{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q15047","secondaryAccessions":["A6NEW2","Q5SZD8","Q5SZD9","Q5SZE0","Q5SZE7","Q96GM9"],"uniProtkbId":"SETB1_HUMAN","entryAudit":{"firstPublicDate":"2002-11-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":244,"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":"Histone-lysine N-methyltransferase SETDB1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11959841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14536086"}],"value":"2.1.1.366"}]},"alternativeNames":[{"fullName":{"value":"ERG-associated protein with SET domain"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14536086"}],"value":"ESET"}]},{"fullName":{"value":"Histone H3-K9 methyltransferase 4"},"shortNames":[{"value":"H3-K9-HMTase 4"}]},{"fullName":{"value":"Lysine N-methyltransferase 1E"}},{"fullName":{"value":"SET domain bifurcated 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11959841"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:10761"}],"value":"SETDB1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14536086"}],"value":"ESET"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7584044"}],"value":"KIAA0067"},{"value":"KMT1E"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11959841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12869583"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14536086"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24623306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26405197"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27029610"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27237050"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27732843"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37938770"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39096901"}],"value":"Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) (PubMed:11959841, PubMed:12869583, PubMed:14536086, PubMed:27237050, PubMed:39096901). 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:11959841, PubMed:12869583, PubMed:14536086, PubMed:27237050, PubMed:39096901). Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes (PubMed:12869583, PubMed:14536086, PubMed:27237050, PubMed:39096901). H3 'Lys-9' trimethylation is coordinated with DNA methylation (PubMed:12869583, PubMed:14536086, PubMed:27237050, PubMed:39096901). Forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation (PubMed:14536086). Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1 (PubMed:14536086). SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins (PubMed:24623306). Required for HUSH-mediated heterochromatin formation and gene silencing (PubMed:27732843). 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 (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). 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:37938770). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). 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 (PubMed:27029610). 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 (PubMed:26405197)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Lacks all domains required for histone methyltransferase activity"}],"commentType":"FUNCTION","molecule":"Isoform 2"},{"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":"11959841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14536086"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60289"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11959841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14536086"}]}]},{"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:0000269","source":"PubMed","id":"26405197"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60281"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26405197"}]}]},{"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:0000269","source":"PubMed","id":"26405197"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:64445"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26405197"}]}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":1.78,"unit":"uM","substrate":"S-adenosyl-L-methionine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14536086"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O88974"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11959841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14536086"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15327775"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15691849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15899859"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16567619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16682412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17066076"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19061646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20871592"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23034801"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24623306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27029610"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30487602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32051553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37179361"}],"value":"Part of a complex containing at least CDYL, REST, WIZ, SETDB1, EHMT1 and EHMT2 (PubMed:19061646). Forms a complex with ATRX, TRIM28 and ZNF274 (PubMed:27029610). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306). Interacts with TRIM28/TIF1B (PubMed:11959841). Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP protects SETDB1 from proteasomal degradation and is required to stimulate histone methyltransferase activity and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9' (PubMed:14536086, PubMed:15691849). Interacts with CBX1 and CBX5 (PubMed:15899859). Interacts with DNMT3A and DNMT3B (PubMed:16682412). Interacts with SUMO2. Interacts with MPHOSPH8 (PubMed:20871592). Interacts with ERG (By similarity). Interacts with HDAC1, HDAC2, SIN3A and SIN3B (By similarity). Interacts with ATRX. Interacts with RESF1 (By similarity). Interacts with ZNF638 (PubMed:30487602). 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 (PubMed:32051553). Interacts with PHF13; the interaction probably enhances SETDB1 chromatin-associated levels and activity (PubMed:23034801). Interacts with VRK1 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High expression in testis"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29234025"}],"value":"The Tudor domains recognize and bind histone H3 methylated at 'Lys-9' and acetylated at 'Lys-14' (H3K9me and H3K19ac, respectively) (PubMed:29234025). The Tudor domain 3 specifically recognizes H3K9me1 or H3K9me2, while the Tudor domain 2 specifically recognizes H3K9me3 (PubMed:29234025). H3K14ac is recognized by residues from Tudor domains 2 and 3, and the linker between them (PubMed:29234025). The Tudor domain 1 contains an incomplete aromatic cage and is inactive (PubMed:29234025)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11959841"}],"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:0000269","source":"PubMed","id":"27732843"}],"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-867 by E2 enzymes of the UBE2E family. The conjugated-Ub is protected from deubiquitination by the SET domain. Monoubiquitination at Lys-867 is required for catalytic activity, H3K9 methylation and endogenous retrovirus silencing"}],"commentType":"PTM"},{"texts":[{"value":"Highly up-regulated in Huntington disease patients, suggesting that participates in the altered chromatin modulation and transcription dysfunction observed in Huntington disease. Its down-regulation has salubrious effects on patients, suggesting that it may be a promising treatment in Huntington disease patients"}],"commentType":"MISCELLANEOUS"},{"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. 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