Methyl-CpG-binding domain protein 2

MBD2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases MBD2, DMTase, NY-CO-41, methyl-CpG binding domain protein 2
External IDs MGI: 1333813 HomoloGene: 2918 GeneCards: MBD2
RNA expression pattern


More reference expression data
Orthologs
Species Human Mouse
Entrez

8932

17191

Ensembl

ENSG00000134046

ENSMUSG00000024513

UniProt

Q9UBB5

Q9Z2E1

RefSeq (mRNA)

NM_015832
NM_003927

NM_010773
NM_001311071

RefSeq (protein)

NP_003918.1
NP_056647.1
NP_056647.1

NP_001298000.1
NP_034903.2

Location (UCSC) Chr 18: 54.15 – 54.22 Mb Chr 18: 70.57 – 70.63 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Methyl-CpG-binding domain protein 2 is a protein that in humans is encoded by the MBD2 gene.[3][4]

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). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1, and MBD2 can also repress transcription from methylated gene promoters. The protein encoded by this gene may function as a mediator of the biological consequences of the methylation signal. It is also reported that this protein functions as a demethylase to activate transcription, as DNA methylation causes gene silencing if present in promoter regions.[5]

Interactions

Methyl-CpG-binding domain protein 2 has been shown to interact with:

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. Hendrich B, Bird A (November 1998). "Identification and Characterization of a Family of Mammalian Methyl-CpG Binding Proteins". Mol Cell Biol. 18 (11): 6538–47. PMC 109239Freely accessible. PMID 9774669.
  4. 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". Mamm Genome. 10 (9): 906–12. doi:10.1007/s003359901112. PMID 10441743.
  5. "Entrez Gene: MBD2 methyl-CpG binding domain protein 2".
  6. 1 2 3 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". J. Biol. Chem. 277 (43): 40958–66. doi:10.1074/jbc.M207467200. PMID 12183469.
  7. 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". Mol. Cell. Biol. 22 (2): 536–46. doi:10.1128/mcb.22.2.536-546.2002. PMC 139742Freely accessible. PMID 11756549.
  8. 1 2 Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (September 1999). "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex". Nat. Genet. 23 (1): 58–61. doi:10.1038/12659. PMID 10471499.
  9. 1 2 3 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 Dev. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920Freely accessible. PMID 10444591.
  10. 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". J. Biol. Chem. 279 (50): 52456–64. doi:10.1074/jbc.M409149200. PMID 15456747.
  11. Sekimata M, Takahashi A, Murakami-Sekimata A, Homma Y (November 2001). "Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2". J. Biol. Chem. 276 (46): 42632–8. doi:10.1074/jbc.M107048200. PMID 11553631.
  12. Boeke J, Ammerpohl O, Kegel S, Moehren U, Renkawitz R (November 2000). "The minimal repression domain of MBD2b overlaps with the methyl-CpG-binding domain and binds directly to Sin3A". J. Biol. Chem. 275 (45): 34963–7. doi:10.1074/jbc.M005929200. PMID 10950960.

Further reading

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