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Search results 101 to 119 out of 119 for Rnf166

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Type Details Score
UniProt Feature
UniProt Feature
Begin: 1
Description: E3 ubiquitin-protein ligase RNF166
Type: chain
End: 237
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Publication
34837535 | -
     
First Author: Hwang IY
Year: 2021
Journal: J Neural Transm (Vienna)
Title: RNF166 plays a dual role for Lys63-linked ubiquitination and sumoylation of its target proteins.
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Interaction Experiment
Hwang IY (2021)
Description: RNF166 plays a dual role for Lys63-linked ubiquitination and sumoylation of its target proteins.
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Publication
23398480 | J:238045
First Author: Dudazy-Gralla S
Year: 2013
Journal: Biosci Rep
Title: Identification of thyroid hormone response elements in vivo using mice expressing a tagged thyroid hormone receptor α1.
Volume: 33
Issue: 2
Pages: e00027
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Publication
27195665 | -
First Author: Han D
Year: 2016
Journal: PLoS One
Title: Ubiquitylation of Rad51d Mediated by E3 Ligase Rnf138 Promotes the Homologous Recombination Repair Pathway.
Volume: 11
Issue: 5
Pages: e0155476
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Publication
26456228 | -
 
First Author: Chen HW
Year: 2015
Journal: Sci Rep
Title: Ring finger protein 166 potentiates RNA virus-induced interferon-β production via enhancing the ubiquitination of TRAF3 and TRAF6.
Volume: 5
Pages: 14770
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Protein Domain
IPR034734 | ZF_C2HC_RNF
Type: Domain
Description: This entry includes the C2HC RNF-type zinc finger.Ubiquitination is a post-translational modification that mediates the covalent attachment of ubiquitin (Ub), a small, highly conserved, cytoplasmic protein of 76 amino acid residues, to target proteins. This conjugation is catalyzed by the sequential action of three enzymes: Ub-activating (E1) enzyme, Ub-conjugating (E2) enzyme and Ub ligase (E3). A large number of RING finger (RNF) proteins are present in eukaryotic cells and the majority of them are believed to act as E3 ubiquitin ligases. The closely related proteins RNF125/TRAC-1, RNF114 (also known as Zpf313), RNF138 (or NARF) and RNF166 contain, apart from the RING domain, a C2HC (Cys2-His-Cys)- and two C2H2 (Cys2-His2)-type zinc fingers, as well as an ubiquitin interacting motif (UIM) [, , , ].Some proteins known to contain a C2HC RNF-type zinc finger are listed below:Mammalian RNF125/T-cell RING protein in activation 1 (TRAC-1)/, a positive regulator of T-cell activation. It negatively regulates RIG-1 mediated antiviral activity via conjugating ubiquitin chains to RIG-1 and MDA5, leading to their degradation by the proteasome.Vertebrate RNF114, acts as negative regulator of NF-kappaB-dependent transcription. It interacts with A20 in T cells and modulates A20 ubiquitylation.Vertebrate RNF138, likely involved in regulating homologous recombination repair pathway.Vertebrate RNF166, potentiates the RNA virus-induced production of IFN-beta via enhancing the ubiquitination of TRAF3 and TRAF6.
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Publication
17990982 | -
First Author: Giannini AL
Year: 2008
Journal: Biochem J
Title: T-cell regulator RNF125/TRAC-1 belongs to a novel family of ubiquitin ligases with zinc fingers and a ubiquitin-binding domain.
Volume: 410
Issue: 1
Pages: 101-11
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Publication
25165885 | -
 
First Author: Rodriguez MS
Year: 2014
Journal: Cell Death Dis
Title: The RING ubiquitin E3 RNF114 interacts with A20 and modulates NF-κB activity and T-cell activation.
Volume: 5
Pages: e1399
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Protein
Q9CSA3
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: true
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Protein
Q3UC35
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
A0A3Q4EHU1
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: true
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Protein
Q9CQE0
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
Q9D9M9
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
Q9D9R0
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
Q8C521
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Protein
A4PBT3
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
A2RS02
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
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Protein
Q9ET26
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: false
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