3.1.13.4: poly(A)-specific ribonuclease
This is an abbreviated version!
For detailed information about poly(A)-specific ribonuclease, go to the full flat file.
Word Map on EC 3.1.13.4
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3.1.13.4
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deadenylation
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polya-specific
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rna-binding
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decapping
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polyadenylation
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polya-binding
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nocturnin
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au-rich
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mirna-mediated
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telomere
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trim
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argonaute
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eif4e
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pirnas
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pumilio
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tristetraprolin
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cap-binding
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congenita
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exonucleolytic
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p-bodies
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dyskeratosis
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oligoadenylation
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pabps
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diagnostics
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miriscs
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poly-a
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are-binding
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microrna-mediated
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medicine
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eif4e-binding
- 3.1.13.4
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deadenylation
-
polya-specific
-
rna-binding
-
decapping
-
polyadenylation
-
polya-binding
- nocturnin
-
au-rich
-
mirna-mediated
-
telomere
-
trim
-
argonaute
- eif4e
-
pirnas
-
pumilio
- tristetraprolin
-
cap-binding
- congenita
-
exonucleolytic
-
p-bodies
-
dyskeratosis
-
oligoadenylation
-
pabps
- diagnostics
-
miriscs
- poly-a
-
are-binding
-
microrna-mediated
- medicine
-
eif4e-binding
Reaction
exonucleolytic cleavage of poly(A) to 5'-AMP =
Synonyms
2',3'-exoribonuclease, 3'-exoribonuclease, adenosine-specific exonuclease, AHG2, AtPARN, BTG1-binding factor 1, Caf1, CCR4, CCR4 deadenylase complex, CCR4-associated factor 1, Ccr4-Not complex, CCR4-NOT transcription complex subunit 7, Ccr4p/Pop2p/Notp complex, CNOT6L nuclease, cytoplasmic deadenylase, deadenylase, hPAN, HsPNLDC1, MMAR_3223, More, nuclease, polyadenylate-specific exoribo-, PAB1P-dependent poly(A)-nuclease, PAN, PAN2, PAN3, PARN, PARN-1, PARN-like domain-containing protein 1, PF2046, PNLDC1, poly(A) nuclease, poly(A) nuclease complex, poly(A) ribonuclease, poly(A)-selective ribonuclease, poly(A)-specific 3'-5' ribonuclease, poly(A)-specific 3'-exoribonuclease, poly(A)-specific mRNA exoribonuclease, poly(A)-specific ribonuclease, poly(A)-specific RNase, Pop2p deadenylase, RNase AS, RNase H
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3.1.13.4 poly(A)-specific ribonucleaseAdvanced search results
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Application on EC 3.1.13.4 - poly(A)-specific ribonuclease
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diagnostics
clinical significance of deadenylases PARN and NOC on the survival in SCC diagnosed patients
medicine
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leukemic cells from patients with acute lymphoblastic leukemia and acute myeloid leukemia display altered expression for CNOT6, CNOT6L, CNOT7 deadenylase and poly(A)-specific ribonuclease with most significant alterations for poly(A)-specific ribonuclease and CNOT7 mRNA levels. In acute lymphoblastic leukemia, a significant amount of poly(A)-specific ribonuclease is phosphorylated
additional information
additional information
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Mg2+ has dual effects on PARN stability, protecting the active site against denaturation, but destabilizing the overall structural stability of the protein
additional information
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R3H domain may stabilize PARN by acting as a protector or intermolecular chaperone of the RRM domain
additional information
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RRM motif of PARN harbors both poly(A) and cap binding properties, RRM plays an important role in PARN activity, i.e. recognition and dependence on both the cap structure and poly(A) tail during poly(A) hydrolysis. Trp475 plays an essential role in PARN cap recognition, whereas Glu455 and especially Trp456 play auxiliary roles. Cap binding is not essential for the hydrolytic activity of PARN. Cap and RNA-binding sites of the RRM are structurally and functionally separated from each other
additional information
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the entire RRM domain not only contributes to the substrate binding and efficient catalysis of PARN, but also stabilizes the overall structures of the protein. p46 contains only one Trp residue (W219), p54 contains two (W219 and W456), and p74 contains six (W219, W456, W474, W526, W531 and W639)
