MEF2D

Protein-coding gene in the species Homo sapiens
MEF2D
Identifiers
AliasesMEF2D, myocyte enhancer factor 2D
External IDsOMIM: 600663 MGI: 99533 HomoloGene: 4327 GeneCards: MEF2D
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for MEF2D
Genomic location for MEF2D
Band1q22Start156,463,727 bp[1]
End156,500,779 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for MEF2D
Genomic location for MEF2D
Band3 F1|3 38.78 cMStart88,049,679 bp[2]
End88,079,393 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gastrocnemius muscle

  • popliteal artery

  • saphenous vein

  • sural nerve

  • gastric mucosa

  • canal of the cervix

  • right coronary artery

  • left ventricle

  • endothelial cell

  • left uterine tube
Top expressed in
  • entorhinal cortex

  • superior frontal gyrus

  • plantaris muscle

  • extensor digitorum longus muscle

  • ankle joint

  • digastric muscle

  • skeletal muscle tissue

  • upper arm

  • triceps brachii muscle

  • extraocular muscle
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • protein dimerization activity
  • protein homodimerization activity
  • DNA-binding transcription factor activity
  • DNA-binding transcription activator activity, RNA polymerase II-specific
  • histone deacetylase binding
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
  • protein binding
  • protein heterodimerization activity
  • enzyme binding
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • cytoplasm
  • intracellular membrane-bounded organelle
  • nucleoplasm
  • nucleus
Biological process
  • cell differentiation
  • regulation of transcription, DNA-templated
  • chondrocyte differentiation
  • adult heart development
  • muscle organ development
  • endochondral ossification
  • transcription by RNA polymerase II
  • transcription, DNA-templated
  • nervous system development
  • multicellular organism development
  • positive regulation of transcription, DNA-templated
  • osteoblast differentiation
  • skeletal muscle cell differentiation
  • positive regulation of transcription by RNA polymerase II
  • apoptotic process
  • positive regulation of vascular associated smooth muscle cell proliferation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4209

17261

Ensembl

ENSG00000116604

ENSMUSG00000001419

UniProt

Q14814

Q63943

RefSeq (mRNA)

NM_001271629
NM_005920

NM_133665
NM_001310587
NM_001310593

RefSeq (protein)

NP_001258558
NP_005911

NP_001297516
NP_001297522
NP_598426

Location (UCSC)Chr 1: 156.46 – 156.5 MbChr 3: 88.05 – 88.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Myocyte-specific enhancer factor 2D is a protein that in humans is encoded by the MEF2D gene.[5][6]

Interactions

MEF2D has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116604 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001419 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Breitbart RE, Liang CS, Smoot LB, Laheru DA, Mahdavi V, Nadal-Ginard B (Aug 1993). "A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage". Development. 118 (4): 1095–1106. doi:10.1242/dev.118.4.1095. PMID 8269842.
  6. ^ "Entrez Gene: MEF2D MADS box transcription enhancer factor 2, polypeptide D (myocyte enhancer factor 2D)".
  7. ^ a b Youn HD, Liu JO (Jul 2000). "Cabin1 represses MEF2-dependent Nur77 expression and T cell apoptosis by controlling association of histone deacetylases and acetylases with MEF2". Immunity. 13 (1): 85–94. doi:10.1016/s1074-7613(00)00010-8. PMID 10933397.
  8. ^ Youn HD, Sun L, Prywes R, Liu JO (Oct 1999). "Apoptosis of T cells mediated by Ca2+-induced release of the transcription factor MEF2". Science. 286 (5440): 790–793. doi:10.1126/science.286.5440.790. PMID 10531067.
  9. ^ Youn HD, Grozinger CM, Liu JO (Jul 2000). "Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4". The Journal of Biological Chemistry. 275 (29): 22563–22567. doi:10.1074/jbc.C000304200. PMID 10825153.
  10. ^ Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (Oct 1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Research. 26 (20): 4771–4777. doi:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.
  11. ^ Ornatsky OI, McDermott JC (Oct 1996). "MEF2 protein expression, DNA binding specificity and complex composition, and transcriptional activity in muscle and non-muscle cells". The Journal of Biological Chemistry. 271 (40): 24927–24933. doi:10.1074/jbc.271.40.24927. PMID 8798771.
  12. ^ Youn HD, Chatila TA, Liu JO (Aug 2000). "Integration of calcineurin and MEF2 signals by the coactivator p300 during T-cell apoptosis". The EMBO Journal. 19 (16): 4323–4331. doi:10.1093/emboj/19.16.4323. PMC 302027. PMID 10944115.
  13. ^ Park SY, Shin HM, Han TH (Sep 2002). "Synergistic interaction of MEF2D and Sp1 in activation of the CD14 promoter". Molecular Immunology. 39 (1–2): 25–30. doi:10.1016/s0161-5890(02)00055-x. PMID 12213324.
  14. ^ Choi SJ, Park SY, Han TH (Jul 2001). "14-3-3tau associates with and activates the MEF2D transcription factor during muscle cell differentiation". Nucleic Acids Research. 29 (13): 2836–2842. doi:10.1093/nar/29.13.2836. PMC 55772. PMID 11433030.

Further reading

  • Hobson GM, Krahe R, Garcia E, Siciliano MJ, Funanage VL (Oct 1995). "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): 704–711. doi:10.1006/geno.1995.9007. PMID 8575763.
  • Ornatsky OI, McDermott JC (Oct 1996). "MEF2 protein expression, DNA binding specificity and complex composition, and transcriptional activity in muscle and non-muscle cells". The Journal of Biological Chemistry. 271 (40): 24927–24933. doi:10.1074/jbc.271.40.24927. PMID 8798771.
  • Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (Oct 1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Research. 26 (20): 4771–4777. doi:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.
  • Zhao M, New L, Kravchenko VV, Kato Y, Gram H, di Padova F, Olson EN, Ulevitch RJ, Han J (Jan 1999). "Regulation of the MEF2 family of transcription factors by p38". Molecular and Cellular Biology. 19 (1): 21–30. doi:10.1128/mcb.19.1.21. PMC 83862. PMID 9858528.
  • Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ (Nov 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Molecular and Cellular Biology. 19 (11): 7816–7827. doi:10.1128/mcb.19.11.7816. PMC 84849. PMID 10523670.
  • Lu J, McKinsey TA, Nicol RL, Olson EN (Apr 2000). "Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases". Proceedings of the National Academy of Sciences of the United States of America. 97 (8): 4070–4075. Bibcode:2000PNAS...97.4070L. doi:10.1073/pnas.080064097. PMC 18151. PMID 10737771.
  • Kato Y, Zhao M, Morikawa A, Sugiyama T, Chakravortty D, Koide N, Yoshida T, Tapping RI, Yang Y, Yokochi T, Lee JD (Jun 2000). "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family". The Journal of Biological Chemistry. 275 (24): 18534–18540. doi:10.1074/jbc.M001573200. PMID 10849446.
  • Youn HD, Chatila TA, Liu JO (Aug 2000). "Integration of calcineurin and MEF2 signals by the coactivator p300 during T-cell apoptosis". The EMBO Journal. 19 (16): 4323–4331. doi:10.1093/emboj/19.16.4323. PMC 302027. PMID 10944115.
  • Slepak TI, Webster KA, Zang J, Prentice H, O'Dowd A, Hicks MN, Bishopric NH (Mar 2001). "Control of cardiac-specific transcription by p300 through myocyte enhancer factor-2D". The Journal of Biological Chemistry. 276 (10): 7575–7585. doi:10.1074/jbc.M004625200. PMID 11096067.
  • Choi SJ, Park SY, Han TH (Jul 2001). "14-3-3tau associates with and activates the MEF2D transcription factor during muscle cell differentiation". Nucleic Acids Research. 29 (13): 2836–2842. doi:10.1093/nar/29.13.2836. PMC 55772. PMID 11433030.
  • Okamoto S, Li Z, Ju C, Scholzke MN, Mathews E, Cui J, Salvesen GS, Bossy-Wetzel E, Lipton SA (Mar 2002). "Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis". Proceedings of the National Academy of Sciences of the United States of America. 99 (6): 3974–3979. Bibcode:2002PNAS...99.3974O. doi:10.1073/pnas.022036399. PMC 122633. PMID 11904443.
  • Park SY, Shin HM, Han TH (Sep 2002). "Synergistic interaction of MEF2D and Sp1 in activation of the CD14 promoter". Molecular Immunology. 39 (1–2): 25–30. doi:10.1016/S0161-5890(02)00055-X. PMID 12213324.
  • Linseman DA, Bartley CM, Le SS, Laessig TA, Bouchard RJ, Meintzer MK, Li M, Heidenreich KA (Oct 2003). "Inactivation of the myocyte enhancer factor-2 repressor histone deacetylase-5 by endogenous Ca(2+) //calmodulin-dependent kinase II promotes depolarization-mediated cerebellar granule neuron survival". The Journal of Biological Chemistry. 278 (42): 41472–41481. doi:10.1074/jbc.M307245200. PMID 12896970.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–12135. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Grégoire S, Yang XJ (Mar 2005). "Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors". Molecular and Cellular Biology. 25 (6): 2273–2287. doi:10.1128/MCB.25.6.2273-2287.2005. PMC 1061617. PMID 15743823.
  • Prima V, Gore L, Caires A, Boomer T, Yoshinari M, Imaizumi M, Varella-Garcia M, Hunger SP (May 2005). "Cloning and functional characterization of MEF2D/DAZAP1 and DAZAP1/MEF2D fusion proteins created by a variant t(1;19)(q23;p13.3) in acute lymphoblastic leukemia". Leukemia. 19 (5): 806–813. doi:10.1038/sj.leu.2403684. PMID 15744350.

External links

  • v
  • t
  • e
  • 1c7u: Complex of the DNA binding core domain of the transcription factor MEF2A with a 20mer oligonucleotide
    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
    1egw: CRYSTAL STRUCTURE OF MEF2A CORE BOUND TO DNA
  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies