Evidence map›Paper›PMID 27798683›Full record

ArticlePloS one2016

Ubiquitination of Lysine 867 of the Human SETDB1 Protein Upregulates Its Histone H3 Lysine 9 (H3K9) Methyltransferase Activity.

Kenji Ishimoto, Natsuko Kawamata, Yoshie Uchihara, Moeka Okubo, Reiko Fujimoto, Eiko Gotoh, Keisuke Kakinouchi, Eiichi Mizohata, Nobumasa Hino, Yoshiaki Okada and 8 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. The Many Faces of SetDB1.Epigenomes · 2026
    Review
  2. Review
  3. Review
  4. Clr4Nature communications · 2024
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Targets of histone H3 lysine 9 methyltransferases.Frontiers in cell and developmental biology · 2022
    Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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

18 authors at 2 institutions in 1 country.

Kenji IshimotoLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Natsuko KawamataLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Yoshie UchiharaLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Moeka OkuboLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Reiko FujimotoLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Eiko GotohLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Keisuke KakinouchiDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
Eiichi MizohataDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
Nobumasa HinoLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Yoshiaki OkadaLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Yasuhiro MochizukiDepartment of Quantitative Biology and Medicine, Research Center for Advanced Science and Technology, The University of Tokyo, Meguro, Tokyo, Japan.
Toshiya TanakaLaboratory for System Biology and Medicine, Research Center for Advanced Science and Technology, The University of Tokyo, Meguro, Tokyo, Japan.
Takao HamakuboDepartment of Quantitative Biology and Medicine, Research Center for Advanced Science and Technology, The University of Tokyo, Meguro, Tokyo, Japan.
Juro SakaiDivision of Metabolic Medicine, Research Center for Advanced Science and Technology, The University of Tokyo, Meguro, Tokyo, Japan.
Tatsuhiko KodamaLaboratory for System Biology and Medicine, Research Center for Advanced Science and Technology, The University of Tokyo, Meguro, Tokyo, Japan.
Tsuyoshi InoueDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
Keisuke TachibanaLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Takefumi DoiLaboratory of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Osaka University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Posttranslational modifications (PTMs) of proteins play a crucial role in regulating protein-protein interactions, enzyme activity, subcellular localization, and stability of the protein. SET domain, bifurcated 1 (SETDB1) is a histone methyltransferase that regulates the methylation of histone H3 on lysine 9 (H3K9), gene silencing, and transcriptional repression. The C-terminal region of SETDB1 is a key site for PTMs, and is essential for its enzyme activity in mammalian and insect cells. In this study, we aimed to evaluate more precisely the effect of PTMs on the H3K9 methyltransferase activity of SETDB1. Using mass spectrometry analysis, we show that the C-terminal region of human SETDB1 purified from insect cells is ubiquitinated. We also demonstrate that the ubiquitination of lysine 867 of the human SETDB1 is necessary for full H3K9 methyltransferase activity in mammalian cells. Finally, we show that SETDB1 ubiquitination regulates the expression of its target gene, serpin peptidase inhibitor, clade E, member 1 (SERPINE1) by methylating H3K9. These results suggest that the ubiquitination of SETDB1 at lysine 867 controls the expression of its target gene by activating its H3K9 methyltransferase activity.

Indexed as

AnimalsCell LineEnzyme ActivationGene Expression RegulationHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansLysineModels, BiologicalProtein BindingProtein Interaction Domains and MotifsProtein MethyltransferasesUbiquitinationHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesLysineProtein MethyltransferasesSETDB1 protein, human

Identifiers

PMID27798683
PMCPMC5087952
OpenAlexW2542012027

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.