ArticleThe Journal of biological chemistry2015
A Proteomic Strategy Identifies Lysine Methylation of Splicing Factor snRNP70 by the SETMAR Enzyme.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 37 citations in OpenAlex.
- αS-SETMAR: Inducing Protective Chaos in Glioblastoma?Cancers · 2026Article
- Decoding the protein methylome: Identification, validation, and functional insights.Bioorganic & medicinal chemistry · 2025Review
- Cytoskeleton remodeling induced by SMYD2 methyltransferase drives breast cancer metastasis.Cell discovery · 2024Article
- In Vivo and In Vitro Characterization of the RNA Binding Capacity of SETD1A (KMT2F).International journal of molecular sciences · 2023Article
- Structural and genome-wide analyses suggest that transposon-derived protein SETMAR alters transcription and splicing.The Journal of biological chemistry · 2022Article
- SETMAR, a case of primate co-opted genes: towards new perspectives.Mobile DNA · 2022Review
- Structure, Activity, and Function of SETMAR Protein Lysine Methyltransferase.Life (Basel, Switzerland) · 2021Review
- Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast.The Journal of biological chemistry · 2021Review
- SETMAR Shorter Isoform: A New Prognostic Factor in Glioblastoma.Frontiers in oncology · 2021Article
- The lysine demethylase KDM4A controls the cell-cycle expression of replicative canonical histone genes.Biochimica et biophysica acta. Gene regulatory mechanisms · 2020Article
- Methyltransferase-like 21C (METTL21C) methylates alanine tRNA synthetase at Lys-943 in muscle tissue.The Journal of biological chemistry · 2020Article
- Distinct roles of structure-specific endonucleases EEPD1 and Metnase in replication stress responses.NAR cancer · 2020Article
- Histone lysine methyltransferases in biology and disease.Nature structural & molecular biology · 2019Review
- Lysine Methylation Regulators Moonlighting outside the Epigenome.Molecular cell · 2019Review
- Lysine methylation signaling of non-histone proteins in the nucleus.Cellular and molecular life sciences : CMLS · 2019Review
- The roles of the human SETMAR (Metnase) protein in illegitimate DNA recombination and non-homologous end joining repair.DNA repair · 2019Article
- Human SETMAR is a DNA sequence-specific histone-methylase with a broad effect on the transcriptome.Nucleic acids research · 2019Article
- Molecular prediction of adjuvant cisplatin efficacy in Non-Small Cell Lung Cancer (NSCLC)-validation in two independent cohorts.PloS one · 2018Article
- RBM25 is a global splicing factor promoting inclusion of alternatively spliced exons and is itself regulated by lysine mono-methylation.The Journal of biological chemistry · 2017Article
- SETMAR isoforms in glioblastoma: A matter of protein stability.Oncotarget · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The lysine methyltransferase (KMT) SETMAR is implicated in the response to and repair of DNA damage, but its molecular function is not clear. SETMAR has been associated with dimethylation of histone H3 lysine 36 (H3K36) at sites of DNA damage. However, SETMAR does not methylate H3K36 in vitro. This and the observation that SETMAR is not active on nucleosomes suggest that H3K36 methylation is not a physiologically relevant activity. To identify potential non-histone substrates, we utilized a strategy on the basis of quantitative proteomic analysis of methylated lysine. Our approach identified lysine 130 of the mRNA splicing factor snRNP70 as a SETMAR substrate in vitro, and we show that the enzyme primarily generates monomethylation at this position. Furthermore, we show that SETMAR methylates snRNP70 Lys-130 in cells. Because snRNP70 is a key early regulator of 5' splice site selection, our results suggest a model in which methylation of snRNP70 by SETMAR regulates constitutive and/or alternative splicing. In addition, the proteomic strategy described here is broadly applicable and is a promising route for large-scale mapping of KMT substrates.
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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.