Automethylation of G9a and its implication in wider substrate specificity and HP1 binding.

doi:10.1093/nar/gkm726

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Article

Automethylation of G9a and its implication in wider substrate specificity and HP1 binding.

Nucleic acids research - 1 Jan 2007

Chin Hang Gyeong, Estève Pierre-Olivier, Pradhan Mihika, Benner Jack, Patnaik Debasis, Carey Michael F, Pradhan Sriharsa

Abstract excerpt

Methylation of lysine residues on histones participates in transcriptional gene regulation. Lysine 9 methylation of histone H3 is a transcriptional repression signal, mediated by a family of SET domain containing AdoMet-dependent enzymes. G9a methyltransferase is a euchromatic histone H3 lysine 9 methyltransferase. Here, G9a is shown to methylate other cellular proteins, apart from histone H3, including...

Topics

Amino Acid Motifs
Amino Acid Sequence
Animals
COS Cells
Cell Line
Chlorocebus aethiops
Chromobox Protein Homolog 5
Chromosomal Proteins, Non-Histone
Histone-Lysine N-Methyltransferase
Lysine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mass Spectrometry

Methylation

Mice

Molecular Sequence Data

Mutation

Protein Processing, Post-Translational

Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 17962312
DOI: 10.1093/nar/gkm726
PMCID: PMC2175347

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-17962312-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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