RUVBL1 (RuvB-like 1 (E. coli))

2009-03-01   Valérie Haurie  , Aude Grigoletto  , Jean Rosenbaum  

INSERM U889, Universite Victor Segalen Bordeaux 2, 146 rue Leo Saignat, 33076 Bordeaux, France

Identity

HGNC
LOCATION
3q21.3
LOCUSID
ALIAS
ECP-54,ECP54,INO80H,NMP
FUSION GENES

DNA/RNA

Description

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

Transcription

1785bp mRNA.

Proteins

Atlas Image

Description

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

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).

Localisation

Cytoplasm and nucleus.

Function

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).

Implicated in

Entity name
Colon cancer
Disease
By immunohistochemistry, RUVBL1 expression was found higher in 22 out of 26 cases where information was available (Lauscher et al., 2007). The staining was increased at the invasive margin of the tumors. Increased RUVBL1 transcripts levels were also reported in a smaller series (Carlson et al., 2003).
Disease
Microarray analysis has identified an overexpression of RUVBL1 in Advanced lymphomas as compared with localized lymphomas (Nishiu et al., 2002).
Entity name
Non Small cell lung cancer
Disease
Microarray analysis and subsequent RT-PCR have shown an overexpression of RUVBL1 in NSCLC (Dehan et al., 2007).
Cytogenetics
There is a frequent amplification of 3q21 in the same samples (Dehan et al., 2007).
Entity name
Hepatocellular carcinoma
Disease
Proteomic analysis found an overexpression of RUVBL1 in 4 out of 10 cases (Li et al., 2005).
Entity name
Autoimmune diseases
Disease
Auto-antibodies to RUVBL1 were found in the serum of patients with polymyositis/dermatomyositis and autoimmune hepatitis (Makino et al., 1998).

Article Bibliography

Pubmed IDLast YearTitleAuthors

Other Information

Locus ID:

NCBI: 8607
MIM: 603449
HGNC: 10474
Ensembl: ENSG00000175792

Variants:

dbSNP: 8607
ClinVar: 8607
TCGA: ENSG00000175792
COSMIC: RUVBL1

RNA/Proteins

Gene IDTranscript IDUniprot
ENSG00000175792ENST00000322623Q9Y265
ENSG00000175792ENST00000322623A0A384MTR5
ENSG00000175792ENST00000464873E7ETR0
ENSG00000175792ENST00000472125H7C4I3
ENSG00000175792ENST00000478892H7C4G5
ENSG00000175792ENST00000585057J3QLR1

Expression (GTEx)

0
10
20
30
40
50
60
70

Pathways

PathwaySourceExternal ID
Wnt signaling pathwayKEGGko04310
Wnt signaling pathwayKEGGhsa04310
Metabolism of proteinsREACTOMER-HSA-392499
Post-translational protein modificationREACTOMER-HSA-597592
Signal TransductionREACTOMER-HSA-162582
Signaling by WntREACTOMER-HSA-195721
TCF dependent signaling in response to WNTREACTOMER-HSA-201681
Formation of the beta-catenin:TCF transactivating complexREACTOMER-HSA-201722
Cell CycleREACTOMER-HSA-1640170
Chromosome MaintenanceREACTOMER-HSA-73886
Nucleosome assemblyREACTOMER-HSA-774815
Deposition of new CENPA-containing nucleosomes at the centromereREACTOMER-HSA-606279
Telomere MaintenanceREACTOMER-HSA-157579
Extension of TelomeresREACTOMER-HSA-180786
Telomere Extension By TelomeraseREACTOMER-HSA-171319
DNA RepairREACTOMER-HSA-73894
Chromatin organizationREACTOMER-HSA-4839726
Chromatin modifying enzymesREACTOMER-HSA-3247509
HATs acetylate histonesREACTOMER-HSA-3214847
Nucleotide Excision RepairREACTOMER-HSA-5696398
Global Genome Nucleotide Excision Repair (GG-NER)REACTOMER-HSA-5696399
DNA Damage Recognition in GG-NERREACTOMER-HSA-5696394
DeubiquitinationREACTOMER-HSA-5688426
UCH proteinasesREACTOMER-HSA-5689603
Ub-specific processing proteasesREACTOMER-HSA-5689880

Protein levels (Protein atlas)

Not detected
Low
Medium
High

References

Pubmed IDYearTitleCitations
370757452023Epigenetic Control of Translation Checkpoint and Tumor Progression via RUVBL1-EEF1A1 Axis.9
373498842023Downregulation of AHNAK2 inhibits cell cycle of lung adenocarcinoma cells by interacting with RUVBL1.1
375411872023Combined CRISPRi and proteomics screening reveal a cohesin-CTCF-bound allele contributing to increased expression of RUVBL1 and prostate cancer progression.3
379623552023Adenovirus E1A binding to DCAF10 targets proteasomal degradation of RUVBL1/2 AAA+ ATPases required for quaternary assembly of multiprotein machines, innate immunity, and responses to metabolic stress.0
370757452023Epigenetic Control of Translation Checkpoint and Tumor Progression via RUVBL1-EEF1A1 Axis.9
373498842023Downregulation of AHNAK2 inhibits cell cycle of lung adenocarcinoma cells by interacting with RUVBL1.1
375411872023Combined CRISPRi and proteomics screening reveal a cohesin-CTCF-bound allele contributing to increased expression of RUVBL1 and prostate cancer progression.3
379623552023Adenovirus E1A binding to DCAF10 targets proteasomal degradation of RUVBL1/2 AAA+ ATPases required for quaternary assembly of multiprotein machines, innate immunity, and responses to metabolic stress.0
350781952022The Expression of the RUVBL1 Component of the R2TP Complex Correlates with Poor Prognosis in DLBCL.1
354932942022Involvement of RUVBL1 in WNT/β-Catenin Signaling in Oral Squamous Cell Carcinoma.5
355085422022RUVBL1 promotes enzalutamide resistance of prostate tumors through the PLXNA1-CRAF-MAPK pathway.9
361533262022Recruitment of LEF1 by Pontin chromatin modifier amplifies TGFBR2 transcription and activates TGFβ/SMAD signalling during gliomagenesis.1
364384862022Hippocalcin-Like 1 blunts liver lipid metabolism to suppress tumorigenesis via directly targeting RUVBL1-mTOR signaling.4
350781952022The Expression of the RUVBL1 Component of the R2TP Complex Correlates with Poor Prognosis in DLBCL.1
354932942022Involvement of RUVBL1 in WNT/β-Catenin Signaling in Oral Squamous Cell Carcinoma.5

Citation

Valérie Haurie ; Aude Grigoletto ; Jean Rosenbaum

RUVBL1 (RuvB-like 1 (E. coli))

Atlas Genet Cytogenet Oncol Haematol. 2009-03-01

Online version: http://atlasgeneticsoncology.org/gene/44415/deep-insight-explorer/favicon/cancer-prone-explorer/