11 exons spamming 42840bp, 1371bp open reading frame.

1785bp mRNA.

456 amino acids, 50.2 kDa.
RUVBL1 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 structure of RuvBL1 has been determined by X-ray crystallography and published in 2006 (Matias et al., 2006).
The monomers contain three domains, of which the first and the third are involved in ATP binding and hydrolysis. The second domain is a DNA/RNA-binding domain as demonstrated by structural homology and nucleic acid binding assays. RUVBL1 assembles into an hexameric structure with a central channel. Pure RUVBL1 displays a marginal ATPase activity in vitro and no detectable helicase activity (Matias et al., 2006).
RUVBL1 interacts with RUVBL2 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 RUVBL1 was reported in metastatic prostate cancer cells (Kim et al., 2007).

Expression is ubiquitous but especially abundant in heart, skeletal muscle and testis (Salzer et al., 1999).
RUVBL1 is overexpressed in several tumors : liver (Li et al., 2005), colon (Carlson et al., 2003; Lauscher et al., 2007), lymphoma (Nishiu et al., 2002), non-small cell lung (Dehan et al., 2007). Overexpression of RUVBL1 in a large number of cancers and its possible role in human cancers have been reported (reviewed in Huber et al., 2008).

Cytoplasm and nucleus.

RUVBL1 plays roles in essential signaling pathways such as the c-Myc and beta-catenin pathways. RUVBL1 appears notably required for the transforming activity of c-myc (Wood et al., 2000), beta-catenin (Feng et al., 2003) and of the viral oncoprotein E1A (Dugan et al., 2002).
RUVBL1 participates in the remodelling of chromatin as a member of several complexes such as TRRAP, several distinct HAT complexes and BAF53 (Wood et al., 2000; Park et al., 2002; Feng et al., 2003).
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).
RUVBL1 has a mitosis-specific function in regulating microtubule assembly (Ducat et al., 2008).
RUVBL1 has been found expressed on the cell surface where it participates in the activation of plasminogen (Hawley et al., 2001).