{PDOC51803}
{PS51803; ZF_C2HC_RNF}
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* Zinc finger C2HC RNF-type profile *
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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-
   beta via enhancing the ubiquitination of TRAF3 and TRAF6.

The profile we developed covers the entire C2HC RNF-type zinc finger.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2016 / First entry.

[ 1] Giannini A.L., Gao Y., Bijlmakers M.-J.
     "T-cell regulator RNF125/TRAC-1 belongs to a novel family of ubiquitin
     ligases with zinc fingers and a ubiquitin-binding domain."
     Biochem. J. 410:101-111(2008).
     PubMed=17990982; DOI=10.1042/BJ20070995
[ 2] 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.
     "The RING ubiquitin E3 RNF114 interacts with A20 and modulates
     NF-kappaB activity  and T-cell activation."
     Cell Death Dis. 5:E1399-E1399(2014).
     PubMed=25165885; DOI=10.1038/cddis.2014.366
[ 3] Han D., Liang J., Lu Y., Xu L., Miao S., Lu L.-Y., Song W., Wang L.
     "Ubiquitylation of Rad51d Mediated by E3 Ligase Rnf138 Promotes the
     Homologous Recombination Repair Pathway."
     PLoS ONE 11:E0155476-E0155476(2016).
     PubMed=27195665; DOI=10.1371/journal.pone.0155476
[ 4] Chen H.W., Yang Y.K., Xu H., Yang W.W., Zhai Z.H., Chen D.Y.
     "Ring finger protein 166 potentiates RNA virus-induced interferon-beta
     production  via enhancing the ubiquitination of TRAF3 and TRAF6."
     Sci. Rep. 5:14770-14770(2015).
     PubMed=26456228; DOI=10.1038/srep14770

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