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Article

Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate.

Communications biology - 16 Sept 2020

Schuhmacher Maren Kirstin, Beldar Serap, Khella Mina S, Bröhm Alexander, Ludwig Jan, Tempel Wolfram, Weirich Sara, Min Jinrong, Jeltsch Albert

Abstract excerpt

SETD2 catalyzes methylation at lysine 36 of histone H3 and it has many disease connections. We investigated the substrate sequence specificity of SETD2 and identified nine additional peptide and one protein (FBN1) substrates. Our data showed that SETD2 strongly prefers amino acids different from those in the H3K36 sequence at several positions of its specificity profile. Based on this, we designed an optimized...

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Share to Amino Acid Sequence
Share to Histone-Lysine N-Methyltransferase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Processing, Post-Translational

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Source

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Identifiers

PMID: 32939018
DOI: 10.1038/s42003-020-01223-6
PMCID: PMC7495481

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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