E3-ligases - OmicsDI

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CHEBI ID

CHEBI:189652 (1)

Metabolite Name

D-Mannose-6-phosphate (2)
L-Aspartate (2)
L-citrulline (2)
Lysine (2)
Trans-8, trans-10-dodecadien-1-ol (1)
Sulfoxaflor (1)
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Isoxazole, 3-[4-(methylsulfonyl)phenyl]-4-phenyl-5-(trifluoromethyl)- (1)
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8-acetyl-6,7-dimethoxycoumarin (1)
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6-aminopyridine-3-carboxamide (1)
5-methyl-5-phenylhydantoin (1)
5-(hydroxymethyl)quinolin-8-ol (1)
4-nitrodiphenylamine (1)
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4-methylcinnamic acid (1)
4-chlorobenzenesulfonamide (1)
3,3-dimethylacrylic acid (1)

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Modification

2x(15)N labeled L-lysine (1)

Study type

Transcription profiling by array (39)
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2000 (1)

Lab affiliation

Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA., Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA (32)
Department of Cell & Developmental Biology, University of California, San Diego, La Jolla, CA (4)
Director, Institute of Biochemistry II Goethe University Medical Faculty University Hospital Building 75 Theodor-Stern-Kai 7 60590 Frankfurt am Main Germany (4)
Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA., Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02215, USA (3)
Department of Microbiology and Molecular Medicine, CMU, University of Geneva, Geneva, Switzerland (3)
Northwestern University, Department of Chemistry (3)
Professor Institute of Biochemistry II Goethe University Medical Faculty University Hospital Building 75 Theodor-Stern-Kai 7 60590 Frankfurt am Main Germany (3)
BCMP, Harvard Medical School, Boston, USA Cancer Biology, Dana-Farber Cancer Institute, Boston, USA (2)
CSIR-CCMB (2)
CSIR-CCMB, Hyderabad, India (2)
Cell Biology and Physiology, University of North Carolina at Chapel Hill, North Carolina, USA (2)
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States (2)
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, 75390, TX, USA (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)
Georgia State University (2)
Harvard Medical School (2)
Institute of Immunology and Department of Orthopaedics of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310058, China (2)
Institute of Molecular Biology (IMB), Mainz, Germany (2)
King's College London, Chemistry Department, 7 Trinity Street, London, SE1 1DB, UK (2)
Lineberger Comprehensive Cancer Center, UNC Chapel Hill (2)
Max Perutz Labs, Vienna Biocenter Campus (VBC), Dr.-Bohr-Gasse 9, 1030, Vienna, Austria. (2)
Max Planck Institute of Biochemistry (2)
1 Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, Québec, Canada. 2 Department of Chemistry, Université de Montréal, Montréal, Québec, Canada. 3 Department of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Québec, Canada. (1)
1Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA 92093 (1)
Amsterdam UMC, Vrije Universiteit Amsterdam, Medical Oncology, Cancer Center Amsterdam, OncoProteomics Laboratory, Amsterdam, Netherlands (1)
Andalusian Center for Moelcular Biology and Regenerative Medicine (CABIMER), University of Sevilla, Spain (1)
Australian Regenerative Medicine Institute, Monash University, Wellington Road, Clayton, VIC 3800, Australia (1)
Bar-Ilan university, Israel (1)
Beijing Proteome Research Center, National Center for Protein Sciences (Beijing) Beijing Institute of Lifeomics， Beijing 102206 P.R. China. (1)
Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, Scotland, United Kingdom (1)

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BioE3 enables the identification of bona fide targets of E3 ligases

The post-translational modification of proteins by ubiquitination is a highly regulated process that involves a dynamic, three-step enzymatic cascade, where more than 600 E3 ligases play a critical role in recognizing specific substrates for modification. Separating bona fide targets of E3s from E3-...

ORGANISM(S): Homo sapiens (Human)

2024-01-26 | PXD041685 | Pride

Combinatorial mapping of E3 ubiquitin ligases to their target substrates

PRJNA982147 | ENA

Repurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies

The majority of current therapeutics targeting plasma membrane receptors function by antagonizing ligand binding or enzymatic activities. Typical mammalian proteins, however, consist of multiple domains executing discrete but coordinated activities, and saturating inhibition of one functional domain...

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

2022-05-25 | MSV000089542 | MassIVE

SIAH ubiquitin E3 ligases as modulators of inflammatory gene expression

PRJNA742677 | ENA

Nt-acetylation independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases

PRJNA989617 | ENA

Repurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies

PRJNA859706 | ENA

The Hace1 E3 Ligase Modulates the Activity of Multiple Tumor Suppressive CRL E3 Ligases by binding to CAND1

The Hace1 E3 ligase is a tumor suppressor in stressed cells. Through unknown mechanisms, Hace1 indirectly targets the cyclin D1 proto-oncogene for proteasomal degradation during nutrient depletion. We now show that Hace1 targets HIF1alpha for VHL-dependent degradation during hypoxia. To better under...

ORGANISM(S): Homo sapiens

2011-07-01 | E-GEOD-25452 | biostudies-arrayexpress

Expanding PROTACtable genome universe of E3 ligases.

Not available

S-EPMC10579327 | biostudies-literature

Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.

Not available

S-EPMC7205596 | biostudies-literature

BioE3 identifies specific substrates of ubiquitin E3 ligases.

Not available

S-EPMC10667490 | biostudies-literature

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