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NameRibonuclease H1
Synonyms
  • 3.1.26.4
  • Ribonuclease H type II
  • RNase H1
  • RNH1
Gene NameRNASEH1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0013656|Ribonuclease H1
MSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKK
FATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKP
SVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQ
TNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVIN
KEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED
Number of residues286
Molecular Weight32064.035
Theoretical pINot Available
GO Classification
Functions
  • nucleic acid binding
  • RNA binding
  • magnesium ion binding
  • ribonuclease activity
  • RNA-DNA hybrid ribonuclease activity
Processes
  • RNA phosphodiester bond hydrolysis
  • RNA phosphodiester bond hydrolysis, endonucleolytic
  • DNA replication, removal of RNA primer
  • RNA catabolic process
Components
  • mitochondrion
General FunctionRna-dna hybrid ribonuclease activity
Specific FunctionEndonuclease that specifically degrades the RNA of RNA-DNA hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II (PubMed:21700224).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDO60930
UniProtKB Entry NameRNH1_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0013657|Ribonuclease H1 (RNASEH1)
ATGTTCTATGCCGTGAGGAGGGGCCGCAAGACCGGGGTCTTTCTGACCTGGAATGAGTGC
AGAGCACAGGTGGACCGGTTTCCTGCTGCCAGATTTAAGAAGTTTGCCACAGAGGATGAG
GCCTGGGCCTTTGTCAGGAAATCTGCAAGCCCGGAAGTTTCAGAAGGGCATGAAAATCAA
CATGGACAAGAATCGGAGGCGAAAGCCAGCAAGCGACTCCGTGAGCCACTGGATGGAGAT
GGACATGAAAGCGCAGAGCCGTATGCAAAGCACATGAAGCCGAGCGTGGAGCCGGCGCCT
CCAGTTAGCAGAGACACGTTTTCCTACATGGGAGACTTCGTCGTCGTCTACACTGATGGC
TGCTGCTCCAGTAATGGGCGTAGAAGGCCGCGAGCAGGAATCGGCGTTTACTGGGGGCCA
GGCCATCCTTTAAATGTAGGCATTAGACTTCCTGGGCGGCAGACAAACCAAAGAGCGGAA
ATTCATGCAGCCTGCAAAGCCATTGAACAAGCAAAGACTCAAAACATCAATAAACTGGTT
CTGTATACAGACAGTATGTTTACGATAAATGGTATAACTAACTGGGTTCAAGGTTGGAAG
AAAAATGGGTGGAAGACAAGTGCAGGGAAAGAGGTGATCAACAAAGAGGACTTTGTGGCA
CTGGAGAGGCTTACCCAGGGGATGGACATTCAGTGGATGCATGTTCCTGGTCATTCGGGA
TTTATAGGCAATGAAGAAGCTGACAGATTAGCCAGAGAAGGAGCTAAACAATCGGAAGAC
TGA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:18466
Chromosome Location2
LocusNot Available
References
  1. Cerritelli SM, Crouch RJ: Cloning, expression, and mapping of ribonucleases H of human and mouse related to bacterial RNase HI. Genomics. 1998 Nov 1;53(3):300-7. 9799596
  2. Wu H, Lima WF, Crooke ST: Molecular cloning and expression of cDNA for human RNase H. Antisense Nucleic Acid Drug Dev. 1998 Feb;8(1):53-61. 9512096
  3. Frank P, Braunshofer-Reiter C, Poltl A, Holzmann K: Cloning, subcellular localization and functional expression of human RNase HII. Biol Chem. 1998 Dec;379(12):1407-12. 9894807
  4. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: 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. 2005;12(2):117-26. 16303743
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  7. Wu H, Lima WF, Crooke ST: Properties of cloned and expressed human RNase H1. J Biol Chem. 1999 Oct 1;274(40):28270-8. 10497183
  8. Skourti-Stathaki K, Proudfoot NJ, Gromak N: Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination. Mol Cell. 2011 Jun 24;42(6):794-805. doi: 10.1016/j.molcel.2011.04.026. 21700224
  9. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. 21406692
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