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