RUVBL2

From Wikipedia, the free encyclopedia

RuvB-like 2 (E. coli)

PDB rendering based on 2cqa.

Available structures: 2cqa

Identifiers

Symbol(s)

RUVBL2; CGI-46; ECP51; RVB2; TIP48; TIP49B

External IDs

OMIM: 604788 MGI: 1342299 HomoloGene: 4856

Gene ontology
Molecular Function:	• nucleotide binding • damaged DNA binding • ATP-dependent DNA helicase activity • ATP binding • hydrolase activity • ATPase activity • identical protein binding • unfolded protein binding
Cellular Component:	• intracellular • nucleus • cytosol • NuA4 histone acetyltransferase complex
Biological Process:	• regulation of cell growth • DNA repair • DNA recombination • transcription • regulation of transcription, DNA-dependent • protein folding • chromatin modification

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006666 (mRNA)
NP_006657 (protein)

NM_011304 (mRNA)
NP_035434 (protein)

Location

Chr 19: 54.01 - 54.21 Mb

Chr 7: 45.29 - 45.31 Mb

Pubmed search

[1]

[2]

RuvB-like 2 (E. coli), also known as RUVBL2, is a human gene.

This gene encodes the second human homologue of the bacterial RuvB gene. Bacterial RuvB protein is a DNA helicase essential for homologous recombination and DNA double-strand break repair. Functional analysis showed that this gene product has both ATPase and DNA helicase activities. This gene is physically linked to the CGB/LHB gene cluster on chromosome 19q13.3, and is very close (55 nt) to the LHB gene, in the opposite orientation.^[1]

[edit] References

^ Entrez Gene: RUVBL2 RuvB-like 2 (E. coli).

[edit] Further reading

Doyon Y, Côté J (2004). "The highly conserved and multifunctional NuA4 HAT complex.". Curr. Opin. Genet. Dev. 14 (2): 147–54. doi:10.1016/j.gde.2004.02.009. PMID 15196461.
Kanemaki M, Kurokawa Y, Matsu-ura T, et al. (1999). "TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a.". J. Biol. Chem. 274 (32): 22437–44. PMID 10428817.
Salzer U, Kubicek M, Prohaska R (1999). "Isolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteins.". Biochim. Biophys. Acta 1446 (3): 365–70. PMID 10524211.
Lai CH, Chou CY, Ch'ang LY, et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics.". Genome Res. 10 (5): 703–13. PMID 10810093.
Wood MA, McMahon SB, Cole MD (2000). "An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc.". Mol. Cell 5 (2): 321–30. PMID 10882073.
Ikura T, Ogryzko VV, Grigoriev M, et al. (2000). "Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis.". Cell 102 (4): 463–73. PMID 10966108.
Parfait B, Giovangrandi Y, Asheuer M, et al. (2000). "Human TIP49b/RUVBL2 gene: genomic structure, expression pattern, physical link to the human CGB/LHB gene cluster on chromosome 19q13.3.". Ann. Genet. 43 (2): 69–74. PMID 10998447.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. PMID 11076863.
Bauer A, Chauvet S, Huber O, et al. (2001). "Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity.". EMBO J. 19 (22): 6121–30. doi:10.1093/emboj/19.22.6121. PMID 11080158.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMID 11256614.
Cho SG, Bhoumik A, Broday L, et al. (2001). "TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage.". Mol. Cell. Biol. 21 (24): 8398–413. doi:10.1128/MCB.21.24.8398-8413.2001. PMID 11713276.
Park J, Wood MA, Cole MD (2002). "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation.". Mol. Cell. Biol. 22 (5): 1307–16. PMID 11839798.
Ohta S, Shiomi Y, Sugimoto K, et al. (2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein.". J. Biol. Chem. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
Watkins NJ, Dickmanns A, Lührmann R (2003). "Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP.". Mol. Cell. Biol. 22 (23): 8342–52. PMID 12417735.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
Cai Y, Jin J, Tomomori-Sato C, et al. (2003). "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex.". J. Biol. Chem. 278 (44): 42733–6. doi:10.1074/jbc.C300389200. PMID 12963728.
Gstaiger M, Luke B, Hess D, et al. (2003). "Control of nutrient-sensitive transcription programs by the unconventional prefoldin URI.". Science 302 (5648): 1208–12. doi:10.1126/science.1088401. PMID 14615539.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.