{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q63HN8","secondaryAccessions":["C9JCP4","D6RI12","F8WKS1","Q658P6","Q69YK7","Q6MZR1","Q8IWF4","Q8IZX1","Q8IZX2","Q8N406","Q8TEU0","Q9H6C9","Q9H6H9","Q9H6P3","Q9H8A9","Q9HCF4","Q9HCL8"],"uniProtkbId":"RN213_HUMAN","entryAudit":{"firstPublicDate":"2007-02-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2012-03-21","entryVersion":184,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"E3 ubiquitin-protein ligase RNF213"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32139119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33842849"}],"value":"2.3.2.27"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24658080"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"26126547"}],"value":"3.6.4.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12112524"}],"value":"ALK lymphoma oligomerization partner on chromosome 17"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"E3 ubiquitin-lipopolysaccharide ligase RNF213"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34012115"}],"value":"2.3.2.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"26126547"}],"value":"Mysterin"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"RING finger protein 213"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:14539"}],"value":"RNF213"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12112524"}],"value":"ALO17"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:14539"}],"value":"C17orf27"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10997877"}],"value":"KIAA1554"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10997877"}],"value":"KIAA1618"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"26126547"}],"value":"MYSTR"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26126547"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26278786"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26766444"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30705059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30846318"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32139119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33842849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34012115"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34599178"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39375464"}],"value":"Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:21799892, PubMed:26126547, PubMed:26278786, PubMed:26766444, PubMed:30705059, PubMed:32139119, PubMed:34012115). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (PubMed:34012115, PubMed:39375464). Also acts indirectly by mediating the recruitment of the LUBAC complex, which conjugates linear polyubiquitin chains (PubMed:34012115). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (PubMed:34012115). Also functions as an intracellular sensor for ISGylated proteins: upon type I interferon stimulation, undergoes ISGylation and oligomerizes on lipid droplets to form a binding platform for ISG15-modified substrate proteins, thereby acting as a broad-spectrum antimicrobial effector. Restricts intracellular bacterial pathogens, such as Listeria monocytogenes, in an ISG15-dependent manner by decorating the bacterial surface with ubiquitin to promote autophagic clearance (PubMed:34599178). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (PubMed:30705059). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (PubMed:30846318). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (PubMed:32139119, PubMed:33842849). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (PubMed:26766444). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (PubMed:34012115)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.","ecNumber":"2.3.2.27","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32139119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33842849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39375464"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24658080"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"26126547"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:13066"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39375464"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24658080"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"26126547"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32139119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33842849"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21799892"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"E9Q555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32139119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33842849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34599178"}],"value":"Monomer (By similarity). Oligomerates upon ISGylation induced by type I interferon (PubMed:34599178). Interacts with UBE2L3/UBCH7; UBE2L3/UBCH7 is the most efficient ubiquitin-conjugating enzyme E2 for the ubiquitin ligase activity (By similarity). Interacts with UBE2N/UBC13; promoting 'Lys-63'-linked ubiquitination of target proteins (PubMed:32139119, PubMed:33842849)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20454556"}],"value":"(Microbial infection) Interacts with M.tuberculosis protein Rv3655c, which impairs caspase-8 activation and suppresses macrophage apoptosis by blocking the extrinsic pathway"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q63HN8-6","intActId":"EBI-10248548"},"interactantTwo":{"uniProtKBAccession":"Q08379","geneName":"GOLGA2","intActId":"EBI-618309"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q63HN8-6","intActId":"EBI-10248548"},"interactantTwo":{"uniProtKBAccession":"Q6A162","geneName":"KRT40","intActId":"EBI-10171697"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q63HN8-6","intActId":"EBI-10248548"},"interactantTwo":{"uniProtKBAccession":"Q04864","geneName":"REL","intActId":"EBI-307352"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q63HN8-6","intActId":"EBI-10248548"},"interactantTwo":{"uniProtKBAccession":"P36406","geneName":"TRIM23","intActId":"EBI-740098"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q63HN8-6","intActId":"EBI-10248548"},"interactantTwo":{"uniProtKBAccession":"P14373","geneName":"TRIM27","intActId":"EBI-719493"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q63HN8-6","intActId":"EBI-10248548"},"interactantTwo":{"uniProtKBAccession":"Q15654","geneName":"TRIP6","intActId":"EBI-742327"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q63HN8-6","intActId":"EBI-10248548"},"interactantTwo":{"uniProtKBAccession":"Q5T124","geneName":"UBXN11","intActId":"EBI-746004"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30705059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34012115"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30705059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34599178"}],"value":"Lipid droplet","id":"SL-0154"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q63HN8-3"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q63HN8-4"],"sequenceIds":["VSP_042417"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q63HN8-5"],"sequenceIds":["VSP_042418","VSP_042419"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["Q63HN8-6"],"sequenceIds":["VSP_042416","VSP_042420"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"}],"value":"Widely expressed (at protein level)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"}],"value":"Major isoform detected in all tissues examined"}],"commentType":"TISSUE SPECIFICITY","molecule":"Isoform 1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"}],"value":"Minor isoform with restricted expression"}],"commentType":"TISSUE SPECIFICITY","molecule":"Isoform 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26070522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26278786"}],"value":"Down-regulated by let-7c miRNA, which binds to the 3'-UTR transcript of RNF213 (PubMed:26070522). Induced by pro-inflammatory cytokines (PubMed:26278786)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20454556"}],"value":"(Microbial infection) Up-regulated in macrophages infected by M.tuberculosis"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"E9Q555"}],"value":"Composed of an N-terminal stalk, a dynein-like core comprised of two catalytically active and four inactive ATPase domains, and a C-terminal E3 module. The ATPase regions do not generate movement but rather act like an intricate molecular 'switch'"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"}],"value":"The RING-type zinc finger domain is required for the ubiquitin-protein ligase activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34012115"}],"value":"The RZ-type (RNF213-ZNFX1) zinc-finger is required for the ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"}],"value":"Autoubiquitinated"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34599178"}],"value":"ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation positively regulates oligomerization on lipid droplets"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40164614"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40205224"}],"value":"(Microbial infection) Ubiquitinated by S.flexneri E3 ubiquitin-protein ligases IpaH1.4 and IpaH2.5, leading to its degradation by the proteasome, thereby preventing formation of the bacterial ubiquitin coat and activation of innate immunity"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Moyamoya disease 2","diseaseAccession":"DI-03059","acronym":"MYMY2","description":"A progressive cerebral angiopathy characterized by bilateral intracranial carotid artery stenosis and telangiectatic vessels in the region of the basal ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral angiogram. Affected individuals can develop transient ischemic attacks and/or cerebral infarction, and rupture of the collateral vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic seizures constitute the prevailing presentation in childhood, while subarachnoid bleeding occurs more frequently in adults.","diseaseCrossReference":{"database":"MIM","id":"607151"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21048783"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22377813"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22688072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22931863"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23110205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23994138"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25278557"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25956231"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26126547"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26198278"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27736983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27787485"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28635953"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29387438"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31645973"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32139119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33568546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34012115"}]},"note":{"texts":[{"value":"Disease susceptibility is associated with variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12112524"}],"value":"A chromosomal aberration involving RNF213 is associated with anaplastic large-cell lymphoma (ALCL). Translocation t(2;17)(p23;q25) with ALK"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"E9Q555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24658080"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26126547"}],"value":"The stoichiometry is unclear: was initially thought to form homohexamers (PubMed:24658080, PubMed:26126547). However, the electron microscopy structure showed that it is monomeric and is composed of six ATPase modules within a single polypeptide chain (By similarity)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAH32220.1","note":"Truncated N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Miscellaneous discrepancy","sequence":"BAB13444.1","note":"Probable cloning artifact.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAB14708.1","note":"Truncated N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAB15212.1","note":"Truncated N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous 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