{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q03164","secondaryAccessions":["E9PQG7","Q13743","Q13744","Q14845","Q16364","Q59FF2","Q6UBD1","Q9HBJ3","Q9UD94","Q9UMA3"],"uniProtkbId":"KMT2A_HUMAN","entryAudit":{"firstPublicDate":"1993-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-05-01","entryVersion":269,"sequenceVersion":5},"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 2A"},"shortNames":[{"value":"Lysine N-methyltransferase 2A"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12453419"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19187761"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25561738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26886794"}],"value":"2.1.1.364"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12453419"}],"value":"ALL-1"}},{"fullName":{"value":"CXXC-type zinc finger protein 7"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cysteine methyltransferase KMT2A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"}],"value":"2.1.1.-"}]},{"fullName":{"value":"Myeloid/lymphoid or mixed-lineage leukemia"}},{"fullName":{"value":"Myeloid/lymphoid or mixed-lineage leukemia protein 1"}},{"fullName":{"value":"Trithorax-like protein"}},{"fullName":{"value":"Zinc finger protein HRX"}}],"contains":[{"recommendedName":{"fullName":{"value":"MLL cleavage product N320"}},"alternativeNames":[{"fullName":{"value":"N-terminal cleavage product of 320 kDa"},"shortNames":[{"value":"p320"}]}]},{"recommendedName":{"fullName":{"value":"MLL cleavage product C180"}},"alternativeNames":[{"fullName":{"value":"C-terminal cleavage product of 180 kDa"},"shortNames":[{"value":"p180"}]}]}]},"genes":[{"geneName":{"value":"KMT2A"},"synonyms":[{"value":"ALL1"},{"value":"CXXC7"},{"value":"HRX"},{"value":"HTRX"},{"value":"MLL"},{"value":"MLL1"},{"value":"TRX1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P55200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10490642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12453419"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15960975"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19187761"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20010842"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21220120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26886794"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20677832"}],"value":"Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60264"},{"database":"Rhea","id":"RHEA-COMP:15543"},{"database":"Rhea","id":"RHEA-COMP:15547"},{"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":"2.1.1.364","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12453419"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19187761"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25561738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26886794"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60265"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19556245"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25561738"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60268"},{"database":"Rhea","id":"RHEA-COMP:15540"},{"database":"Rhea","id":"RHEA-COMP:15543"},{"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":"19187761"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25561738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26886794"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:60269"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25561738"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-cysteinyl-[protein] + S-adenosyl-L-methionine = S-methyl-L-cysteinyl-[protein] + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66544"},{"database":"Rhea","id":"RHEA-COMP:10131"},{"database":"Rhea","id":"RHEA-COMP:10132"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:82612"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66545"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"}]}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":10.4,"unit":"uM","substrate":"S-adenosyl-L-methionine (for histone-lysine N-methyltransferase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"}]},{"constant":6.5,"unit":"uM","substrate":"S-adenosyl-L-methionine (for protein-cysteine methyltransferase)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P55200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10490642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12482972"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14636557"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15199122"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15960975"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16253272"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16990798"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17500065"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18829459"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18840606"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19187761"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20541251"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20677832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21220120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22327296"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22665483"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23178126"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23651431"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25082813"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25305204"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25561738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26886794"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29997176"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9537414"}],"value":"MLL cleavage product N320 heterodimerizes with MLL cleavage product C180 (via SET and FYRC domains). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as well as the facultative components BACC1, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15199122, PubMed:15960975, PubMed:17500065, PubMed:19187761, PubMed:19556245, PubMed:23508102, PubMed:26886794). Forms a core complex with the evolutionary conserved subcomplex WRAD composed of WDR5, RBBP5, ASH2L/ASH2 and DPY30 subunits; WRAD differentially stimulates the methyltransferase activity (PubMed:25561738). Interacts (via WIN motif) with WDR5; the interaction is direct (PubMed:18829459, PubMed:18840606, PubMed:19556245, PubMed:22665483). Interaction with WDR5 is required for stable interaction with ASH2L and RBBP5, and thereby also for optimal histone methyltransferase activity (PubMed:26886794). Interacts with KAT8/MOF; the interaction is direct (PubMed:15960975). Interacts with SBF1 and PPP1R15A (PubMed:10490642, PubMed:9537414). Interacts with ZNF335 (PubMed:23178126). Interacts with CLOCK and BMAL1 in a circadian manner (By similarity). Interacts with PPIE; this results in decreased histone H3 methyltransferase activity (PubMed:20541251, PubMed:20677832). Interacts with CREBBP (PubMed:16253272). Interacts with the WRAD complex composed of WDR5, RBBP5, ASH2L and DPY30 (PubMed:22665483). Interacts (via MBM motif) with MEN1 (PubMed:22327296, PubMed:22936661, PubMed:25305204). Interacts (via IBM motifs) with PSIP1 (via IBD domain) with moderate affinity whereas the KMT2A-MEN1 complex interacts with a greater affinity; MEN1 enhances interaction of KMT2A with PSIP1 (PubMed:22327296, PubMed:25082813, PubMed:25305204, PubMed:29997176). Phosphorylation increases its affinity for PSIP1 (PubMed:29997176). Forms a complex with CREBBP and CREB1 (PubMed:23651431)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34850113"}],"value":"(Microbial infection) Interacts with herpes virus 8/HHV-8 protein LANA1; this interaction regulates the MLL1 histone methyltransferase activity on viral DNA"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"P10275","geneName":"AR","intActId":"EBI-608057"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q9UBL3-3","geneName":"ASH2L","intActId":"EBI-16130425"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q6P1J9","geneName":"CDC73","intActId":"EBI-930143"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q6PD62","geneName":"CTR9","intActId":"EBI-1019583"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"P68431","geneName":"H3C12","intActId":"EBI-79722"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q9H7Z6","geneName":"KAT8","intActId":"EBI-896414"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q03164","geneName":"KMT2A","intActId":"EBI-591370"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"O00255-2","geneName":"MEN1","intActId":"EBI-9869387"},"numberOfExperiments":12,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q8N7H5","geneName":"PAF1","intActId":"EBI-2607770"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q9UNP9","geneName":"PPIE","intActId":"EBI-591818"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q15291","geneName":"RBBP5","intActId":"EBI-592823"},"numberOfExperiments":12,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"P26373","geneName":"RPL13","intActId":"EBI-356849"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q96EB6","geneName":"SIRT1","intActId":"EBI-1802965"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q13309-1","geneName":"SKP2","intActId":"EBI-15490084"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"P61964","geneName":"WDR5","intActId":"EBI-540834"},"numberOfExperiments":17,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"Q9WTL8","geneName":"Bmal1","intActId":"EBI-644534"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"O08785","geneName":"Clock","intActId":"EBI-79859"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q03164","intActId":"EBI-591370"},"interactantTwo":{"uniProtKBAccession":"P45481","geneName":"Crebbp","intActId":"EBI-296306"},"numberOfExperiments":7,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000390949","intActId":"EBI-2610266"},"interactantTwo":{"uniProtKBAccession":"Q02548","geneName":"PAX5","intActId":"EBI-296331"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000390950","intActId":"EBI-2638616"},"interactantTwo":{"uniProtKBAccession":"Q92794","geneName":"KAT6A","intActId":"EBI-948013"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000390950","intActId":"EBI-2638616"},"interactantTwo":{"uniProtKBAccession":"P61964","geneName":"WDR5","intActId":"EBI-540834"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12482972"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25593309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34850113"}],"value":"Nucleus","id":"SL-0191"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"MLL cleavage product N320","subcellularLocations":[{"location":{"value":"Nucleus","id":"SL-0191"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"MLL cleavage product C180","note":{"texts":[{"value":"Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320"}]},"subcellularLocations":[{"location":{"value":"Nucleus","id":"SL-0191"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q03164-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"value":"14P-18B"}],"isoformIds":["Q03164-2"],"sequenceIds":["VSP_006666"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q03164-3"],"sequenceIds":["VSP_046879"],"isoformSequenceStatus":"Described"}]},{"texts":[{"value":"Heart, lung, brain and T- and B-lymphocytes"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17467953"}],"value":"The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19187761"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26886794"}],"value":"The SET domain structure is atypical and is not in an optimal position to have methyltransferase activity. It requires other components of the MLL1/MLL complex, such as ASH2L or RBBP5, to order the active site and obtain optimal histone methyltransferase activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16990798"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20010842"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29276034"}],"value":"The CXXC-type zinc finger binds to DNA sequence elements containing unnmethylated CpG dinucleotides"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20541251"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20677832"}],"value":"The third PHD-type zinc-finger binds both trimethylated histone H3K4me3 and PPIE; histone and PPIE bind to distinct surfaces (PubMed:20541251, PubMed:20677832). Nevertheless, PPIE binding and histone binding are mutually inhibitory (PubMed:20677832). Isomerization of a peptidylproline bond in the linker between the third PHD-type zinc-finger and the bromo domain disrupts the interaction between the bromo domain and the third PHD-type zinc-finger, and thereby facilitates interaction with PPIE (PubMed:20541251)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12482972"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14636557"}],"value":"Proteolytic cleavage by TASP1 generates MLL cleavage product N320 and MLL cleavage product C180, which reassemble through a non-covalent association. 2 cleavage sites exist, cleavage site 1 (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products N320 and C180. CS2 is the major site"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29997176"}],"value":"Phosphorylation increases its interaction with PSIP1"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24235145"}],"value":"Auto-methylated at Cys-3882: auto-methylation is inhibited by the WRAD complex and unmodified histone H3"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Wiedemann-Steiner syndrome","diseaseAccession":"DI-03533","acronym":"WDSTS","description":"A syndrome characterized by hairy elbows (hypertrichosis cubiti), intellectual disability, a distinctive facial appearance, and short stature. Facial characteristics include long eyelashes, thick or arched eyebrows with a lateral flare, and downslanting and vertically narrow palpebral fissures.","diseaseCrossReference":{"database":"MIM","id":"605130"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22795537"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10490642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22936661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25305204"}],"value":"Chromosomal aberrations involving KMT2A are a cause of acute leukemias. Translocation t(1;11)(q21;q23) with MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21; translocation t(3,11)(q25,q23) with GMPS; translocation t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation t(6;11)(q27;q23) with AFDN; translocation t(9;11)(p22;q23) with MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1; translocation t(10;11)(p12;q23) with MLLT10/AF10; t(11;15)(q23;q14) with KNL1 and ZFYVE19; translocation t(11;17)(q23;q21) with MLLT6/AF17; translocation t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3) with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7; translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation t(4;11)(p12;q23) with FRYL. Fusion proteins KMT2A-MLLT1, KMT2A-MLLT3 and KMT2A-ELL interact with PPP1R15A and, on the contrary to unfused KMT2A, inhibit PPP1R15A-induced apoptosis. Fusion protein KMT2A-MLLT3 interacts with MEN1 and PSIP1 (PubMed:22936661, PubMed:25305204)"}]}},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10490642"}],"value":"A chromosomal aberration involving KMT2A may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00190"}],"value":"Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. 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