{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q01196","secondaryAccessions":["A8MV94","B2RMS4","D3DSG1","O60472","O60473","O76047","O76089","Q13081","Q13755","Q13756","Q13757","Q13758","Q13759","Q15341","Q15343","Q16122","Q16284","Q16285","Q16286","Q16346","Q16347","Q92479"],"uniProtkbId":"RUNX1_HUMAN","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-11-25","entryVersion":268,"sequenceVersion":3},"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":"Runt-related transcription factor 1"}},"alternativeNames":[{"fullName":{"value":"Acute myeloid leukemia 1 protein"}},{"fullName":{"value":"Core-binding factor subunit alpha-2"},"shortNames":[{"value":"CBF-alpha-2"}]},{"fullName":{"value":"Oncogene AML-1"}},{"fullName":{"value":"Polyomavirus enhancer-binding protein 2 alpha B subunit"},"shortNames":[{"value":"PEA2-alpha B"},{"value":"PEBP2-alpha B"}]},{"fullName":{"value":"SL3-3 enhancer factor 1 alpha B subunit"}},{"fullName":{"value":"SL3/AKV core-binding factor alpha B subunit"}}]},"genes":[{"geneName":{"value":"RUNX1"},"synonyms":[{"value":"AML1"},{"value":"CBFA2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q03347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10207087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11965546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14970218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17377532"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17431401"},{"evidenceCode":"ECO:0000305"}],"value":"Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis (PubMed:17431401). Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter (PubMed:10207087, PubMed:14970218). Inhibits KAT6B-dependent transcriptional activation (By similarity). Involved in lineage commitment of immature T cell precursors. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells (PubMed:17377532). Positively regulates the expression of RORC in T-helper 17 cells (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q03347"}],"value":"Isoform AML-1G shows higher binding activities for target genes and binds TCR-beta-E2 and RAG-1 target site with threefold higher affinity than other isoforms. It is less effective in the context of neutrophil terminal differentiation"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9199349"}],"value":"Isoform AML-1L interferes with the transactivation activity of RUNX1"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q03347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10207087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10545320"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10856244"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11276260"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11742995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11965546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12377125"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917624"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14970218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16652147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17377532"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17431401"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18280240"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28533407"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9119228"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9751710"}],"value":"Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Isoform AML-1L can neither bind DNA nor heterodimerize. Interacts with TLE1 and ALYREF/THOC4 (PubMed:9119228, PubMed:9751710). Interacts with ELF1, ELF2 and SPI1 (PubMed:10207087). Interacts via its Runt domain with the ELF4 N-terminal region (PubMed:10207087). Interaction with ELF2 isoform 2 (NERF-1a) may act to repress RUNX1-mediated transactivation (PubMed:14970218). Interacts with KAT6A and KAT6B (PubMed:11742995, PubMed:11965546). Interacts with SUV39H1, leading to abrogation of transactivating and DNA-binding properties of RUNX1 (PubMed:12917624, PubMed:16652147). Interacts with YAP1 (PubMed:18280240). Interacts with HIPK2 (By similarity). Interaction with CDK6 prevents myeloid differentiation, reducing its transcription transactivation activity. Found in a complex with PRMT5, RUNX1 and CBFB. Interacts with FOXP3 (PubMed:17377532). Interacts with TBX21 (By similarity). Interacts with DPF2 (PubMed:28533407)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q01196","intActId":"EBI-925904"},"interactantTwo":{"uniProtKBAccession":"Q13951","geneName":"CBFB","intActId":"EBI-718750"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196","intActId":"EBI-925904"},"interactantTwo":{"uniProtKBAccession":"Q00534","geneName":"CDK6","intActId":"EBI-295663"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196","intActId":"EBI-925904"},"interactantTwo":{"uniProtKBAccession":"Q15723","geneName":"ELF2","intActId":"EBI-956941"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196","intActId":"EBI-925904"},"interactantTwo":{"uniProtKBAccession":"Q9H2X6","geneName":"HIPK2","intActId":"EBI-348345"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196","intActId":"EBI-925904"},"interactantTwo":{"uniProtKBAccession":"P52926","geneName":"HMGA2","intActId":"EBI-912511"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196","intActId":"EBI-925904"},"interactantTwo":{"uniProtKBAccession":"P17542","geneName":"TAL1","intActId":"EBI-1753878"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196","intActId":"EBI-925904"},"interactantTwo":{"uniProtKBAccession":"P46937","geneName":"YAP1","intActId":"EBI-1044059"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-1","intActId":"EBI-925940"},"interactantTwo":{"uniProtKBAccession":"Q04724","geneName":"TLE1","intActId":"EBI-711424"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-1","intActId":"EBI-925940"},"interactantTwo":{"uniProtKBAccession":"P59633","geneName":"3b","intActId":"EBI-25489004"},"numberOfExperiments":6,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q01196-1","intActId":"EBI-925940"},"interactantTwo":{"uniProtKBAccession":"P16371","geneName":"gro","intActId":"EBI-153866"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q01196-2","intActId":"EBI-925944"},"interactantTwo":{"uniProtKBAccession":"Q04724","geneName":"TLE1","intActId":"EBI-711424"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"O95817","geneName":"BAG3","intActId":"EBI-747185"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"O95429","geneName":"BAG4","intActId":"EBI-2949658"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q13951","geneName":"CBFB","intActId":"EBI-718750"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"O75909-2","geneName":"CCNK","intActId":"EBI-12010594"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q8WU58","geneName":"FAM222B","intActId":"EBI-2807642"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q96EF6","geneName":"FBXO17","intActId":"EBI-2510157"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q96CN9","geneName":"GCC1","intActId":"EBI-746252"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"O14964","geneName":"HGS","intActId":"EBI-740220"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q8NI38","geneName":"NFKBID","intActId":"EBI-10271199"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q7RTU3","geneName":"OLIG3","intActId":"EBI-10225049"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"P09234","geneName":"SNRPC","intActId":"EBI-766589"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q15562-2","geneName":"TEAD2","intActId":"EBI-9370956"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q15561","geneName":"TEAD4","intActId":"EBI-747736"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"Q96M29","geneName":"TEKT5","intActId":"EBI-10239812"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q01196-8","intActId":"EBI-12001422"},"interactantTwo":{"uniProtKBAccession":"A5D8V6","geneName":"VPS37C","intActId":"EBI-2559305"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR 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Highest levels in thymus, bone marrow and peripheral blood"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25134913"}],"value":"Up-regulated by phorbol myristate acetate (PMA)"}],"commentType":"INDUCTION"},{"texts":[{"value":"A proline/serine/threonine rich region at the C-terminus is necessary for transcriptional activation of target genes"}],"commentType":"DOMAIN"},{"texts":[{"value":"Phosphorylated in its C-terminus upon IL-6 treatment. Phosphorylation enhances interaction with KAT6A"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917624"}],"value":"Methylated"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18695000"}],"value":"Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA. This phosphorylation promotes subsequent EP300 phosphorylation"}],"commentType":"PTM"},{"commentType":"DISEASE","note":{"texts":[{"value":"A chromosomal aberration involving RUNX1/AML1 is a cause of M2 type acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1T1"}]}},{"commentType":"DISEASE","note":{"texts":[{"value":"A chromosomal aberration involving RUNX1/AML1 is a cause of therapy-related myelodysplastic syndrome (T-MDS). Translocation t(3;21)(q26;q22) with EAP or MECOM"}]}},{"commentType":"DISEASE","note":{"texts":[{"value":"A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22) with EAP or MECOM"}]}},{"commentType":"DISEASE","note":{"texts":[{"value":"A chromosomal aberration involving RUNX1/AML1 is found in childhood acute lymphoblastic leukemia (ALL). Translocation t(12;21)(p13;q22) with TEL. The translocation fuses the 3'-end of TEL to the alternate 5'-exon of AML-1H"}]}},{"commentType":"DISEASE","note":{"texts":[{"value":"A chromosomal aberration involving RUNX1 is found in acute leukemia. Translocation t(11,21)(q13;q22) that forms a MACROD1-RUNX1 fusion protein"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Familial platelet disorder with associated myeloid malignancy","diseaseAccession":"DI-01597","acronym":"FPDMM","description":"Autosomal dominant disease characterized by qualitative and quantitative platelet defects, and propensity to develop acute myelogenous leukemia.","diseaseCrossReference":{"database":"MIM","id":"601399"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10508512"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","note":{"texts":[{"value":"A chromosomal aberration involving RUNX1/AML1 is found in therapy-related myeloid malignancies. 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