ING2 recruits histone methyltransferase activity with methylation site specificity distinct from histone H3 lysines 4 and 9.

doi:10.1016/j.bbamcr.2008.04.019

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Article

ING2 recruits histone methyltransferase activity with methylation site specificity distinct from histone H3 lysines 4 and 9.

Biochimica et biophysica acta - 1 Oct 2008

Goeman Frauke, Otto Katja, Kyrylenko Sergiy, Schmidt Oliver, Baniahmad Aria

Abstract excerpt

p33ING2 belongs to the ING-gene family that is involved in tumor suppression, DNA repair, cell cycle regulation, and cellular senescence. Most functions are dependent on the tumor suppressor p53. p33ING2 was also shown to bind to trimethylated lysine 4 of histone H3. Here, we show that p33ING2 contains a transferable silencing function, which is independent of p53. p33ING2-mediated gene silencing is resistant to...

Topics

Animals
Cell Line
Chlorocebus aethiops
Gene Deletion
Gene Silencing
Histone Methyltransferases
Histone-Lysine N-Methyltransferase
Histones
Homeodomain Proteins
Humans
Lysine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Methylation

Mice

Mutation

Protein Methyltransferases

Receptors, Cytoplasmic and Nuclear

Substrate Specificity

Transcription, Genetic

Source

Open in PubMed

Identifiers

PMID: 18513492
DOI: 10.1016/j.bbamcr.2008.04.019

Genes

ING2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-18513492-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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