RING box protein: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel

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-<StructureSection load='4f52' size='340' side='right' caption='Human RING finger protein 1 (green and yellow) complex with cullin-1 (grey and pink),  glomulin (magenta and cyan) 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 ==
+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:21103004</ref>.
-== Structural highlights ==
 </StructureSection>
 == 3D Structures of RING box protein ==
+[[Ring box protein 3D structures]]
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Ring box protein 1
-**[[2lgv]] – hRBX1 residues 12-108 (mutant) – human - NMR <br />
-**[[1ldj]] – hRBX1 + hCullin-1  <br />
-**[[3rtr]] – hRBX1 + hCullin-1 residues 411-766 (mutant)  <br />
-**[[1ldk]] – hRBX1 + hCullin-1 + cyclin A/Cdk2-asociated protein + Skp2-like protein <br />
-**[[1u6g]] – hRBX1 + hCullin-1 + TIP120 protein  <br />
-**[[4f52]] – hRBX1 + hCullin-1 residues 411-690 (mutant) + glomulin<br />
-**[[4p5o]] – hRBX1 + hCullin-1 residues 411-776 + Dcn1-like protein + NEDD8-conjugating enzyme Ubc12 +  NEDD8-conjugating enzyme Ubc12 + NEDD8 <br />
-**[[2hye]] – hRBX1 + hCullin-4A + DNA damage-binding protein 1 + nonstructural protein <br />
-**[[4a0k]] – hRBX1 + hCullin-4A + DNA damage-binding protein 1 + DNA damage-binding protein 2 + DNA<br />
-**[[3dpl]] – hRBX1 + hCullin-5 residues 401-780 (mutant)  <br />
-**[[3dqv]] – hRBX1 + hCullin-5 residues 401-780 (mutant) + NEDD8 <br />
-**[[4a0c]] – hRBX1 + hCullin-4B residues 192-913 + Cullin-associated NEDD8-dissociated protein <br />
-**[[4a0l]] – hRBX1 + hCullin-4B + DNA damage-binding protein 1 + DNA damage-binding protein 2 + DNA<br />
-*Ring box protein 2
-**[[2ecl]] – hRBX2 RING domain - NMR <br />
-}}
 == References ==
 <references/>
+[[Category:Topic Page]]