Evidence map›Paper›PMID 17130240›Full record

ArticleMolecular and cellular biology2007

The human SETMAR protein preserves most of the activities of the ancestral Hsmar1 transposase.

Danxu Liu, Julien Bischerour, Azeem Siddique, Nicolas Buisine, Yves Bigot, Ronald Chalmers

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

72 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. ThebioRxiv : the preprint server for biology · 2025
    Article
  3. A novel transposable element-mediated mechanism causes antiviral resistance inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Evolution ofMobile DNA · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Transposable elements in cancer.Nature reviews. Cancer · 2017
    Review
  18. Article
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Danxu LiuUniversity of Oxford, Department of Biochemistry, South Parks Road, Oxford OX1 3QU, United Kingdom.
Julien Bischerour
Azeem Siddique
Nicolas Buisine
Yves Bigot
Ronald Chalmers
University of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Transposons have contributed protein coding sequences to a unexpectedly large number of human genes. Except for the V(D)J recombinase and telomerase, all remain of unknown function. Here we investigate the activity of the human SETMAR protein, a highly expressed fusion between a histone H3 methylase and a mariner family transposase. Although SETMAR has demonstrated methylase activity and a DNA repair phenotype, its mode of action and the role of the transposase domain remain obscure. As a starting point to address this problem, we have dissected the activity of the transposase domain in the context of the full-length protein and the isolated transposase domain. Complete transposition of an engineered Hsmar1 transposon by the transposase domain was detected, although the extent of the reaction was limited by a severe defect for cleavage at the 3' ends of the element. Despite this problem, SETMAR retains robust activity for the other stages of the Hsmar1 transposition reaction, namely, site-specific DNA binding to the transposon ends, assembly of a paired-ends complex, cleavage of the 5' end of the element in Mn(2+), and integration at a TA dinucleotide target site. SETMAR is unlikely to catalyze transposition in the human genome, although the nicking activity may have a role in the DNA repair phenotype. The key activity for the mariner domain is therefore the robust DNA-binding and looping activity which has a high potential for targeting the histone methylase domain to the many thousands of specific binding sites in the human genome provided by copies of the Hsmar1 transposon.

Indexed as

Amino Acid SequenceBase SequenceDNA Transposable ElementsExonsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHumansMethyltransferasesMolecular Sequence DataProtein MethyltransferasesProtein Structure, TertiaryDNA Transposable ElementsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesMethyltransferasesProtein MethyltransferasesSETMAR protein, human

Identifiers

PMID17130240
PMCPMC1800679
OpenAlexW1990700106

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.