Speedway

MXD1

Not to be confused with Mothers against decapentaplegic.
MXD1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMXD1, BHLHC58, MAD, MAD1, MAX dimerization protein 1
External IDsOMIM: 600021; MGI: 96908; HomoloGene: 1767; GeneCards: MXD1; OMA:MXD1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

4084

17119

Ensembl

ENSG00000059728

ENSMUSG00000001156

UniProt

Q05195

P50538

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 MbChr 6: 86.62 – 86.65 Mb
PubMed search[3][4]
Wikidata
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]

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. ^ 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:". 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. ^ 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. 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. ^ 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. 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

  • Overview of all the structural information available in the PDB for UniProt: Q05195 (Max dimerization protein 1) at the PDBe-KB.
Quelle: http://en.wikipedia.org/wiki/MXD1