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{{Infobox_gene}}
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'''MAD protein''' is a [[protein]] that in humans is encoded by the ''MXD1'' [[gene]].<ref name="pmid7829091">{{cite journal |vauthors=Shapiro DN, Valentine V, Eagle L, Yin X, Morris SW, Prochownik EV | title = Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13 and 10q24-q25 | journal = Genomics | volume = 23 | issue = 1 | pages = 282–5 |date=February 1995 | pmid = 7829091 | pmc =  | doi = 10.1006/geno.1994.1496 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MXD1 MAX dimerization protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4084| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_MXD1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nlw.
| PDB = {{PDB2|1nlw}}
| Name = MAX dimerization protein 1
| HGNCid = 6761
| Symbol = MXD1
| AltSymbols =; MAD; MAD1; MGC104659
| OMIM = 600021
| ECnumber = 
| Homologene = 1767
| MGIid = 96908
| GeneAtlas_image1 = PBB_GE_MXD1_206877_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4084
    | Hs_Ensembl = ENSG00000059728
    | Hs_RefseqProtein = NP_002348
    | Hs_RefseqmRNA = NM_002357
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 69995707
    | Hs_GenLoc_end = 70023581
    | Hs_Uniprot = Q05195
    | Mm_EntrezGene = 17119
    | Mm_Ensembl = ENSMUSG00000001156
    | Mm_RefseqmRNA = NM_010751
    | Mm_RefseqProtein = NP_034881
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 86615467
    | Mm_GenLoc_end = 86634730
    | Mm_Uniprot = Q4FK19
  }}
}}
'''MAX dimerization protein 1''', also known as '''MXD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MXD1 MAX dimerization protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4084| accessdate = }}</ref>


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{{PBB_Summary
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| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: MXD1 MAX dimerization protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4084| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez" />
}}
}}  The MAD-MAX [[protein]] dimer may be a reference to the popular [[cult classic]] film [[Mad Max]] (1979).
 
==Interactions==
MXD1 has been shown to [[Protein-protein interaction|interact]] with [[Histone deacetylase 2]],<ref name=pmid9150134>{{cite journal |doi=10.1016/S0092-8674(00)80215-9 |last=Laherty |first=C D |authorlink= |author2=Yang W M |author3=Sun J M |author4=Davie J R |author5=Seto E |author6=Eisenman R N  |date=May 1997 |title=Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression |journal=Cell |volume=89 |issue=3 |pages=349–56 |publisher= |location = UNITED STATES| issn = 0092-8674| pmid = 9150134 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid11101889>{{cite journal |last=Spronk |first=C A |authorlink= |author2=Tessari M |author3=Kaan A M |author4=Jansen J F |author5=Vermeulen M |author6=Stunnenberg H G |author7=Vuister G W  |date=December 2000  |title=The Mad1-Sin3B interaction involves a novel helical fold |journal=Nat. Struct. Biol. |volume=7 |issue=12 |pages=1100–4 |publisher= |location = UNITED STATES| issn = 1072-8368| pmid = 11101889 |doi = 10.1038/81944 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[SMC3 (gene)|SMC3]],<ref name=pmid9528857>{{cite journal |last=Gupta |first=K |authorlink= |author2=Anand G |author3=Yin X |author4=Grove L |author5=Prochownik E V  |date=March 1998  |title=Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc |journal=Oncogene |volume=16 |issue=9 |pages=1149–59 |publisher= |location = ENGLAND| issn = 0950-9232| pmid = 9528857 |doi = 10.1038/sj.onc.1201634 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[MLX (gene)|MLX]],<ref name=pmid11230181>{{cite journal |doi=10.1093/hmg/10.6.617 |last=Cairo |first=S |authorlink= |author2=Merla G |author3=Urbinati F |author4=Ballabio A |author5=Reymond A  |date=March 2001  |title=WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network |journal=Hum. Mol. Genet. |volume=10 |issue=6 |pages=617–27 |publisher= |location = England| issn = 0964-6906| pmid = 11230181 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid10918583>{{cite journal |last=Meroni |first=G |authorlink= |author2=Cairo S |author3=Merla G |author4=Messali S |author5=Brent R |author6=Ballabio A |author7=Reymond A  |date=July 2000  |title=Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway? |journal=Oncogene |volume=19 |issue=29 |pages=3266–77 |publisher= |location = ENGLAND| issn = 0950-9232| pmid = 10918583 |doi = 10.1038/sj.onc.1203634 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[SIN3A]]<ref name=pmid15235594>{{cite journal |last=Swanson |first=Kurt A |authorlink= |author2=Knoepfler Paul S |author3=Huang Kai |author4=Kang Richard S |author5=Cowley Shaun M |author6=Laherty Carol D |author7=Eisenman Robert N |author8=Radhakrishnan Ishwar  |date=August 2004  |title=HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations |journal=Nat. Struct. Mol. Biol. |volume=11 |issue=8 |pages=738–46 |publisher= |location = United States| issn = 1545-9993| pmid = 15235594 |doi = 10.1038/nsmb798 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid11106735>{{cite journal |doi=10.1016/S0092-8674(00)00168-9 |last=Brubaker |first=K |authorlink= |author2=Cowley S M |author3=Huang K |author4=Loo L |author5=Yochum G S |author6=Ayer D E |author7=Eisenman R N |author8=Radhakrishnan I  |date=November 2000  |title=Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex |journal=Cell |volume=103 |issue=4 |pages=655–65 |publisher= |location = UNITED STATES| issn = 0092-8674| pmid = 11106735 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid7889570>{{cite journal |doi=10.1016/0092-8674(95)90355-0 |last=Ayer |first=D E |authorlink= |author2=Lawrence Q A |author3=Eisenman R N  |date=March 1995  |title=Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3 |journal=Cell |volume=80 |issue=5 |pages=767–76 |publisher= |location = UNITED STATES| issn = 0092-8674| pmid = 7889570 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[MAX (gene)|MAX]].<ref name=pmid9528857/><ref name=pmid12391307>{{cite journal |last=Lee |first=Clement M |authorlink= |author2=Onésime Djamila |author3=Reddy C Damodara |author4=Dhanasekaran N |author5=Reddy E Premkumar  |date=October 2002  |title=JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors |journal=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=99 |issue=22 |pages=14189–94 |publisher= |location = United States| issn = 0027-8424| pmid = 12391307 |doi = 10.1073/pnas.232310199 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=137859 }}</ref><ref name=pmid8425218>{{cite journal |doi=10.1016/0092-8674(93)90661-9 |last=Ayer |first=D E |authorlink= |author2=Kretzner L |author3=Eisenman R N  |date=January 1993  |title=Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity |journal=Cell |volume=72 |issue=2 |pages=211–22 |publisher= |location = UNITED STATES| issn = 0092-8674| pmid = 8425218 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid12553908>{{cite journal |doi=10.1016/S0092-8674(02)01284-9 |last=Nair |first=Satish K |authorlink= |author2=Burley Stephen K |date=January 2003  |title=X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors |journal=Cell |volume=112 |issue=2 |pages=193–205 |publisher= |location = United States| issn = 0092-8674| pmid = 12553908 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Grandori C, Cowley SM, James LP, Eisenman RN |title=The Myc/Max/Mad network and the transcriptional control of cell behavior. |journal=Annu. Rev. Cell Dev. Biol. |volume=16 |issue=  |pages= 653-99 |year= 2001 |pmid= 11031250 |doi= 10.1146/annurev.cellbio.16.1.653 }}
*{{cite journal  |vauthors=Grandori C, Cowley SM, James LP, Eisenman RN |title=The Myc/Max/Mad network and the transcriptional control of cell behavior. |journal=Annu. Rev. Cell Dev. Biol. |volume=16 |issue=  1|pages= 653–99 |year= 2001 |pmid= 11031250 |doi= 10.1146/annurev.cellbio.16.1.653 }}
*{{cite journal  | author=Lüscher B |title=Function and regulation of the transcription factors of the Myc/Max/Mad network. |journal=Gene |volume=277 |issue= 1-2 |pages= 1-14 |year= 2001 |pmid= 11602341 |doi= }}
*{{cite journal  | author=Lüscher B |title=Function and regulation of the transcription factors of the Myc/Max/Mad network. |journal=Gene |volume=277 |issue= 1-2 |pages= 1–14 |year= 2001 |pmid= 11602341 |doi=10.1016/S0378-1119(01)00697-7  }}
*{{cite journal  | author=Shapiro DN, Valentine V, Eagle L, ''et al.'' |title=Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13 and 10q24-q25. |journal=Genomics |volume=23 |issue= 1 |pages= 282-5 |year= 1995 |pmid= 7829091 |doi= 10.1006/geno.1994.1496 }}
*{{cite journal  |vauthors=Ayer DE, Lawrence QA, Eisenman RN |title=Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. |journal=Cell |volume=80 |issue= 5 |pages= 767–76 |year= 1995 |pmid= 7889570 |doi=10.1016/0092-8674(95)90355-0 }}
*{{cite journal  | author=Ayer DE, Lawrence QA, Eisenman RN |title=Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. |journal=Cell |volume=80 |issue= 5 |pages= 767-76 |year= 1995 |pmid= 7889570 |doi=  }}
*{{cite journal   |vauthors=Edelhoff S, Ayer DE, Zervos AS, etal |title=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. |journal=Oncogene |volume=9 |issue= 2 |pages= 665–8 |year= 1994 |pmid= 8290278 |doi=  }}
*{{cite journal | author=Edelhoff S, Ayer DE, Zervos AS, ''et al.'' |title=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. |journal=Oncogene |volume=9 |issue= 2 |pages= 665-8 |year= 1994 |pmid= 8290278 |doi=  }}
*{{cite journal  |vauthors=Ayer DE, Kretzner L, Eisenman RN |title=Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. |journal=Cell |volume=72 |issue= 2 |pages= 211–22 |year= 1993 |pmid= 8425218 |doi=10.1016/0092-8674(93)90661-9 }}
*{{cite journal  | author=Ayer DE, Kretzner L, Eisenman RN |title=Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. |journal=Cell |volume=72 |issue= 2 |pages= 211-22 |year= 1993 |pmid= 8425218 |doi=  }}
*{{cite journal   |vauthors=Hassig CA, Fleischer TC, Billin AN, etal |title=Histone deacetylase activity is required for full transcriptional repression by mSin3A. |journal=Cell |volume=89 |issue= 3 |pages= 341–7 |year= 1997 |pmid= 9150133 |doi=10.1016/S0092-8674(00)80214-7 }}
*{{cite journal | author=Hassig CA, Fleischer TC, Billin AN, ''et al.'' |title=Histone deacetylase activity is required for full transcriptional repression by mSin3A. |journal=Cell |volume=89 |issue= 3 |pages= 341-7 |year= 1997 |pmid= 9150133 |doi=  }}
*{{cite journal   |vauthors=Laherty CD, Yang WM, Sun JM, etal |title=Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. |journal=Cell |volume=89 |issue= 3 |pages= 349–56 |year= 1997 |pmid= 9150134 |doi=10.1016/S0092-8674(00)80215-9 }}
*{{cite journal | author=Laherty CD, Yang WM, Sun JM, ''et al.'' |title=Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. |journal=Cell |volume=89 |issue= 3 |pages= 349-56 |year= 1997 |pmid= 9150134 |doi=  }}
*{{cite journal   |vauthors=Gupta K, Anand G, Yin X, etal |title=Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc. |journal=Oncogene |volume=16 |issue= 9 |pages= 1149–59 |year= 1998 |pmid= 9528857 |doi= 10.1038/sj.onc.1201634 }}
*{{cite journal | author=Gupta K, Anand G, Yin X, ''et al.'' |title=Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc. |journal=Oncogene |volume=16 |issue= 9 |pages= 1149-59 |year= 1998 |pmid= 9528857 |doi= 10.1038/sj.onc.1201634 }}
*{{cite journal   |vauthors=FitzGerald MJ, Arsura M, Bellas RE, etal |title=Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc. |journal=Oncogene |volume=18 |issue= 15 |pages= 2489–98 |year= 1999 |pmid= 10229200 |doi= 10.1038/sj.onc.1202611 }}
*{{cite journal | author=FitzGerald MJ, Arsura M, Bellas RE, ''et al.'' |title=Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc. |journal=Oncogene |volume=18 |issue= 15 |pages= 2489-98 |year= 1999 |pmid= 10229200 |doi= 10.1038/sj.onc.1202611 }}
*{{cite journal   |vauthors=Khan MM, Nomura T, Kim H, etal |title=Role of PML and PML-RARalpha in Mad-mediated transcriptional repression. |journal=Mol. Cell |volume=7 |issue= 6 |pages= 1233–43 |year= 2001 |pmid= 11430826 |doi=10.1016/S1097-2765(01)00257-X }}
*{{cite journal | author=Khan MM, Nomura T, Kim H, ''et al.'' |title=Role of PML and PML-RARalpha in Mad-mediated transcriptional repression. |journal=Mol. Cell |volume=7 |issue= 6 |pages= 1233-43 |year= 2001 |pmid= 11430826 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Nikiforov MA, Popov N, Kotenko I, etal |title=The Mad and Myc basic domains are functionally equivalent. |journal=J. Biol. Chem. |volume=278 |issue= 13 |pages= 11094–9 |year= 2003 |pmid= 12538578 |doi= 10.1074/jbc.M212298200 }}
*{{cite journal | author=Nikiforov MA, Popov N, Kotenko I, ''et al.'' |title=The Mad and Myc basic domains are functionally equivalent. |journal=J. Biol. Chem. |volume=278 |issue= 13 |pages= 11094-9 |year= 2003 |pmid= 12538578 |doi= 10.1074/jbc.M212298200 }}
*{{cite journal  |vauthors=Nair SK, Burley SK |title=X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors. |journal=Cell |volume=112 |issue= 2 |pages= 193–205 |year= 2003 |pmid= 12553908 |doi=10.1016/S0092-8674(02)01284-9 }}
*{{cite journal  | author=Nair SK, Burley SK |title=X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors. |journal=Cell |volume=112 |issue= 2 |pages= 193-205 |year= 2003 |pmid= 12553908 |doi=  }}
*{{cite journal  |vauthors=Siegel PM, Shu W, Massagué J |title=Mad upregulation and Id2 repression accompany transforming growth factor (TGF)-beta-mediated epithelial cell growth suppression. |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 35444–50 |year= 2003 |pmid= 12824180 |doi= 10.1074/jbc.M301413200 }}
*{{cite journal  | author=Siegel PM, Shu W, Massagué J |title=Mad upregulation and Id2 repression accompany transforming growth factor (TGF)-beta-mediated epithelial cell growth suppression. |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 35444-50 |year= 2003 |pmid= 12824180 |doi= 10.1074/jbc.M301413200 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Hillier LW, Graves TA, Fulton RS, etal |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 }}
*{{cite journal | author=Hillier LW, Graves TA, Fulton RS, ''et al.'' |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724-31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 }}
*{{cite journal   |vauthors=Zada AA, Pulikkan JA, Bararia D, etal |title=Proteomic discovery of Max as a novel interacting partner of C/EBPalpha: a Myc/Max/Mad link. |journal=Leukemia |volume=20 |issue= 12 |pages= 2137–46 |year= 2007 |pmid= 17082780 |doi= 10.1038/sj.leu.2404438 }}
*{{cite journal | author=Zada AA, Pulikkan JA, Bararia D, ''et al.'' |title=Proteomic discovery of Max as a novel interacting partner of C/EBPalpha: a Myc/Max/Mad link. |journal=Leukemia |volume=20 |issue= 12 |pages= 2137-46 |year= 2007 |pmid= 17082780 |doi= 10.1038/sj.leu.2404438 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=4084}}


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Revision as of 07:10, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

MAD protein is a protein that in humans is encoded by the MXD1 gene.[1][2]

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.[2] The MAD-MAX protein dimer may be a reference to the popular cult classic film Mad Max (1979).

Interactions

MXD1 has been shown to interact with Histone deacetylase 2,[3][4] SMC3,[5] MLX,[6][7] SIN3A[8][9][10] and MAX.[5][11][12][13]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: MXD1 MAX dimerization protein 1".
  3. ↑ 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. doi:10.1016/S0092-8674(00)80215-9. ISSN 0092-8674. PMID 9150134.
  4. ↑ 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. doi:10.1038/81944. ISSN 1072-8368. PMID 11101889.
  5. ↑ 5.0 5.1 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. doi:10.1038/sj.onc.1201634. ISSN 0950-9232. PMID 9528857.
  6. ↑ 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. doi:10.1093/hmg/10.6.617. ISSN 0964-6906. PMID 11230181.
  7. ↑ 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. doi:10.1038/sj.onc.1203634. ISSN 0950-9232. PMID 10918583.
  8. ↑ 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. doi:10.1038/nsmb798. ISSN 1545-9993. PMID 15235594.
  9. ↑ 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. doi:10.1016/S0092-8674(00)00168-9. ISSN 0092-8674. PMID 11106735.
  10. ↑ 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. doi:10.1016/0092-8674(95)90355-0. ISSN 0092-8674. PMID 7889570.
  11. ↑ 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. doi:10.1073/pnas.232310199. ISSN 0027-8424. PMC 137859. PMID 12391307.
  12. ↑ 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. doi:10.1016/0092-8674(93)90661-9. ISSN 0092-8674. PMID 8425218.
  13. ↑ 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. doi:10.1016/S0092-8674(02)01284-9. ISSN 0092-8674. PMID 12553908.

Further reading


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