RING box protein: Difference between revisions

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<StructureSection load='4f52' size='340' side='right' caption='Human RING finger protein 1 (green) complex with cullin-1 (grey),  glomulin (magenta) and Zn+2 ions (grey) (PDB code [[4f52]])' scene=''>
<StructureSection load='4f52' size='340' side='right' caption='Human RING finger protein 1 (green) complex with cullin-1 (grey),  glomulin (magenta) and Zn+2 ions (grey) (PDB code [[4f52]])' scene=''>
'''RING box protein''' (RBX) makes a heterodimer with cullin.  The heterodimer is essential for the protein ubiquitination process.  RBX1 is a component of the SCF (Skp1-cullin-F box protein) E3 ubiquitin ligase complex.  RBX contains a RING-type zinc finger domain.  The RING domain is 40 to 60 residues long and binds two Zn atoms.  It is involved in protein-protein interaction.
'''RING box protein''' (RBX) makes a heterodimer with cullin.  The heterodimer is essential for the protein ubiquitination process.  RBX1 is a component of the SCF (Skp1-cullin-F box protein) E3 ubiquitin ligase complex<ref>PMID:21115485</ref>.  RBX contains a RING-type zinc finger domain.  The RING domain is 40 to 60 residues long and binds two Zn atoms.  It is involved in protein-protein interaction.
 
== Function ==
 
== Disease ==


== Relevance ==
== Relevance ==
 
Overexpression of RBX1 contributes to tumor progression and poor prognosis of non-muscle-invasive bladder transitional cell carcinoma<ref>PMID:23609182</ref>.  RBX1 and RBX2 are overexpressed in multiple human cancer tissues and required for the growth and survival of cancer cells<ref>PMID:2102004</ref>.
== Structural highlights ==
 
</StructureSection>
</StructureSection>