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PROSITE documentation PDOC51803Zinc finger C2HC RNF-type profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51803
Ubiquitination is a posttranslational 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) (see <PDOC00449>) 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) (see <PDOC50330>) [1,2,3,4].
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- β via enhancing the ubiquitination of TRAF3 and TRAF6.
The profile we developed covers the entire C2HC RNF-type zinc finger.
Last update:June 2016 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Giannini A.L. Gao Y. Bijlmakers M.-J. |
| Title | T-cell regulator RNF125/TRAC-1 belongs to a novel family of ubiquitin ligases with zinc fingers and a ubiquitin-binding domain. | |
| Source | Biochem. J. 410:101-111(2008). | |
| PubMed ID | 17990982 | |
| DOI | 10.1042/BJ20070995 |
| 2 | Authors | Rodriguez M.S. Egana I. Lopitz-Otsoa F. Aillet F. Lopez-Mato M.P. Dorronsoro A. Lobato-Gil S. Sutherland J.D. Barrio R. Trigueros C. Lang V. |
| Title | The RING ubiquitin E3 RNF114 interacts with A20 and modulates NF-kappaB activity and T-cell activation. | |
| Source | Cell Death Dis. 5:E1399-E1399(2014). | |
| PubMed ID | 25165885 | |
| DOI | 10.1038/cddis.2014.366 |
| 3 | Authors | Han D. Liang J. Lu Y. Xu L. Miao S. Lu L.-Y. Song W. Wang L. |
| Title | Ubiquitylation of Rad51d Mediated by E3 Ligase Rnf138 Promotes the Homologous Recombination Repair Pathway. | |
| Source | PLoS ONE 11:E0155476-E0155476(2016). | |
| PubMed ID | 27195665 | |
| DOI | 10.1371/journal.pone.0155476 |
| 4 | Authors | Chen H.W. Yang Y.K. Xu H. Yang W.W. Zhai Z.H. Chen D.Y. |
| Title | Ring finger protein 166 potentiates RNA virus-induced interferon-beta production via enhancing the ubiquitination of TRAF3 and TRAF6. | |
| Source | Sci. Rep. 5:14770-14770(2015). | |
| PubMed ID | 26456228 | |
| DOI | 10.1038/srep14770 |
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