DHX58

DEXH (Asp-Glu-X-His) box polypeptide 58
Rendering based on PDB 2RQA.
Available structures PDB 2RQA, 2W4R, 3EQT
Identifiers
Symbols	DHX58; D11LGP2; D11lgp2e; LGP2
External IDs	OMIM: 608588 MGI: 1931560 HomoloGene: 69371 GeneCards: DHX58 Gene
EC number	3.6.4.13
Gene Ontology Molecular function • nucleotide binding • DNA binding • RNA binding • helicase activity • protein binding • ATP binding • zinc ion binding • hydrolase activity, acting on acid anhydrides • metal ion binding Cellular component • cytoplasm Biological process • innate immune response Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	79132	80861
Ensembl	ENSG00000108771	ENSMUSG00000017830
UniProt	Q96C10	Q3U606
RefSeq (mRNA)	NM_024119	NM_030150.2
RefSeq (protein)	NP_077024	NP_084426.2
Location (UCSC)	Chr 17: 40.25 – 40.26 Mb	Chr 11: 100.56 – 100.57 Mb
PubMed search	[1]	[2]

Probable ATP-dependent RNA helicase DHX58, also called LGP2 (Laboratory of Genetics and Physiology 2), is an enzyme that in humans is encoded by the DHX58 gene.^[1][2] It is speculated that LGP2 is a negative regulator of host innate immune defense against viruses. The repressor domain of DHX58 interacts with DDX58 and negatively regulates DDX58-mediated signaling. Binds dsRNA produced during viral replication, in particuliar Hepatitis C Virus RNA. ^[3]

References

1. ^ Cui Y, Li M, Walton KD, Sun K, Hanover JA, Furth PA, Hennighausen L (Dec 2001). "The Stat3/5 locus encodes novel endoplasmic reticulum and helicase-like proteins that are preferentially expressed in normal and neoplastic mammary tissue". Genomics 78 (3): 129–34. doi:10.1006/geno.2001.6661. PMID 11735219. 
2. ^ "Entrez Gene: LGP2 likely ortholog of mouse D11lgp2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79132. 
3. ^ "Probable ATP-dependent RNA helicase DHX58 - Homo sapiens (Human)". http://www.uniprot.org/uniprot/Q96C10#section_comments. 

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. 
• Yoneyama M, Kikuchi M, Matsumoto K, et al. (2005). "Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity.". J. Immunol. 175 (5): 2851–8. PMID 16116171. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Komuro A, Horvath CM (2007). "RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2.". J. Virol. 80 (24): 12332–42. doi:10.1128/JVI.01325-06. PMC 1676302. PMID 17020950. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1676302.