# Myocyte-specific enhancer factor 2A

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Protein-coding gene in the species Homo sapiens

MEF2A Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1C7U, 1EGW, 1LEW, 3KOV, 3MU6, 3P57 Identifiers Aliases MEF2A, ADCAD1, RSRFC4, RSRFC9, mef2, myocyte enhancer factor 2A External IDs OMIM: 600660; MGI: 99532; HomoloGene: 4080; GeneCards: MEF2A; OMA:MEF2A - orthologs Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q26.3 Start 99,565,417 bp[1] End 99,716,488 bp[1] Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 C|7 36.72 cM Start 67,231,163 bp[2] End 67,372,858 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon myocardium cardiac muscle tissue of right atrium right ventricle myocardium of left ventricle biceps brachii Skeletal muscle tissue of biceps brachii skin of thigh middle temporal gyrus tibia Top expressed in medial dorsal nucleus lateral geniculate nucleus lateral septal nucleus medial geniculate nucleus atrioventricular valve stroma of bone marrow right ventricle atrium cerebellar vermis ankle More reference expression data BioGPS More reference expression data Gene ontology Molecular function sequence-specific DNA binding transcription coactivator activity DNA binding protein dimerization activity DNA-binding transcription factor activity DNA-binding transcription activator activity, RNA polymerase II-specific histone deacetylase binding chromatin binding RNA polymerase II cis-regulatory region sequence-specific DNA binding protein binding histone acetyltransferase binding protein heterodimerization activity transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding SMAD binding protein kinase binding RNA polymerase II transcription regulatory region sequence-specific DNA binding DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component transcription regulator complex nucleoplasm nucleus cytosol Biological process cellular response to calcium ion cell differentiation regulation of transcription, DNA-templated mitochondrial genome maintenance dendrite morphogenesis positive regulation of muscle cell differentiation muscle organ development negative regulation of transcription by RNA polymerase II transcription, DNA-templated nervous system development ERK5 cascade multicellular organism development positive regulation of transcription, DNA-templated development of the heart cardiac conduction mitochondrion distribution ventricular cardiac myofibril assembly positive regulation of transcription by RNA polymerase II apoptotic process positive regulation of cardiac muscle hypertrophy transcription by RNA polymerase II MAPK cascade positive regulation of glucose import Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 4205 17258 Ensembl ENSG00000068305 ENSMUSG00000030557 UniProt Q02078 Q60929 RefSeq (mRNA) NM_001130926 NM_001130927 NM_001130928 NM_001171894 NM_005587 NM_001319206 NM_001352614 NM_001352615 NM_001352616 NM_001352617 NM_001352618 NM_001365201 NM_001365202 NM_001365203 NM_001365204 NM_001365205 NM_001365206 NM_001365207 NM_001365208 NM_001365209 NM_001365210 NM_001365211 NM_001393558 NM_001393559 NM_001393560 NM_001393561 NM_001033713 NM_001291191 NM_001291192 NM_001291195 NM_001291196 NM_001357324 NM_001357325 RefSeq (protein) NP_001124398 NP_001124399 NP_001124400 NP_001165365 NP_001306135 NP_005578 NP_001339543 NP_001339544 NP_001339545 NP_001339546 NP_001339547 NP_001352130 NP_001352131 NP_001352132 NP_001352133 NP_001352134 NP_001352135 NP_001352136 NP_001352137 NP_001352138 NP_001352139 NP_001352140 NP_001028885 NP_001278120 NP_001278121 NP_001278124 NP_001278125 NP_001344253 NP_001344254 Location (UCSC) Chr 15: 99.57 – 99.72 Mb Chr 7: 67.23 – 67.37 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Myocyte-specific enhancer factor 2A** is a [protein](/source/Protein) that in humans is encoded by the *MEF2A* [gene](/source/Gene).[5][6] MEF2A is a [transcription factor](/source/Transcription_factor) in the [Mef2](/source/Mef2) family. In humans it is located on [chromosome 15q26](/source/Chromosome_15_(human)). Certain [mutations](/source/Mutation) in MEF2A cause an [autosomal dominant](/source/Autosomal_dominant) form of [coronary artery disease](/source/Coronary_artery_disease) and [myocardial infarction](/source/Myocardial_infarction).

## Function

The process of differentiation from mesodermal precursor cells to myoblasts has led to the discovery of a variety of tissue-specific factors that regulate muscle gene expression. The myogenic basic helix-loop-helix proteins, including myoD (MIM 159970), myogenin (MIM 159980), MYF5 (MIM 159990), and MRF4 (MIM 159991) are 1 class of identified factors. A second family of DNA binding regulatory proteins is the myocyte-specific enhancer factor-2 (MEF2) family. Each of these proteins binds to the MEF2 target DNA sequence present in the regulatory regions of many, if not all, muscle-specific genes. The MEF2 genes are members of the MADS gene family (named for the yeast mating type-specific transcription factor MCM1, the plant homeotic genes 'agamous' and 'deficiens' and the human serum response factor SRF (MIM 600589)), a family that also includes several homeotic genes and other transcription factors, all of which share a conserved DNA-binding domain.[supplied by OMIM][6]

## Interactions

Myocyte-specific enhancer factor 2A has been shown to [interact](/source/Protein-protein_interaction) with:

- [ASCL1](/source/ASCL1),[7]

- [EP300](/source/EP300),[8]

- [HDAC4](/source/HDAC4),[9][10]

- [HDAC9](/source/HDAC9),[9][10]

- [Histone deacetylase 5](/source/Histone_deacetylase_5),[10]

- [MAPK14](/source/MAPK14),[11][12]

- [MEF2D](/source/MEF2D),[13]

- [Mothers against decapentaplegic homolog 2](/source/Mothers_against_decapentaplegic_homolog_2),[14] and

- [Thyroid hormone receptor alpha](/source/Thyroid_hormone_receptor_alpha)[8] and

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000068305](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000068305) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000030557](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000030557) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=4205). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=17258). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid1516833_5-0)** Yu YT, Breitbart RE, Smoot LB, Lee Y, Mahdavi V, Nadal-Ginard B (October 1992). ["Human myocyte-specific enhancer factor 2 comprises a group of tissue-restricted MADS box transcription factors"](https://doi.org/10.1101%2Fgad.6.9.1783). *Genes Dev*. **6** (9): 1783–98. [doi](/source/Doi_(identifier)):[10.1101/gad.6.9.1783](https://doi.org/10.1101%2Fgad.6.9.1783). [PMID](/source/PMID_(identifier)) [1516833](https://pubmed.ncbi.nlm.nih.gov/1516833).

1. ^ [***a***](#cite_ref-entrez_6-0) [***b***](#cite_ref-entrez_6-1) ["Entrez Gene: MEF2A MADS box transcription enhancer factor 2, polypeptide A (myocyte enhancer factor 2A)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=4205).

1. **[^](#cite_ref-pmid8662987_7-0)** Mao Z, Nadal-Ginard B (June 1996). ["Functional and physical interactions between mammalian achaete-scute homolog 1 and myocyte enhancer factor 2A"](https://doi.org/10.1074%2Fjbc.271.24.14371). *J. Biol. Chem*. **271** (24): 14371–5. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.24.14371](https://doi.org/10.1074%2Fjbc.271.24.14371). [PMID](/source/PMID_(identifier)) [8662987](https://pubmed.ncbi.nlm.nih.gov/8662987).

1. ^ [***a***](#cite_ref-pmid12371907_8-0) [***b***](#cite_ref-pmid12371907_8-1) De Luca A, Severino A, De Paolis P, Cottone G, De Luca L, De Falco M, Porcellini A, Volpe M, Condorelli G (February 2003). ["p300/cAMP-response-element-binding-protein ('CREB')-binding protein (CBP) modulates co-operation between myocyte enhancer factor 2A (MEF2A) and thyroid hormone receptor-retinoid X receptor"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223100). *Biochem. J*. **369** (Pt 3): 477–84. [doi](/source/Doi_(identifier)):[10.1042/BJ20020057](https://doi.org/10.1042%2FBJ20020057). [PMC](/source/PMC_(identifier)) [1223100](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223100). [PMID](/source/PMID_(identifier)) [12371907](https://pubmed.ncbi.nlm.nih.gov/12371907).

1. ^ [***a***](#cite_ref-pmid10487761_9-0) [***b***](#cite_ref-pmid10487761_9-1) Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T (September 1999). ["HDAC4 deacetylase associates with and represses the MEF2 transcription factor"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171580). *EMBO J*. **18** (18): 5099–107. [doi](/source/Doi_(identifier)):[10.1093/emboj/18.18.5099](https://doi.org/10.1093%2Femboj%2F18.18.5099). [PMC](/source/PMC_(identifier)) [1171580](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171580). [PMID](/source/PMID_(identifier)) [10487761](https://pubmed.ncbi.nlm.nih.gov/10487761).

1. ^ [***a***](#cite_ref-pmid10748098_10-0) [***b***](#cite_ref-pmid10748098_10-1) [***c***](#cite_ref-pmid10748098_10-2) Lemercier C, Verdel A, Galloo B, Curtet S, Brocard MP, Khochbin S (May 2000). ["mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity"](https://hal.archives-ouvertes.fr/hal-00379796/document). *J. Biol. Chem*. **275** (20): 15594–9. [doi](/source/Doi_(identifier)):[10.1074/jbc.M908437199](https://doi.org/10.1074%2Fjbc.M908437199). [PMID](/source/PMID_(identifier)) [10748098](https://pubmed.ncbi.nlm.nih.gov/10748098).

1. **[^](#cite_ref-pmid9858528_11-0)** Zhao M, New L, Kravchenko VV, Kato Y, Gram H, di Padova F, Olson EN, Ulevitch RJ, Han J (January 1999). ["Regulation of the MEF2 family of transcription factors by p38"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC83862). *Mol. Cell. Biol*. **19** (1): 21–30. [doi](/source/Doi_(identifier)):[10.1128/mcb.19.1.21](https://doi.org/10.1128%2Fmcb.19.1.21). [PMC](/source/PMC_(identifier)) [83862](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC83862). [PMID](/source/PMID_(identifier)) [9858528](https://pubmed.ncbi.nlm.nih.gov/9858528).

1. **[^](#cite_ref-pmid10330143_12-0)** Yang SH, Galanis A, Sharrocks AD (June 1999). ["Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC104362). *Mol. Cell. Biol*. **19** (6): 4028–38. [doi](/source/Doi_(identifier)):[10.1128/mcb.19.6.4028](https://doi.org/10.1128%2Fmcb.19.6.4028). [PMC](/source/PMC_(identifier)) [104362](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC104362). [PMID](/source/PMID_(identifier)) [10330143](https://pubmed.ncbi.nlm.nih.gov/10330143).

1. **[^](#cite_ref-pmid8798771_13-0)** Ornatsky OI, McDermott JC (October 1996). ["MEF2 protein expression, DNA binding specificity and complex composition, and transcriptional activity in muscle and non-muscle cells"](https://doi.org/10.1074%2Fjbc.271.40.24927). *J. Biol. Chem*. **271** (40): 24927–33. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.40.24927](https://doi.org/10.1074%2Fjbc.271.40.24927). [PMID](/source/PMID_(identifier)) [8798771](https://pubmed.ncbi.nlm.nih.gov/8798771).

1. **[^](#cite_ref-pmid11160896_14-0)** Quinn ZA, Yang CC, Wrana JL, McDermott JC (February 2001). ["Smad proteins function as co-modulators for MEF2 transcriptional regulatory proteins"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC30396). *Nucleic Acids Res*. **29** (3): 732–42. [doi](/source/Doi_(identifier)):[10.1093/nar/29.3.732](https://doi.org/10.1093%2Fnar%2F29.3.732). [PMC](/source/PMC_(identifier)) [30396](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC30396). [PMID](/source/PMID_(identifier)) [11160896](https://pubmed.ncbi.nlm.nih.gov/11160896).

## Further reading

- Wang Q (2005). ["Advances in the Genetic Basis of Coronary Artery Disease"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1783687). *Current Atherosclerosis Reports*. **7** (3): 235–41. [doi](/source/Doi_(identifier)):[10.1007/s11883-005-0012-6](https://doi.org/10.1007%2Fs11883-005-0012-6). [PMC](/source/PMC_(identifier)) [1783687](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1783687). [PMID](/source/PMID_(identifier)) [15811259](https://pubmed.ncbi.nlm.nih.gov/15811259).

- Wang Q (2005). ["Molecular genetics of coronary artery disease"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1579824). *Curr. Opin. Cardiol*. **20** (3): 182–8. [doi](/source/Doi_(identifier)):[10.1097/01.hco.0000160373.77190.f1](https://doi.org/10.1097%2F01.hco.0000160373.77190.f1). [PMC](/source/PMC_(identifier)) [1579824](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1579824). [PMID](/source/PMID_(identifier)) [15861005](https://pubmed.ncbi.nlm.nih.gov/15861005).

- Funk WD, Wright WE (1992). ["Cyclic amplification and selection of targets for multicomponent complexes: myogenin interacts with factors recognizing binding sites for basic helix-loop-helix, nuclear factor 1, myocyte-specific enhancer-binding factor 2, and COMP1 factor"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC50156). *Proc. Natl. Acad. Sci. U.S.A*. **89** (20): 9484–8. [Bibcode](/source/Bibcode_(identifier)):[1992PNAS...89.9484F](https://ui.adsabs.harvard.edu/abs/1992PNAS...89.9484F). [doi](/source/Doi_(identifier)):[10.1073/pnas.89.20.9484](https://doi.org/10.1073%2Fpnas.89.20.9484). [PMC](/source/PMC_(identifier)) [50156](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC50156). [PMID](/source/PMID_(identifier)) [1329097](https://pubmed.ncbi.nlm.nih.gov/1329097).

- Pollock R, Treisman R (1992). ["Human SRF-related proteins: DNA-binding properties and potential regulatory targets"](https://doi.org/10.1101%2Fgad.5.12a.2327). *Genes Dev*. **5** (12A): 2327–41. [doi](/source/Doi_(identifier)):[10.1101/gad.5.12a.2327](https://doi.org/10.1101%2Fgad.5.12a.2327). [PMID](/source/PMID_(identifier)) [1748287](https://pubmed.ncbi.nlm.nih.gov/1748287).

- Molkentin JD, Black BL, Martin JF, Olson EN (1996). ["Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteins"](https://doi.org/10.1016%2F0092-8674%2895%2990139-6). *Cell*. **83** (7): 1125–36. [doi](/source/Doi_(identifier)):[10.1016/0092-8674(95)90139-6](https://doi.org/10.1016%2F0092-8674%2895%2990139-6). [PMID](/source/PMID_(identifier)) [8548800](https://pubmed.ncbi.nlm.nih.gov/8548800).

- Hobson GM, Krahe R, Garcia E, Siciliano MJ, Funanage VL (1996). "Regional chromosomal assignments for four members of the MADS domain transcription enhancer factor 2 (MEF2) gene family to human chromosomes 15q26, 19p12, 5q14, and 1q12-q23". *Genomics*. **29** (3): 704–11. [doi](/source/Doi_(identifier)):[10.1006/geno.1995.9007](https://doi.org/10.1006%2Fgeno.1995.9007). [PMID](/source/PMID_(identifier)) [8575763](https://pubmed.ncbi.nlm.nih.gov/8575763).

- Mao Z, Nadal-Ginard B (1996). ["Functional and physical interactions between mammalian achaete-scute homolog 1 and myocyte enhancer factor 2A"](https://doi.org/10.1074%2Fjbc.271.24.14371). *J. Biol. Chem*. **271** (24): 14371–5. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.24.14371](https://doi.org/10.1074%2Fjbc.271.24.14371). [PMID](/source/PMID_(identifier)) [8662987](https://pubmed.ncbi.nlm.nih.gov/8662987).

- Suzuki E, Lowry J, Sonoda G, Testa JR, Walsh K (1996). "Structures and chromosome locations of the human MEF2A gene and a pseudogene MEF2AP". *Cytogenet. Cell Genet*. **73** (3): 244–9. [doi](/source/Doi_(identifier)):[10.1159/000134348](https://doi.org/10.1159%2F000134348). [PMID](/source/PMID_(identifier)) [8697817](https://pubmed.ncbi.nlm.nih.gov/8697817).

- Ornatsky OI, McDermott JC (1996). ["MEF2 protein expression, DNA binding specificity and complex composition, and transcriptional activity in muscle and non-muscle cells"](https://doi.org/10.1074%2Fjbc.271.40.24927). *J. Biol. Chem*. **271** (40): 24927–33. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.40.24927](https://doi.org/10.1074%2Fjbc.271.40.24927). [PMID](/source/PMID_(identifier)) [8798771](https://pubmed.ncbi.nlm.nih.gov/8798771).

- Black BL, Molkentin JD, Olson EN (1998). ["Multiple Roles for the MyoD Basic Region in Transmission of Transcriptional Activation Signals and Interaction with MEF2"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC121453). *Mol. Cell. Biol*. **18** (1): 69–77. [doi](/source/Doi_(identifier)):[10.1128/mcb.18.1.69](https://doi.org/10.1128%2Fmcb.18.1.69). [PMC](/source/PMC_(identifier)) [121453](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC121453). [PMID](/source/PMID_(identifier)) [9418854](https://pubmed.ncbi.nlm.nih.gov/9418854).

- Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (1998). ["Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC147902). *Nucleic Acids Res*. **26** (20): 4771–7. [doi](/source/Doi_(identifier)):[10.1093/nar/26.20.4771](https://doi.org/10.1093%2Fnar%2F26.20.4771). [PMC](/source/PMC_(identifier)) [147902](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC147902). [PMID](/source/PMID_(identifier)) [9753748](https://pubmed.ncbi.nlm.nih.gov/9753748).

- Zhao M, New L, Kravchenko VV, Kato Y, Gram H, di Padova F, Olson EN, Ulevitch RJ, Han J (1999). ["Regulation of the MEF2 Family of Transcription Factors by p38"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC83862). *Mol. Cell. Biol*. **19** (1): 21–30. [doi](/source/Doi_(identifier)):[10.1128/mcb.19.1.21](https://doi.org/10.1128%2Fmcb.19.1.21). [PMC](/source/PMC_(identifier)) [83862](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC83862). [PMID](/source/PMID_(identifier)) [9858528](https://pubmed.ncbi.nlm.nih.gov/9858528).

- Yang SH, Galanis A, Sharrocks AD (1999). ["Targeting of p38 Mitogen-Activated Protein Kinases to MEF2 Transcription Factors"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC104362). *Mol. Cell. Biol*. **19** (6): 4028–38. [doi](/source/Doi_(identifier)):[10.1128/mcb.19.6.4028](https://doi.org/10.1128%2Fmcb.19.6.4028). [PMC](/source/PMC_(identifier)) [104362](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC104362). [PMID](/source/PMID_(identifier)) [10330143](https://pubmed.ncbi.nlm.nih.gov/10330143).

- Iida K, Hidaka K, Takeuchi M, Nakayama M, Yutani C, Mukai T, Morisaki T (1999). ["Expression of MEF2 genes during human cardiac development"](https://doi.org/10.1620%2Ftjem.187.15). *Tohoku J. Exp. Med*. **187** (1): 15–23. [doi](/source/Doi_(identifier)):[10.1620/tjem.187.15](https://doi.org/10.1620%2Ftjem.187.15). [PMID](/source/PMID_(identifier)) [10458488](https://pubmed.ncbi.nlm.nih.gov/10458488).

- Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T (1999). ["HDAC4 deacetylase associates with and represses the MEF2 transcription factor"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171580). *EMBO J*. **18** (18): 5099–107. [doi](/source/Doi_(identifier)):[10.1093/emboj/18.18.5099](https://doi.org/10.1093%2Femboj%2F18.18.5099). [PMC](/source/PMC_(identifier)) [1171580](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171580). [PMID](/source/PMID_(identifier)) [10487761](https://pubmed.ncbi.nlm.nih.gov/10487761).

- Mao Z, Bonni A, Xia F, Nadal-Vicens M, Greenberg ME (1999). "Neuronal activity-dependent cell survival mediated by transcription factor MEF2". *Science*. **286** (5440): 785–90. [doi](/source/Doi_(identifier)):[10.1126/science.286.5440.785](https://doi.org/10.1126%2Fscience.286.5440.785). [PMID](/source/PMID_(identifier)) [10531066](https://pubmed.ncbi.nlm.nih.gov/10531066).

- Lu J, McKinsey TA, Nicol RL, Olson EN (2000). ["Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC18151). *Proc. Natl. Acad. Sci. U.S.A*. **97** (8): 4070–5. [Bibcode](/source/Bibcode_(identifier)):[2000PNAS...97.4070L](https://ui.adsabs.harvard.edu/abs/2000PNAS...97.4070L). [doi](/source/Doi_(identifier)):[10.1073/pnas.080064097](https://doi.org/10.1073%2Fpnas.080064097). [PMC](/source/PMC_(identifier)) [18151](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC18151). [PMID](/source/PMID_(identifier)) [10737771](https://pubmed.ncbi.nlm.nih.gov/10737771).

- Lemercier C, Verdel A, Galloo B, Curtet S, Brocard MP, Khochbin S (2000). ["mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity"](https://hal.archives-ouvertes.fr/hal-00379796/file/Lemercier_JBC_2000.pdf) (PDF). *J. Biol. Chem*. **275** (20): 15594–9. [doi](/source/Doi_(identifier)):[10.1074/jbc.M908437199](https://doi.org/10.1074%2Fjbc.M908437199). [PMID](/source/PMID_(identifier)) [10748098](https://pubmed.ncbi.nlm.nih.gov/10748098). [S2CID](/source/S2CID_(identifier)) [39220205](https://api.semanticscholar.org/CorpusID:39220205).

- Youn HD, Grozinger CM, Liu JO (2000). ["Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4"](https://doi.org/10.1074%2Fjbc.C000304200). *J. Biol. Chem*. **275** (29): 22563–7. [doi](/source/Doi_(identifier)):[10.1074/jbc.C000304200](https://doi.org/10.1074%2Fjbc.C000304200). [PMID](/source/PMID_(identifier)) [10825153](https://pubmed.ncbi.nlm.nih.gov/10825153).

## External links

- [FactorBook](/source/ENCODE#FactorBook) [MEF2A](https://www.factorbook.org/mediawiki/index.php/MEF2A)

v t e PDB gallery 1c7u: Complex of the DNA binding core domain of the transcription factor MEF2A with a 20mer oligonucleotide 1egw: CRYSTAL STRUCTURE OF MEF2A CORE BOUND TO DNA

v t e Transcription factors and intracellular receptors (1) Basic domains (1.1) Basic leucine zipper (bZIP) Activating transcription factor AATF 1 2 3 4 5 6 7 AP-1 c-Fos FOSB FOSL1 FOSL2 JDP2 c-Jun JUNB JunD BACH 1 2 BATF BLZF1 C/EBP α β γ δ ε ζ CREB 1 3 L1 CREM DBP DDIT3 GABPA GCN4 HLF MAF B sMaf F G K NFE 2 L1 L2 L3 NFIL3 NRL NRF 1 2 3 XBP1 (1.2) Basic helix–loop–helix (bHLH) Group A AS-C ASCL1 ASCL2 ATOH1 HAND 1 2 MESP2 Myogenic regulatory factors MyoD Myogenin MYF5 MYF6 NeuroD 1 2 Neurogenins 1 2 3 OLIG 1 2 Paraxis TCF15 Scleraxis SLC LYL1 TAL 1 2 Twist Group B FIGLA Myc c-Myc l-Myc n-Myc MXD4 TCF4 Group C bHLH-PAS AhR AHRR ARNT ARNTL ARNTL2 CLOCK HIF 1A EPAS1 3A NPAS 1 2 3 PER 1 2 3 Period SIM 1 2 Group D DEC 1 2 BHLHA9 Pho4 ID 1 2 3 4 Group E HES 1 2 3 4 5 6 7 HEY 1 2 L Group F bHLH-COE EBF1 (1.3) bHLH-ZIP AP-4 MAX MXD1 MXD3 MITF MNT MLX MLXIPL MXI1 Myc SREBP 1 2 USF1 (1.4) NF-1 NFI A B C X SMAD R-SMAD 1 2 3 5 9 I-SMAD 6 7 4) (1.5) RF-X RFX 1 2 3 4 5 6 ANK (1.6) Basic helix-span-helix (bHSH) AP-2 α β γ δ ε (2) Zinc finger DNA-binding domains (2.1) Nuclear receptor (Cys4) subfamily 1 Thyroid hormone α β CAR FXR LXR α β PPAR α β/δ γ PXR RAR α β γ ROR α β γ Rev-ErbA α β VDR subfamily 2 COUP-TF (I II Ear-2 HNF4 α γ PNR RXR α β γ Testicular receptor 2 4 TLX subfamily 3 Steroid hormone Androgen Estrogen α β Glucocorticoid Mineralocorticoid Progesterone Estrogen related α β γ subfamily 4 NUR NGFIB NOR1 NURR1 subfamily 5 LRH-1 SF1 subfamily 6 GCNF subfamily 0 DAX1 SHP (2.2) Other Cys4 GATA 1 2 3 4 5 6 MTA 1 2 3 TRPS1 (2.3) Cys2His2 General transcription factors TFIIA TFIIB TFIID TFIIE 1 2 TFIIF 1 2 TFIIH 1 2 4 2I 3A 3C1 3C2 ATBF1 BCL 6 11A 11B CTCF E4F1 EGR 1 2 3 4 ERV3 GFI1 GLI family 1 2 3 REST S1 S2 YY1 HIC 1 2 HIVEP 1 2 3 IKZF 1 2 3 ILF 2 3 Sp/KLF family KLF 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 17 SP 1 2 4 7 8 MTF1 MYT1 OSR1 PRDM9 SALL 1 2 3 4 TSHZ3 WT1 Zbtb7 7A 7B ZBTB 11 16 17 20 21 32 33 40 zinc finger 3 7 9 10 19 22 24 33B 34 35 41 43 44 51 74 143 146 148 165 202 217 219 238 239 259 267 268 281 300 318 330 346 350 365 366 384 423 451 452 471 593 638 644 649 655 804A (2.4) Cys6 HIVEP1 (2.5) Alternating composition AIRE DIDO1 GRLF1 ING 1 2 4 JARID 1A 1B 1C 1D 2 JMJD1B (2.6) WRKY WRKY (3) Helix-turn-helix domains (3.1) Homeodomain Antennapedia ANTP class protoHOX Hox-like ParaHox Gsx 1 2 Xlox PDX1 Cdx 1 2 4 extended Hox: Evx1 Evx2 MEOX1 MEOX2 Homeobox A1 A2 A3 A4 A5 A7 A9 A10 A11 A13 B1 B2 B3 B4 B5 B6 B7 B8 B9 B13 C4 C5 C6 C8 C9 C10 C11 C12 C13 D1 D3 D4 D8 D9 D10 D11 D12 D13 GBX1 GBX2 MNX1 metaHOX NK-like BARHL1 BARHL2 BARX1 BARX2 BSX DBX 1 2 DLX 1 2 3 4 5 6 EMX 1 2 EN 1 2 HHEX HLX LBX1 LBX2 MSX 1 2 NANOG NKX 2-1 2-2 2-3 2-5 3-1 3-2 HMX1 HMX2 HMX3 6-1 6-2 NOTO TLX1 TLX2 TLX3 VAX1 VAX2 other ARX CRX CUTL1 FHL 1 2 3 HESX1 HOPX LMX 1A 1B NOBOX TALE IRX 1 2 3 4 5 6 MKX MEIS 1 2 PBX 1 2 3 PKNOX 1 2 SIX 1 2 3 4 5 PHF 1 3 6 8 10 16 17 20 21A POU domain PIT-1 BRN-3: A B C Octamer transcription factor: 1 2 3/4 6 7 11 SATB2 ZEB 1 2 (3.2) Paired box PAX 1 2 3 4 5 6 7 8 9 PRRX 1 2 PROP1 PHOX 2A 2B RAX SHOX SHOX2 VSX1 VSX2 Bicoid GSC BICD2 OTX 1 2 PITX 1 2 3 (3.3) Fork head / winged helix E2F 1 2 3 4 5 FOX proteins A1 A2 A3 B1 B2 C1 C2 D1 D2 D3 D4 D4L1 D4L3 D4L4 D4L5 D4L6 E1 E3 F1 F2 G1 H1 I1 I2 I3 J1 J2 J3 K1 K2 L1 L2 M1 N1 N2 N3 N4 O1 O3 O4 O6 P1 P2 P3 P4 Q1 R1 R2 S1 (3.4) Heat shock factors HSF 1 2 4 (3.5) Tryptophan clusters ELF 2 4 5 EHF ELK 1 3 4 ERF ETS 1 2 ERG SPIB ETV 1 4 5 6 FLI1 Interferon regulatory factors 1 2 3 4 5 6 7 8 MYB MYBL2 (3.6) TEA domain transcriptional enhancer factor 1 2 3 4 (4) β-Scaffold factors with minor groove contacts (4.1) Rel homology region NF-κB NFKB1 NFKB2 REL RELA RELB NFAT C1 C2 C3 C4 5 (4.2) STAT STAT 1 2 3 4 5 6 (4.3) p53-like p53 p63 p73 family p53 TP63 p73 TBX 1 2 3 5 19 21 22 TBR1 TBR2 TFT MYRF (4.4) MADS box Mef2 A B C D SRF (4.6) TATA-binding proteins TBP TBPL1 (4.7) High-mobility group BBX HMGB 1 2 3 4 HMGN 1 2 3 4 HNF 1A 1B SOX 1 2 3 4 5 6 8 9 10 11 12 13 14 15 17 18 21 SRY SSRP1 TCF/LEF TCF 1 3 4 LEF1 TOX 1 2 3 4 (4.9) Grainyhead TFCP2 (4.10) Cold-shock domain CSDA YBX1 (4.11) Runt CBF CBFA2T2 CBFA2T3 RUNX1 RUNX2 RUNX3 RUNX1T1 (0) Other transcription factors (0.2) HMGI(Y) HMGA 1 2 HBP1 (0.3) Pocket domain Rb RBL1 RBL2 (0.5) AP-2/EREBP-related factors Apetala 2 EREBP B3 (0.6) Miscellaneous ARID 1A 1B 2 3A 3B 4A CAP IFI 16 35 MLL 2 3 T1 MNDA NFY A B C Rho/Sigma see also transcription factor/coregulator deficiencies

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Adapted from the Wikipedia article [Myocyte-specific enhancer factor 2A](https://en.wikipedia.org/wiki/Myocyte-specific_enhancer_factor_2A) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Myocyte-specific_enhancer_factor_2A?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.