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. ^ a b c GRCh38: Ensembl release 89: ENSG00000070444 - Ensembl, May 2017
  2. ^ a b c 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. ^ a b 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. ^ a b 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

External links

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


Transcription factors and intracellular receptors
Categories