Evidence map›Paper›PMID 30329085›Full record

ArticleNucleic acids research2019

Human SETMAR is a DNA sequence-specific histone-methylase with a broad effect on the transcriptome.

Michael Tellier, Ronald Chalmers

Abstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Evolutionary innovation through fusion of sequences from across the tree of life.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. A novel transposable element-mediated mechanism causes antiviral resistance inProceedings of the National Academy of Sciences of the United States of America · 2022
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  8. Review
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  14. NONO Inhibits Lymphatic Metastasis of Bladder Cancer via Alternative Splicing of SETMAR.Molecular therapy : the journal of the American Society of Gene Therapy · 2021
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  18. Review
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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

2 authors.

Michael TellierSchool of Life Sciences, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK.
Ronald ChalmersSchool of Life Sciences, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/J014508/1
6 · The paper itself

Abstract

Transposons impart dynamism to the genomes they inhabit and their movements frequently rewire the control of nearby genes. Occasionally, their proteins are domesticated when they evolve a new function. SETMAR is a protein methylase with a sequence-specific DNA binding domain. It began to evolve about 50 million years ago when an Hsmar1 transposon integrated downstream of a SET-domain methylase gene. Here we show that the DNA-binding domain of the transposase targets the enzyme to transposon-end remnants and that this is capable of regulating gene expression, dependent on the methylase activity. When SETMAR was modestly overexpressed in human cells, almost 1500 genes changed expression by more than 2-fold (65% up- and 35% down-regulated). These genes were enriched for the KEGG Pathways in Cancer and include several transcription factors important for development and differentiation. Expression of a similar level of a methylase-deficient SETMAR changed the expression of many fewer genes, 77% of which were down-regulated with no significant enrichment of KEGG Pathways. Our data is consistent with a model in which SETMAR is part of an anthropoid primate-specific regulatory network centered on the subset of genes containing a transposon end.

Indexed as

AnimalsDNA-Binding ProteinsDNA Transposable ElementsGene Expression Regulation, NeoplasticGene Regulatory NetworksHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansMethylationNeoplasmsPrimatesSignal TransductionTranscription FactorsTranscriptomeDNA-Binding ProteinsDNA Transposable ElementsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesSETMAR protein, humanTranscription Factors

Identifiers

PMID30329085
PMCPMC6326780

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Registered trials

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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.