{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O43463","secondaryAccessions":["B2R6E8","B4DST0","Q53G60","Q6FHK6"],"uniProtkbId":"SUV91_HUMAN","entryAudit":{"firstPublicDate":"2002-11-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-06-01","entryVersion":232,"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":"Histone-lysine N-methyltransferase SUV39H1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10949293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18004385"}],"value":"2.1.1.-"}]},"alternativeNames":[{"fullName":{"value":"Histone H3-K9 methyltransferase 1"},"shortNames":[{"value":"H3-K9-HMTase 1"}]},{"fullName":{"value":"Lysine N-methyltransferase 1A"}},{"fullName":{"value":"Position-effect variegation 3-9 homolog"}},{"fullName":{"value":"Suppressor of variegation 3-9 homolog 1"},"shortNames":[{"value":"Su(var)3-9 homolog 1"}]}]},"genes":[{"geneName":{"value":"SUV39H1"},"synonyms":[{"value":"KMT1A"},{"value":"SUV39H"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O54864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10949293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11242053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11484059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14765126"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16449642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16818776"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16858404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18004385"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18485871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30111536"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40440427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41094145"}],"value":"Histone methyltransferase that specifically mediates trimethylation of 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' (H3K9me1) as substrate (PubMed:10949293, PubMed:11242053, PubMed:18004385, PubMed:40440427). Also weakly methylates histone H1 (in vitro) (PubMed:10949293). 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:10949293, PubMed:11242053, PubMed:18004385). Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions (By similarity). H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats (PubMed:41094145). SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length (PubMed:11484059, PubMed:14765126, PubMed:16449642, PubMed:16818776, PubMed:16858404, PubMed:30111536). Involved in the maintenance of H3K9me3 mark following DNA replication, when histone marks are diluted: HP1 recognizes the preexisting H3K9me3 mark and serves as a platform to recruit SUV39H1 to modify the adjacent newly incorporated histones (PubMed:10949293, PubMed:11242053, PubMed:40440427). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes (PubMed:18485871). The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus (PubMed:18485871). Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29170282"}],"value":"(Microbial infection) Plays a role in defense against mycobacterial infections. Methylates M.tuberculosis HupB on 'Lys-140', probably methylates HupB of M.bovis also. Methylation has an inhibitory effect on mycobacterial growth in the host. Macrophages expressing about 60% SUV39H1 are slightly more susceptible to M.bovis or M.tuberculosis infection. Chaetocin (an inhibitor of this enzyme) increases macrophage survival of M.tuberculosis. This protein inhibits biofilm formation by M.tuberculosis via 'Lys-140' trimethylation"}],"commentType":"FUNCTION"},{"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":"10949293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18004385"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60285"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10949293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18004385"}]}]},{"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:0000269","source":"PubMed","id":"10949293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18004385"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60289"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10949293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18004385"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16519522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19218236"}],"value":"Inhibited by S-adenosyl-L-homocysteine. Negatively regulated by CCAR2"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O54864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10202156"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10848615"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11242053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11484059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12101246"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12711603"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12789259"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917624"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15107829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16103223"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16652147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16688220"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16858404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18485871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19218236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23695662"}],"value":"Interacts with H3 and H4 histones. Interacts with GFI1B, DNMT3B, CBX1, CBX4, CCAR2, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1. Interacts with SBF1 through the SET domain. Interacts with HDAC1 and HDAC2 through the N-terminus and associates with the core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Interacts (via SET domain) with MECOM; enhances MECOM transcriptional repression activity. Interacts with LMNA; the interaction increases stability of SUV39H1. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. Interacts with ZNF152; this interaction initiates heterochromatin formation (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16409643"}],"value":"(Microbial infection) Interacts with HTLV-1 Tax protein, leading to abrogate Tax transactivation of HTLV-1 LTR"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"O95260","geneName":"ATE1","intActId":"EBI-1043378"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q86V38","geneName":"ATN1","intActId":"EBI-11954292"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q9C0K0","geneName":"BCL11B","intActId":"EBI-6597578"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q6P047","geneName":"C8orf74","intActId":"EBI-8466055"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"P83916","geneName":"CBX1","intActId":"EBI-78129"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q13185","geneName":"CBX3","intActId":"EBI-78176"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"P45973","geneName":"CBX5","intActId":"EBI-78219"},"numberOfExperiments":18,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q9BXL8","geneName":"CDCA4","intActId":"EBI-1773949"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q8NHQ1","geneName":"CEP70","intActId":"EBI-739624"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"P49761","geneName":"CLK3","intActId":"EBI-745579"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q5TAQ9","geneName":"DCAF8","intActId":"EBI-740686"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q92997","geneName":"DVL3","intActId":"EBI-739789"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q15910","geneName":"EZH2","intActId":"EBI-530054"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q6ZNL6","geneName":"FGD5","intActId":"EBI-7962481"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"A6NEM1","geneName":"GOLGA6L9","intActId":"EBI-5916454"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q9NWQ4","geneName":"GPATCH2L","intActId":"EBI-5666657"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q9BX10","geneName":"GTPBP2","intActId":"EBI-6115579"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q13547","geneName":"HDAC1","intActId":"EBI-301834"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q92769","geneName":"HDAC2","intActId":"EBI-301821"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"V9HWG0","geneName":"HEL25","intActId":"EBI-10183977"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q96ED9","geneName":"HOOK2","intActId":"EBI-743290"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"Q96ED9-2","geneName":"HOOK2","intActId":"EBI-10961706"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O43463","intActId":"EBI-349968"},"interactantTwo":{"uniProtKBAccession":"P49639","geneName":"HOXA1","intActId":"EBI-740785"},"numberOfExperiments":2,"organismD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