MXD1

Last updated
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 OMIM: 600021; MGI: 96908; HomoloGene: 1767; GeneCards: MXD1; OMA:MXD1 - orthologs
Orthologs
SpeciesHumanMouse
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: 86.62 – 86.65 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]

Contents

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]

Interactions

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

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000059728 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000001156 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. 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. 1 2 "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. 89 (3). UNITED STATES: 349–56. doi: 10.1016/S0092-8674(00)80215-9 . ISSN   0092-8674. PMID   9150134. S2CID   13490886.
  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. 7 (12). UNITED STATES: 1100–4. doi:10.1038/81944. hdl: 2066/79474 . ISSN   1072-8368. PMID   11101889. S2CID   12451972.
  9. 1 2 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. 16 (9). ENGLAND: 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. 10 (6). England: 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. 19 (29). ENGLAND: 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. 11 (8). United States: 738–46. doi:10.1038/nsmb798. ISSN   1545-9993. PMID   15235594. S2CID   44324333.
  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. 103 (4). UNITED STATES: 655–65. doi: 10.1016/S0092-8674(00)00168-9 . ISSN   0092-8674. PMID   11106735. S2CID   17476603.
  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. 80 (5). UNITED STATES: 767–76. doi: 10.1016/0092-8674(95)90355-0 . ISSN   0092-8674. PMID   7889570. S2CID   8749951.
  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. 99 (22). United States: 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. 72 (2). UNITED STATES: 211–22. doi:10.1016/0092-8674(93)90661-9. ISSN   0092-8674. PMID   8425218. S2CID   13317223.
  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. 112 (2). United States: 193–205. doi: 10.1016/S0092-8674(02)01284-9 . ISSN   0092-8674. PMID   12553908. S2CID   16142388.

Further reading