MAX (gene)

From Wikipedia, the free encyclopedia

MYC associated factor X

PDB rendering based on 1an2.

Available structures: 1an2, 1hlo, 1nkp, 1nlw, 1r05

Identifiers

Symbol(s)

MAX; MGC10775; MGC11225; MGC18164; MGC34679; MGC36767; orf1

External IDs

OMIM: 154950 MGI: 96921 HomoloGene: 1786

Gene ontology
Molecular Function:	• transcription factor activity • transcription coactivator activity • protein binding • transcription regulator activity
Cellular Component:	• nucleus
Biological Process:	• regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • regulation of transcription

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_002382 (mRNA)
NP_002373 (protein)

XM_001002021 (mRNA)
XP_001002021 (protein)

Location

Chr 14: 64.54 - 64.64 Mb

n/a

Pubmed search

[1]

[2]

MYC associated factor X, also known as MAX, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: MAX MYC associated factor X.

[edit] 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.

[edit] External links

MeSH MAX+protein,+human

This article on a gene on chromosome 14 is a stub. You can help Wikipedia by expanding it.

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

v • d • 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, 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 • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1

(1.3) bHLH-ZIP	MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)

(1.6) Basic helix-span-helix (bHSH)	AP-2

(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 (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • 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)

(2.3) Cys₂His₂	ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • 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, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, 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, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • 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

(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	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(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 • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD

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MAX (gene)

From Wikipedia, the free encyclopedia

[edit] References

[edit] Further reading

[edit] External links

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