MBD3

MBD3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2MB7
Identifiers
Aliases	MBD3, methyl-CpG binding domain protein 3
External IDs	OMIM: 603573; MGI: 1333812; HomoloGene: 2917; GeneCards: MBD3; OMA:MBD3 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.3 Start 1,573,596 bp End 1,592,865 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10 C1|10 39.72 cM Start 80,228,373 bp End 80,235,384 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart right frontal lobe cingulate gyrus anterior cingulate cortex amygdala mucosa of transverse colon anterior pituitary left uterine tube right hemisphere of cerebellum Brodmann area 10 Top expressed in ventricular zone dentate gyrus of hippocampal formation granule cell lip yolk sac muscle of thigh superior frontal gyrus choroid plexus of fourth ventricle right kidney epiblast primary visual cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methyl-CpG binding DNA binding nucleosomal DNA binding RNA polymerase II cis-regulatory region sequence-specific DNA binding protein binding chromatin binding histone deacetylase activity Cellular component nucleus nucleoplasm heterochromatin chromosome NuRD complex cytoplasm chromatin protein-containing complex Biological process response to estradiol tissue development embryonic organ development regulation of DNA methylation in utero embryonic development response to organic cyclic compound regulation of transcription, DNA-templated heart development DNA methylation-dependent heterochromatin assembly histone acetylation negative regulation of transcription by RNA polymerase II ageing brain development response to nutrient levels transcription, DNA-templated regulation of signal transduction by p53 class mediator histone deacetylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 53615 17192 Ensembl ENSG00000071655 ENSMUSG00000035478 UniProt O95983 Q9Z2D8 RefSeq (mRNA) NM_003926 NM_001281453 NM_001281454 NM_013595 NM_001306143 RefSeq (protein) NP_001268382 NP_001268383 NP_001293072 NP_038623 Location (UCSC) Chr 19: 1.57 – 1.59 Mb Chr 10: 80.23 – 80.24 Mb PubMed search
Wikidata
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Methyl-CpG-binding domain protein 3 is a protein that in humans is encoded by the MBD3 gene.

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 [1]. 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.

Interactions

MBD3 has been shown to interact with:

• AURKA,
• GATAD2B,
• HDAC1,
• MTA2, and
• MBD2.

Further reading

• Shen L, Zhang Y (2013). "5-Hydroxymethylcytosine: generation, fate, and genomic distribution". Current Opinion in Cell Biology. 25 (3): 289–96. doi:10.1016/j.ceb.2013.02.017. PMC 4060438. PMID 23498661.
• Abbott WM, Mellor A, Edwards Y, Feizi T (1989). "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". Biochem. J. 259 (1): 283–90. PMC 1138502. PMID 2470348.
• Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (1998). "The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities". Cell. 95 (2): 279–89. doi:10.1016/S0092-8674(00)81758-4. PMID 9790534.
• Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature. 395 (6705): 917–21. doi:10.1038/27699. PMID 9804427.
• 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.
• Wade PA, Gegonne A, Jones PL, Ballestar E, Aubry F, Wolffe AP (1999). "Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation". Nat. Genet. 23 (1): 62–6. doi:10.1038/12664. PMID 10471500.
• Tatematsu KI, Yamazaki T, Ishikawa F (2000). "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase". Genes Cells. 5 (8): 677–88. doi:10.1046/j.1365-2443.2000.00359.x. PMID 10947852.
• Humphrey GW, Wang Y, Russanova VR, Hirai T, Qin J, Nakatani Y, Howard BH (2001). "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1". J. Biol. Chem. 276 (9): 6817–24. doi:10.1074/jbc.M007372200. PMID 11102443.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM (2001). "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation". Genes Dev. 15 (9): 1140–51. doi:10.1101/gad.871201. PMC 312688. PMID 11331609.
• 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.
• Schlegel J, Güneysu S, Mennel HD (2002). "Expression of the genes of methyl-binding domain proteins in human gliomas". Oncol. Rep. 9 (2): 393–5. doi:10.3892/or.9.2.393. PMID 11836615.
• 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F (2003). "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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Fujita N, Jaye DL, Kajita M, Geigerman C, Moreno CS, Wade PA (2003). "MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer". Cell. 113 (2): 207–19. doi:10.1016/S0092-8674(03)00234-4. PMID 12705869.
• Fujita N, Jaye DL, Geigerman C, Akyildiz A, Mooney MR, Boss JM, Wade PA (2004). "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation". Cell. 119 (1): 75–86. doi:10.1016/j.cell.2004.09.014. PMID 15454082.