{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9H9B1","secondaryAccessions":["B1AQ58","B1AQ59","Q86X08","Q8TCN7","Q96F53","Q96JF1","Q96KH4"],"uniProtkbId":"EHMT1_HUMAN","entryAudit":{"firstPublicDate":"2002-11-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-03-08","entryVersion":232,"sequenceVersion":4},"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":"Histone-lysine N-methyltransferase EHMT1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12004135"}],"value":"2.1.1.-"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12004135"}],"value":"2.1.1.367"}]},"alternativeNames":[{"fullName":{"value":"Euchromatic histone-lysine N-methyltransferase 1"},"shortNames":[{"value":"Eu-HMTase1"}]},{"fullName":{"value":"G9a-like protein 1"},"shortNames":[{"value":"GLP"},{"value":"GLP1"}]},{"fullName":{"value":"Histone H3-K9 methyltransferase 5"},"shortNames":[{"value":"H3-K9-HMTase 5"}]},{"fullName":{"value":"Lysine N-methyltransferase 1D"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17974005"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:24650"}],"value":"EHMT1"},"synonyms":[{"value":"EUHMTASE1"},{"value":"GLP"},{"value":"KIAA1876"},{"value":"KMT1D"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5DW34"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12004135"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20118233"}],"value":"Histone methyltransferase that specifically mono-, di- and trimethylates 'Lys-9' of histone H3 (H3K9me1, H3K9me2 and H3K9me3, respectively) in euchromatin (PubMed:12004135). H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones (PubMed:12004135). Also weakly methylates 'Lys-27' of histone H3 (H3K27me) (PubMed:12004135). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently (By similarity). Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1 (PubMed:12004135). During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle (PubMed:12004135). Involved in the differentiation of myoblastic precursors into brown adipose cells: following recruitment to chromatin by PRDM16, mediates formation of H3K9me2 and H3K9me3, inhibiting the expression of white adipose-selective genes (By similarity). Also involved in the differentiation of beige adipocytes from white adipose cells following recruitment by PRDM16 (By similarity). EHMT1 also promotes protein stabilization of PRDM16, by preventing PRDM16 ubiquitination and degradation (By similarity). In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53 (PubMed:20118233). Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with probable chromatin reader BAZ2B (By similarity)"}],"commentType":"FUNCTION"},{"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"}],"ecNumber":"2.1.1.367","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12004135"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60284"},{"database":"Rhea","id":"RHEA-COMP:15541"},{"database":"Rhea","id":"RHEA-COMP:15542"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:61929"},{"database":"ChEBI","id":"CHEBI:61976"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12004135"}]}},{"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"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5DW34"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60289"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5DW34"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20434463"}],"value":"Methyltransferase activity is inhibited by BIX-01294. Efficiently inhibited by compound E72, a BIX-01294 derivative in which the diazepane ring and the benzyl are replaced with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B and C, respectively"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5DW34"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12004135"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16702210"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18264113"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19061646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20084102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20118233"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20434463"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20871592"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21515635"}],"value":"Heterodimer; heterodimerizes with EHMT2. Interacts with WIZ and EHMT2. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts (via ANK repeats) with RELA (when monomethylated at 'Lys-310') (PubMed:21515635). Interacts with MPHOSPH8. Interacts with CDYL. Interacts with REST only in the presence of CDYL. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2. Interacts with BAZ2B (By similarity). Interacts with PRDM16; promoting EHMT1 recruitment to chromatin, differentiation of brown adipose cells and stabilization of PRDM16 (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9H9B1","intActId":"EBI-766087"},"interactantTwo":{"uniProtKBAccession":"Q99549","geneName":"MPHOSPH8","intActId":"EBI-2653928"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9H9B1","intActId":"EBI-766087"},"interactantTwo":{"uniProtKBAccession":"Q04206","geneName":"RELA","intActId":"EBI-73886"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9H9B1","intActId":"EBI-766087"},"interactantTwo":{"uniProtKBAccession":"Q04207","geneName":"Rela","intActId":"EBI-644400"},"numberOfExperiments":5,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5DW34"}],"value":"Associates with euchromatic regions"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5DW34"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5DW34"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q9H9B1-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q9H9B1-2"],"sequenceIds":["VSP_002222","VSP_002223"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q9H9B1-3"],"sequenceIds":["VSP_002224","VSP_002225"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["Q9H9B1-4"],"sequenceIds":["VSP_040717","VSP_040718"],"isoformSequenceStatus":"Described"}],"note":{"texts":[{"value":"Experimental confirmation may be lacking for some isoforms."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11347906"}],"value":"Widely expressed"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5DW34"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18264113"}],"value":"The ANK repeats specifically recognize and bind H3K9me1 and H3K9me2 (PubMed:18264113). 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Although it is not known if and to what extent other genes in the 9q34.3 region contribute to the syndrome observed in deletion cases, EHMT1 seems to be the major determinant of the core disease phenotype (PubMed:19264732)"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00190"}],"value":"Belongs to the class V-like SAM-binding methyltransferase superfamily"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous translation","sequence":"BAB14321.1","note":"Wrong choice of CDS.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Miscellaneous discrepancy","sequence":"CAD28534.1","note":"Intron 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