MAX (gene)

MYC associated factor X
File:PBB Protein MAX image.jpg PDB rendering based on 1an2.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1an2​, 1hlo​, 1nkp​, 1nlw​, 1r05​
Identifiers
Symbols	MAX ; MGC10775; MGC11225; MGC18164; MGC34679; MGC36767; orf1
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1786
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE MAX 214108 at tn.png
File:PBB GE MAX 208403 x at tn.png
File:PBB GE MAX 209331 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

MYC associated factor X, also known as MAX, is a human gene.

The protein encoded by this gene is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Multiple alternatively spliced transcript variants have been described for this gene but the full-length nature for some of them is unknown.

Further reading

• Grandori C, Cowley SM, James LP, Eisenman RN (2001). "The Myc/Max/Mad network and the transcriptional control of cell behavior". Annu. Rev. Cell Dev. Biol. 16: 653–99. doi:10.1146/annurev.cellbio.16.1.653. PMID 11031250.CS1 maint: Multiple names: authors list (link)
• Lüscher B (2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network". Gene. 277 (1–2): 1–14. PMID 11602341.
• Wechsler DS, Dang CV (1992). "Opposite orientations of DNA bending by c-Myc and Max". Proc. Natl. Acad. Sci. U.S.A. 89 (16): 7635–9. PMID 1323849.
• Wagner AJ, Le Beau MM, Diaz MO, Hay N (1992). "Expression, regulation, and chromosomal localization of the Max gene". Proc. Natl. Acad. Sci. U.S.A. 89 (7): 3111–5. PMID 1557420.CS1 maint: Multiple names: authors list (link)
• Mäkelä TP, Koskinen PJ, Västrik I, Alitalo K (1992). "Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation". Science. 256 (5055): 373–7. PMID 1566084.CS1 maint: Multiple names: authors list (link)
• Gilladoga AD, Edelhoff S, Blackwood EM; et al. (1992). "Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in situ hybridization". Oncogene. 7 (6): 1249–51. PMID 1594250.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Blackwood EM, Eisenman RN (1991). "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc". Science. 251 (4998): 1211–7. PMID 2006410.
• Zervos AS, Faccio L, Gatto JP; et al. (1995). "Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein". Proc. Natl. Acad. Sci. U.S.A. 92 (23): 10531–4. PMID 7479834.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bousset K, Henriksson M, Lüscher-Firzlaff JM; et al. (1993). "Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers". Oncogene. 8 (12): 3211–20. PMID 8247525.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ayer DE, Kretzner L, Eisenman RN (1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell. 72 (2): 211–22. PMID 8425218.CS1 maint: Multiple names: authors list (link)
• Västrik I, Koskinen PJ, Alitalo R, Mäkelä TP (1993). "Alternative mRNA forms and open reading frames of the max gene". Oncogene. 8 (2): 503–7. PMID 8426752.CS1 maint: Multiple names: authors list (link)
• Ferré-D'Amaré AR, Prendergast GC, Ziff EB, Burley SK (1993). "Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain". Nature. 363 (6424): 38–45. doi:10.1038/363038a0. PMID 8479534.CS1 maint: Multiple names: authors list (link)
• Hurlin PJ, Quéva C, Koskinen PJ; et al. (1996). "Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation". EMBO J. 14 (22): 5646–59. PMID 8521822.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Grandori C, Mac J, Siëbelt F; et al. (1996). "Myc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivo". EMBO J. 15 (16): 4344–57. PMID 8861962.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Brownlie P, Ceska T, Lamers M; et al. (1997). "The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control". Structure. 5 (4): 509–20. PMID 9115440.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Meroni G, Reymond A, Alcalay M; et al. (1997). "Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor". EMBO J. 16 (10): 2892–906. doi:10.1093/emboj/16.10.2892. PMID 9184233.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gupta MP, Amin CS, Gupta M; et al. (1997). "Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression". Mol. Cell. Biol. 17 (7): 3924–36. PMID 9199327.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gupta K, Anand G, Yin X; et al. (1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lavigne P, Crump MP, Gagné SM; et al. (1998). "Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper". J. Mol. Biol. 281 (1): 165–81. doi:10.1006/jmbi.1998.1914. PMID 9680483.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• FitzGerald MJ, Arsura M, Bellas RE; et al. (1999). "Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc". Oncogene. 18 (15): 2489–98. doi:10.1038/sj.onc.1202611. PMID 10229200.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

External links

• MAX+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.