Pp2a - OmicsDI

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Homo sapiens (76)
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unidentified (2)
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Technology Type

Mass Spectrometry (133)
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Illumina HiSeq 2500 (1)
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SWATH MS (1)
SRM/MRM (1)
Top-down proteomics (1)

Instrument Platform

Q Exactive Plus (13)
Orbitrap Fusion Lumos (11)
Orbitrap Fusion (8)
Illumina NovaSeq 6000 (6)
LTQ Orbitrap Velos (3)
Enriched phosphopeptides were loaded onto a 50 cm EN C18 PepMap column with elution over a 1 h acquisition driven by a Waters mClass nanoUPLC. Eluted peptides were measured using a Thermo Orbitrap Fusion Tribrid mass spectrometer, with MS spectra acquired in the Orbitrap and MS2 spectra acquired in parallel, following HCD fragmentation, in the linear ion trap. (2)
Q Exactive (2)
Liquid Chromatography MS - positive - hilic (2)
Applied Biosystems 1700 Chemiluminescent Microarray Analyzer (1)
Illumina HiSeq X (1)
NextSeq 550 (1)
NextSeq 500 (1)
Orbitrap eclipse w/FAIMS (1)
LTQ (1)
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Orbitrap Eclipse (1)
Liquid Chromatography MS - negative - reverse phase (1)
Liquid Chromatography MS - positive - reverse phase (1)
Liquid Chromatography MS - negative - hilic (1)

Publication Date

2024 (71)
2023 (57)
2025 (46)
2005 (41)
2026 (36)
2021 (33)
2020 (31)
2022 (30)
2012 (27)
2015 (20)
2016 (17)
2010 (17)
2019 (17)
2018 (15)
2017 (14)
2013 (14)
2014 (12)
2009 (11)
2011 (8)
2007 (3)
2008 (2)
2006 (2)
2004 (1)
2003 (1)

UNIPROT ID/AC

P04049 (5)
Q02750 (5)
P61225 (4)
P51452 (4)
P27361 (4)
P05132 (3)
Q3U214 (3)
Q99PS2 (2)
Q03114 (2)
Q00362 (2)
Q9UD71 (2)
P32562 (2)
P38987 (2)
P40316 (2)
P47035 (2)
Q03018 (2)
P53197 (2)
P26309 (2)
P27636 (2)
Q00684 (2)
P24869 (2)
O95996 (1)
Q5TA35 (1)
P01097 (1)
O15169 (1)
P30086 (1)
Q9UJU2 (1)
P35222 (1)
P49841 (1)
P00546 (1)

CHEBI ID

CHEBI:28842 (3)
CHEBI:17295 (3)
CHEBI:15354 (3)
CHEBI:15756 (3)
CHEBI:17596 (3)
CHEBI:17368 (3)
CHEBI:16347 (3)
CHEBI:17489 (2)
CHEBI:29108 (2)
CHEBI:16027 (2)
CHEBI:5298 (2)
CHEBI:9658 (2)
CHEBI:28934 (2)
CHEBI:72844 (2)
CHEBI:31169 (2)
CHEBI:145255 (2)
CHEBI:9629 (2)
CHEBI:59265 (2)
CHEBI:36005 (2)
CHEBI:64575 (2)
CHEBI:64565 (2)
CHEBI:64549 (2)
CHEBI:64566 (2)
CHEBI:64560 (2)
CHEBI:42504 (2)
CHEBI:28177 (2)
CHEBI:34494 (2)
CHEBI:16828 (2)
CHEBI:28716 (2)
CHEBI:33704 (1)

Metabolite Name

Stearic acid (3)
Palmitoleic Acid (2)
15-OxoEDE (2)
Oleamide (2)
L-Tryptophan (2)
Hypoxanthine (2)
Choline (2)
Cytidine (2)
3-amino-2,6-diphenyl-4,7-dihydro-2H-pyrazolo[3,4-d]pyrimidin-4-one (1)
N1-[2-(2-pyridyl)ethyl]-2-aminobenzamide (1)
8(9)-EET Ethanolamide (1)
1-hydroxy-1-(4-methoxyphenyl)propan-2-yl 4-methoxybenzoate (1)
¦Á-Hydroxymidazolam (1)
Ethyl 5-hydroxy-4-oxo-4H-chromene-2-carboxylate (1)
Sparteine (1)
-Aspartylphenylalanine (1)
Delta-Tocopherol (1)
Hydroxymethylglutaric acid (1)
2,3-Dihydroxybiphenyl (1)
Raspberry ketone (1)
Bonactin (1)
3-HYDROXYBUTANOIC ACID (1)
Acetyl phosphate (1)
Uracil 1-beta-D-arabinofuranoside (1)
5-hydroxy-2-phenyl-4H-chromen-4-one (1)
7-methylpyrimido[4,5-d]pyrimidin-4-amine (1)
2-(3,4-dihydroxyphenyl)-3,5,7-trihydroxy-6-methyl-4H-chromen-4-one (1)
Cis-Resveratrol (1)
3-methoxy-2-phenyl-4H-furo[2,3-h]chromen-4-one (1)
IMH (1)

First Public Date

2023 (37)
2024 (28)
2025 (24)
2026 (21)
2014 (21)
2021 (15)
2022 (13)
2019 (10)
2018 (9)
2020 (8)
2016 (4)
2017 (2)
2013 (2)

Modelling Approach

Ordinary differential equation model (53)

Study status

Not yet recruiting (2)

Lab affiliation

IRIC-Université de Montréal (5)
Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth (3)
Laboratory of RNA Processing and Decay, Institute of Biochemistry and Biophysics, Warsaw, Poland (3)
Department of Biochemistry, University of Oxford (3)
Mass Spectrometry Facility, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria (2)
Department of Biochemsitry, University of Oxford (2)
1. Barts Cancer Institute Queen Mary, University of London John Vane Science Centre, Charterhouse Square, London EC1M 6BQ 2. Instituto de Parasitología y Biomedicina López-Neyra, Consejo Superior de Investigaciones Científicas (CSIC), Granada, 18016, Spain (2)
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Adolfa Pawińskiego 5A, 02-106 Warsaw, Poland (2)
State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, Gansu Province 730046, PR China (2)
Department of Biology, University of Fribourg Chemin du Musée 10, 1700 Fribourg, Switzerland T +41 26 300 8631 (2)
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh (1)
Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) TUM School of Life Sciences Technical University Munich (TUM) Gregor-Mendel-Straße 4 85354 Freising (1)
Department of Cellular and Molecular Medicine, KU Leuven, Belgium (1)
Proteomic facility of Institut Jacques Monod, UMR7592 (CNRS and Paris University), 75013 Paris, France (lab head) (1)
- University of Cambridge, Department of Genetics, Downing Street, Cambridge CB2 3EH, UK - Division of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd, Pasadena, California 91125, USA (1)
Department of Microbiology; Icahn School of Medicine at Mount Sinai; New York, NY, 10029; USA (1)
John Cijiang He, MD/PhD Division of Nephrology, Box 1243 Mount Sinai School of Medicine One Gustave L Levy Place, New York NY 10029 Tel: 212-659-1703, Fax: 212-987-0389 (1)
Mass Spectrometry Proteomics Science Technology Platform, The Francis Crick Institute (1)
Department of Human Genetics, University of Miami, Miller School of Medicine, Sylvester Comprehensive Cancer Center, Miami, FL, USA (1)
The Sainsbury Laboratory, Colney Lane, NR4 7UH, Norwich, Norfolk, United Kingdom (1)
Human Immunological Diseases Section, Laboratory of Clinical Immunology and Microbiology, Division of Intramural Research, NIAID, NIH, Department of Health and Human Services, Unites States Government (1)
Proteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA. (1)
Carnegie Institution for Science (1)
Cell Cycle Group Cancer Epigenetics and Biology Program (PEBC) Bellvitge Isntitute of Biomedical Research (IDIBELL) Hospital Duran i Reynals Avinguda de la Gran Via de l'Hospitalet, 199-203 08908 - L'Hospitalet de Llobregat (1)
Turku Bioscience Centre, University of Turku and Åbo Akademi University, 20520 Turku, Finland Institute of Biomedicine, University of Turku, 20520 Turku, Finland (1)
Head of Proteomics Unit Spanish National Cancer Research Centre (CNIO) Address: Melchor Férnandez Almagro, 3. 28029 Madrid. SPAIN (1)
Sainsbury Laboratory Norwich (1)
Université Paris cité, CNRS, Institut Jacques Monod, F-75006 Paris, France (1)
Center for Medical Biochemistry, Max Perutz Labs, Medical University of Vienna, Austria (1)
Institute of Experimental Pharmacology and Toxicology; University Medical Center Hamburg-Eppendorf (1)

Keyword

LB100 (2)
Gastrointestinal Neoplasms (2)
Immune checkpoint inhibitors (1)
Microsatellite stable (1)
Azenosertib (1)
PP2A (1)
WEE1 (1)
Atezolizumab (1)
Digestive System Neoplasms (1)
Metastatic colorectal cancer (1)

IsPrivate

False (53)

Model Flag

Non Miriam (2)
Non Kinetic (1)

Classification

fungi (1)
protozoa (1)

Study type

Transcription profiling by array (80)
RNA-seq of coding RNA (15)
ChIP-seq (4)
ChIP-chip by tiling array (3)
Genotyping by array (3)
Comparative genomic hybridization by array (3)
Unknown experiment type (2)
RNA-seq of coding RNA from single cells (2)
Interventional (2)
Transcription profiling by SAGE (1)
Methylation profiling by array (1)
Genotyping by high throughput sequencing (1)
RNA-seq of total RNA (1)
RNA-seq of non coding RNA (1)

Release Date

2020 (136)
2021 (124)
2019 (119)
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2017 (105)
2016 (103)
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2024 (97)
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2010 (55)
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2007 (24)
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2006 (9)
2005 (8)
2000 (6)
2003 (4)
2004 (3)
1999 (2)
1998 (2)
2002 (1)
2001 (1)
1997 (1)

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Phosphoproteomic Effects of Acute Depletion of PP2A Regulatory Subunit Cdc55

Protein phosphatase regulatory subunits are increasingly recognized as promising drug targets. In the absence of an existing drug, inducible degradation provides a means of predicting candidate targets. We here employed auxin-inducible degradation of S. cerevisiae PP2A regulatory subunit Cdc55 in co...

ORGANISM(S): Saccharomyces Cerevisiae

2021-01-27 | PXD019534 | panorama

Targeting c-MYC by antagonizing PP2A inhibitors in breast cancer

Inhibition of SET by siRNA or SET antagonist and CIP2A by siRNA can downregulate c-MYC and c-MYC target genes. Cells were treated with a SET antagonist (1μMOP449) for 12 hours, or siRNA for 48 hours.

ORGANISM(S): Homo sapiens

2014-05-28 | E-GEOD-58008 | biostudies-arrayexpress

HeLa phosphoproteome regulated by PP2A related proteins

HeLa cells were treated with siRNAs of PP2A related proteins or with okadaic acid, in triplicates. Tryptic digests of extracted proteins were analyzed using a Q Exactive mass spectrometer, before and after TiO2 phosphopeptide enrichment. Data were searched with Mascot via Proteome Discoverer. For ph...

ORGANISM(S): Homo Sapiens (human)

2020-02-19 | PXD016102 | JPOST Repository

TBP ChIP-chip on Jurkat cells

During mitosis, TATA-binding protein(TBP), which remains bound to DNA during mitosis, recruits PP2A and also interacts with a subunit of the condensin complex to allow efficient dephosphorylation and inactivation of condensin near these promoters to inhibit their compaction. These result suggest tha...

ORGANISM(S): Homo sapiens

2010-04-03 | E-GEOD-12256 | biostudies-arrayexpress

The yeast PP2A-CDC55 phosphatase regulates the transcriptional response to hyperosmolarity stress by regulating Msn2 and Msn4

The yeast PP2A-Cdc55 Serine/Threonine phosphatase regulates transcription under certain conditions. It is required for full activation of the environmental stress response mediated by the transcription factors Msn2 and Msn4. PP2A-Cdc55 contributes to sustained nuclear accumulation of Msn2 and Msn4 a...

ORGANISM(S): Saccharomyces cerevisiae

2012-06-07 | E-GEOD-38565 | biostudies-arrayexpress

A PP2A-Integrator complex fine-tunes transcription by opposing CDK9

In this study, we discovered that CDK9-mediated, RNAPII-driven transcription is functionally opposed by a protein phosphatase 2A (PP2A) complex that is recruited to transcription sites by the Integrator complex subunit INTS6. PP2A dynamically antagonises phosphorylation of key CDK9 substrates includ...

ORGANISM(S): Homo sapiens (Human)

2022-08-12 | PXD025060 | Pride

The yeast PP2A-CDC55 phosphatase regulates the transcriptional response to hyperosmolarity stress by regulating Msn2 and Msn4

This SuperSeries is composed of the following subset Series: GSE38565: The yeast PP2A-CDC55 phosphatase regulates the transcriptional response to hyperosmolarity stress by regulating Msn2 and Msn4 [Time course 1] GSE42033: The yeast PP2A-CDC55 phosphatase regulates the transcriptional response to hy...

ORGANISM(S): Saccharomyces cerevisiae

2012-11-06 | E-GEOD-42034 | biostudies-arrayexpress

PP2A is essential for Th17 differentiaiton

PRJNA490432 | ENA

The yeast PP2A-CDC55 phosphatase regulates the transcriptional response to hyperosmolarity stress by regulating Msn2 and Msn4 [Time course 2]

ORGANISM(S): Saccharomyces cerevisiae W303

2012-11-06 | E-GEOD-42033 | biostudies-arrayexpress

Cytokinetic Abscission in Toxoplasma gondii is governed by Protein Phosphatase 2A and the Daughter Cell Scaffold Complex

Cytokinetic abscission is the last step of cell division during which the daughter cells physically separate through the generation of barriers in the form of new plasma membrane or cell wall. While the contractile ring is a prominent structure during cytokinesis in bacteria, fungi and animal cells,...

ORGANISM(S): Toxoplasma gondii Toxoplasma gondii

2024-06-13 | PXD051495 | Pride

Toxoplasma gondii Cellular abscission Tachyzoites Pp2a complex Lc-esi- ms/ms

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