{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P01106","secondaryAccessions":["A0A024R9L7","A0A087WUS5","A8WFE7","H0YBT0","P01107","Q14026"],"uniProtkbId":"MYC_HUMAN","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-02-22","entryVersion":282,"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":{"value":"Myc proto-oncogene protein"}},"alternativeNames":[{"fullName":{"value":"Class E basic helix-loop-helix protein 39"},"shortNames":[{"value":"bHLHe39"}]},{"fullName":{"value":"Proto-oncogene c-Myc"}},{"fullName":{"value":"Transcription factor p64"}}]},"genes":[{"geneName":{"value":"MYC"},"synonyms":[{"value":"BHLHE39"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P01108"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20010808"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24940000"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25956029"}],"value":"Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3' (PubMed:24940000, PubMed:25956029). Activates the transcription of growth-related genes (PubMed:24940000, PubMed:25956029). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed:24940000, PubMed:25956029). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P01108"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15103331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15674325"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15723054"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17308053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17311883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17558397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17632056"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17873522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22719065"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25775507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25956029"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38225354"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9680483"}],"value":"Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (PubMed:9680483). Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-73 and Ser-77) with FBXW7 (PubMed:17558397, PubMed:25775507). Interacts with PIM2. Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6 (By similarity). Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (PubMed:25956029). Interacts with CIP2A; leading to the stabilization of MYC (PubMed:17632056). Interacts with NUP205 (PubMed:22719065). Interacts with HEATR1; the interaction is required for localization of MYC to the nucleolus (PubMed:38225354)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q9UBB4","geneName":"ATXN10","intActId":"EBI-702390"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"O15169","geneName":"AXIN1","intActId":"EBI-710484"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"O00499-10","geneName":"BIN1","intActId":"EBI-7689134"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"O00499-11","geneName":"BIN1","intActId":"EBI-7689211"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q15059","geneName":"BRD3","intActId":"EBI-1383460"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"P55212","geneName":"CASP6","intActId":"EBI-718729"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"P45973","geneName":"CBX5","intActId":"EBI-78219"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q8N163","geneName":"CCAR2","intActId":"EBI-355410"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"P06307","geneName":"CCK","intActId":"EBI-6624398"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"A5D8W4","geneName":"CDH1","intActId":"EBI-7793316"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"P11802","geneName":"CDK4","intActId":"EBI-295644"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q86XR8","geneName":"CEP57","intActId":"EBI-308614"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"P28329-3","geneName":"CHAT","intActId":"EBI-25837549"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q14839","geneName":"CHD4","intActId":"EBI-372916"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"O15111","geneName":"CHUK","intActId":"EBI-81249"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q8TCG1","geneName":"CIP2A","intActId":"EBI-1379376"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q01658","geneName":"DR1","intActId":"EBI-750300"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q15029","geneName":"EFTUD2","intActId":"EBI-357897"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q96L91","geneName":"EP400","intActId":"EBI-399163"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q96L91-2","geneName":"EP400","intActId":"EBI-15698003"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q969H0","geneName":"FBXW7","intActId":"EBI-359574"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"Q8N3Y1","geneName":"FBXW8","intActId":"EBI-914770"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01106","intActId":"EBI-447544"},"interactantTwo":{"uniProtKBAccession":"P22607","geneName":"FGFR3","intActId":"EBI-348399"},"numberOfExperiments":3,"o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LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30158517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38225354"}],"value":"Association with chromatin is reduced by hyperphosphorylation (PubMed:30158517). Localization to the nucleolus is dependent on HEATR1 (PubMed:38225354)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17558397"}],"value":"Nucleus, nucleoplasm","id":"SL-0190"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17558397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25775507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38225354"}],"value":"Nucleus, nucleolus","id":"SL-0188"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22719065"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38225354"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22719065"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30158517"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing","Alternative initiation"],"isoforms":[{"name":{"value":"2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3277717"}],"value":"c-myc 1"}],"isoformIds":["P01106-2"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3277717"}],"value":"c-myc 2"}],"isoformIds":["P01106-1"],"sequenceIds":["VSP_061778"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["P01106-3"],"sequenceIds":["VSP_061779"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34342803"}],"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:0000250","source":"UniProtKB","id":"P01108"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15103331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1597196"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17558397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19966300"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20713526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22307329"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25438055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25803737"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30158517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8386367"}],"value":"Phosphorylated by PRKDC (PubMed:1597196). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence (PubMed:19966300, PubMed:20713526). Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73 (PubMed:22307329). Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:8386367). Dephosphorylation at multiple sites by the PNUTS-PP1 complex promotes MYC stability by preventing ubiquitination by the SCF(FBXW7) complex (PubMed:30158517). Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (PubMed:25438055, PubMed:25803737)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P01108"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15103331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17558397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17873522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20551172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25775507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29779948"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30158517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33208877"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478862"}],"value":"Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-73 and Ser-77, leading to its degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:25775507, PubMed:30158517). In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation (PubMed:17558397, PubMed:17873522). In the nucleolus, however, ubiquitination is not counteracted by USP28 but by USP36, due to the lack of interaction between isoform 3 of FBXW7 (FBW7gamma) and USP28, explaining the selective MYC degradation in the nucleolus (PubMed:17558397, PubMed:25775507). Also polyubiquitinated by the DCX(TRPC4AP) complex (PubMed:20551172, PubMed:29779948). Ubiquitinated by UBR5 when not forming a heterodimer with another bHLH protein, leading to its degradation: UBR5 recognizes and binds a degron that is only available upon heterodimer dissociation (PubMed:33208877, PubMed:37478862). Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By similarity)"}],"commentType":"PTM"},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2069907"}],"value":"A chromosomal aberration involving MYC may be a cause of a form of B-cell chronic lymphocytic leukemia. Translocation t(8;12)(q24;q22) with BTG1"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Burkitt lymphoma","diseaseAccession":"DI-02613","acronym":"BL","description":"A form of undifferentiated malignant lymphoma commonly manifested as a large osteolytic lesion in the jaw or as an abdominal mass.","diseaseCrossReference":{"database":"MIM","id":"113970"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2166998"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8220424"}]},"note":{"texts":[{"value":"The gene represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving MYC are usually found in Burkitt lymphoma. Translocations t(8;14), t(8;22) or t(2;8) which juxtapose MYC to one of the heavy or light chain immunoglobulin gene loci"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18035408"}],"value":"POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3277717"}],"value":"Alternative translation initiation from an upstream, in-frame non-ATG (CTG) codon or a downstream ATG start site results in the production of 2 isoforms with distinct N-termini, shown in this entry as isoforms 2/3 and isoform 1, respectively"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3277717"}],"value":"Produced by alternative translation initiation from a CTG codon, which is translated as Met"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3277717"}],"value":"Produced by alternative translation initiation from a CTG codon, which is translated as Met, and alternative splicing"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 3"},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/27/MYC","ftp":false},{"commentType":"WEB RESOURCE","resourceName":"Wikipedia","resourceUrl":"https://en.wikipedia.org/wiki/Myc","ftp":false,"note":"Myc entry"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"Myc proto-oncogene protein","featureId":"PRO_0000127293"},{"type":"Domain","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"bHLH","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00981"}]},{"type":"Region","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Basic motif","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00981"}]},{"type":"Region","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"Helix-loop-helix motif","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00981"}]},{"type":"Region","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":449,"modifier":"EXACT"}},"description":"Leucine-zipper"},{"type":"Motif","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"9aaTAD","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34342803"}]},{"type":"Motif","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"UBR5-degron","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478862"}]},{"type":"Compositional bias","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"20068231"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Phosphothreonine; 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