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Information on EC 3.1.13.1 - exoribonuclease II and Organism(s) Homo sapiens and UniProt Accession Q9H0D6

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.13 Exoribonucleases producing 5′-phosphomonoesters
                3.1.13.1 exoribonuclease II
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Homo sapiens
UNIPROT: Q9H0D6 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
rnase, exoribonuclease, rnase r, rnase ii, rrp44, rnase 2, ribonuclease r, rnaser, ribonuclease 2, rc-rnase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'->3' exoribonuclease 2
-
3’-5’exoribonuclease
-
-
Dis3
-
-
exonuclease ISG20
-
-
ribonuclease 2
-
-
ribonuclease II
ribonuclease Q
-
-
-
-
RNase
-
-
RNase 2
-
-
RNase II
-
-
Rrp44
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates
show the reaction diagram
acts in a processive manner
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-24-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
duplex RNA + H2O
?
show the reaction diagram
-
-
-
-
?
mRNA + H2O
5'-phosphomononucleotide
show the reaction diagram
-
-
-
-
?
mRNA + H2O
5'-phosphomononucleotides
show the reaction diagram
oligoribonucleotide + H2O
?
show the reaction diagram
-
final end product of Rrp44 is 4-nt
-
-
?
poly(A) + H2O
5'-AMP + oligonucleotide
show the reaction diagram
poly(A) + H2O
?
show the reaction diagram
-
-
-
-
?
poly(C) + H2O
5'-CMP + oligonucleotide
show the reaction diagram
-
-
-
?
siRNA + H2O
?
show the reaction diagram
-
with 2-nt 3' overhangs
-
-
?
ss RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
tRNA
?
show the reaction diagram
-
tRNA from Escherichia coli
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ss RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
additional information
?
-
interactions between NKRF, 5'->3' exoribonuclease 2 (XRN2) and the negative elongation factor (NELF)-E in HeLa cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
required for activity
Mn2+
-
can partially replace Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
-
a salt concentration of 0.05 M inhibits 50% of the activity, salt optimum: 0.01 M
poly(A) binding protein
-
inhibits degradation of poly(A)+-strands
-
RNA with a terminal 3'-phosphate group
-
on the potential substrate molecule
ss DNA oligonucleotides
-
-
-
additional information
-
not inhibited by RNase A-type inhibitor
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
NaCl
-
salt 0.01 M
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
-
substrate: poly(A)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
strong interaction between NKRF-TAP and endogenous XRN2 in HeLa cells
Manually annotated by BRENDA team
-
T-lymphoblastoid
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
DFC region
Manually annotated by BRENDA team
additional information
-
Cajal bodies
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
NF-kappaB-repressing factor phosphorylation regulates transcription elongation via its interactions with 5'->3' exoribonuclease 2 and negative elongation factor. Interleukin-1 has a more drastic effect on NELF-E or XRN2 binding to NKRF than the M1 mutation
physiological function
interactions between NKRF, 5'->3' exoribonuclease 2 (XRN2) and the negative elongation factor (NELF)-E in HeLa cells. Interleukin IL-1 stimulation leads to decrease in NKRF amino acids 421-429 phosphorylation and dissociation of NELF-E and XRN2 by concomitant resumption of transcription elongation of a synthetic reporter or the endogenous NKRF target gene, interleukin IL-8. 5'->3' exoribonuclease 2 (XRN2) is implicated in inhibition of transcription elongation via the termination of initiated transcripts in many RNA Pol II-dependent promoters
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XRN2_HUMAN
950
0
108582
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
SDS-PAGE
37000
-
native state gel filtration
67000
-
1 * 67000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 67000
additional information
-
human Rrp44 proteins shows an overall structure similar to that of Escherichia coli RNase II
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C425A
-
cannot be classified as polymorphic in the Japanese population. In the Korean, Mongolian, Ovambo, Turkish, and German DNA no genotype other than homozygotic 425C allele in RNASE2 at each single nucleotide polymorphism site is found
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
for 1 min completely destroys enzyme activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10-ml fractions containing 1 mg trypsin inhibitor carrier protein because RNase II loses activity under this conditions at protein concentrations below 0.1 mg/ml
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
5300-26500fold, to homogeneity
-
partial purification, 500-700fold
-
purified by inmunoprecipitation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA fragments corresponding to the entire open reading frame in each gene are subcloned into a TA cloning vector
-
expressed in Escherichia coli strain BL21(DE3)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
new factor in the IFN-mediated antiviral barrier against HIV-1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ning Kwan, C.
A cytoplasmic exoribonuclease from HeLa cells
Biochim. Biophys. Acta
479
322-331
1977
Homo sapiens
Manually annotated by BRENDA team
Caruccio, N.; Ross, J.
Purification of a human polyribosome-associated 3'-5'exoribonuclease
J. Biol. Chem.
269
31814-31821
1994
Homo sapiens
Manually annotated by BRENDA team
Jiang, T.; Altman, S.
A protein subunit of human RNase P, Rpp14, and its interacting partner, OIP2, have 3'->5' exoribonuclease activity
Proc. Natl. Acad. Sci. USA
99
5295-5300
2002
Homo sapiens
Manually annotated by BRENDA team
Espert, L.; Eldin, P.; Gongora, C.; Bayard, B.; Harper, F.; Chelbi-Alix, M.K.; Bertrand, E.; Degols, G.; Mechti, N.
The exonuclease ISG20 mainly localizes in the nucleolus and the Cajal (Coiled) bodies and is associated with nuclear SMN protein-containing complexes
J. Cell. Biochem.
98
1320-1333
2006
Homo sapiens
Manually annotated by BRENDA team
Espert, L.; Degols, G.; Lin, Y.L.; Vincent, T.; Benkirane, M.; Mechti, N.
Interferon-induced exonuclease ISG20 exhibits an antiviral activity against human immunodeficiency virus type 1
J. Gen. Virol.
86
2221-2229
2005
Homo sapiens
Manually annotated by BRENDA team
Kennedy, S.; Wang, D.; Ruvkun, G.
A conserved siRNA-degrading RNase negatively regulates RNA interference in C. elegans
Nature
427
645-649
2004
Caenorhabditis elegans, Homo sapiens
Manually annotated by BRENDA team
Bollenbach, T.J.; Schuster, G.; Stern, D.B.
Cooperation of endo- and exoribonucleases in chloroplast mRNA turnover
Prog. Nucleic Acid Res. Mol. Biol.
78
305-337
2004
Synechocystis sp., Saccharomyces cerevisiae, Caenorhabditis elegans, Chlamydomonas sp., Drosophila sp. (in: flies), Escherichia coli, Haloferax volcanii, Embryophyta, Homo sapiens, Mammalia, no activity in archaebacteria, Streptomyces coelicolor, uncultured Gammaproteobacteria bacterium
Manually annotated by BRENDA team
Barbas, A.; Matos, R.G.; Amblar, M.; Lpez-Vinas, E.; Gomez-Puertas, P.; Arraiano, C.M.
New insights into the mechanism of RNA degradation by ribonuclease II identification of the residue responsible for setting the RNase II end product
J. Biol. Chem.
283
13070-13076
2008
Homo sapiens, Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
Ueki, M.; Takeshita, H.; Fujihara, J.; Takatsuka, H.; Yuasa, I.; Iida, R.; Yasuda, T.
Three single nucleotide polymorphisms leading to non-synonymous amino acid substitution in the human ribonuclease 2 and angiogenin genes exhibit markedly less genetic heterogeneity in six populations
Cell Biochem. Funct.
26
718-722
2008
Homo sapiens
Manually annotated by BRENDA team
Rother, S.; Bartels, M.; Schweda, A.T.; Resch, K.; Pallua, N.; Nourbakhsh, M.
NF-kappaB-repressing factor phosphorylation regulates transcription elongation via its interactions with 5'->3' exoribonuclease 2 and negative elongation factor
FASEB J.
30
174-185
2016
Homo sapiens (Q9H0D6)
Manually annotated by BRENDA team