MXD1

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MXD1
Protein MXD1 PDB 1nlw.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases MXD1, BHLHC58, MAD, MAD1, MAX dimerization protein 1
External IDs MGI: 96908 HomoloGene: 1767 GeneCards: MXD1
Gene location (Human)
Human chromosome 2
Chr. Chromosome 2 (human)[1]
Human chromosome 2
Genomic location for MXD1
Genomic location for MXD1
Band No data available Start 69,897,688 bp[1]
End 69,942,945 bp[1]
RNA expression pattern
PBB GE MXD1 206877 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002357
NM_001202513
NM_001202514

NM_010751

RefSeq (protein)

NP_001189442
NP_001189443
NP_002348

n/a

Location (UCSC) Chr 2: 69.9 – 69.94 Mb Chr 6: 86.65 – 86.67 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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] The MAD-MAX protein dimer may be a reference to the popular cult classic film Mad Max (1979).

Interactions[edit]

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]

References[edit]

  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. PMID 7829091. doi:10.1006/geno.1994.1496. 
  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. ISSN 0092-8674. PMID 9150134. doi:10.1016/S0092-8674(00)80215-9. 
  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. ISSN 1072-8368. PMID 11101889. doi:10.1038/81944. 
  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. ISSN 0950-9232. PMID 9528857. doi:10.1038/sj.onc.1201634. 
  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. ISSN 0964-6906. PMID 11230181. doi:10.1093/hmg/10.6.617. 
  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. ISSN 0950-9232. PMID 10918583. doi:10.1038/sj.onc.1203634. 
  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. ISSN 1545-9993. PMID 15235594. doi:10.1038/nsmb798. 
  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. ISSN 0092-8674. PMID 11106735. doi:10.1016/S0092-8674(00)00168-9. 
  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. ISSN 0092-8674. PMID 7889570. doi:10.1016/0092-8674(95)90355-0. 
  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. ISSN 0027-8424. PMC 137859Freely accessible. PMID 12391307. doi:10.1073/pnas.232310199. 
  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. ISSN 0092-8674. PMID 8425218. doi:10.1016/0092-8674(93)90661-9. 
  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. ISSN 0092-8674. PMID 12553908. doi:10.1016/S0092-8674(02)01284-9. 

Further reading[edit]