post translational modifications

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Organisms

Homo sapiens (230)
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synthetic construct (3)
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Technology Type

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Instrument Platform

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UNIPROT ID/AC

Q6A4J8 (2)
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P21583 (1)
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Q04864 (1)
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Q9H0F6 (1)
Q96EP0 (1)

ENSEMBL ID

ENSG00000170477 (171)
ENSG00000229353 (122)
ENSG00000147251 (120)
ENSG00000204131 (81)
ENSG00000247315 (81)
ENSG00000176092 (36)
ENSG00000003402 (1)
ENSG00000171791 (1)
ENST00000333681.5 (1)
ENSSSCT00065044848.1 (1)
ENST00000371199.8 (1)
ENST00000612899.5 (1)
ENSG00000101966 (1)
ENST00000216797.10 (1)
ENSG00000100906 (1)
ENSG00000118503 (1)

CHEBI ID

CHEBI:30769 (4)
CHEBI:28044 (3)
CHEBI:38264 (2)
CHEBI:17822 (2)
CHEBI:25094 (2)
CHEBI:22660 (2)
CHEBI:18186 (2)
CHEBI:28300 (2)
CHEBI:17361 (2)
CHEBI:25017 (2)
CHEBI:16958 (2)
CHEBI:15741 (2)
CHEBI:16335 (2)
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CHEBI:16449 (2)
CHEBI:29016 (2)
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CHEBI:32816 (2)
CHEBI:16027 (2)
CHEBI:30915 (2)
CHEBI:33697 (1)
CHEBI:36080 (1)
CHEBI:39026 (1)
CHEBI:144347 (1)
CHEBI:144346 (1)
CHEBI:144345 (1)
CHEBI:144344 (1)
CHEBI:144342 (1)
CHEBI:144322 (1)

Metabolite Name

Arginine (4)
Alanine (4)
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Pro-val (2)
Flumethasone pivalate (2)
His-Ser (2)
Leu-Gln (2)
Ile-Asn (2)
1-stearoyl-rac-glycerol (2)
His-Leu (2)
Dephospho-CoA (2)
Primaquine (2)
Vardenafil (2)
Acetoacetic acid (2)
Melezitose (2)
Forskolin (2)
Arg-Thr (2)
Ser-Arg (2)
Phenylacetaldehyde (2)
Val-Lys (2)
Val-Glu (2)

First Public Date

2026 (105)
2024 (91)
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2014 (64)
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2017 (28)
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2016 (17)
2018 (16)
2015 (10)

Modelling Approach

Ordinary differential equation model (5)
Petri net (1)
Other (1)
Differential equation model (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)
Department of Neurobiology, Boston Children's Hospital, Harvard Medical School, Boston, MA, USA (11)
Institute for Research in Immunology and Cancer, Department of Biochemistry, Department of Chemistry, Université de Montréal, Québec, Canada H3T 1J4 (11)
Whitehead Institute for Biomedical Research and Massachusetts Institute of Technology (10)
European Institute of Oncology (10)
University of Washington (10)
Centre for Proteome Research, University of Liverpool, Liverpool, UK (9)
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States (9)
Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark (8)
Department of Cellular & Molecular Physiology, Yale School of Medicine, New Haven, CT 06520, USA. Systems Biology Institute, Yale University, New Haven, CT 06516, USA (7)
EDyP (7)
BioArCh, University of York, UK (6)
Whitehead Institute and MIT (5)
European Institute of Oncology, Milan (5)
Department of Molecular and Cellular Neurobiology, Center for Neurogenomics & Cognitive Research, Neuroscience Campus Amsterdam, VU University, Amsterdam, The Netherlands (5)
ProGenTomics, Laboratory of Pharmaceutical Biotechnology, Ghent University, B-9000 Ghent, Belgium (5)
Key Lab of Integrated Crop Pest Management of Shandong, College of Plant Health and Medicine, Qingdao Agricultural University, Qingdao, China (5)
Tokyo Metropolitan Institute of Medical Science (4)
Agronomy College, Henan Agricultural University, China (4)
Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark (4)
Institute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Bâtiment 23A, 1 avenue de la Terrasse, F-91198 Gif-sur-Yvette cedex, France. (4)
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 USA (4)
Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania (4)
Carnegie Mass Spectrometry Facility (4)
School of Pharmacy, University of Wisconsin-Madison (4)
Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia (4)
Proteomics Core Facility and Research Group Proteomics, CEITEC-MU, Masaryk University, Brno, Czech Republic (4)
Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Denmark (4)
Gansu Provincial Key Lab of Aridland Crop Science/ Gansu Agricultural University, Lanzhou, China (3)
Division of Cell Matrix Biology & Regenerative Medicine (L5) / Division of Cell Matrix Biology & Regenerative Medicine, University of Manchester (3)

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Model Flag

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Classification

protozoa (10)
viruses (5)
bacteria (2)
fungi (1)

Modification

N6 (32)
N6-dimethyl-L-lysine (14)
4-tetrahydrothiazine-3-carboxylic acid (6)
2x(15)N labeled L-lysine (4)
4x(15)N labeled L-arginine (4)
Not available (3)
4x(2)H labeled dimethylated L-lysine (2)
+3amu) (2)
45.029395 (1)
56.026215 (1)
4'-dihydroxyphenylalanine (1)
4x(2)H labeled dimethylated residue (1)
42.010565 (1)
15.994915 (1)
58.005479 (1)
4 (1)

Study type

Transcription profiling by array (64)
ChIP-seq (51)
ChIP-chip by tiling array (26)
RNA-seq of coding RNA (18)
RNA-seq of non coding RNA (6)
Methylation profiling by array (4)
Proteomic profiling by array (4)
Other (3)
Methylation profiling by high throughput sequencing (3)
Cell line - High-throughput sequencing (2)
Hi-C (2)
DNA-seq (2)
GRO-seq (1)
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Animal - High-throughput sequencing (1)
Comparative genomic hybridization by array (1)
ATAC-seq (1)
CUT&RUN (1)
RNA-seq of coding RNA from single cells (1)
RNA-seq of total RNA (1)

Release Date

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2017 (325)
2016 (309)
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2014 (268)
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2005 (10)
2004 (7)
2001 (6)
2003 (5)
2002 (2)
2000 (2)
1997 (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

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

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

Translational repression of viral RNA mediates arbovirus persistence in mosquitoes

Persistent infection of mosquito vectors is essential for the transmission of arboviruses, yet how these viruses produce sufficient progeny without compromising host cell fitness remains unclear. Arbovirus genomes exhibit suboptimal codon usage for both human and mosquito hosts, raising questions...

2026-02-12 | MTBLS12760 | MetaboLights

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

Integrated proteomic analysis of post-translational modifications by serial enrichment.

Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA. Nat Methods 2013, 10, 634-7. doi: 10.1038/nmeth.2518.

2013-12-10 | MSV000078509 | MassIVE

Linking post-translational modifications and protein turnover by site-resolved protein turnover (SPOT) profiling

Proteome-wide measurements of protein turnover have largely ignored the impact of post-translational modifications (PTMs). To address this gap, we employ stable isotope labelling and mass spectrometry to measure the turnover of >120,000 peptidoforms including >33,000 phosphorylated, acetylated, and ...

ORGANISM(S): Homo Sapiens

2022-03-14 | PXD023234 | panorama

Peptide collision cross section of 22 post-translational modifications

The present study investigates the ion mobility characteristics of synthetic peptides carrying 22 different post-translational modifications by Ion Mobility-Mass Spectrometry. Samples were kindly provided by the ProteomeTools project.

ORGANISM(S): Homo sapiens (Human)

2023-08-25 | PXD042416 | Pride

The NAE1-mediated Neddylation operates as an essential post-translational modification checkpoint for effector CD8+ T cells

Cells were lysed with TFA, and precipitated with cold acetone. The precipitates were transferred to E3filters and digestion was performed overnight with trypsin. The peptides were desalted with StageTips, and were analyzed on Eclipse Orbitrap with DIA mode. For MS1, the resolution was set to 120,00...

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

2024-02-27 | MSV000094179 | MassIVE

Systematic characterization of 21 post-translational modification using synthetic peptides

The data presented in this study in the - context of the ProteoemTools project - is based on the synthesis of about 5000 synthetic peptides carrying 21 different post-translational modifications to systematically characterize their chromatographic and mass spectrometric properties using multimodal L...

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

2023-04-05 | MSV000091649 | MassIVE

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