SETMAR

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Protein-coding gene in the species Homo sapiens

title: "SETMAR" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["genes-mutated-in-mice"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/genes-mutated-in-mice" source: "https://en.wikipedia.org/wiki/SETMAR" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Histone-lysine N-methyltransferase SETMAR is an enzyme that in humans is encoded by the SETMAR gene.

Function

SETMAR contains a SET domain that confers its histone methyltransferase activity, on Lys-4 and Lys-36 of Histone H3, both of which are specific tags for epigenetic activation. It has been identified as a repair protein as it mediates dimethylation at Lys-36 at double-strand break locations, a signal enhancing NHEJ repair.

Anthropoid primates, including humans, have a version of the protein fused to a Mariner/Tc1 transposase. This fusion region provides the DNA-binding abilities for the protein as well as some nuclease activity. The transposase activity is lost due to the presence of several inactivating mutations, including the D610N mutation. However, the domesticated transposase domain retains its ability to bind to the mariner repeat elements in the genome. SETMAR has been found to affect the expression and splicing of genes close to or containing mariner repeat elements via its functions in histone methylation. Both the SET, via its methyltransferase activity, and the mariner, with its DNA-binding and nuclease activities, domains of SETMAR have been shown to act in non-homologous end joining (NHEJ) to repair DNA double strand breaks.

References

References

  1. (December 1997). "Molecular evolution of an ancient mariner transposon, Hsmar1, in the human genome". Gene.
  2. "Entrez Gene: SETMAR SET domain and mariner transposase fusion gene".
  3. (December 2021). "Structure, Activity, and Function of SETMAR Protein Lysine Methyltransferase". Life.
  4. (April 2022). "SETMAR, a case of primate co-opted genes: towards new perspectives". Mobile DNA.
  5. (December 2005). "The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair". Proceedings of the National Academy of Sciences of the United States of America.
  6. (January 2011). "Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining". Proceedings of the National Academy of Sciences of the United States of America.
  7. (2020-01-10). "Compensating for over-production inhibition of the Hsmar1 transposon in ''Escherichia coli'' using a series of constitutive promoters". Mobile DNA.
  8. (June 2007). "The ancient mariner sails again: transposition of the human Hsmar1 element by a reconstructed transposase and activities of the SETMAR protein on transposon ends". Molecular and Cellular Biology.
  9. (February 2007). "The human SETMAR protein preserves most of the activities of the ancestral Hsmar1 transposase". Molecular and Cellular Biology.
  10. (January 2019). "Human SETMAR is a DNA sequence-specific histone-methylase with a broad effect on the transcriptome". Nucleic Acids Research.
  11. (May 2021). "Two repeated motifs enriched within some enhancers and origins of replication are bound by SETMAR isoforms in human colon cells". Genomics.
  12. (2021-01-01). "Genome-wide mapping of binding sites of the transposase-derived SETMAR protein in the human genome". Computational and Structural Biotechnology Journal.
  13. (May 2022). "Structural and genome-wide analyses suggest that transposon-derived protein SETMAR alters transcription and splicing". The Journal of Biological Chemistry.
  14. (August 2019). "The roles of the human SETMAR (Metnase) protein in illegitimate DNA recombination and non-homologous end joining repair". DNA Repair.
  15. (April 2008). "Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair". The Journal of Biological Chemistry.
  16. (December 2008). "The human set and transposase domain protein Metnase interacts with DNA Ligase IV and enhances the efficiency and accuracy of non-homologous end-joining". DNA Repair.
  17. (May 2011). "Biochemical characterization of metnase's endonuclease activity and its role in NHEJ repair". Biochemistry.
  18. (June 2013). "Trimming of damaged 3' overhangs of DNA double-strand breaks by the Metnase and Artemis endonucleases". DNA Repair.
  19. (April 2014). "The DDN catalytic motif is required for Metnase functions in non-homologous end joining (NHEJ) repair and replication restart". The Journal of Biological Chemistry.

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