MBD3
From Wikipedia, the free encyclopedia
| Methyl-CpG binding domain protein 3 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbol | MBD3 | ||||||||||||
| External IDs | OMIM: 603573 MGI: 1333812 HomoloGene: 2917 GeneCards: MBD3 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 53615 | 17192 | |||||||||||
| Ensembl | ENSG00000071655 | ENSMUSG00000035478 | |||||||||||
| UniProt | O95983 | Q9Z2D8 | |||||||||||
| RefSeq (mRNA) | NM_003926 | NM_013595 | |||||||||||
| RefSeq (protein) | NP_003917 | NP_038623 | |||||||||||
| Location (UCSC) | Chr 19: 1.58 – 1.59 Mb | Chr 10: 80.39 – 80.4 Mb | |||||||||||
| PubMed search | |||||||||||||
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. 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
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 "Entrez Gene: MBD3 methyl-CpG binding domain protein 3".
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 7.0 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.
- ↑ 8.0 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.
- ↑ 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
- 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, et al. (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, et al. (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, et al. (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, et al. (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, et al. (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.
- Shi Y, Downes M, Xie W, et al. (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, et al. (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. 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.
- 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.
- Sakai H, Urano T, Ookata K, et al. (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.
- 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Fujita N, Jaye DL, Kajita M, et al. (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.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.
- Fujita N, Jaye DL, Geigerman C, et al. (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.
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