8S24
Structure of the E3 ubiquitin ligase RNF213, determined by cryoEM
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001525 | biological_process | angiogenesis |
A | 0002040 | biological_process | sprouting angiogenesis |
A | 0002376 | biological_process | immune system process |
A | 0003824 | molecular_function | catalytic activity |
A | 0004842 | molecular_function | ubiquitin-protein transferase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005730 | cellular_component | nucleolus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005811 | cellular_component | lipid droplet |
A | 0005829 | cellular_component | cytosol |
A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016020 | cellular_component | membrane |
A | 0016567 | biological_process | protein ubiquitination |
A | 0016740 | molecular_function | transferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0019216 | biological_process | regulation of lipid metabolic process |
A | 0042742 | biological_process | defense response to bacterium |
A | 0046872 | molecular_function | metal ion binding |
A | 0051865 | biological_process | protein autoubiquitination |
A | 0061630 | molecular_function | ubiquitin protein ligase activity |
A | 0070534 | biological_process | protein K63-linked ubiquitination |
A | 0098792 | biological_process | xenophagy |
A | 0120323 | biological_process | lipid ubiquitination |
A | 0140042 | biological_process | lipid droplet formation |
A | 2000051 | biological_process | negative regulation of non-canonical Wnt signaling pathway |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 39 |
Details | ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175 |
Chain | Residue | Details |
A | CYS3997-LEU4036 |
site_id | SWS_FT_FI2 |
Number of Residues | 72 |
Details | ZN_FING: RZ-type => ECO:0000255|PROSITE-ProRule:PRU01325, ECO:0000269|PubMed:34012115 |
Chain | Residue | Details |
A | MET4483-THR4555 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile; for E3 ubiquitin-lipopolysaccharide ligase activity => ECO:0000255|PROSITE-ProRule:PRU01325 |
Chain | Residue | Details |
A | CYS4516 |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:E9Q555 |
Chain | Residue | Details |
A | GLY1995 | |
A | HIS4014 | |
A | CYS4017 | |
A | CYS4020 | |
A | CYS4032 | |
A | CYS4035 | |
A | GLU2098 | |
A | ASP2155 | |
A | ARG2216 | |
A | LYS2499 | |
A | SER2574 | |
A | CYS3997 | |
A | CYS4000 | |
A | CYS4012 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01325 |
Chain | Residue | Details |
A | CYS4505 | |
A | HIS4509 | |
A | CYS4525 | |
A | CYS4528 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER208 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER217 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER1258 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER2273 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 |
Chain | Residue | Details |
A | LYS1151 |