15 exons, 14 introns (Parfait et al., 2000).

1518bp mRNA with 463aa open reading frame.

463 amino acids, 52 kDa.
RUVBL2 belongs to the AAA+ ATPase superfamily (ATPases associated with diverse cellular activities) sharing conserved Walker A and B motifs, arginine fingers, and sensor domains. The monomers contain two domains, which are involved in ATP binding and hydrolysis respectively. RUVBL2 assembles into an hexameric structure with a central channel.
RUVBL2 interacts with RUVBL1 to form a dodecamer (Puri et al., 2007). This RUVBL1/RUVBL2 complex displays a significant ATPase activity and is likely one of the functional forms of the proteins.
Sumoylation of RUVBL2 has been reported on Lys456 in invasive prostate cancer cells (Kim et al., 2006).
RUVBL2 is phosphorylated on an ATM/ATR consensus site following DNA damage (Matsuoka et al., 2007).

Expression of RUVBL2 is ubiquitous but especially abundant in thymus and testis (Salzer et al., 1999; Parfait et al., 2000).
RUVBL2 is overexpressed in hepatocellular carcinoma (Rousseau et al., 2007). Overexpression of RUVBL2 in several cancers and its possible role in human cancers has been reported (reviewed in Huber et al., 2008).

Cytoplasm and nucleus.

RUVBL2 interacts with c-myc (Wood et al., 2000) and also modulates transcriptional regulation by the beta-catenin/TCF-LEF complex (Bauer et al., 2000) and ATF2 (Cho et al., 2001).
RUVBL2 participates in the remodelling of chromatin as a member of several complexes such as TIP60 (Ikura et al., 2000), INO80 (Jin et al., 2005), SRCAP (Cai et al., 2005).
It is also involved in transcriptional regulation (reviewed in Gallant, 2007), DNA repair (Gospodinov et al., 2008), snoRNP biogenesis (Watkins et al., 2002), and telomerase activity (Venteicher et al., 2008).
RUVBL2 silencing in fibroblasts induces a senescent phenotype (Chan et al., 2005).