| SETD7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | SETD7 , KMT7, SET7, SET7/9, SET9, SET domain containing lysine methyltransferase 7, SET domain containing 7, histone lysine methyltransferase | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 606594 MGI: 1920501 HomoloGene: 12741 GeneCards: SETD7 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene. [5] [6] [7]
In biology, histones are highly basic proteins abundant in lysine and arginine residues that are found in eukaryotic cell nuclei. They act as spools around which DNA winds to create structural units called nucleosomes. Nucleosomes in turn are wrapped into 30-nanometer fibers that form tightly packed chromatin. Histones prevent DNA from becoming tangled and protect it from DNA damage. In addition, histones play important roles in gene regulation and DNA replication. Without histones, unwound DNA in chromosomes would be very long. For example, each human cell has about 1.8 meters of DNA if completely stretched out; however, when wound about histones, this length is reduced to about 90 micrometers (0.09 mm) of 30 nm diameter chromatin fibers.
Histone methyltransferases (HMT) are histone-modifying enzymes, that catalyze the transfer of one, two, or three methyl groups to lysine and arginine residues of histone proteins. The attachment of methyl groups occurs predominantly at specific lysine or arginine residues on histones H3 and H4. Two major types of histone methyltranferases exist, lysine-specific and arginine-specific. In both types of histone methyltransferases, S-Adenosyl methionine (SAM) serves as a cofactor and methyl donor group.
The genomic DNA of eukaryotes associates with histones to form chromatin. The level of chromatin compaction depends heavily on histone methylation and other post-translational modifications of histones. Histone methylation is a principal epigenetic modification of chromatin that determines gene expression, genomic stability, stem cell maturation, cell lineage development, genetic imprinting, DNA methylation, and cell mitosis.
Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossmann fold for binding S-Adenosyl methionine (SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain histone methyltransferases, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a SN2-like nucleophilic attack where the methionine sulfur serves as the leaving group and the methyl group attached to it acts as the electrophile that transfers the methyl group to the enzyme substrate. SAM is converted to S-Adenosyl homocysteine (SAH) during this process. The breaking of the SAM-methyl bond and the formation of the substrate-methyl bond happen nearly simultaneously. These enzymatic reactions are found in many pathways and are implicated in genetic diseases, cancer, and metabolic diseases. Another type of methyl transfer is the radical S-Adenosyl methionine (SAM) which is the methylation of unactivated carbon atoms in primary metabolites, proteins, lipids, and RNA.
Histone-binding protein RBBP4 is a protein that in humans is encoded by the RBBP4 gene.
Enhancer of zeste homolog 2 (EZH2) is a histone-lysine N-methyltransferase enzyme encoded by EZH2 gene, that participates in histone methylation and, ultimately, transcriptional repression. EZH2 catalyzes the addition of methyl groups to histone H3 at lysine 27, by using the cofactor S-adenosyl-L-methionine. Methylation activity of EZH2 facilitates heterochromatin formation thereby silences gene function. Remodeling of chromosomal heterochromatin by EZH2 is also required during cell mitosis.
Methyl-CpG-binding domain protein 2 is a protein that in humans is encoded by the MBD2 gene.
Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 gene.
Histone-lysine N-methyltransferase SETDB1 is an enzyme that in humans is encoded by the SETDB1 gene. SETDB1 is also known as KMT1E or H3K9 methyltransferase ESET.
Polycomb protein SUZ12 is a protein that in humans is encoded by the SUZ12 gene.
DNA (cytosine-5)-methyltransferase 3-like is an enzyme that in humans is encoded by the DNMT3L gene.
Histone H3.1 is a protein that in humans is encoded by the HIST1H3F gene.
SET domain containing 2 is an enzyme that in humans is encoded by the SETD2 gene.
N-lysine methyltransferase KMT5A is an enzyme that in humans is encoded by the KMT5A gene. The enzyme is a histone methyltransferase, SET domain-containing and lysine-specific. The enzyme transfers one methyl group to histone H4 lysine residue at position 20. S-Adenosyl methionine (SAM) is both the cofactor and the methyl group donor. The lysine residue is converted to N6-methyllysine residue.
Histone-lysine N-methyltransferase KMT5B is an enzyme that in humans is encoded by the KMT5B gene. The enzyme along with WHSC1 is responsible for dimethylation of lysine 20 on histone H4 in mouse and humans.
DOT1-like, histone H3K79 methyltransferase, also known as DOT1L, is a protein found in humans, as well as other eukaryotes. The methylation of histone H3 lysine 79 (H3K79) by DOT1L which is a conserved epigenetic mark in many eukaryotic epigenomes, increases progressively along the aging process, suggesting that "DOT1L might function as a vital clock, ticking the hours impassively".
The SET domain is a protein domain that typically has methyltransferase activity. It was originally identified as part of a larger conserved region present in the Drosophila Trithorax protein and was subsequently identified in the Drosophila Su(var)3-9 and 'Enhancer of zeste' proteins, from which the acronym SET is derived [Su(var)3-9, Enhancer-of-zeste and Trithorax].
Euchromatic histone-lysine N-methyltransferase 1, also known as G9a-like protein (GLP), is a protein that in humans is encoded by the EHMT1 gene.
SET domain containing 6 is a protein in humans that is encoded by the SETD6 gene.
SET domain containing 1B is a protein that in humans is encoded by the SETD1B gene.
SET domain containing 3 (SETD3) is a protein that in humans is encoded by the SETD3 gene. It is a methyl transferase implicated in the replication of all enteroviruses. A mouse line deficient in SETD3 expression was shown to be immune to enterovirus infection. This could pave the way for the prevention of diseases like the common cold, myocarditis, aseptic meningitis and polio. SETD3 is capable of methylating the cytoskeletal protein actin on histidine residues.
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