul2-RING ubiquitin ligase complex |
| A | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| A | 0051321 | biological_process | meiotic cell cycle |
| A | 0140627 | biological_process | ubiquitin-dependent protein catabolic process via the C-end degron rule pathway |
| A | 1990756 | molecular_function | ubiquitin-like ligase-substrate adaptor activity |
| B | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| B | 0030891 | cellular_component | VCB complex |
| B | 0070449 | cellular_component | elongin complex |
| C | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00299 |
| Number of Residues | 26 |
| Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
| Chain | Residue | Details |
| D | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 52 |
| Details | Repeat: {"description":"Kelch 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 50 |
| Details | Repeat: {"description":"Kelch 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 50 |
| Details | Repeat: {"description":"Kelch 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 58 |
| Details | Repeat: {"description":"Kelch 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 50 |
| Details | Repeat: {"description":"Kelch 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 65 |
| Details | Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| 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 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 75 |
| Details | Domain: {"description":"Ubiquitin-like 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
