MBD3

From Wikipedia, the free encyclopedia

Methyl-CpG binding domain protein 3

Identifiers

External IDs

OMIM: 603573 MGI: 1333812 HomoloGene: 2917

Gene ontology
Molecular Function:	• DNA binding • chromatin binding • protein binding
Cellular Component:	• heterochromatin • nucleus • NuRD complex
Biological Process:	• negative regulation of transcription from RNA polymerase II promoter • methylation-dependent chromatin silencing • transcription • regulation of transcription, DNA-dependent • histone acetylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003926 (mRNA)
NP_003917 (protein)

NM_013595 (mRNA)
NP_038623 (protein)

Location

Chr 19: 1.53 - 1.54 Mb

Chr 10: 79.8 - 79.8 Mb

Pubmed search

[1]

[2]

Methyl-CpG binding domain protein 3, also known as MBD3, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: MBD3 methyl-CpG binding domain protein 3.

[edit] 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. PMID 2470348.
Hendrich B, Bird A (1998). "Identification and characterization of a family of mammalian methyl-CpG binding proteins.". Mol. Cell. Biol. 18 (11): 6538–47. PMID 9774669.
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. 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.
Hendrich B, Abbott C, McQueen H, et al. (1999). "Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes.". Mamm. Genome 10 (9): 906–12. PMID 10441743.
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. 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. 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. 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. 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. 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. 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.