{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O43791","secondaryAccessions":["B2R6S3","D3DTW7","Q53HJ1"],"uniProtkbId":"SPOP_HUMAN","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-06-01","entryVersion":218,"sequenceVersion":1},"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":"Speckle-type POZ protein"}},"alternativeNames":[{"fullName":{"value":"HIB homolog 1"}},{"fullName":{"value":"Roadkill homolog 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:11254"}],"value":"SPOP"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6ZWS8"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14528312"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15897469"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16524876"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19818708"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22085717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22632832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32109420"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37622993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37796126"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38018242"}],"value":"Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL. Involved in the regulation of bromodomain and extra-terminal motif (BET) proteins BRD2, BRD3, BRD4 stability (PubMed:32109420). Plays an essential role for proper translation, but not for their degradation, of critical DNA replication licensing factors CDT1 and CDC6, thereby participating in DNA synthesis and cell proliferation (PubMed:36791496). Regulates interferon regulatory factor 1/IRF1 proteasomal turnover by targeting S/T-rich degrons in IRF1 (PubMed:37622993). Facilitates the lysosome-dependent degradation of enterovirus EV71 protease 2A by inducing its 'Lys-48'-linked polyubiquitination, which ultimately restricts EV71 replication (PubMed:37796126). Acts as an antiviral factor also against hepatitis B virus/HBV by promoting ubiquitination and subsequent degradation of HNF1A (PubMed:38018242). In turn, inhibits HBV transcription and replication by preventing HNF1A stimulating activity of HBV preS1 promoter and enhancer II (PubMed:38018242). Involved in ubiquitination of BRDT and promotes its degradation, thereby regulates histone removal in early condensing spermatids prior to histone-to-protamine exchange (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14528312"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15897469"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16524876"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19818708"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22085717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22632832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32109420"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14528312"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15240113"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15897469"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16524876"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19818708"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22085717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22632832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37622993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38018242"}],"value":"Interacts with GLI2 and GLI3 (By similarity). Homodimer and homooligomer. Heterodimer with SPOPL. Each dimer interacts with two CUL3 molecules. Part of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that contain CUL3 and homodimeric SPOP, or the heterodimer formed by SPOP and SPOPL, plus a target protein, such as MACROH2A1, PDX1/IPF1, BMI1, BRMS1 and DAXX. Interacts with IRF1; this interaction mediates IRF1 proteasomal degradation (PubMed:37622993). Interacts with HNF1A 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