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DNA (cytosine-5-)-methyltransferase 3 beta
Protein DNMT3B PDB 1khc.png
PDB rendering based on 1khc.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols DNMT3B ; ICF; ICF1; M.HsaIIIB
External IDs OMIM602900 MGI1261819 HomoloGene56000 ChEMBL: 6095 GeneCards: DNMT3B Gene
EC number
RNA expression pattern
PBB GE DNMT3B 220668 s at tn.png
More reference expression data
Species Human Mouse
Entrez 1789 13436
Ensembl ENSG00000088305 ENSMUSG00000027478
UniProt Q9UBC3 O88509
RefSeq (mRNA) NM_001207055 NM_001003960
RefSeq (protein) NP_001193984 NP_001003960
Location (UCSC) Chr 20:
31.35 – 31.4 Mb
Chr 2:
153.65 – 153.69 Mb
PubMed search [1] [2]

DNA (cytosine-5-)-methyltransferase 3 beta, also known as DNMT3B, is a protein associated with immunodeficiency, centromere instability and facial anomalies syndrome.


CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a DNA methyltransferase which is thought to function in de novo methylation, rather than maintenance methylation. The protein localizes primarily to the nucleus and its expression is developmentally regulated. Mutations in this gene cause the immunodeficiency-centromeric instability-facial anomalies (ICF) syndrome. Eight alternatively spliced transcript variants have been described. The full length sequences of variants 4 and 5 have not been determined.[1]


DNMT3B has been shown to interact with:


  1. ^ "Entrez Gene: DNMT3B DNA (cytosine-5-)-methyltransferase 3 beta". 
  2. ^ a b c Lehnertz B, Ueda Y, Derijck AA, Braunschweig U, Perez-Burgos L, Kubicek S, Chen T, Li E, Jenuwein T, Peters AH (Jul 2003). "Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to major satellite repeats at pericentric heterochromatin". Curr. Biol. 13 (14): 1192–200. doi:10.1016/s0960-9822(03)00432-9. PMID 12867029. 
  3. ^ a b Kim GD, Ni J, Kelesoglu N, Roberts RJ, Pradhan S (Aug 2002). "Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases". EMBO J. 21 (15): 4183–95. doi:10.1093/emboj/cdf401. PMC 126147. PMID 12145218. 
  4. ^ Ling Y, Sankpal UT, Robertson AK, McNally JG, Karpova T, Robertson KD. "Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription". Nucleic Acids Res. 32 (2): 598–610. doi:10.1093/nar/gkh195. PMC 373322. PMID 14752048. 
  5. ^ a b c Geiman TM, Sankpal UT, Robertson AK, Chen Y, Mazumdar M, Heale JT, Schmiesing JA, Kim W, Yokomori K, Zhao Y, Robertson KD. "Isolation and characterization of a novel DNA methyltransferase complex linking DNMT3B with components of the mitotic chromosome condensation machinery". Nucleic Acids Res. 32 (9): 2716–29. doi:10.1093/nar/gkh589. PMC 419596. PMID 15148359. 
  6. ^ a b Kang ES, Park CW, Chung JH (Dec 2001). "Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1". Biochem. Biophys. Res. Commun. 289 (4): 862–8. doi:10.1006/bbrc.2001.6057. PMID 11735126. 

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