MXD1

In today's world, MXD1 has become increasingly important in society. Whether due to its impact on culture, politics, the economy or people's daily lives, MXD1 has managed to position itself as a relevant topic of discussion and debate. Its influence extends to different fields and its presence is increasingly evident in various aspects of life. This is why it is relevant to fully explore the scope and implications of MXD1 today, as well as analyze its evolution over time and its potential impact in the future. This article seeks to delve into the world of MXD1 to understand its importance and relevance in contemporary society.

Protein-coding gene in the species Homo sapiens

Not to be confused with Mothers against decapentaplegic.

MXD1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1E91, 1G1E, 1NLW, 1PD7, 1S5Q
Identifiers
Aliases	MXD1, BHLHC58, MAD, MAD1, MAX dimerization protein 1
External IDs	OMIM: 600021; MGI: 96908; HomoloGene: 1767; GeneCards: MXD1; OMA:MXD1 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p13.3 Start 69,897,688 bp[1] End 69,942,945 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6 D1|6 37.75 cM Start 86,624,024 bp[2] End 86,646,143 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell mucosa of pharynx oocyte secondary oocyte amniotic fluid blood oral cavity jejunal mucosa mucosa of colon mucosa of sigmoid colon Top expressed in granulocyte left colon blood retinal pigment epithelium duodenum ciliary body secondary oocyte epithelium of stomach jejunum conjunctival fornix More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription factor activity RNA polymerase II cis-regulatory region sequence-specific DNA binding DNA binding DNA-binding transcription repressor activity, RNA polymerase II-specific protein binding transcription coregulator activity protein dimerization activity transcription corepressor activity DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component nucleus nucleoplasm mitochondrion cytosol Biological process multicellular organism development cell population proliferation regulation of transcription, DNA-templated negative regulation of transcription by RNA polymerase II transcription, DNA-templated Sources:Amigo / QuickGO
Orthologs Species Human Mouse 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 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]

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

• Grandori C, Cowley SM, James LP, Eisenman RN (2001). "The Myc/Max/Mad network and the transcriptional control of cell behavior". Annu. Rev. Cell Dev. Biol. 16 (1): 653–99. doi:10.1146/annurev.cellbio.16.1.653. PMID 11031250.
• Lüscher B (2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network". Gene. 277 (1–2): 1–14. doi:10.1016/S0378-1119(01)00697-7. PMID 11602341.
• Ayer DE, Lawrence QA, Eisenman RN (1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. 80 (5): 767–76. doi:10.1016/0092-8674(95)90355-0. PMID 7889570. S2CID 8749951.
• Edelhoff S, Ayer DE, Zervos AS, et al. (1994). "Mapping of two genes encoding members of a distinct subfamily of MAX interacting proteins: MAD to human chromosome 2 and mouse chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome 19". Oncogene. 9 (2): 665–8. PMID 8290278.
• Ayer DE, Kretzner L, Eisenman RN (1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell. 72 (2): 211–22. doi:10.1016/0092-8674(93)90661-9. PMID 8425218. S2CID 13317223.
• Hassig CA, Fleischer TC, Billin AN, et al. (1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/S0092-8674(00)80214-7. PMID 9150133. S2CID 14233219.
• Laherty CD, Yang WM, Sun JM, et al. (1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. 89 (3): 349–56. doi:10.1016/S0092-8674(00)80215-9. PMID 9150134. S2CID 13490886.
• Gupta K, Anand G, Yin X, et al. (1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
• FitzGerald MJ, Arsura M, Bellas RE, et al. (1999). "Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc". Oncogene. 18 (15): 2489–98. doi:10.1038/sj.onc.1202611. PMID 10229200.
• Khan MM, Nomura T, Kim H, et al. (2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Mol. Cell. 7 (6): 1233–43. doi:10.1016/S1097-2765(01)00257-X. PMID 11430826.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Nikiforov MA, Popov N, Kotenko I, et al. (2003). "The Mad and Myc basic domains are functionally equivalent". J. Biol. Chem. 278 (13): 11094–9. doi:10.1074/jbc.M212298200. PMID 12538578.
• Nair SK, Burley SK (2003). "X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors". Cell. 112 (2): 193–205. doi:10.1016/S0092-8674(02)01284-9. PMID 12553908. S2CID 16142388.
• Siegel PM, Shu W, Massagué J (2003). "Mad upregulation and Id2 repression accompany transforming growth factor (TGF)-beta-mediated epithelial cell growth suppression". J. Biol. Chem. 278 (37): 35444–50. doi:10.1074/jbc.M301413200. PMID 12824180.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
• Zada AA, Pulikkan JA, Bararia D, et al. (2007). "Proteomic discovery of Max as a novel interacting partner of C/EBPalpha: a Myc/Max/Mad link". Leukemia. 20 (12): 2137–46. doi:10.1038/sj.leu.2404438. PMID 17082780.

External links

• Overview of all the structural information available in the PDB for UniProt: Q05195 (Max dimerization protein 1) at the PDBe-KB.