| Modification Notes |
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF5 (ring finger protein 5), also known as RMA1, NG2, G16 or RING5, is a 180 amino acid protein that localizes to the membrane and contains one RING-type zinc finger. Expressed in a wide variety of tissues, RNF5 functions as a ubiquitin ligase that can regulate cell motility by controlling the ubiquitination of paxillin, a focal adhesion phosphoprotein that is localized to the cytoskeleton. RNF5 can target paxillin for ubiquitination, thereby altering the localization of paxillin and effecting its ability to recruit signaling molecules to focal adhesions. While overexpression of RNF5 is associated with the progression of breast cancer, lowered expression levels are observed in muscular disorders, indicating an important role for RNF5 in the regulation of cytoskeletal activity. |