Ubiquitin homeostasis

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Organisms

Mus musculus (67)
Homo sapiens (52)
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Corynebacterium glutamicum ATCC 13032 (1)
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Mass Spectrometry (148)
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Instrument Platform

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UNIPROT ID/AC

P37840 (1)

CHEBI ID

CHEBI:16977 (3)
CHEBI:15891 (3)
CHEBI:18095 (2)
CHEBI:16283 (2)
CHEBI:17196 (2)
CHEBI:16347 (2)
CHEBI:17203 (2)
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CHEBI:15428 (2)
CHEBI:17750 (2)
CHEBI:25094 (2)
CHEBI:24898 (2)
CHEBI:16811 (2)
CHEBI:16027 (1)
CHEBI:26523 (1)
CHEBI:16761 (1)
CHEBI:15422 (1)

Metabolite Name

L-Asparagine (3)
D-Fructose-6-phosphate (2)
L-Aspartate (2)
Allantoic acid (2)
Allantoin (2)
L-Cystine (2)
L-Ornithine (2)
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Acetylcarnitine (2)
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Creatine (2)
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Glutamine (2)
Methionine (2)
Creatinine (2)
Betaine (2)
7-Methylguanine (2)
Uracil (2)
Kynurenic acid (2)
Hippuric acid (2)
Lysine (2)
Tyrosine (2)
Serine (2)
Adenosine (2)
Isoleucine (2)
Taurine (2)

First Public Date

2026 (59)
2025 (31)
2024 (22)
2023 (15)
2014 (11)
2020 (9)
2022 (7)
2021 (7)
2018 (7)
2019 (6)
2015 (6)
2017 (3)

Modelling Approach

Ordinary differential equation model (2)

Lab affiliation

Institute of Molecular Biology (IMB), 55128 Mainz, Germany; Institute of Developmental Biology and Neurobiology (IDN), Johannes Gutenberg University, 55128 Mainz, Germany (5)
Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan (3)
Institute for Research in Immunology and Cancer (IRIC) Université de Montréal, Department of Chemistry, Université de Montréal, MIL campus, Montréal, H2V 0B3, Canada (3)
Sun Yat-sen University (3)
Aarhus University Department of Biomedicine DK-8000 Aarhus (3)
TIGEM (3)
Department of Molecular Cell Biology, Institute of Biochemistry, Splaiul Independentei 296, 060031 Bucharest 17, Romania (2)
Head Proteomics Group, Leiden University Medical Center, Center for Proteomics and Metabolomics, PO Box 9600, Postal zone P1-Q, 2300 RC Leiden, The Netherlands (2)
Institute of Molecular Biology (IMB), Mainz, Germany (2)
Instituto de Investigaciones Sanitarias de Santiago de Compostela (2)
Erasmus MC (2)
Institute of Molecular Biology, D-55118 Mainz, Germany (1)
Head of Discovery Proteomics Facility, Oxford (1)
Max-Planck-Institute for Multidisciplinary Sciences Bioanalytical Mass Spectrometry Group Am Fassberg 11 D-37077 Goettingen Germany (1)
Mass spectrometry facility, Functional Proteomics, SFB 815 Core Unit, Goethe-Universität, Frankfurt am Main, Germany (1)
Department of Immunology and Cell Biology Faculty of Medicine and Health Sciences, University of Sherbrooke Canada (1)
Max Planck Institute for Multidisciplinary Sciences, Bioanalytical Mass Spectrometry Group, Am Fassberg 11, 37077 Göttingen, Germany University Medical Center Goettingen, Institute for Clinical Chemistry, Bioanalytics, Robert-Koch-Strasse 40, 37075 Göttingen, Germany (1)
Vividion Therapeutics (1)
Central European Institute of Technology, Masaryk University, Brno, Czech Republic National Centre for Biomolecular research, Masaryk University, Brno, Czech Republic (1)
Departments of Biology and Chemistry, Vanderbilt University, USA (1)
UniSA (1)
Centro Nacional de Biotecnología (CNB-CSIC), Darwin, 3, 28049 Madrid, Spain (1)
Department of Experimental Medicine and Surgery, University of Rome "Tor Vergata", Rome, and Santa Lucia IRCCS Foundation, Rome, Italy (1)
MRC Protein Phosphorylation and Ubiquitylation Unit School of Life Sciences, University of Dundee Sir James Black Centre Dundee, DD1 5EH United Kingdom (1)
Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai 980-8578, Japan (1)
Univeristy Of Toronto (1)
Department of Hepatobiliary and Pancreatic Surgery, the First Affiliated Hospital, Zhejiang University School of Medicine (1)
Professor, Medicine and Cellular and Molecular Medicine Founding Director, Institute for Network Medicine University of California San Diego (1)
Institute of Physiology of the Czech Academy of Sciences, Laboratory of Structural Biology of Signaling Proteins, Division BIOCEV, Prumyslova 595, 252 50 Vestec, Czech Republic (1)
Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA, USA. (1)

IsPrivate

False (2)

Classification

fungi (4)
protozoa (1)
bacteria (1)

Study type

Transcription profiling by array (120)
RNA-seq of coding RNA (26)
RNA-seq of coding RNA from single cells (11)
ChIP-seq (9)
Single nucleus RNA sequencing (3)
Unknown experiment type (2)
RNA-seq of total RNA (2)
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Comparative genomic hybridization by array (1)
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DNA-seq (1)

Release Date

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2015 (90)
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2019 (81)
2013 (57)
2014 (52)
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2012 (48)
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2005 (7)
2007 (5)
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2002 (2)
2003 (1)

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Proctor2007 - Age related decline of proteolysis, ubiquitin-proteome system

Proctor2007 - Age related decline of proteolysis, ubiquitin-proteome system This is a stochastic model of the ubiquitin-proteasome system for a generic pool of native proteins (NatP), which have a half-life of about 10 hours under normal conditions. It is assumed that these ...

2024-09-02 | BIOMD0000000105 | BioModels

Endo-Lysosomal Proteins and Ubiquitin CSF Concentrations in Alzheimer’s and Parkinson’s Disease

Alzheimer’s (AD) and Parkinson’s disease (PD) are neurodegenerative disorders characterized by an accumulation of protein aggregates in the brain. AD is the most common cause of dementia and presents with impairment of memory and cognition. PD results from the loss of dopaminergic neurons which resu...

ORGANISM(S): Homo Sapiens

2019-10-27 | PXD013451 | panorama

To identify potential ubiquitin ligases that regulate BIK1 homeostasis

PRJNA945931 | ENA

A cullin-RING ubiquitin ligase promotes thermotolerance as part of the Intracellular Pathogen Response in C. elegans.

Intracellular pathogen infection leads to proteotoxic stress in host organisms. Previously we described a physiological program in the nematode C. elegans called the Intracellular Pathogen Response (IPR), which promotes resistance to proteotoxic stress and appears to be distinct from canonical prote...

ORGANISM(S): Caenorhabditis Elegans (ncbitaxon:6239)

2020-02-07 | MSV000084936 | MassIVE

Ubiquitin-like proteins NEDD8 and SUMO2 control epithelial homeostasis, regeneration, and inflammation [RNA-Seq]

PRJNA1445702 | ENA

Ubiquitin-like proteins NEDD8 and SUMO2 control epithelial homeostasis, regeneration, and inflammation [scRNA-seq]

PRJNA1446691 | ENA

Ubiquitin-like proteins NEDD8 and SUMO2 control epithelial homeostasis, regeneration, and inflammation [RNA-Seq epithelial]

PRJNA1454082 | ENA

Ubiquitin-like proteins NEDD8 and SUMO2 control epithelial homeostasis, regeneration, and inflammation [RNA-Seq mouse]

PRJNA1445698 | ENA

The E3 ubiquitin ligase DDB1 controls homeostasis of hematopoietic stem and progenitor cells

Hematopoietic stem cells (HSC) are regulated to keep the balance between self-renewal and differentiation. However, little is known about post-translational regulations in HSCs. In this study, we characterize the role of DDB1, a component of the Cul4A-DDB1 E3 ubiquitin ligase complex, in HSCs and pr...

ORGANISM(S): Mus musculus

2015-07-10 | E-GEOD-70658 | biostudies-arrayexpress

Ubiquitin-like proteins NEDD8 and SUMO2 control epithelial homeostasis, regeneration, and inflammation [Xenium]

PRJNA1446694 | ENA

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2264 Results

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