Histone posttranslational modification

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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)
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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)
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Mepirapim (1)
Tyr-His-Arg (1)
Solasodine base + 2h, 1o, o-hex-hex-hex (1)
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(z)-2-octylpent-2-enedioic acid (1)
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Ser-Ser-Arg (1)
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.alpha.-galactosyl-n-stearoylsphingosine (1)

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Modelling Approach

Differential equation model (1)

Modification

N6 (2)
3x(2)H labeled N6-acetyl-L-lysine (1)
N6-dimethyl-L-lysine (1)

Study type

ChIP-chip by tiling array (25)
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2011 (38)
2012 (31)
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Lab affiliation

Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania (4)
Department of Biology – Cellular Proteostasis and Mass Spectrometry, University of Konstanz (3)
Division of Gastroenterology and Hepatology; Shanghai Institute of Digestive Disease; NHC Key Laboratory of Digestive Diseases; State Key Laboratory for Oncogenes and Related Genes; Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 200001, China (2)
ProGenTomics, Laboratory of Pharmaceutical Biotechnology, Ghent University, B-9000 Ghent, Belgium (2)
Key Laboratory of Animal Infectious Diseases in Northeast China, Ministry of Education; Key Laboratory of Zoonosis, Shenyang Agricultural University, 120 Dongling Road, Shenyang 110166, China. (1)
CEITEC Masaryk University (1)
Core Unit Proteomics, Berlin Institute of Health at Charite - Universitaetsmedizin Berlin and Max-Delbrueck-Center for Molecular Medicine, Berlin, Germany (1)
Hainan Normal University (1)
College of Agronomy, Shandong Agricultural University, Tai’an, China (1)
1 Population Health and Immunity Division, The Walter and Eliza Hall Institute of Medical Research, Melbourne, VIC, Australia Department of Veterinary Biosciences, Melbourne Veterinary School, Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, VIC, Australia (1)
National Laboratory of Biosciences (LNBio/CNPEM) (1)
Laboratory of Protein Mass Spectrometry, Faculty of Biotechnology, University of Wroclaw, Poland (1)
Institute of Molecular Biology (IMB), Germany (1)
Shohei Koide Professor and Chair, Department of Biochemistry and Biophysics Box 712, Rm 3-6710 University of Rochester Medical Center 601 Elmwood Ave Rochester, NY 14642 (1)
1 Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic 2 Faculty of Science, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic (1)
Functional Proteo-Metabolomics Department of Biochemistry University of Innsbruck Austria (1)
Quantitative Proteomics Ackermannweg 4 55122 Mainz Germany (1)
Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China (1)
Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA Arkansas Children’s Research Institute, 13 Children’s Way, Little Rock, AR 72202, USA (1)
Department of Peptide-based Immunotherapy, University and University Hospital Tübingen, Tübingen, Germany (lab head) (1)
Mount Sinai School of Medicine (1)
Laboratório de Pesquisa em Apicomplexa - Instituto Carlos Chagas – FIOCRUZ/PR. (1)
Department of Orthopedics, The Fourth Medical Centre, Chinese PLA General Hospital, Beijing, China National Clinical Research Center for Orthopedics, Sports Medicine & Rehabilitation, Beijing, China (1)
Biomedical Center Munich Molecular Biology Großhaderner Strasse 9 82152 Planegg-Martinsried (1)
Peking University School of Stomatology (1)
University of Minnesota at Twin Cities (1)
Protein Analysis Unit ZfP LMU Munich BioMedical Center Grosshaderner Strasse 9 82152 Planegg-Martinsried Tel. +49 89 2180 71804 (1)
Department of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, Zhejiang, China (1)
Department of Biochemistry and Molecular Biology University of Arkansas for Medical Sciences USA (1)
Dr. rer. nat. Birgit Knebel Institute for Clinical Biochemistry and Pathobiochemistry German Diabetes Center (DDZ) Leibniz Center for Diabetes Research at Heinrich Heine University Düsseldorf Auf´m Hennekamp 65 40225 Düsseldorf, Germany (1)

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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

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

Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification

We report the identification of 67 previously undescribed histone modifications, increasing the current number of known histone marks by about 70%. We further investigated one of the marks, lysine crotonylation (Kcr), confirming that it represents an evolutionarily-conserved histone posttranslationa...

ORGANISM(S): Mus musculus

2011-10-06 | E-GEOD-32663 | biostudies-arrayexpress

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

5HT - Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3

we provide evidence for a new class of histone posttranslational modification (PTM): serotonylation.

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

2023-12-04 | MSV000093567 | MassIVE

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

H3K36ac is an evolutionary conserved histone modification that marks active genes in plants

In eukaryotic cells, DNA is tightly packed in the nucleus in chromatin which has histones as its main protein component. Histones are subject to a large number of distinct post-translational modifications, whose sequential or combinatorial action affects genome function. Here, we report the identifi...

ORGANISM(S): Arabidopsis thaliana

2016-04-05 | E-GEOD-74841 | biostudies-arrayexpress

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

Nitric oxide regulates gene expression in cancers by controlling histone posttranslational modifications [HiSeq 2000]

Dynamic changes in histone posttranslational modifications (PTMs) are important regulators of chromatin structure and gene transcription in both normal and disease settings. Herein, we describe a novel signaling mechanism of nitric oxide (â€¢NO) by demonstrating its ability to modulate gene expressi...

ORGANISM(S): Homo sapiens

2015-11-05 | E-GEOD-66318 | biostudies-arrayexpress

Distribution of active (H3K4me1, H3K4me3, H3K27ac) and inactive (H3K9me3, H3K27me3) histone PTMs in WT and HIRA KO HeLa cells

We profiled the enrichment of active (H3K4me1, H3K4me3, H3K27ac) and inactive (H3K9me3, H3K27me3) histone PTMs in cells that are wild-type (WT) or knock-out (KO) for the H3.3-specific chaperone HIRA. We performed native ChIP-seq following MNase digestion to isolate nucleosomes in H3.1-SNAP and H3.3-...

ORGANISM(S): Homo sapiens

2025-08-07 | E-MTAB-14416 | biostudies-arrayexpress

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