{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P42568","secondaryAccessions":["B1AMQ2","B2R7B3","B7Z755","D3DRJ8","Q8IVB0"],"uniProtkbId":"AF9_HUMAN","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-11-25","entryVersion":203,"sequenceVersion":2},"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":"Protein AF-9"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10861294"}],"value":"ALL1-fused gene from chromosome 9 protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16001262"}],"value":"Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein"}},{"fullName":{"value":"YEATS domain-containing protein 3"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16001262"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:7136"}],"value":"MLLT3"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10861294"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"39794553"}],"value":"AF9"},{"value":"YEATS3"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2AM29"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20159561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20471948"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25417107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27105114"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27545619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30374167"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30385749"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31776511"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39794553"}],"value":"Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (PubMed:20159561, PubMed:20471948, PubMed:25417107, PubMed:27105114, PubMed:27545619). Specifically recognizes and binds acylated histone H3, with a preference for histone H3 that is crotonylated (PubMed:25417107, PubMed:27105114, PubMed:27545619, PubMed:30374167, PubMed:30385749). Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25417107, PubMed:27105114, PubMed:27545619). Recognizes and binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114). Also recognizes and binds histone H3 acetylated and butyrylated at 'Lys-9' (H3K9ac and H3K9bu, respectively), but with lower affinity than crotonylated histone H3 (PubMed:25417107, PubMed:27105114, PubMed:30385749). In the SEC complex, MLLT3 is required to recruit the complex to crotonylated histones (PubMed:27105114, PubMed:27545619). Recruitment of the SEC complex to crotonylated histones promotes recruitment of DOT1L on active chromatin to deposit histone H3 'Lys-79' methylation (H3K79me) (PubMed:25417107). Plays a key role in hematopoietic stem cell (HSC) maintenance by preserving, rather than conferring, HSC stemness (PubMed:31776511). Acts by binding to the transcription start site of active genes in HSCs and sustaining level of H3K79me2, probably by recruiting DOT1L (PubMed:31776511). Required for DOT1L-mediated H3K79 hypermethylation at the SCNN1A promoter, resulting in transcriptional repression (By similarity). May play a role in leukemogenic gene transcription (PubMed:39794553)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30374167"}],"value":"Crotonylated lysine binding is strongly inhibited by the peptide XL-07i, carrying a 2-furancarbonyl side chain and capped with a hydrophobic carboxybenzyl group (PubMed:30374167). XL-07i targets the unique pi-pi-pi stacking interaction at the crotonylation recognition site (PubMed:30374167)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2AM29"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10898795"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11313972"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20159561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20471948"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22195968"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23145062"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23260655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25417107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30134174"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39794553"}],"value":"Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3) (PubMed:20159561, PubMed:20471948, PubMed:22195968, PubMed:23260655, PubMed:25417107, PubMed:30134174). Interacts with BCOR (PubMed:10898795). Interacts with CBX8 (PubMed:11313972). Interacts with ALKBH4 (PubMed:23145062). Interacts with acetylated or crotonylated KAT6A/MOZ; the interaction is direct (PubMed:39794553). Interacts with DOT1L; the interaction in involved in transcriptional repression of SCNN1A (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"P51825","geneName":"AFF1","intActId":"EBI-2610180"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q9UHB7","geneName":"AFF4","intActId":"EBI-395282"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q9NXW9","geneName":"ALKBH4","intActId":"EBI-8637516"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q92624","geneName":"APPBP2","intActId":"EBI-743771"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q6W2J9-1","geneName":"BCOR","intActId":"EBI-16028932"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q9HC52","geneName":"CBX8","intActId":"EBI-712912"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q8TEK3","geneName":"DOT1L","intActId":"EBI-2619253"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q8IZU1","geneName":"FAM9A","intActId":"EBI-8468186"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q5JXC2","geneName":"MIIP","intActId":"EBI-2801965"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q5SQQ9-2","geneName":"VAX1","intActId":"EBI-12227803"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P42568","intActId":"EBI-716132"},"interactantTwo":{"uniProtKBAccession":"Q7Z3I7","geneName":"ZNF572","intActId":"EBI-10172590"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25417107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27105114"}],"value":"Colocalizes with acylated histone H3 (PubMed:25417107, PubMed:27105114). Colocalizes with histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00376"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27105114"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25417107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27105114"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P42568-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P42568-2"],"sequenceIds":["VSP_054924"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31776511"}],"value":"Enriched in undifferentiated hematopoietic stem cells in fetal liver, cord blood and bone marrow"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25417107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27105114"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27545619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30374167"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30385749"}],"value":"The YEATS domain specifically recognizes and binds acylated histones, with a marked preference for histones that are crotonylated (PubMed:27105114, PubMed:27545619). Also binds histone H3 acetylated at 'Lys-9' (H3K9ac), but with lower affinity (PubMed:25417107, PubMed:27105114). Binds crotonylated lysine through a non-canonical pi-pi-pi stacking mechanism (PubMed:30374167, PubMed:30385749). The YEATS domain also binds DNA (PubMed:30385749)"}],"commentType":"DOMAIN"},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10861294"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22936661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25305204"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8506309"}],"value":"A chromosomal aberration involving MLLT3 is associated with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1. The result is a rogue activator protein. Fusion protein KMT2A-MLLT3 interacts with MEN1 and PSIP1 (PubMed:22936661, PubMed:25305204)"}]}},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16001262"}],"value":"A chromosomal aberration involving MLLT3 was observed in a patient with neuromotor development delay, cerebellar ataxia and epilepsy. Translocation t(4;9)(q35;p22)"}]}},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/5/mllt3","ftp":false}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"Protein AF-9","featureId":"PRO_0000215921"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"YEATS","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00376"}]},{"type":"Region","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Histone H3K9cr 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