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Ubiquitin-Protein Ligases (Ubiquitin-Protein Ligase)

Subscribe to New Research on Ubiquitin-Protein Ligases

A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.

Also Known As:

Ubiquitin-Protein Ligase; E3 Ligase; E3 Ubiquitin Ligase; Ubiquitin Ligase E3; Ubiquitin-Protein Ligase E3; E3, Ubiquitin Ligase; Ligase E3, Ubiquitin; Ligase E3, Ubiquitin-Protein; Ligase, E3; Ligase, E3 Ubiquitin; Ligase, Ubiquitin-Protein; Ligases, Ubiquitin-Protein; Ubiquitin Ligase, E3; Ubiquitin Protein Ligase; Ubiquitin Protein Ligase E3; Ubiquitin Protein Ligases

Networked: 1227 relevant articles (5 outcomes, 77 trials/studies)

Relationship Network

Bio-Agent Context: Research Results

Enzymes and Coenzymes
- Enzymes: 34502
  - Ligases: 2113
    - Ubiquitin-Protein Ligase Complexes: 2
      - Ubiquitin-Protein Ligases: 1227
        Proto-Oncogene Proteins c-mdm2: 209
        Von Hippel-Lindau Tumor Suppressor Protein: 96
        autocrine motility factor receptor: 52
        parkin protein: 24
        SKP Cullin F-Box Protein Ligases: 18
        Proto-Oncogene Proteins c-cbl: 5
        Arabidopsis ASK11 protein
        Arabidopsis ATL31 protein
        Arabidopsis AtPUB14 protein
        Arabidopsis BIG BROTHER protein
        Arabidopsis CHIP protein
        Arabidopsis COP1 protein
        Arabidopsis HUB1 protein
        Arabidopsis HUB2 protein
        Arabidopsis KEG protein
        Arabidopsis NLA protein
        Arabidopsis PRT6 protein
        Arabidopsis RIN2 protein
        Arabidopsis RIN3 protein
        Arabidopsis Rma2 protein
        Arabidopsis SDIR1 protein
        Arabidopsis UPL2 protein
        Arabidopsis XBAT32 protein
        Bovine herpesvirus 1 bICP0 protein
        C elegans ari-1 protein
        C elegans brd-1 protein
        C elegans CHIP protein
        C elegans EEL-1 protein
        C elegans HRD-1 protein
        C elegans HRDL-1 protein
        C elegans MARC-6 protein
        C elegans RLE-1 protein
        C elegans RNF-121 protein
        C elegans WWP1 protein
        Drosophila ari-2 protein
        Drosophila elfless protein
        Drosophila hyperplastic discs protein
        Drosophila lack protein
        Drosophila Mind bomb protein
        Drosophila neur protein
        Drosophila no poles protein
        Drosophila parkin protein
        Drosophila supernumerary limbs protein
        Drosophila Suppressor of deltex protein
        Drosophila Topors protein
        Drosophila Ube3a protein
        Fanconi Anemia Complementation Group L Protein
        GRAIL protein
        human ARIH2 protein
        human BARD1 protein
        human BRAP protein
        human CBLL1 protein
        human DTX3L protein
        human DZIP3 protein
        human FBXL14 protein
        human FBXL5 protein
        human FBXW11 protein
        human FBXW7 protein
        human HACE1 protein
        human HECTD2 protein
        human Hectd3 protein
        human HectH9 protein
        human HECW1 protein
        human HERC4 protein
        human HERC6 protein
        Human herpesvirus 1 Vmw110 protein
        human HOIL-1 protein
        human HUWE1 protein
        human ITCH protein
        human KCMF1 protein
        human KIAA1333 protein
        human Klhdc5 protein
        human LNX1 protein
        human LRSAM1 protein
        human MARCH1 protein
        human MARCH5 protein
        human MARCH6 protein
        human MARCH7 protein
        human MARCH9 protein
        human MGRN1 protein
        human MIB1 protein
        human MIB2 protein
        human MITOL protein
        human MYCBP2 protein
        human MYLIP protein
        human NEURL2 protein
        human NSPc1 protein
        human OSTM1 protein
        human PIR2 protein
        human PJA1 protein
        human POSH2 protein
        human RCHY1 protein
        human REUL protein
        human RFWD2 protein
        human RFWD3 protein
        human ring finger protein 105
        human ring finger protein 181
        human ring finger protein 212
        human RN181 protein
        human RNF111 protein

Experts

1.	Sun, Yi: 12 articles (01/2015 - 07/2003)
2.	Ohh, Michael: 12 articles (08/2014 - 03/2003)
3.	Penninger, Josef M: 11 articles (03/2014 - 02/2005)
4.	Tanaka, Keiji: 10 articles (10/2015 - 03/2003)
5.	Dawson, Ted M: 10 articles (12/2014 - 05/2004)
6.	Boutell, Chris: 9 articles (11/2015 - 01/2002)
7.	Brice, Alexis: 9 articles (09/2014 - 06/2003)
8.	Jia, Lijun: 8 articles (10/2015 - 01/2009)
9.	Wei, Wenyi: 8 articles (09/2015 - 09/2010)
10.	Langdon, Wallace Y: 8 articles (03/2015 - 11/2004)

Related Diseases

1.	Neoplasms (Cancer) 11/03/2015 - "In this study, we report that SOX10 is a direct substrate of Fbxw7α E3 ubiquitin ligase, a tumor suppressor in multiple cancers. " 01/01/2015 - "Recent studies have shown that WW domain containing E3 ubiquitin protein ligase 1 (WWP1) is frequently amplified in various cancers. " 01/01/2015 - "Although early studies show that Mdm2 is the primary E3 ubiquitin ligase for the p53 tumor suppressor, an increasing amount of data suggests that p53 ubiquitination and degradation are more complex than once thought. " 12/01/2014 - "This study for the first time demonstrated the role of TRIM13, ER resident RING E3 ligase as a novel regulator of NEMO ubiquitination, negative regulator of NF-κB signaling and its role as a tumor suppressor. " 10/30/2014 - "Taken together, our study, using both genetic and pharmaceutical approaches, demonstrates that Sag is essential for embryonic vasculogenesis and tumor angiogenesis, and provides the proof-of-concept evidence that targeting Sag E3 ubiquitin ligase may have clinical value for anti-angiogenesis therapy of human cancer."
2.	Anoxia (Hypoxia) 05/03/2012 - "The VHL protein is best known as an E3 ubiquitin ligase that targets hypoxia-inducible factor-α (HIF-α), but many diverse, non-canonical cellular functions have also been assigned to VHL, mainly based on studies in cell culture systems. " 10/14/2010 - "In this study we identify PIASy as a specific E3 ligase for hypoxia-induced HIF1α SUMOylation. " 06/16/2015 - "E3 Ubiquitin Ligase VHL Regulates Hypoxia-Inducible Factor-1α to Maintain Regulatory T Cell Stability and Suppressive Capacity." 01/15/2015 - "Thus, we identified Wwox as a novel molecule in the HIF-1α-HDM2 regulatory loop, necessary for the dynamic regulation of the HIF-1α amount, and we suggested that the reduction of endogenous Wwox free pool under hypoxia might also be due to the interaction with HDM2, sequestering the E3 ubiquitin ligase. " 01/01/2015 - "We demonstrate that the E3 ubiquitin ligase SIAH2 stimulates YAP by destabilizing LATS2, a critical component of the Hippo pathway, in response to hypoxia. "
3.	Pneumonia (Pneumonitis) 07/08/2015 - "These studies describe an unreported innate immune pathway and suggest that mutation or antagonism of the E3 ligase HECTD2 results in reduced severity of lung inflammation by selectively modulating the abundance of the anti-inflammatory protein PIAS1. " 05/01/2011 - "The results provide a unique model of calcium-regulated intermolecular competition between an E3 ligase subunit and an antagonist that is critically relevant to pneumonia and lipid homeostasis." 07/08/2015 - "We discovered a ubiquitin E3 ligase, HECTD2, which ubiquitinated and mediated the degradation of PIAS1, thus increasing inflammation in an experimental pneumonia model. " 04/24/2014 - "E3 ligase subunit Fbxo15 and PINK1 kinase regulate cardiolipin synthase 1 stability and mitochondrial function in pneumonia."
4.	Lafora Disease 01/01/2014 - "Lafora disease can be caused by defects in the EPM2A gene, which encodes the laforin protein phosphatase, or in the NHLRC1 gene (also called EPM2B) codifying the malin E3 ubiquitin ligase. " 06/14/2005 - "Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin." 07/01/2012 - "Mutations in either EPM2A, the gene encoding a dual-specificity phosphatase named laforin, or NHLRC1, the gene encoding an E3 ubiquitin ligase named malin, cause Lafora disease in humans. " 12/01/2010 - "Lafora disease is caused by deficiency of either the laforin glycogen phosphatase or the malin E3 ubiquitin ligase. " 07/25/2014 - "Lafora disease is a progressive myoclonus epilepsy caused by mutations in the EPM2A or EPM2B genes that encode a glycogen phosphatase, laforin, and an E3 ubiquitin ligase, malin, respectively. "
5.	Heart Diseases (Heart Disease) 01/01/2008 - "Appetite for destruction: E3 ubiquitin-ligase protection in cardiac disease." 01/01/2008 - "Therefore, focusing on specific regulatory components of the proteasome, such as members of the E3 ubiquitin-ligase family of proteins, may hold promise for targeted therapeutics of cardiac disease. "

Related Drugs and Biologics

1.	Proteins (Proteins, Gene)
2.	Ubiquitin
3.	Proteasome Endopeptidase Complex (Proteasome)
4.	Transcription Factors (Transcription Factor)
5.	Staphylococcal Protein A (A, Protein)
6.	Ligases
7.	Vascular Endothelial Growth Factor A (Vascular Endothelial Growth Factor)
8.	polyglucosan
9.	Cyclin D1
10.	DNA (Deoxyribonucleic Acid)

Related Therapies and Procedures

1.	Therapeutics
2.	Drug Therapy (Chemotherapy)
3.	Radiotherapy
4.	Castration
5.	Heterologous Transplantation (Xenotransplantation)