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{{Infobox_gene}}
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'''Methyl-CpG-binding domain protein 3''' is a [[protein]] that in humans is encoded by the ''MBD3'' [[gene]].<ref name="pmid9774669">{{cite journal | vauthors = Hendrich B, Bird A | title = Identification and characterization of a family of mammalian methyl-CpG binding proteins | journal = Mol Cell Biol | volume = 18 | issue = 11 | pages = 6538–47 | date = Nov 1998 | pmid = 9774669 | pmc = 109239 | doi =  }}</ref><ref name="pmid10441743">{{cite journal | vauthors = Hendrich B, Abbott C, McQueen H, Chambers D, Cross S, Bird A | title = Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes | journal = Mamm Genome | volume = 10 | issue = 9 | pages = 906–12 | date = Sep 1999 | pmid = 10441743 | pmc = | doi = 10.1007/s003359901112 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MBD3 methyl-CpG binding domain protein 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53615| accessdate = }}</ref>
| require_manual_inspection = no
| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Methyl-CpG binding domain protein 3
| HGNCid = 6918
| Symbol = MBD3
| AltSymbols =;
| OMIM = 603573
| ECnumber = 
| Homologene = 2917
| MGIid = 1333812
| GeneAtlas_image1 = PBB_GE_MBD3_41160_at_tn.png
| GeneAtlas_image2 = PBB_GE_MBD3_202463_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000792 |text = heterochromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0016581 |text = NuRD complex}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006346 |text = methylation-dependent chromatin silencing}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0016573 |text = histone acetylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 53615
    | Hs_Ensembl = ENSG00000071655
    | Hs_RefseqProtein = NP_003917
    | Hs_RefseqmRNA = NM_003926
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 1527678
    | Hs_GenLoc_end = 1543710
    | Hs_Uniprot = O95983
    | Mm_EntrezGene = 17192
    | Mm_Ensembl = ENSMUSG00000035478
    | Mm_RefseqmRNA = NM_013595
    | Mm_RefseqProtein = NP_038623
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 79795670
    | Mm_GenLoc_end = 79802608
    | Mm_Uniprot = Q9Z2D8
  }}
}}
'''Methyl-CpG binding domain protein 3''', also known as '''MBD3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MBD3 methyl-CpG binding domain protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53615| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins [[MECP2]], [[MBD1]], [[MBD2]], MBD3, and [[MBD4]] comprise a family of nuclear proteins related by the presence in each of a [[Methyl-CpG-binding domain|methyl-CpG binding domain]] (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA but instead binds to [[5-Hydroxymethylcytosine|hydroxymethylated DNA]] [http://www.sciencedirect.com/science/article/pii/S0092867411014498]. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3.  MBD3 is a subunit of the [[Mi-2/NuRD complex|NuRD]], a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3.  MBD3 is a subunit of the NuRD, a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.<ref name="entrez">{{cite web | title = Entrez Gene: MBD3 methyl-CpG binding domain protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53615| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
MBD3 has been shown to [[Protein-protein interaction|interact]] with:
* [[Aurora A kinase|AURKA]],<ref name = pmid12354758>{{cite journal | vauthors = Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F | title = MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase | journal = J. Biol. Chem. | volume = 277 | issue = 50 | pages = 48714–23 | year = 2002 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 }}</ref>
* [[GATAD2B]],<ref name = pmid12183469>{{cite journal | vauthors = Brackertz M, Boeke J, Zhang R, Renkawitz R | title = Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3 | journal = J. Biol. Chem. | volume = 277 | issue = 43 | pages = 40958–66 | year = 2002 | pmid = 12183469 | doi = 10.1074/jbc.M207467200 }}</ref><ref name = pmid11756549>{{cite journal | vauthors = Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y | title = Identification and functional characterization of the p66/p68 components of the MeCP1 complex | journal = Mol. Cell. Biol. | volume = 22 | issue = 2 | pages = 536–46 | year = 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002 }}</ref>
* [[HDAC1]],<ref name = pmid12354758/><ref name = pmid10444591>{{cite journal | vauthors = Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D | title = Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation | journal = Genes Dev. | volume = 13 | issue = 15 | pages = 1924–35 | year = 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924 }}</ref><ref name = pmid12124384>{{cite journal | vauthors = Saito M, Ishikawa F | title = The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2 | journal = J. Biol. Chem. | volume = 277 | issue = 38 | pages = 35434–9 | year = 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 }}</ref>
* [[MTA2]],<ref name = pmid12354758/><ref name = pmid10444591/><ref name = pmid12124384/> and
* [[Methyl-CpG-binding domain protein 2|MBD2]].<ref name = pmid10444591/><ref name = pmid15456747>{{cite journal | vauthors = Jiang CL, Jin SG, Pfeifer GP | title = MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex | journal = J. Biol. Chem. | volume = 279 | issue = 50 | pages = 52456–64 | year = 2004 | pmid = 15456747 | doi = 10.1074/jbc.M409149200 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Shen L, Zhang Y | title = 5-Hydroxymethylcytosine: generation, fate, and genomic distribution | journal = Current Opinion in Cell Biology | volume = 25 | issue = 3 | pages = 289–96 | year = 2013 | pmid = 23498661 | doi = 10.1016/j.ceb.2013.02.017 | pmc=4060438}}
| citations =  
* {{cite journal | vauthors = Abbott WM, Mellor A, Edwards Y, Feizi T | title = Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein. | journal = Biochem. J. | volume = 259 | issue = 1 | pages = 283–90 | year = 1989 | pmid = 2470348 | pmc = 1138502 | doi =  }}
*{{cite journal | author=Abbott WM, Mellor A, Edwards Y, Feizi T |title=Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein. |journal=Biochem. J. |volume=259 |issue= 1 |pages= 283-90 |year= 1989 |pmid= 2470348 |doi= }}
* {{cite journal | vauthors = Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D | title = The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. | journal = Cell | volume = 95 | issue = 2 | pages = 279–89 | year = 1998 | pmid = 9790534 | doi = 10.1016/S0092-8674(00)81758-4 }}
*{{cite journal  | author=Hendrich B, Bird A |title=Identification and characterization of a family of mammalian methyl-CpG binding proteins. |journal=Mol. Cell. Biol. |volume=18 |issue= 11 |pages= 6538-47 |year= 1998 |pmid= 9774669 |doi=  }}
* {{cite journal | vauthors = Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL | title = Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. | journal = Nature | volume = 395 | issue = 6705 | pages = 917–21 | year = 1998 | pmid = 9804427 | doi = 10.1038/27699 }}
*{{cite journal | author=Zhang Y, LeRoy G, Seelig HP, ''et al.'' |title=The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. |journal=Cell |volume=95 |issue= 2 |pages= 279-89 |year= 1998 |pmid= 9790534 |doi= }}
* {{cite journal | vauthors = Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D | title = Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. | journal = Genes Dev. | volume = 13 | issue = 15 | pages = 1924–35 | year = 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924 }}
*{{cite journal | author=Tong JK, Hassig CA, Schnitzler GR, ''et al.'' |title=Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. |journal=Nature |volume=395 |issue= 6705 |pages= 917-21 |year= 1998 |pmid= 9804427 |doi= 10.1038/27699 }}
* {{cite journal | vauthors = Wade PA, Gegonne A, Jones PL, Ballestar E, Aubry F, Wolffe AP | title = Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation. | journal = Nat. Genet. | volume = 23 | issue = 1 | pages = 62–6 | year = 1999 | pmid = 10471500 | doi = 10.1038/12664 }}
*{{cite journal | author=Hendrich B, Abbott C, McQueen H, ''et al.'' |title=Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes. |journal=Mamm. Genome |volume=10 |issue= 9 |pages= 906-12 |year= 1999 |pmid= 10441743 |doi=  }}
* {{cite journal | vauthors = Tatematsu KI, Yamazaki T, Ishikawa F | title = MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase. | journal = Genes Cells | volume = 5 | issue = 8 | pages = 677–88 | year = 2000 | pmid = 10947852 | doi = 10.1046/j.1365-2443.2000.00359.x }}
*{{cite journal  | author=Zhang Y, Ng HH, Erdjument-Bromage H, ''et al.'' |title=Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. |journal=Genes Dev. |volume=13 |issue= 15 |pages= 1924-35 |year= 1999 |pmid= 10444591 |doi= }}
* {{cite journal | vauthors = Humphrey GW, Wang Y, Russanova VR, Hirai T, Qin J, Nakatani Y, Howard BH | title = Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. | journal = J. Biol. Chem. | volume = 276 | issue = 9 | pages = 6817–24 | year = 2001 | pmid = 11102443 | doi = 10.1074/jbc.M007372200 }}
*{{cite journal | author=Wade PA, Gegonne A, Jones PL, ''et al.'' |title=Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation. |journal=Nat. Genet. |volume=23 |issue= 1 |pages= 62-6 |year= 1999 |pmid= 10471500 |doi= 10.1038/12664 }}
* {{cite journal | vauthors = Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM | title = Sharp, an inducible cofactor that integrates nuclear receptor repression and activation. | journal = Genes Dev. | volume = 15 | issue = 9 | pages = 1140–51 | year = 2001 | pmid = 11331609 | pmc = 312688 | doi = 10.1101/gad.871201 }}
*{{cite journal | author=Tatematsu KI, Yamazaki T, Ishikawa F |title=MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase. |journal=Genes Cells |volume=5 |issue= 8 |pages= 677-88 |year= 2000 |pmid= 10947852 |doi= }}
* {{cite journal | vauthors = Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y | title = Identification and functional characterization of the p66/p68 components of the MeCP1 complex. | journal = Mol. Cell. Biol. | volume = 22 | issue = 2 | pages = 536–46 | year = 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002 }}
*{{cite journal | author=Humphrey GW, Wang Y, Russanova VR, ''et al.'' |title=Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6817-24 |year= 2001 |pmid= 11102443 |doi= 10.1074/jbc.M007372200 }}
* {{cite journal | vauthors = Schlegel J, Güneysu S, Mennel HD | title = Expression of the genes of methyl-binding domain proteins in human gliomas. | journal = Oncol. Rep. | volume = 9 | issue = 2 | pages = 393–5 | year = 2002 | pmid = 11836615 | doi = 10.3892/or.9.2.393 }}
*{{cite journal | author=Shi Y, Downes M, Xie W, ''et al.'' |title=Sharp, an inducible cofactor that integrates nuclear receptor repression and activation. |journal=Genes Dev. |volume=15 |issue= 9 |pages= 1140-51 |year= 2001 |pmid= 11331609 |doi= 10.1101/gad.871201 }}
* {{cite journal | vauthors = Saito M, Ishikawa F | title = The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2. | journal = J. Biol. Chem. | volume = 277 | issue = 38 | pages = 35434–9 | year = 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 }}
*{{cite journal | author=Feng Q, Cao R, Xia L, ''et al.'' |title=Identification and functional characterization of the p66/p68 components of the MeCP1 complex. |journal=Mol. Cell. Biol. |volume=22 |issue= 2 |pages= 536-46 |year= 2002 |pmid= 11756549 |doi= }}
* {{cite journal | vauthors = Brackertz M, Boeke J, Zhang R, Renkawitz R | title = Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3. | journal = J. Biol. Chem. | volume = 277 | issue = 43 | pages = 40958–66 | year = 2002 | pmid = 12183469 | doi = 10.1074/jbc.M207467200 }}
*{{cite journal | author=Schlegel J, Güneysu S, Mennel HD |title=Expression of the genes of methyl-binding domain proteins in human gliomas. |journal=Oncol. Rep. |volume=9 |issue= 2 |pages= 393-5 |year= 2002 |pmid= 11836615 |doi= }}
* {{cite journal | vauthors = Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F | title = MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase. | journal = J. Biol. Chem. | volume = 277 | issue = 50 | pages = 48714–23 | year = 2003 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 }}
*{{cite journal | author=Saito M, Ishikawa F |title=The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35434-9 |year= 2002 |pmid= 12124384 |doi= 10.1074/jbc.M203455200 }}
* {{cite journal | vauthors = Fujita N, Jaye DL, Kajita M, Geigerman C, Moreno CS, Wade PA | title = MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer. | journal = Cell | volume = 113 | issue = 2 | pages = 207–19 | year = 2003 | pmid = 12705869 | doi = 10.1016/S0092-8674(03)00234-4 }}
*{{cite journal | author=Brackertz M, Boeke J, Zhang R, Renkawitz R |title=Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40958-66 |year= 2002 |pmid= 12183469 |doi= 10.1074/jbc.M207467200 }}
* {{cite journal | vauthors = Fujita N, Jaye DL, Geigerman C, Akyildiz A, Mooney MR, Boss JM, Wade PA | title = MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation. | journal = Cell | volume = 119 | issue = 1 | pages = 75–86 | year = 2004 | pmid = 15454082 | doi = 10.1016/j.cell.2004.09.014 }}
*{{cite journal | author=Sakai H, Urano T, Ookata K, ''et al.'' |title=MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase. |journal=J. Biol. Chem. |volume=277 |issue= 50 |pages= 48714-23 |year= 2003 |pmid= 12354758 |doi= 10.1074/jbc.M208461200 }}
*{{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  | author=Fujita N, Jaye DL, Kajita M, ''et al.'' |title=MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer. |journal=Cell |volume=113 |issue= 2 |pages= 207-19 |year= 2003 |pmid= 12705869 |doi=  }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Grimwood J, Gordon LA, Olsen A, ''et al.'' |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529-35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 }}
*{{cite journal | author=Fujita N, Jaye DL, Geigerman C, ''et al.'' |title=MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation. |journal=Cell |volume=119 |issue= 1 |pages= 75-86 |year= 2004 |pmid= 15454082 |doi= 10.1016/j.cell.2004.09.014 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
[[Category:Human proteins]]
{{WikiDoc Sources}}

Revision as of 06:12, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Methyl-CpG-binding domain protein 3 is a protein that in humans is encoded by the MBD3 gene.[1][2][3]

Function

DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA but instead binds to hydroxymethylated DNA [2]. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 is a subunit of the NuRD, a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.[3]

Interactions

MBD3 has been shown to interact with:

References

  1. Hendrich B, Bird A (Nov 1998). "Identification and characterization of a family of mammalian methyl-CpG binding proteins". Mol Cell Biol. 18 (11): 6538–47. PMC 109239. PMID 9774669.
  2. Hendrich B, Abbott C, McQueen H, Chambers D, Cross S, Bird A (Sep 1999). "Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes". Mamm Genome. 10 (9): 906–12. doi:10.1007/s003359901112. PMID 10441743.
  3. 3.0 3.1 "Entrez Gene: MBD3 methyl-CpG binding domain protein 3".
  4. 4.0 4.1 4.2 Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F (2002). "MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase". J. Biol. Chem. 277 (50): 48714–23. doi:10.1074/jbc.M208461200. PMID 12354758.
  5. Brackertz M, Boeke J, Zhang R, Renkawitz R (2002). "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3". J. Biol. Chem. 277 (43): 40958–66. doi:10.1074/jbc.M207467200. PMID 12183469.
  6. Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y (2002). "Identification and functional characterization of the p66/p68 components of the MeCP1 complex". Mol. Cell. Biol. 22 (2): 536–46. doi:10.1128/MCB.22.2.536-546.2002. PMC 139742. PMID 11756549.
  7. 7.0 7.1 7.2 Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
  8. 8.0 8.1 Saito M, Ishikawa F (2002). "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2". J. Biol. Chem. 277 (38): 35434–9. doi:10.1074/jbc.M203455200. PMID 12124384.
  9. Jiang CL, Jin SG, Pfeifer GP (2004). "MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex". J. Biol. Chem. 279 (50): 52456–64. doi:10.1074/jbc.M409149200. PMID 15456747.

Further reading