MBD3: Difference between revisions

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{{null|date=May 2011}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''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 = Molecular and Cellular Biology | volume = 18 | issue = 11 | pages = 6538–47 | date = November 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 = Mammalian Genome | volume = 10 | issue = 9 | pages = 906–12 | date = September 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| access-date = }}</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- 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]].<ref name="Yildirim_2011">{{cite journal | vauthors = Yildirim O, Li R, Hung JH, Chen PB, Dong X, Ee LS, Weng Z, Rando OJ, Fazzio TG | title = Mbd3/NURD complex regulates expression of 5-hydroxymethylcytosine marked genes in embryonic stem cells | journal = Cell | volume = 147 | issue = 7 | pages = 1498–510 | date = December 2011 | pmid = 22196727 | pmc = 3252821 | doi = 10.1016/j.cell.2011.11.054 }}</ref> 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==
MBD3 also contains the [[coiled coil|coiled‐coil]] domain common to all three MBD3 isoforms. The coiled‐coil domain, but not the MBD domain, helps to maintain pluripotency of embryonic stem cells via the recruitment of [[polycomb repressive complex 2]] to a subset of genes linked to development and organogenesis, thus establishing stable transcriptional repression.<ref name="Hirasaki_2018">{{cite journal | vauthors = Hirasaki M, Ueda A, Asaka MN, Uranishi K, Suzuki A, Kohda M, Mizuno Y, Okazaki Y, Nishimoto M, Sharif J, Koseki H, Okuda A | title = Identification of the Coiled-Coil Domain as an Essential Mbd3 Element for Preserving Lineage Commitment Potential of Embryonic Stem Cells | journal = Stem Cells | volume = | issue = | date = May 2018 | pmid = 29761578 | doi = 10.1002/stem.2849 }}</ref>
{{reflist|2}}
 
==Further reading==
== Interactions ==
{{refbegin | 2}}
 
{{PBB_Further_reading
MBD3 has been shown to [[Protein-protein interaction|interact]] with:
| citations =
* [[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 = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48714–23 | date = December 2002 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 }}</ref>
*{{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= }}
* [[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 = The Journal of Biological Chemistry | volume = 277 | issue = 43 | pages = 40958–66 | date = October 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 = Molecular and Cellular Biology | volume = 22 | issue = 2 | pages = 536–46 | date = January 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002 }}</ref>
*{{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= }}
* [[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 & Development | volume = 13 | issue = 15 | pages = 1924–35 | date = August 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 = The Journal of Biological Chemistry | volume = 277 | issue = 38 | pages = 35434–9 | date = September 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 }}</ref>
*{{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= }}
* [[MTA2]],<ref name = pmid12354758/><ref name = pmid10444591/><ref name = pmid12124384/> and
*{{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 }}
* [[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 = The Journal of Biological Chemistry | volume = 279 | issue = 50 | pages = 52456–64 | date = December 2004 | pmid = 15456747 | doi = 10.1074/jbc.M409149200 }}</ref>
*{{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 | 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= }}
== References ==
*{{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 }}
{{reflist|32em}}
*{{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= }}
{{clear}}
*{{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 | 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 }}
== Further reading ==
*{{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= }}
{{refbegin|32em}}
*{{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 = 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 | date = June 2013 | pmid = 23498661 | pmc = 4060438 | doi = 10.1016/j.ceb.2013.02.017 }}
*{{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 = 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 = The Biochemical Journal | volume = 259 | issue = 1 | pages = 283–90 | date = April 1989 | pmid = 2470348 | pmc = 1138502 | doi = }}
*{{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 = 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 | date = October 1998 | pmid = 9790534 | doi = 10.1016/S0092-8674(00)81758-4 }}
*{{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 | 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 | date = October 1998 | pmid = 9804427 | doi = 10.1038/27699 }}
*{{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 = 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 & Development | volume = 13 | issue = 15 | pages = 1924–35 | date = August 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924 }}
*{{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 | 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 = Nature Genetics | volume = 23 | issue = 1 | pages = 62–6 | date = September 1999 | pmid = 10471500 | doi = 10.1038/12664 }}
*{{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 | 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 to Cells | volume = 5 | issue = 8 | pages = 677–88 | date = August 2000 | pmid = 10947852 | doi = 10.1046/j.1365-2443.2000.00359.x }}
*{{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 | 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 = The Journal of Biological Chemistry | volume = 276 | issue = 9 | pages = 6817–24 | date = March 2001 | pmid = 11102443 | doi = 10.1074/jbc.M007372200 }}
*{{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 }}
* {{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 & Development | volume = 15 | issue = 9 | pages = 1140–51 | date = May 2001 | pmid = 11331609 | pmc = 312688 | doi = 10.1101/gad.871201 }}
}}
* {{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 = Molecular and Cellular Biology | volume = 22 | issue = 2 | pages = 536–46 | date = January 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002 }}
* {{cite journal | vauthors = Schlegel J, Güneysu S, Mennel HD | title = Expression of the genes of methyl-binding domain proteins in human gliomas | journal = Oncology Reports | volume = 9 | issue = 2 | pages = 393–5 | year = 2002 | pmid = 11836615 | doi = 10.3892/or.9.2.393 }}
* {{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 = The Journal of Biological Chemistry | volume = 277 | issue = 38 | pages = 35434–9 | date = September 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 }}
* {{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 = The Journal of Biological Chemistry | volume = 277 | issue = 43 | pages = 40958–66 | date = October 2002 | pmid = 12183469 | doi = 10.1074/jbc.M207467200 }}
* {{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 = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48714–23 | date = December 2002 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 }}
* {{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 | date = April 2003 | pmid = 12705869 | doi = 10.1016/S0092-8674(03)00234-4 }}
* {{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 | date = October 2004 | pmid = 15454082 | doi = 10.1016/j.cell.2004.09.014 }}
{{refend}}
{{refend}}


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

Latest revision as of 19:02, 24 May 2018

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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
PubMed searchn/an/a
Wikidata
View/Edit Human

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.[4] 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]

MBD3 also contains the coiled‐coil domain common to all three MBD3 isoforms. The coiled‐coil domain, but not the MBD domain, helps to maintain pluripotency of embryonic stem cells via the recruitment of polycomb repressive complex 2 to a subset of genes linked to development and organogenesis, thus establishing stable transcriptional repression.[5]

Interactions

MBD3 has been shown to interact with:

References

  1. ↑ Hendrich B, Bird A (November 1998). "Identification and characterization of a family of mammalian methyl-CpG binding proteins". Molecular and Cellular Biology. 18 (11): 6538–47. PMC 109239. PMID 9774669.
  2. ↑ Hendrich B, Abbott C, McQueen H, Chambers D, Cross S, Bird A (September 1999). "Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes". Mammalian 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. ↑ Yildirim O, Li R, Hung JH, Chen PB, Dong X, Ee LS, Weng Z, Rando OJ, Fazzio TG (December 2011). "Mbd3/NURD complex regulates expression of 5-hydroxymethylcytosine marked genes in embryonic stem cells". Cell. 147 (7): 1498–510. doi:10.1016/j.cell.2011.11.054. PMC 3252821. PMID 22196727.
  5. ↑ Hirasaki M, Ueda A, Asaka MN, Uranishi K, Suzuki A, Kohda M, Mizuno Y, Okazaki Y, Nishimoto M, Sharif J, Koseki H, Okuda A (May 2018). "Identification of the Coiled-Coil Domain as an Essential Mbd3 Element for Preserving Lineage Commitment Potential of Embryonic Stem Cells". Stem Cells. doi:10.1002/stem.2849. PMID 29761578.
  6. ↑ 6.0 6.1 6.2 Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F (December 2002). "MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase". The Journal of Biological Chemistry. 277 (50): 48714–23. doi:10.1074/jbc.M208461200. PMID 12354758.
  7. ↑ Brackertz M, Boeke J, Zhang R, Renkawitz R (October 2002). "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3". The Journal of Biological Chemistry. 277 (43): 40958–66. doi:10.1074/jbc.M207467200. PMID 12183469.
  8. ↑ Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y (January 2002). "Identification and functional characterization of the p66/p68 components of the MeCP1 complex". Molecular and Cellular Biology. 22 (2): 536–46. doi:10.1128/MCB.22.2.536-546.2002. PMC 139742. PMID 11756549.
  9. ↑ 9.0 9.1 9.2 Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (August 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes & Development. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
  10. ↑ 10.0 10.1 Saito M, Ishikawa F (September 2002). "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2". The Journal of Biological Chemistry. 277 (38): 35434–9. doi:10.1074/jbc.M203455200. PMID 12124384.
  11. ↑ Jiang CL, Jin SG, Pfeifer GP (December 2004). "MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex". The Journal of Biological Chemistry. 279 (50): 52456–64. doi:10.1074/jbc.M409149200. PMID 15456747.

Further reading

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