
-   Protein Accession: O94844
-   Size: 696 amino acids
-   Molecular mass: 79417 Da
-   Domains: BTB/POZ_dom, P-loop_NTPase, SKP1/BTB/POZ_sf, Small_GTPase, Small_GTPase_Rho
-   Family: Belongs to the small GTPase superfamily. Rho family Family
-   The PhoBTB1 has a GTPase domain, followed by a proline-rich region, a tandem of two BTB (broad complex, tramtrack, and bric-a-brac) domains (the first one is bipartite) and a carboxyl terminal BACK (BTB and C-terminal Kelch) domain. An intramolecular interaction of the GTPase domain with the first BTB domain maintains the molecule inactive. Interaction with specific ligands would provoke a conformational change that disrupts the intramolecular interaction. The GTPase domain would then be able to bind and hydrolyze GTP and the first BTB domain would be free to assemble a cullin 3-dependent ubiquitin ligase complex that would tag the ligands, as well as RhoBTB itself, for degradation in the proteasome. The proline-rich region is a potential SH3 domain-binding site. BTB domains participate in homomeric and heteromeric associations with other BTB domains and function as components of multimeric cullin 3-dependent ubiquitin ligase complexes. [PMID: 27314390].
