MXD1

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Protein-coding gene in the species Homo sapiens

title: "MXD1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/MXD1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

MAD protein is a protein that in humans is encoded by the MXD1 gene.

MAD-MAX dimerization protein belongs to a subfamily of MAX-interacting proteins. This protein competes with MYC for binding to MAX to form a sequence-specific DNA-binding complex, acts as a transcriptional repressor (while MYC appears to function as an activator) and is a candidate tumor suppressor.

Interactions

MXD1 has been shown to interact with Histone deacetylase 2, SMC3, MLX, SIN3A and MAX.

References

References

  1. (February 1995). "Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13 and 10q24-q25". Genomics.
  2. "Entrez Gene: MXD1 MAX dimerization protein 1".
  3. Laherty, C D. (May 1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell.
  4. Spronk, C A. (December 2000). "The Mad1-Sin3B interaction involves a novel helical fold". Nat. Struct. Biol..
  5. Gupta, K. (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene.
  6. Cairo, S. (March 2001). "WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network". Hum. Mol. Genet..
  7. Meroni, G. (July 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene.
  8. Swanson, Kurt A. (August 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nat. Struct. Mol. Biol..
  9. Brubaker, K. (November 2000). "Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex". Cell.
  10. Ayer, D E. (March 1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell.
  11. Lee, Clement M. (October 2002). "JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors". [[PNAS.
  12. Ayer, D E. (January 1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell.
  13. Nair, Satish K. (January 2003). "X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors". Cell.

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