MNT
Identifiers
AliasesMNT, MAD6, MXD6, ROX, bHLHd3, MAX network transcriptional repressor, lncRNA-HAL
External IDsOMIM: 603039 MGI: 109150 HomoloGene: 7842 GeneCards: MNT
Orthologs
SpeciesHumanMouse
Entrez

4335

17428

Ensembl

ENSG00000070444

ENSMUSG00000000282

UniProt

Q99583

O08789

RefSeq (mRNA)

NM_020310

NM_010813

RefSeq (protein)

NP_064706

NP_034943

Location (UCSC)Chr 17: 2.38 – 2.4 MbChr 11: 74.72 – 74.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

MNT (Max-binding protein MNT) is a Max-binding protein that is encoded by the MNT gene[5][6][7]

Function

The Myc/Max/Mad network comprises a group of transcription factors that co-interact to regulate gene-specific transcriptional activation or repression. This gene encodes a protein member of the Myc/Max/Mad network. This protein has a basic-Helix-Loop-Helix-zipper domain (bHLHzip) with which it binds the canonical DNA sequence CANNTG, known as the E box, following heterodimerization with Max proteins. Its delta signature is 44. This protein is a transcriptional repressor and an antagonist of Myc-dependent transcriptional activation and cell growth. This protein represses transcription by binding to DNA and recruiting Sin3 corepressor proteins through its N-terminal Sin3-interaction domain [5][8]

Interactions

MNT (gene) has been shown to interact with MLX,[9][10] SIN3A[11] and MAX.[11]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000070444 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000282 - 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. 1 2 Hurlin, Peter; Queva, Christoph; Eisenman, Robert (January 1, 1997). "Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites". Genes & Development. 11 (1): 44–58. doi:10.1101/gad.11.1.44. PMID 9000049.
  6. Lo Nigro C, Venesio T, Reymond A, Meroni G, Alberici P, Cainarca S, Enrico F, Stack M, Ledbetter DH, Liscia DS, Ballabio A, Carrozzo R (Apr 1998). "The human ROX gene: genomic structure and mutation analysis in human breast tumors". Genomics. 49 (2): 275–82. doi:10.1006/geno.1998.5241. PMID 9598315.
  7. "Entrez Gene: MNT MAX binding protein".
  8. Merroni, G; Reymond, A; Alcalay, M; Borsani, G; Tanigami, A; Tonlorenzi, R; Lo Nigro, C; Messali, S; Zollo, M; Ledbetter, DH; Brent, R; Ballabio, A; Carrozzo, R (May 15, 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): 2892–2906. doi:10.1093/emboj/16.10.2892. PMC 1169897. PMID 9184233.
  9. Cairo S, Merla G, Urbinati F, Ballabio A, Reymond A (Mar 2001). "WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network". Human Molecular Genetics. 10 (6): 617–27. doi:10.1093/hmg/10.6.617. PMID 11230181.
  10. Meroni G, Cairo S, Merla G, Messali S, Brent R, Ballabio A, Reymond A (Jul 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene. 19 (29): 3266–77. doi:10.1038/sj.onc.1203634. PMID 10918583.
  11. 1 2 Meroni G, Reymond A, Alcalay M, Borsani G, Tanigami A, Tonlorenzi R, Lo Nigro C, Messali S, Zollo M, Ledbetter DH, Brent R, Ballabio A, Carrozzo R (May 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". The EMBO Journal. 16 (10): 2892–906. doi:10.1093/emboj/16.10.2892. PMC 1169897. PMID 9184233.

Further reading

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


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