GPN-loop GTPase 2 (GPN2)

**GPN-loop GTPase 2 (GPN2)** is a member of the evolutionarily conserved GPN-loop GTPase enzyme family, defined by a unique Gly-Pro-Asn (GPN) motif in the G-domain, typically involved in GTP binding and hydrolysis. In humans, there are three paralogs: GPN1, GPN2, and GPN3. GPN2 functions as an essential assembly chaperone for the biogenesis of the 12-subunit RNA polymerase II (Pol II) complex, preventing misassembly or aggregation by binding and releasing hydrophobic peptide regions in subunits through a GTP-dependent mechanism involving large conformational changes. It forms part of a broader family (SIMIBI class) of GTPases that typically assemble as homo- or heterodimers and operate via a "lock-switch-rock" mechanism to facilitate complex allosteric assembly processes. Loss-of-function of GPN2 in yeast is lethal, underlining its essential cellular role. There are currently no known direct pharmacologic agents, disease associations, or clinical biomarkers based on available data[1][2]. **Notes:** - GPN2 is NOT considered a direct therapeutic target or receptor but rather an essential enzyme for assembly of critical cellular complexes[1][2]. - There are no current drugs, biomarkers, or safety concerns associated with GPN2 based on present knowledge. - No evidence of incorrect assignment, spelling, or concept.

Other names

GPN2ATPBD1BATP-binding domain 1 family member BUNQ5828/PRO19647FLJ10349