Histone post-translational modifications

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Organisms

Homo sapiens (127)
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Arabidopsis thaliana (10)
Caenorhabditis elegans (5)
Neurospora crassa (4)
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Mass Spectrometry (289)
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Affinity purification coupled with mass spectrometry proteomics (27)
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Illumina HiSeq 2000, Illumina HiSeq 2500 (1)
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Instrument Platform

Orbitrap Fusion Lumos (14)
Q Exactive (12)
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TripleTOF 5600 (4)
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Ultimate 3000 nano UHPLC system (ThermoFisher Scientific, USA) with a Q Exactive HF hybrid quadrupole-Orbitrap mass spectrometer (Thermo Fisher Scientific, USA), an ESI nanospray source, a higher energy collisional dissociation (HCD) fragmentation mode and data-dependent acquisition (DDA) mode for peptide sequencing. (1)
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Publication Date

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2008 (2)
2007 (1)

Metabolite Name

Thr-Pro-Arg (1)
Thr-Gly-Arg (1)
Ser-Asp-Arg (1)
Pyroglu-Asn-Arg (1)
L-valine, n-[[1-(5-fluoropentyl)-1h-indol-3-yl]carbonyl]-, methyl ester (1)
Cys-His-Arg (1)
5-methoxy-4-methyl-3-phenylcoumarin (1)
4-phenylbutan-2-ol (1)
3-quinolinecarboxamide, 1,4-dihydro-8-methoxy-4-oxo-1-pentyl-n-tricyclo[3.3.1.13,7]dec-1-yl- (1)
2-methyl-6(s)-(3-pyridyl)tetrahydro-1,2-oxazine (1)
2-furancarboxylic acid, 5-[3-[4-[2-(4-fluorophenyl)ethoxy]phenyl]propyl]- (1)
1h-indole-3-carboxylic acid, 1-(5-fluoropentyl)-, 8-quinolinyl ester (1)
[1,1':4',1''-terphenyl]-3,4'',5-triol (1)
[[4-[5r-chloro-2z-[3r-cyclohexyl-3s-hydroxy-1r-propenyl]-3s-hydroxycyclopentyl]-2r-butenyl]oxy]-acetic acid, isopropyl ester (1)
(s)-n-(1-amino-1-oxo-3-phenylpropan-2-yl)-1-pentyl-1h-indole-3-carboxamide (1)
(3as,5r,5as,8as,9ar)-5,8a-dimethyl-1-methylidene-3a,4,5,5a,6,7,9,9a-octahydroazuleno[6,7-b]furan-2,8-dione (1)
L-myo-inositol-1,4,5-triphosphate (1)
Arg-asp (1)
2-hdeahpda [dmed-fahfa] (1)
Mepirapim (1)
Tyr-His-Arg (1)
Solasodine base + 2h, 1o, o-hex-hex-hex (1)
Cyanidin 3-o-[2''-o-(xylosyl)-6''-o-(p-o-(glucosyl)-p-coumaroyl) glucoside] 5-o-glucoside (1)
Combrestatin a4 (1)
6-oxomometasone furoate (1)
(z)-2-octylpent-2-enedioic acid (1)
Cocamidoprpylbetaine (1)
Ser-Ser-Arg (1)
Glycerol trioleate (1)
.alpha.-galactosyl-n-stearoylsphingosine (1)

First Public Date

2026 (55)
2023 (49)
2024 (43)
2025 (35)
2022 (35)
2014 (35)
2021 (25)
2017 (19)
2020 (18)
2019 (16)
2016 (14)
2013 (10)
2018 (9)
2015 (8)

Classification

protozoa (5)
fungi (1)

Modification

N6 (28)
N6-dimethyl-L-lysine (12)
4x(2)H labeled dimethylated L-lysine (2)
2x(15)N labeled L-lysine (1)
4x(15)N labeled L-arginine (1)
+3amu) (1)
Not available (1)

Study type

ChIP-seq (42)
ChIP-chip by tiling array (26)
Transcription profiling by array (23)
RNA-seq of coding RNA (5)
Methylation profiling by array (4)
Proteomic profiling by array (3)
Methylation profiling by high throughput sequencing (3)
Hi-C (2)
Other (2)
GRO-seq (1)
Cell line - High-throughput sequencing (1)
Comparative genomic hybridization by array (1)
ATAC-seq (1)
DNA-seq (1)
CUT&RUN (1)
RNA-seq of total RNA (1)
RNA-seq of non coding RNA (1)

Release Date

2022 (111)
2025 (94)
2018 (87)
2021 (84)
2023 (84)
2020 (84)
2017 (73)
2016 (72)
2015 (70)
2024 (69)
2019 (66)
2014 (65)
2011 (65)
2012 (57)
2013 (46)
2010 (36)
2009 (24)
2008 (18)
2026 (12)
2007 (7)
2006 (3)
2005 (3)
2004 (2)
2002 (2)
2003 (1)
2001 (1)
2000 (1)

Lab affiliation

Departments of Chemical and Biological Engineering, Chemistry, and Molecular Biosciences, the Chemistry of Life Processes Institute, and the Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, United States (60)
European Institute of Oncology (10)
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States (9)
European Institute of Oncology, Milan (5)
ProGenTomics, Laboratory of Pharmaceutical Biotechnology, Ghent University, B-9000 Ghent, Belgium (5)
Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania (4)
Plant Physiology Group Westfälische WIlhelms-Universität Münster Germany (3)
European Institute of Oncology, Milan, Italy (3)
Division of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, China (2)
Laboratório de Biologia Molecular e Sistêmica de Tripanossomatídeos, Instituto Carlos Chagas, Fundação Oswaldo Cruz, Curitiba, Parana, Brazil (2)
Departament de Bioquímica i Biologia Molecular Universitat de Valencia (2)
Department of Experimental Oncology, IEO, Milan (2)
Affiliation of Qiutao Xu: State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Agriculture, Guangxi University, Nanning 530004, China (2)
Agronomy College, Henan Agricultural University, China (2)
Department of Laboratory Medicine and Pathology, Mayo Clinic (2)
Jiangsu Key Laboratory of Crop Genetics and Physiology/Co-Innovation Center for Modern Production Technology of Grain Crops, Key Laboratory of Plant Functional Genomics of the Ministry of Education, Yangzhou University, Yangzhou 225009, China (2)
Raymond H. Wittcoff Distinguished Professor and Head Department of Biochemistry and Molecular Biophysics Washington University School of Medicine St. Louis, MO 63110 (2)
Mendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, Brno, Czech Republic (2)
Institute of Microbiology, College of Life Sciences, Zhejiang University, Hangzhou, 310058, China (2)
EDyP (2)
Pacific Northwest National Laboratory, USA (2)
Head of the Curie Institute Mass Spectrometry Platform (2)
Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Denmark (2)
Raymond H. Wittcoff Distinguished Professor and Head Department of Biochemistry and Molecular Biophysics Washington University School of Medicine St. Louis, MO 63110 United States of America (1)
Rosalind Franklin Institute, Harwell Science and Innovation Campus, Oxford OX11 0FA, UK; Department of Pharmacology, University of Oxford, Oxford OX1 3QT, UK (1)
Mass Spectrometry Core, Van Andel Institute, Grand Rapids, MI, USA (1)
Faculty of Pharmaceutical Sciences, Department of Pharmaceutics, Laboratory of Pharmaceutical Biotechnology, Ghent University, Belgium (1)
Wellcome Centre for Cell Biology, The University of Edinburgh (1)
Institut Curie, PSL Research University, CNRS, UMR 144, 26 rue d’Ulm, F-75005, Paris, France. (1)
Dr. Richard Bartfai ; Department of Molecular Biology ; Faculty of Science ; Radboud University ; Geert Grooteplein 28 ; 6525GA Nijmegen, The Netherlands; Tel.: +31 (0)24-3610561 ; r.bartfai@science.ru.nl (1)

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Environmental Conditions Elicit a Slow but Enduring Response of Histone Post-Translational Modifications in Mozambique Tilapia

Histone post-translational modifications (PTMs) are epigenetic marks that operate within the central dogma of molecular biology: upon an environmental stimulus, the histone PTMs surrounding DNA can be changed in a way that modifies gene expression, and, therefore, the abundance and composition of RN...

ORGANISM(S): Oreochromis Mossambicus

2024-12-10 | PXD042718 | panorama

Posttranslational modification analysis of Histone H3t

Comprehensive posttranslational modifications in the testis-specific histone variant H3t protein validated in tagged knock-in mice.

ORGANISM(S): Mus Musculus (mouse)

2024-09-13 | PXD052428 | JPOST Repository

Data for: A practical guide for analysis of histone post-translational modifications by mass spectrometry: best practices and pitfalls

Histone proteomics from 5 human cell lines, discussed in publication: "A practical guide for analysis of histone post-translational modifications by mass spectrometry: best practices and pitfalls". Further explanation of data types, methods, and analysis are available in Data Explanation document in...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

MSV000084298 | MassIVE

Pathology tissue-quantitative mass spectrometry analysis to profile histone post-translational modification patterns in patient samples

Histone post-translational modifications (hPTMs) generate a complex combinatorial code that has been implicated with various pathologies, including cancer. Dissecting such a code in physiological and diseased states may be exploited for epigenetic biomarker discovery, but hPTM analysis in clinical s...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090)

2016-08-25 | MSV000080100 | MassIVE

Histone serotonylation promotes pancreatic cancer development via lipid metabolism remodeling

Neurotransmitter serotonin (5-hydroxytryptamine [5-HT]) has emerged to play parallel roles in both neurobiology and oncology. Apart from receptor-mediated signaling transduction pattern, serotonin can be covalently integrated into histone (the post-translational modification known as histone sero...

2025-06-13 | MTBLS12569 | MetaboLights

Development of a high-throughput (10 minute microflow gradient) platform for quantitation of histone modifications on a new QTOF instrument

Histone post-translational modifications (PTMs) regulate gene expression patterns through epigenetic mechanisms. The 5 histone proteins (H1, H2A, H2B, H3, and H4) are extensively modified, with over 75 distinct modification types spanning more than 200 sites. Despite strong advances in mass spectrom...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

2024-05-06 | MSV000094695 | MassIVE

Development of a high-throughput (10 minute microflow gradient) platform for quantitation of histone modifications on a new QTOF instrument

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

2024-05-06 | MSV000094696 | MassIVE

Histone post-translational modification analysis of Aspergillus strains

Chemical modifications of DNA and histone proteins impact the organization of chromatin within the nucleus. Changes in these modifications, catalyzed by different chromatin-modifying enzymes, influence chromatin organization, which in turn is thought to impact the spatial and temporal regulation of ...

ORGANISM(S): Aspergillus niger Neosartorya fumigata (Aspergillus fumigatus) Emericella nidulans (Aspergillus nidulans)

2022-06-30 | PXD033478 | Pride

Aspergillus Histone post-translational modifications

Histone post-translational modifications of Trypanosoma cruzi: a high-confidence comprehensive map

In humans and other eukaryotes, histone post-translational modifications (hPTMs) play an essential role in the epigenetic control of gene expression. In trypanosomatid parasites, conversely, gene regulation occurs mainly at the post-transcriptional level. However, our group has recently shown that h...

ORGANISM(S): Trypanosoma cruzi

2021-01-04 | PXD019104 | Pride

Post-translational modifications Trypanosoma cruzi Histone Trypanosomatids

A strategy to characterize the global histone PTM landscape within tissues of non-model organisms

Histone post-translational modifications (PTMs) are epigenetic marks that play a critical role in the expression and maintenance of DNA, but they remain largely uninvestigated in non-model organisms due to technical challenges. To begin alleviating this issue, we developed a workflow for histone PTM...

ORGANISM(S): Oreochromis Mossambicus

2024-02-29 | PXD040536 | panorama

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