posttranslational modifications

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Unknown (2171)
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Organisms

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Nothobranchius furzeri (1)

Organisms

Homo sapiens (46)
Mus musculus (42)
Drosophila melanogaster (6)
Arabidopsis thaliana (6)
Xenopus laevis (3)
Rattus norvegicus (3)
Petromyzon marinus (2)
Caenorhabditis elegans (2)
Danio rerio (2)
synthetic construct (2)
Listeria monocytogenes 10403S (1)
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Cryptococcus neoformans (1)
Nothobranchius furzeri (1)
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Repository

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Technology Type

Mass Spectrometry (330)
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Illumina HiSeq 2000, Illumina HiSeq 2500 (1)
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Proteogenomics (1)

Instrument Platform

Q Exactive (46)
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LTQ Orbitrap (8)
TripleTOF 5600 (8)
Illumina NovaSeq 6000 (7)
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TripleTOF 6600 (4)
Instrument (3)
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Ion Torrent Proton (1)

Publication Date

2024 (108)
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2019 (59)
2017 (44)
2020 (42)
2015 (41)
2011 (39)
2018 (36)
2026 (34)
2016 (28)
2012 (28)
2013 (21)
2010 (9)
2008 (8)
2007 (2)
2009 (1)
2006 (1)

UNIPROT ID/AC

14331_ORYSJ (1)
14332_ORYSJ (1)
14333_ORYSJ (1)
14334_ORYSJ (1)
14335_ORYSJ (1)
14336_ORYSJ (1)
2ABA_ORYSJ (1)
3HAO_YEAST (1)
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40G2_ORYSJ (1)
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4CL4_ORYSJ (1)
4CLL1_ORYSJ (1)
4CLL4_ORYSJ (1)
4CLL5_ORYSJ (1)
5811.TGME49_004050 (1)
5811.TGME49_005250 (1)
5811.TGME49_027920 (1)
5811.TGME49_044150 (1)
5811.TGME49_054560 (1)
5811.TGME49_094800 (1)
5811.TGME49_102050 (1)
5811.TGME49_119870 (1)
5811.TGME49_119920 (1)
6PGD1_ORYSJ (1)
6PGD1_YEAST (1)
6PGD2_ORYSJ (1)
6PGL2_ORYSJ (1)
6PGL3_ORYSJ (1)

ENSEMBL ID

ENSG00000170477 (53)
ENSG00000229353 (26)
ENSG00000147251 (25)
ENSG00000247315 (14)
ENSG00000204131 (6)
ENSG00000176092 (2)

CHEBI ID

CHEBI:17822 (2)
CHEBI:25094 (2)
CHEBI:18186 (2)
CHEBI:16958 (2)
CHEBI:28044 (2)
CHEBI:27266 (2)
CHEBI:7916 (2)
CHEBI:30769 (2)
CHEBI:39026 (1)
CHEBI:144347 (1)
CHEBI:144346 (1)
CHEBI:144345 (1)
CHEBI:144344 (1)
CHEBI:144342 (1)
CHEBI:144322 (1)
CHEBI:144341 (1)
CHEBI:144340 (1)
CHEBI:144338 (1)
CHEBI:23623 (1)
CHEBI:144337 (1)
CHEBI:144336 (1)
CHEBI:144335 (1)
CHEBI:144333 (1)
CHEBI:144332 (1)
CHEBI:144331 (1)
CHEBI:144329 (1)
CHEBI:144320 (1)
CHEBI:144328 (1)
CHEBI:144327 (1)
CHEBI:144326 (1)

Metabolite Name

1-stearoyl-rac-glycerol (2)
Arginine (2)
Glutamine (2)
Creatinine (2)
Creatine (2)
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)
Low-density lipoprotein (1)
Very-low-density lipoprotein (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)

First Public Date

2014 (19)
2024 (17)
2026 (15)
2025 (15)
2019 (14)
2023 (10)
2022 (10)
2013 (10)
2015 (9)
2017 (6)
2018 (5)
2020 (4)
2016 (4)
2021 (3)

Modelling Approach

Differential equation model (1)

Lab affiliation

IRIC-Université de Montréal (8)
Leibniz Institute on Aging – Fritz Lipmann Institute (FLI), 07745 Jena, Germany (5)
MDC (5)
Cellular Proteomics, Helmholtz Centre for Infection Research, Braunschweig, Germany (4)
Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania (4)
Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, Switzerland Faculty of Science, University of Zurich, Zurich, Switzerland (4)
Department of Biology – Cellular Proteostasis and Mass Spectrometry, University of Konstanz (3)
The Forsyth Institute (3)
Université de Montréal (3)
Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, 100191, China. (2)
Centre for Developmental Neurobiology, King's College London (2)
Copenhagen Center for Glycomics and Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen N, Denmark (2)
Cornell University (2)
Department of Biology, University of Konstanz, Universitaetsstrasse 10, 78457 Konstanz (2)
Department of Chemistry and Chemical Biology, Harvard University (2)
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 65 Stockholm, Sweden (2)
Department of Molecular Biology, Princeton University (2)
Dept. of Biochemistry & Molecular Biology, Complex Carbohydrate Research Center, Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, Dept. of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104 USA (2)
Institute of Dendrology Polish Academy of Sciences, Parkowa 5, 62-035 Kórnik, Poland (2)
Max Delbruck Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13092 Berlin, Germany (2)
Natural History Museum of Denmark University of Copenhagen, Øster Voldgade 5–7, 1350 Copenhagen, Denmark (2)
Ottawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada (2)
Ph.D., Professor, Vice Dean (2)
ProGenTomics, Laboratory of Pharmaceutical Biotechnology, Ghent University, B-9000 Ghent, Belgium (2)
Proteomics Core Facility and Research Group Proteomics, CEITEC-MU, Masaryk University, Brno, Czech Republic (2)
Shanghai Institute of Materia Medica (2)
University of Cologne, Germany (2)
University of East Anglia/John Innes Centre, Norwich, UK (2)
University of Wisconsin-Madison, Department of Chemistry (2)
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)

IsPrivate

False (1)

Classification

fungi (3)
bacteria (1)

Modification

N6 (4)
-17.026549 (1)
15.994915 (1)
3x(2)H labeled N6-acetyl-L-lysine (1)
4 (1)
4-tetrahydrothiazine-3-carboxylic acid (1)
42.010565 (1)
56.026215 (1)
58.005479 (1)
59.036279 (1)
N6-dimethyl-L-lysine (1)
Not available (1)

Study type

Transcription profiling by array (38)
ChIP-chip by tiling array (24)
ChIP-seq (20)
RNA-seq of coding RNA (12)
Methylation profiling by array (6)
Methylation profiling by high throughput sequencing (5)
Proteomic profiling by array (4)
Hi-C (2)
Other (2)
RNA-seq of non coding RNA (2)
GRO-seq (1)
Unknown experiment type (1)
Cell line - One-color microarray (1)
ChIP-chip by array (1)
Comparative genomic hybridization by array (1)
ATAC-seq (1)
DNA-seq (1)
CUT&RUN (1)
RNA-seq of total RNA (1)

Release Date

2021 (227)
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2016 (127)
2014 (123)
2015 (122)
2024 (120)
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2018 (113)
2012 (93)
2013 (81)
2010 (65)
2008 (49)
2009 (41)
2007 (30)
2006 (24)
2026 (19)
2005 (10)
2004 (10)
2003 (7)
2002 (5)
1999 (5)
2000 (3)
2001 (2)
1998 (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

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

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

Fine mapping of posttranslational modifications of the linker histone H1 from Drosophila melanogaster.

Not available

S-EPMC2212714 | biostudies-literature

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

Impact of posttranslational modifications on atomistic structure of fibrinogen.

Not available

S-EPMC6988951 | biostudies-literature

Posttranslational Modifications of RAS Proteins.

Not available

S-EPMC6035883 | biostudies-literature

Posttranslational modification of ABCG2-Q141K

The analysis of posttranslational modification of Q141K of ABCG2 protein

ORGANISM(S): Homo Sapiens (human)

2022-12-19 | PXD030512 | JPOST Repository