{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q96SW2","secondaryAccessions":["B2R6H4","C9IZA9","C9JAH6","Q6AI62","Q6NVZ0","Q9UHW4"],"uniProtkbId":"CRBN_HUMAN","entryAudit":{"firstPublicDate":"2005-08-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-12-01","entryVersion":189,"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":{"value":"Protein cereblon"}}},"genes":[{"geneName":{"value":"CRBN"},"orfNames":[{"value":"AD-006"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8C7D2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18414909"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20223979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24328678"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043012"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25108355"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29530986"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31620128"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41565821"}],"value":"Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2, ILF2, GLUL, IKZF1 and CSNK1A1 (PubMed:26990986, PubMed:33009960, PubMed:41565821). Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 (PubMed:20223979, PubMed:24328678, PubMed:25043012, PubMed:25108355). Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons (PubMed:18414909, PubMed:29530986). Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (PubMed:18414909). May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism (By similarity). Plays a negative role in TLR4 signaling by interacting with TRAF6 and ECSIT, leading to inhibition of ECSIT ubiquitination, an important step of the signaling (PubMed:31620128)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20223979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41565821"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25108355"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q56AP7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20223979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24328678"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043012"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25108355"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31620128"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33009960"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41565821"}],"value":"Component of a DCX (DDB1-CUL4-X-box) protein ligase complex, at least composed of CRBN, CUL4A, DDB1 and RBX1 (PubMed:25043012, PubMed:41565821). Interacts (via Lon N-terminal domain) with DDB1 (via WD40 beta-propellers A and C); the interaction is direct (PubMed:25043012, PubMed:25108355, PubMed:41565821). Interacts with IKZF1 and IKZF3; the interaction is direct and requires the presence of thalidomide or its derivatives (PubMed:24328678, PubMed:41565821). Interacts with CSNK1A1; the interaction is direct (PubMed:41565821). Interacts with ILF2 (PubMed:33009960). Interacts with TRAF6 and ECSIT (PubMed:31620128). Interacts with KCNT1 (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q96SW2","intActId":"EBI-2510250"},"interactantTwo":{"uniProtKBAccession":"Q96A83-2","geneName":"COL26A1","intActId":"EBI-21553822"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2","intActId":"EBI-2510250"},"interactantTwo":{"uniProtKBAccession":"P48729","geneName":"CSNK1A1","intActId":"EBI-1383726"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2","intActId":"EBI-2510250"},"interactantTwo":{"uniProtKBAccession":"Q16531","geneName":"DDB1","intActId":"EBI-350322"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2","intActId":"EBI-2510250"},"interactantTwo":{"uniProtKBAccession":"O14901","geneName":"KLF11","intActId":"EBI-948266"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2","intActId":"EBI-2510250"},"interactantTwo":{"uniProtKBAccession":"Q8IVT2","geneName":"MISP","intActId":"EBI-2555085"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2","intActId":"EBI-2510250"},"interactantTwo":{"uniProtKBAccession":"Q9P286","geneName":"PAK5","intActId":"EBI-741896"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2","intActId":"EBI-2510250"},"interactantTwo":{"uniProtKBAccession":"A0A6Q8PF08","geneName":"PMP22","intActId":"EBI-50433196"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2","intActId":"EBI-2510250"},"interactantTwo":{"uniProtKBAccession":"Q93062","geneName":"RBPMS","intActId":"EBI-740322"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2-2","intActId":"EBI-10693561"},"interactantTwo":{"uniProtKBAccession":"Q16531","geneName":"DDB1","intActId":"EBI-350322"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96SW2-2","intActId":"EBI-10693561"},"interactantTwo":{"uniProtKBAccession":"Q13422-7","geneName":"IKZF1","intActId":"EBI-11522367"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20223979"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20223979"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q56AP7"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q56AP7"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q96SW2-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q96SW2-2"],"sequenceIds":["VSP_015209"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15557513"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17380424"}],"value":"Widely expressed. Highly expressed in brain"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25108355"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41565821"}],"value":"The CULT domain binds thalidomide and its derivatives, such as pomalidomide and lenalidomide (PubMed:25108355, PubMed:41565821). The helical bundle within the Lon N-terminal domain binds to allosteric ligands (PubMed:41565821). Ligand binding to these domains modulates the substrate specificity and enzyme activity of the human DCX (DDB1-CUL4-X-box) E3 protein ligase complex (PubMed:25108355, PubMed:41565821). However, such change in substrate specificity is not observed in rodents (PubMed:25108355)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20223979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25043012"}],"value":"Ubiquitinated, ubiquitination is mediated by its own DCX protein ligase complex"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Intellectual developmental disorder, autosomal recessive 2","diseaseAccession":"DI-00715","acronym":"MRT2","description":"A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT2 patients display mild intellectual disability with a standard IQ ranged from 50 to 70. IQ scores are lower in males than females. Developmental milestones are mildly delayed. There are no dysmorphic or autistic features.","diseaseCrossReference":{"database":"MIM","id":"607417"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15557513"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28143899"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20223979"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25108355"}],"value":"Thalidomide was widely prescribed to pregnant women in the late 1950s as a sedative and as treatment against morning sickness. Thalidomide was found to be teratogenic, causing multiple birth defects. More recently, thalidomide use has increased for the treatment of multiple myeloma and erythema nodosum leprosum, a painful complication of leprosy. Binding of pomalidomide and other thalidomide-related drugs leads to a change in substrate specificity of the human DCX (DDB1-CUL4-X-box) E3 protein ligase complex, and this is probably the underlying cause of the teratogenic activity of thalidomide, possibly due to abnormal regulation of the BMP and FGF8 signaling pathways (PubMed:20223979). The thalidomide-induced change in substrate specificity leads to decreased degradation of MEIS2 and other target proteins and increased degradation of MYC, IRF4, IKZF1 and IKZF3, and this is probably the reason for the anti-proliferative and immunomodulatory effects of thalidomide and related drugs (PubMed:25108355). Thalidomide is also teratogenic in chicken and zebrafish, but not in mice"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the CRBN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Although it contains a Lon N-terminal domain also found in proteases of the peptidase S16 family, it does not contain the ATP-binding and catalytic domains, suggesting that it has no protease activity"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAF17211.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAG35471.1","note":"Truncated N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE 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