RNASEH1

Protein-coding gene in the species Homo sapiens
RNASEH1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2QK9, 2QKB, 2QKK, 3BSU

Identifiers
AliasesRNASEH1, H1RNA, RNH1, PEOB2, ribonuclease H1
External IDsOMIM: 604123; MGI: 1335073; HomoloGene: 2202; GeneCards: RNASEH1; OMA:RNASEH1 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for RNASEH1
Genomic location for RNASEH1
Band2p25.3Start3,541,430 bp[1]
End3,558,333 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for RNASEH1
Genomic location for RNASEH1
Band12|12 A2Start28,699,601 bp[2]
End28,709,588 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • endothelial cell

  • middle temporal gyrus

  • nipple

  • visceral pleura

  • parietal pleura

  • tibia

  • Brodmann area 23

  • cerebellar vermis

  • saphenous vein
Top expressed in
  • Paneth cell

  • saccule

  • otic placode

  • secondary oocyte

  • primitive streak

  • morula

  • medullary collecting duct

  • yolk sac

  • spermatocyte

  • facial motor nucleus
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • nuclease activity
  • endonuclease activity
  • RNA-DNA hybrid ribonuclease activity
  • ribonuclease activity
  • hydrolase activity
  • magnesium ion binding
  • metal ion binding
  • RNA binding
  • nucleic acid binding
Cellular component
  • cytoplasm
  • nucleus
Biological process
  • nucleic acid phosphodiester bond hydrolysis
  • RNA catabolic process
  • DNA replication, removal of RNA primer
  • RNA phosphodiester bond hydrolysis
  • RNA phosphodiester bond hydrolysis, endonucleolytic
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

246243

19819

Ensembl

ENSG00000171865

ENSMUSG00000020630

UniProt

O60930

E9QLN8

RefSeq (mRNA)
NM_001286834
NM_001286837
NM_002936
NM_001378271
NM_001378272

NM_001378273

NM_001286865
NM_011275

RefSeq (protein)
NP_001273763
NP_001273766
NP_002927
NP_001365200
NP_001365201

NP_001365202

NP_001273794
NP_035405

Location (UCSC)Chr 2: 3.54 – 3.56 MbChr 12: 28.7 – 28.71 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ribonuclease H1 also known as RNase H1 is an enzyme that in humans is encoded by the RNASEH1 gene.[5][6][7] The RNase H1 is a non-specific endonuclease and catalyzes the cleavage of RNA via a hydrolytic mechanism.

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171865 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020630 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: ribonuclease H1".
  6. ^ ten Asbroek AL, van Groenigen M, Jakobs ME, Koevoets C, Janssen B, Baas F (June 2002). "Ribonuclease H1 maps to chromosome 2 and has at least three pseudogene loci in the human genome". Genomics. 79 (6): 818–23. doi:10.1006/geno.2002.6776. PMID 12036296.
  7. ^ Nowotny M, Gaidamakov SA, Ghirlando R, Cerritelli SM, Crouch RJ, Yang W (October 2007). "Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription". Mol. Cell. 28 (2): 264–76. doi:10.1016/j.molcel.2007.08.015. PMID 17964265.

Further reading

  • Nowotny M, Cerritelli SM, Ghirlando R, et al. (2008). "Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD". EMBO J. 27 (7): 1172–81. doi:10.1038/emboj.2008.44. PMC 2323259. PMID 18337749.
  • Lima WF, Wu H, Nichols JG, et al. (2003). "Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate". J. Biol. Chem. 278 (50): 49860–7. doi:10.1074/jbc.M306543200. PMID 14506260.
  • Lima WF, Rose JB, Nichols JG, et al. (2007). "The positional influence of the helical geometry of the heteroduplex substrate on human RNase H1 catalysis". Mol. Pharmacol. 71 (1): 73–82. doi:10.1124/mol.106.025429. PMID 17028157. S2CID 27765676.
  • Lima WF, Nichols JG, Wu H, et al. (2004). "Structural requirements at the catalytic site of the heteroduplex substrate for human RNase H1 catalysis". J. Biol. Chem. 279 (35): 36317–26. doi:10.1074/jbc.M405035200. PMID 15205459.
  • Otsuki T, Ota T, Nishikawa T, et al. (2005). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
  • Wu H, Lima WF, Crooke ST (1999). "Properties of cloned and expressed human RNase H1". J. Biol. Chem. 274 (40): 28270–8. doi:10.1074/jbc.274.40.28270. PMID 10497183.
  • Frank P, Braunshofer-Reiter C, Pöltl A, Holzmann K (1998). "Cloning, subcellular localization and functional expression of human RNase HII". Biol. Chem. 379 (12): 1407–12. doi:10.1515/bchm.1998.379.12.1407. PMID 9894807. S2CID 19692186.
  • Wu H, Lima WF, Zhang H, et al. (2004). "Determination of the role of the human RNase H1 in the pharmacology of DNA-like antisense drugs". J. Biol. Chem. 279 (17): 17181–9. doi:10.1074/jbc.M311683200. PMID 14960586.
  • Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
  • Lima WF, Wu H, Nichols JG, et al. (2003). "Human RNase H1 activity is regulated by a unique redox switch formed between adjacent cysteines". J. Biol. Chem. 278 (17): 14906–12. doi:10.1074/jbc.M211279200. PMID 12473655.
  • ten Asbroek AL, van Groenigen M, Nooij M, Baas F (2002). "The involvement of human ribonucleases H1 and H2 in the variation of response of cells to antisense phosphorothioate oligonucleotides". Eur. J. Biochem. 269 (2): 583–92. doi:10.1046/j.0014-2956.2001.02686.x. PMID 11856317.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • 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.
  • Cerritelli SM, Crouch RJ (1998). "Cloning, expression, and mapping of ribonucleases H of human and mouse related to bacterial RNase HI". Genomics. 53 (3): 300–7. doi:10.1006/geno.1998.5497. PMID 9799596.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Cerritelli SM, Frolova EG, Feng C, et al. (2003). "Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice". Mol. Cell. 11 (3): 807–15. doi:10.1016/S1097-2765(03)00088-1. PMID 12667461.
  • Lima WF, Rose JB, Nichols JG, et al. (2007). "Human RNase H1 discriminates between subtle variations in the structure of the heteroduplex substrate". Mol. Pharmacol. 71 (1): 83–91. doi:10.1124/mol.106.025015. PMID 17028158. S2CID 24995048.

External links

  • Overview of all the structural information available in the PDB for UniProt: O60930 (Human Ribonuclease H1 (RNASEH1)) at the PDBe-KB.
  • v
  • t
  • e
3.1.1: Carboxylic
ester hydrolases3.1.2: Thioesterase3.1.3: Phosphatase3.1.4:
Phosphodiesterase3.1.6: SulfataseNuclease (includes
deoxyribonuclease
and ribonuclease)
3.1.11-16:
Exonuclease
Exodeoxyribonuclease
Exoribonuclease
3.1.21-31:
Endonuclease
Endodeoxyribonuclease
Endoribonuclease
either deoxy- or ribo-    
  • v
  • t
  • e
Initiation
Prokaryotic
(initiation)
Eukaryotic
(preparation in
G1 phase)
Both
Replication
Prokaryotic
(elongation)
Eukaryotic
(synthesis in
S phase)
Both
Termination


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