{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O88974","secondaryAccessions":["Q6AXH8","Q78N64","Q78N65","Q80U84","Q8BTV6","Q8CIX7","Q922K1"],"uniProtkbId":"SETB1_MOUSE","entryAudit":{"firstPublicDate":"2002-11-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-11-01","entryVersion":194,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Histone-lysine N-methyltransferase SETDB1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11791185"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22939622"}],"value":"2.1.1.366"}]},"alternativeNames":[{"fullName":{"value":"ERG-associated protein with SET domain"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20164836"}],"value":"ESET"}]},{"fullName":{"value":"SET domain bifurcated 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"MGI","id":"MGI:1934229"}],"value":"Setdb1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20164836"}],"value":"Eset"},{"value":"Kiaa0067"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11791185"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20164836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22939622"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27237050"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29728365"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39096901"}],"value":"Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) (PubMed:11791185, PubMed:22939622). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones (PubMed:11791185, PubMed:22939622). Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes (PubMed:27237050, PubMed:39096901). H3 'Lys-9' trimethylation is coordinated with DNA methylation (By similarity). Forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation (By similarity). Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1 (By similarity). SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins (By similarity). Required for HUSH-mediated heterochromatin formation and gene silencing (By similarity). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (By similarity). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (By similarity). In ESCs, in collaboration with TRIM28, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (PubMed:20164836, PubMed:27237050, PubMed:29728365). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (By similarity). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (By similarity). Also catalyzes mono- and dimethylation of 'Lys-9' of free histone H3 (H3K9me1 and H3K9me2) during translation in the cytoplasm, which is then transported to the nucleus and incorporated into nucleosomes (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60288"},{"database":"Rhea","id":"RHEA-COMP:15538"},{"database":"Rhea","id":"RHEA-COMP:15541"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:61961"},{"database":"ChEBI","id":"CHEBI:61976"}],"ecNumber":"2.1.1.366","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00906"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11791185"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22939622"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60289"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11791185"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22939622"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60280"},{"database":"Rhea","id":"RHEA-COMP:15542"},{"database":"Rhea","id":"RHEA-COMP:15546"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:61929"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60281"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-methionine = N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-homocysteine + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64444"},{"database":"Rhea","id":"RHEA-COMP:15541"},{"database":"Rhea","id":"RHEA-COMP:15546"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:61976"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:64445"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11791185"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12398767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29728365"}],"value":"Part of a complex containing at least CDYL, REST, WIZ, SETDB1, EHMT1 and EHMT2. Forms a complex with ATRX, TRIM28 and ZNF274 (By similarity). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with TRIM28/TIF1B. Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP is required to stimulate histone methyltransferase activity and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9'. Interacts with MBD1; interaction is abolished when MBD1 is sumoylated. Interacts with CBX1 and CBX5. Interacts with DNMT3A and DNMT3B. Interacts with SUMO2. Interacts with MPHOSPH8 (By similarity). Interacts with ERG (PubMed:11791185). Interacts with HDAC1, HDAC2, SIN3A, SIN3B (PubMed:12398767). Interacts with ATRX. Interacts with RESF1 (PubMed:29728365). Interacts with ZNF638 (By similarity). Interacts with ZNF263; recruited to the SIX3 promoter along with other proteins involved in chromatin modification and transcriptional corepression where it contributes to transcriptional repression (By similarity). Interacts with PHF13; the interaction probably enhances SETDB1 chromatin-associated levels and activity (By similarity). Interacts with VRK1 (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O88974","intActId":"EBI-79658"},"interactantTwo":{"uniProtKBAccession":"P81270","geneName":"Erg","intActId":"EBI-79647"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O88974","intActId":"EBI-79658"},"interactantTwo":{"uniProtKBAccession":"E9Q5K9","geneName":"Ythdc1","intActId":"EBI-647644"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}],"value":"Associated with non-pericentromeric regions of chromatin. Recruited to H3K9me and H3K19ac marks on chromatin. Excluded from nucleoli and islands of condensed chromatin"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29728365"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29728365"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["O88974-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["O88974-2"],"sequenceIds":["VSP_002219","VSP_002220"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["O88974-3"],"sequenceIds":["VSP_002221"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["O88974-4"],"sequenceIds":["VSP_024031"],"isoformSequenceStatus":"Described"},{"name":{"value":"5"},"isoformIds":["O88974-5"],"sequenceIds":["VSP_024032"],"isoformSequenceStatus":"Described"},{"name":{"value":"6"},"isoformIds":["O88974-6"],"sequenceIds":["VSP_024031","VSP_024032"],"isoformSequenceStatus":"Described"},{"name":{"value":"7"},"isoformIds":["O88974-7"],"sequenceIds":["VSP_024033"],"isoformSequenceStatus":"Described"}],"note":{"texts":[{"value":"Experimental confirmation may be lacking for some isoforms."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14522075"}],"value":"Ubiquitously expressed (PubMed:14522075). Strong expression in liver and testis (PubMed:14522075)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}],"value":"The Tudor domains recognize and bind histone H3 methylated at 'Lys-9' and acetylated at 'Lys-14' (H3K9me and H3K19ac, respectively). The Tudor domain 3 specifically recognizes H3K9me1 or H3K9me2, while the Tudor domain 2 specifically recognizes H3K9me3. H3K14ac is recognized by residues from Tudor domains 2 and 3, and the linker between them. The Tudor domain 1 contains an incomplete aromatic cage and is inactive"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}],"value":"The pre-SET, SET and post-SET domains are all required for methyltransferase activity. The 347-amino-acid insertion in the SET domain has no effect on the catalytic activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O43463"}],"value":"In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15047"}],"value":"Degraded by the proteasome, shielded by interaction with ATF7IP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27237050"}],"value":"Monoubiquitinated at Lys-884 by E2 enzymes UBE2E family. The conjugated-Ub is protected from deubiquitination through the SET domain. Monoubiquitination at Lys-884 is required for catalytic activity and H3K9 methylation and endogenous retrovirus silencing"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00906"}],"value":"Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31112734"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34272044"}],"value":"Was previously reported to interact with TASOR. 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