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Protein MXD1 PDB 1nlw.png
Available structures
PDBOrtholog search: PDBe RCSB
AliasesMXD1, BHLHC58, MAD, MAD1, MAX dimerization protein 1
External IDsMGI: 96908 HomoloGene: 1767 GeneCards: MXD1
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for MXD1
Genomic location for MXD1
Band2p13.3Start69,897,688 bp[1]
End69,942,945 bp[1]
RNA expression pattern
PBB GE MXD1 206877 at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 2: 69.9 – 69.94 MbChr 6: 86.65 – 86.67 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

MAD protein is a protein that in humans is encoded by the MXD1 gene.[5][6]

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.[6]


MXD1 has been shown to interact with Histone deacetylase 2,[7][8] SMC3,[9] MLX,[10][11] SIN3A[12][13][14] and MAX.[9][15][16][17]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000059728 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001156 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ Shapiro DN, Valentine V, Eagle L, Yin X, Morris SW, Prochownik EV (February 1995). "Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13 and 10q24-q25". Genomics. 23 (1): 282–5. doi:10.1006/geno.1994.1496. PMID 7829091.
  6. ^ a b "Entrez Gene: MXD1 MAX dimerization protein 1".
  7. ^ Laherty, C D; Yang W M; Sun J M; Davie J R; Seto E; Eisenman R N (May 1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. UNITED STATES. 89 (3): 349–56. doi:10.1016/S0092-8674(00)80215-9. ISSN 0092-8674. PMID 9150134.
  8. ^ Spronk, C A; Tessari M; Kaan A M; Jansen J F; Vermeulen M; Stunnenberg H G; Vuister G W (December 2000). "The Mad1-Sin3B interaction involves a novel helical fold". Nat. Struct. Biol. UNITED STATES. 7 (12): 1100–4. doi:10.1038/81944. ISSN 1072-8368. PMID 11101889.
  9. ^ a b Gupta, K; Anand G; Yin X; Grove L; Prochownik E V (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. ENGLAND. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. ISSN 0950-9232. PMID 9528857.
  10. ^ Cairo, S; Merla G; Urbinati F; Ballabio A; Reymond A (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. England. 10 (6): 617–27. doi:10.1093/hmg/10.6.617. ISSN 0964-6906. PMID 11230181.
  11. ^ Meroni, G; Cairo S; Merla G; Messali S; Brent R; Ballabio A; Reymond A (July 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene. ENGLAND. 19 (29): 3266–77. doi:10.1038/sj.onc.1203634. ISSN 0950-9232. PMID 10918583.
  12. ^ Swanson, Kurt A; Knoepfler Paul S; Huang Kai; Kang Richard S; Cowley Shaun M; Laherty Carol D; Eisenman Robert N; Radhakrishnan Ishwar (August 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nat. Struct. Mol. Biol. United States. 11 (8): 738–46. doi:10.1038/nsmb798. ISSN 1545-9993. PMID 15235594.
  13. ^ Brubaker, K; Cowley S M; Huang K; Loo L; Yochum G S; Ayer D E; Eisenman R N; Radhakrishnan I (November 2000). "Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex". Cell. UNITED STATES. 103 (4): 655–65. doi:10.1016/S0092-8674(00)00168-9. ISSN 0092-8674. PMID 11106735.
  14. ^ Ayer, D E; Lawrence Q A; Eisenman R N (March 1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. UNITED STATES. 80 (5): 767–76. doi:10.1016/0092-8674(95)90355-0. ISSN 0092-8674. PMID 7889570.
  15. ^ Lee, Clement M; Onésime Djamila; Reddy C Damodara; Dhanasekaran N; Reddy E Premkumar (October 2002). "JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors". Proc. Natl. Acad. Sci. U.S.A. United States. 99 (22): 14189–94. Bibcode:2002PNAS...9914189L. doi:10.1073/pnas.232310199. ISSN 0027-8424. PMC 137859. PMID 12391307.
  16. ^ Ayer, D E; Kretzner L; Eisenman R N (January 1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell. UNITED STATES. 72 (2): 211–22. doi:10.1016/0092-8674(93)90661-9. ISSN 0092-8674. PMID 8425218.
  17. ^ Nair, Satish K; Burley Stephen K (January 2003). "X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors". Cell. United States. 112 (2): 193–205. doi:10.1016/S0092-8674(02)01284-9. ISSN 0092-8674. PMID 12553908.

Further reading[edit]