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8S24

Structure of the E3 ubiquitin ligase RNF213, determined by cryoEM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001525biological_processangiogenesis
A0002040biological_processsprouting angiogenesis
A0002376biological_processimmune system process
A0003824molecular_functioncatalytic activity
A0004842molecular_functionubiquitin-protein transferase activity
A0005524molecular_functionATP binding
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0006629biological_processlipid metabolic process
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0019216biological_processregulation of lipid metabolic process
A0042742biological_processdefense response to bacterium
A0046872molecular_functionmetal ion binding
A0051865biological_processprotein autoubiquitination
A0061630molecular_functionubiquitin protein ligase activity
A0070534biological_processprotein K63-linked ubiquitination
A0098792biological_processxenophagy
A0120323biological_processlipid ubiquitination
A0140042biological_processlipid droplet formation
A2000051biological_processnegative regulation of non-canonical Wnt signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"E9Q555","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01325","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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