a DNA methyltransferase required for genome wide de novo methylation and essential for development. DNA methylation is coordinated with methylation of histones. Prefers CpG methylation to CpA, CpT, and CpC methylation. Methylates CpG sites at a rate much slower than DNMT1, but greater than DNMT3b. Methylation is coordinated with methylation of histones. Binds the ZNF238 transcriptional repressor. Interacts with SETDB1 and DNMT1. Can co-localize with heterochromatin protein (HP1 ) and methyl-CpG binding protein (MeCBP). Associates with HDAC1 through its ADD-type zinc-finger. Highly expressed in fetal tissues, skeletal muscle, heart, peripheral blood mononuclear cells, kidney, and at lower levels in placenta, brain, liver, colon, spleen, small intestine and lung. Note: This description may include information from UniProtKB.
Protein type: Methyltransferase, DNA; EC 188.8.131.52; Methyltransferase; Amino Acid Metabolism - cysteine and methionine
Molecular Function: DNA (cytosine-5-)-methyltransferase activity; protein binding; DNA binding; unmethylated CpG binding; DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates; metal ion binding; chromatin binding
Biological Process: cytosine methylation within a CG sequence; genetic imprinting; methylation-dependent chromatin silencing; DNA methylation during gametogenesis; DNA methylation; S-adenosylmethioninamine metabolic process; S-adenosylhomocysteine metabolic process; spermatogenesis; negative regulation of transcription from RNA polymerase II promoter; DNA methylation during embryonic development
Alt. Names/Synonyms: DNA (cytosine-5)-methyltransferase 3A; DNA (cytosine-5-)-methyltransferase 3 alpha; DNA cytosine methyltransferase 3A2; DNA methyltransferase HsaIIIA; DNA MTase HsaIIIA; DNM3A; DNMT3A; DNMT3A2; M.HsaIIIA
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.