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Search results 101 to 185 out of 185 for Parn

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Hits by Strain

Type Details Score
Gene
428595 | PNLDC1
Type: gene
Organism: chicken
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Gene
707835 | PNLDC1
Type: gene
Organism: macaque, rhesus
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Protein
Q8VDG3
Organism: Mus musculus/domesticus
Length: 624  
Fragment?: false
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Protein
Q3TUQ8
Organism: Mus musculus/domesticus
Length: 624  
Fragment?: false
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Protein
A0A0R4J0P6
Organism: Mus musculus/domesticus
Length: 624  
Fragment?: false
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Protein
A0A2R8VHG7
Organism: Mus musculus/domesticus
Length: 82  
Fragment?: false
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Protein
A0A2R8VKA3
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
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Publication
16601207 | -
First Author: Moraes KC
Year: 2006
Journal: RNA
Title: CUG-BP binds to RNA substrates and recruits PARN deadenylase.
Volume: 12
Issue: 6
Pages: 1084-91
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Publication
15247430 | -
First Author: Reverdatto SV
Year: 2004
Journal: RNA
Title: mRNA deadenylation by PARN is essential for embryogenesis in higher plants.
Volume: 10
Issue: 8
Pages: 1200-14
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DO Term
DOID:0070024 | autosomal recessive dyskeratosis congenita 6
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Publication
36733269 | J:333029
 
First Author: Pärn A
Year: 2022
Journal: Front Mol Neurosci
Title: PCSK9 deficiency alters brain lipid composition without affecting brain development and function.
Volume: 15
Pages: 1084633
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Publication
9736620 | -
First Author: Körner CG
Year: 1998
Journal: EMBO J
Title: The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes.
Volume: 17
Issue: 18
Pages: 5427-37
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Protein Domain
IPR014789 | PolyA-riboNase_RNA-binding
Type: Domain
Description: This domain corresponds to the RNA binding domain of Poly(A)-specific ribonuclease (PARN). PARN is a 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails [].
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Publication
22442037 | -
First Author: Berndt H
Year: 2012
Journal: RNA
Title: Maturation of mammalian H/ACA box snoRNAs: PAPD5-dependent adenylation and PARN-dependent trimming.
Volume: 18
Issue: 5
Pages: 958-72
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Publication
25049417 | -
First Author: Boele J
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: PAPD5-mediated 3' adenylation and subsequent degradation of miR-21 is disrupted in proliferative disease.
Volume: 111
Issue: 31
Pages: 11467-72
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Protein Domain
IPR040136 | TENT4B
Type: Family
Description: TENT4B, also known as PAPD5, is a noncanonical poly(A) polymerase that contains a C-terminal RNA binding domain []. It is responsible for addition of the oligo(A) tails of H/ACA box snoRNA followed by its 3'-to-5' trimming by the exoribonuclease PARN which enhances snoRNA stability and maturation [, ]. Together with the poly(A)-specific ribonuclease PARN, PAPD5 is involved in miR-21 degradation [].
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Publication
16281054 | -
First Author: Wu M
Year: 2005
Journal: EMBO J
Title: Structural insight into poly(A) binding and catalytic mechanism of human PARN.
Volume: 24
Issue: 23
Pages: 4082-93
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Publication
17624302 | -
First Author: Liu WF
Year: 2007
Journal: Biochem Biophys Res Commun
Title: The R3H domain stabilizes poly(A)-specific ribonuclease by stabilizing the RRM domain.
Volume: 360
Issue: 4
Pages: 846-51
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Publication
11424938 | -
First Author: Copeland PR
Year: 2001
Journal: RNA
Title: The mechanism and regulation of deadenylation: identification and characterization of Xenopus PARN.
Volume: 7
Issue: 6
Pages: 875-86
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Protein Domain
IPR034042 | PARN_R3H
Type: Domain
Description: This is the R3H domain of Poly(A)-specific ribonuclease (PARN). PARN is a poly(A)-specific 3' exonuclease from the RNase D family which, in Xenopus deadenylates a specific class of maternal mRNAs that results in their translational repression [, , ]. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA [].
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Publication
32320679 | J:355247
First Author: Nagpal N
Year: 2020
Journal: Cell Stem Cell
Title: Small-Molecule PAPD5 Inhibitors Restore Telomerase Activity in Patient Stem Cells.
Volume: 26
Issue: 6
Pages: 896-909.e8
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Publication
26942679 | J:237091
First Author: Bukhari SIA
Year: 2016
Journal: Mol Cell
Title: A Specialized Mechanism of Translation Mediated by FXR1a-Associated MicroRNP in Cellular Quiescence.
Volume: 61
Issue: 5
Pages: 760-773
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Publication
27515512 | J:239185
First Author: Anastasakis D
Year: 2016
Journal: Nucleic Acids Res
Title: Mammalian PNLDC1 is a novel poly(A) specific exonuclease with discrete expression during early development.
Volume: 44
Issue: 18
Pages: 8908-8920
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Publication
28053121 | J:249961
First Author: Anantharaman A
Year: 2017
Journal: Nucleic Acids Res
Title: ADAR2 regulates RNA stability by modifying access of decay-promoting RNA-binding proteins.
Volume: 45
Issue: 7
Pages: 4189-4201
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Publication
31749682 | J:310663
 
First Author: Baquero J
Year: 2019
Journal: Front Mol Neurosci
Title: Nuclear Tau, p53 and Pin1 Regulate PARN-Mediated Deadenylation and Gene Expression.
Volume: 12
Pages: 242
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Publication
15215893 | -
First Author: Temme C
Year: 2004
Journal: EMBO J
Title: A complex containing the CCR4 and CAF1 proteins is involved in mRNA deadenylation in Drosophila.
Volume: 23
Issue: 14
Pages: 2862-71
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Publication
15769875 | -
First Author: Bianchin C
Year: 2005
Journal: RNA
Title: Conservation of the deadenylase activity of proteins of the Caf1 family in human.
Volume: 11
Issue: 4
Pages: 487-94
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Publication
23388391 | -
First Author: He GJ
Year: 2013
Journal: Biochim Biophys Acta
Title: Distinct roles of the R3H and RRM domains in poly(A)-specific ribonuclease structural integrity and catalysis.
Volume: 1834
Issue: 6
Pages: 1089-98
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Publication
20379136 | -
First Author: Cevher MA
Year: 2010
Journal: EMBO J
Title: Nuclear deadenylation/polyadenylation factors regulate 3' processing in response to DNA damage.
Volume: 29
Issue: 10
Pages: 1674-87
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Protein Domain
IPR006941 | RNase_CAF1
Type: Family
Description: The major pathways of mRNA turnover in eukaryotes initiate with shortening of the poly(A) tail. CAF1 (also known as CCR4-associated factor 1) is an RNase of the DEDD superfamily, and a subunit of the CCR4-NOT complex that mediates 3' to 5' mRNA deadenylation [, ]. In yeast, CAF1 () is also known as POP2, and encodes a critical component of the major cytoplasmic deadenylase [, ]. It is required for normal mRNA deadenylation in vivoand localises to the cytoplasm. CAF1 copurifies with a CCR4-dependent poly(A)-specific exonuclease activity. The crystal structure of Saccharomyces cerevisiae POP2 has been resolved [].Some members of this family contain a single-stranded nucleic acid binding domain, R3H, such aspoly(A)-specific ribonuclease (PARN), which also contains an RRM domain []. PARN is only conserved in vertebrates and may be important in regulated deadenylation such as early developmentand DNA damage response [, ].
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Publication
14618157 | -
First Author: Thore S
Year: 2003
Journal: EMBO Rep
Title: X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex.
Volume: 4
Issue: 12
Pages: 1150-5
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Publication
11410650 | -
First Author: Daugeron MC
Year: 2001
Journal: Nucleic Acids Res
Title: The yeast POP2 gene encodes a nuclease involved in mRNA deadenylation.
Volume: 29
Issue: 12
Pages: 2448-55
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Protein
F6UPY1
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Publication
21788334 | -
First Author: Rammelt C
Year: 2011
Journal: RNA
Title: PAPD5, a noncanonical poly(A) polymerase with an unusual RNA-binding motif.
Volume: 17
Issue: 9
Pages: 1737-46
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Publication
30026317 | -
First Author: Lim J
Year: 2018
Journal: Science
Title: Mixed tailing by TENT4A and TENT4B shields mRNA from rapid deadenylation.
Volume: 361
Issue: 6403
Pages: 701-704
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Publication
8948631 | -
First Author: Timchenko LT
Year: 1996
Journal: Nucleic Acids Res
Title: Identification of a (CUG)n triplet repeat RNA-binding protein and its expression in myotonic dystrophy.
Volume: 24
Issue: 22
Pages: 4407-14
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Publication
16862542 | -
First Author: Leroy O
Year: 2006
Journal: J Neurosci Res
Title: ETR-3 represses Tau exons 2/3 inclusion, a splicing event abnormally enhanced in myotonic dystrophy type I.
Volume: 84
Issue: 4
Pages: 852-9
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Publication
11124939 | -
First Author: Timchenko NA
Year: 2001
Journal: J Biol Chem
Title: RNA CUG repeats sequester CUGBP1 and alter protein levels and activity of CUGBP1.
Volume: 276
Issue: 11
Pages: 7820-6
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Publication
18267972 | -
First Author: Graindorge A
Year: 2008
Journal: Nucleic Acids Res
Title: Identification of CUG-BP1/EDEN-BP target mRNAs in Xenopus tropicalis.
Volume: 36
Issue: 6
Pages: 1861-70
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Publication
16836486 | -
First Author: Cosson B
Year: 2006
Journal: Biol Cell
Title: Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding.
Volume: 98
Issue: 11
Pages: 653-65
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Publication
11577082 | -
First Author: Anant S
Year: 2001
Journal: J Biol Chem
Title: Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factor.
Volume: 276
Issue: 50
Pages: 47338-51
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Publication
15226369 | -
First Author: Ladd AN
Year: 2004
Journal: J Cell Sci
Title: Multiple domains control the subcellular localization and activity of ETR-3, a regulator of nuclear and cytoplasmic RNA processing events.
Volume: 117
Issue: Pt 16
Pages: 3519-29
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Protein
Q60809
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: false
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Protein
Q9D8X5
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: false
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Protein
B2RXZ1
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
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Protein
F6ZMT3
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: true
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Protein
Q3TLK9
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
Q3V476
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: false
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Protein
Q3V231
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: false
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Protein
A0A3B2WD69
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: true
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Protein
A0A3B2WCF7
Organism: Mus musculus/domesticus
Length: 315  
Fragment?: false
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Protein
A0A3B2WCS3
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: false
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Protein
Q3UTD2
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
Q543X5
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: false
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Publication
11239395 | -
First Author: Tucker M
Year: 2001
Journal: Cell
Title: The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae.
Volume: 104
Issue: 3
Pages: 377-86
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Protein Domain
IPR034198 | CELF1/2_RRM2
Type: Domain
Description: The human CELF family has six members, which can be divided into two subfamilies based on their phylogeny: CELF1-2 and CELF3-6. This entry represents the RNA recognition motif 2 (RRM2) of CELF-1 and CELF-2 protein. CELF-1 and CELF-2 belong to the CELF (CUGBP and ETR-3 Like Factor)/Bruno-like protein family, whose members play important roles in the regulation of alternative splicing and translation. CELF-1 and CELF-2 share sequence similarity to the Drosophila Bruno protein and binds to the Bruno response elements (cis-acting sequences in the 3'-untranslated region (UTR) ofoskar mRNA) [].The human CELF-1 (also known as CUG-BP or BRUNOL-2) binds to RNA substrates and recruits PARN deadenylase []. It preferentially targets UGU-rich mRNA elements []. CELF-1 has been implicated in onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene [, ]. CELF-1 contain three highly conserved RNA recognition motifs (RRMs): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C terminus of the protein. The Xenopus homologue of CELF-1 is EDEN-BP (embryo deadenylation element-binding protein), which mediates sequence-specific deadenylation of Eg5 mRNA. It binds specifically to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression []. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding []. CELF-2 (also known as CUGBP2 or ETR-3) shares high sequence identity with CELF-1, but shows different binding specificity; it binds preferentially to sequences with UG repeats and UGUU motifs. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing []. CELF-2 also contains three highly conserved RRMs. It binds to RNA via the first two RRMs, which are also important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C terminus, within RRM3 [].
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Protein Domain
IPR034199 | CELF1/2_RRM3
Type: Domain
Description: The human CELF family has six members, which can be divided into two subfamilies based on their phylogeny: CELF1-2 and CELF3-6. This entry represents the RNA recognition motif 3 (RRM3) of CELF-1 andCELF-2 protein. CELF-1 and CELF-2 belong to the CELF (CUGBP and ETR-3 Like Factor)/Bruno-like protein family, whose members play important roles in the regulation of alternative splicing and translation. CELF-1 and CELF-2 share sequence similarity to the Drosophila Bruno protein and binds to the Bruno response elements (cis-acting sequences in the 3'-untranslated region (UTR) ofoskar mRNA) [].The human CELF-1 (also known as CUG-BP or BRUNOL-2) binds to RNA substrates and recruits PARN deadenylase []. It preferentially targets UGU-rich mRNA elements []. CELF-1 has been implicated in onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene [, ]. CELF-1 contain three highly conserved RNA recognition motifs (RRMs): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C terminus of the protein. The Xenopus homologue of CELF-1 is EDEN-BP (embryo deadenylation element-binding protein), which mediates sequence-specific deadenylation of Eg5 mRNA. It binds specifically to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression []. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding []. CELF-2 (also known as CUGBP2 or ETR-3) shares high sequenceidentity with CELF-1, but shows different binding specificity; it binds preferentially to sequences with UG repeats and UGUU motifs. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing []. CELF-2 also contains three highly conserved RRMs. It binds to RNA via the first two RRMs, which are also important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C terminus, within RRM3 [].
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Publication
10893231 | J:74955
First Author: Good PJ
Year: 2000
Journal: J Biol Chem
Title: A family of human RNA-binding proteins related to the Drosophila Bruno translational regulator.
Volume: 275
Issue: 37
Pages: 28583-92
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Protein
P28659
Organism: Mus musculus/domesticus
Length: 486  
Fragment?: false
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Protein
A0A0R4J0T5
Organism: Mus musculus/domesticus
Length: 487  
Fragment?: false
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Protein
Q68ED3
Organism: Mus musculus/domesticus
Length: 633  
Fragment?: false
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Protein
E9QJT6
Organism: Mus musculus/domesticus
Length: 680  
Fragment?: false
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Protein
B7ZMU2
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: false
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Protein
F8WI26
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: false
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Publication
25723530 | -
First Author: Kim G
Year: 2015
Journal: PLoS Genet
Title: Region-specific activation of oskar mRNA translation by inhibition of Bruno-mediated repression.
Volume: 11
Issue: 2
Pages: e1004992
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Protein Domain
IPR034196 | CELF1/2_RRM1
Type: Domain
Description: The human CELF family has six members, which can be divided into two subfamilies based on their phylogeny: CELF1-2 and CELF3-6. This entry represents the RNA recognition motif 1 (RRM1) of CELF-1 and CELF-2 protein. CELF-1 and CELF-2 belong to the CELF (CUGBP and ETR-3 Like Factor)/Bruno-like protein family, whose members play important roles in the regulation of alternative splicing and translation. CELF-1 and CELF-2 share sequence similarity to the Drosophila Bruno protein and binds to the Bruno response elements (cis-acting sequences in the 3'-untranslated region (UTR) ofoskar mRNA) [].The human CELF-1 (also known as CUG-BP or BRUNOL-2) binds to RNA substrates and recruits PARN deadenylase []. It preferentially targets UGU-rich mRNA elements []. CELF-1 has been implicated in onset of type 1 myotonic dystrophy (DM1), a neuromuscular disease associated with an unstable CUG triplet expansion in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene [, ]. CELF-1 contain three highly conserved RNA recognition motifs (RRMs): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C terminus of the protein. The Xenopus homologue of CELF-1 is EDEN-BP (embryo deadenylation element-binding protein), which mediates sequence-specific deadenylation of Eg5 mRNA. It binds specifically to the EDEN motif in the 3'-untranslated regions of maternal mRNAs and targets these mRNAs for deadenylation and translational repression []. The two N-terminal RRMs of EDEN-BP are necessary for the interaction with EDEN as well as a part of the linker region (between RRM2 and RRM3). Oligomerization of EDEN-BP is required for specific mRNA deadenylation and binding []. CELF-2 (also known as CUGBP2 or ETR-3) shares high sequence identity with CELF-1, but shows different binding specificity; it binds preferentially to sequences with UG repeats and UGUU motifs. It also binds to the 3'-UTR of cyclooxygenase-2 messages, affecting both translation and mRNA stability, and binds to apoB mRNA, regulating its C to U editing []. CELF-2 also contains three highly conserved RRMs. It binds to RNA via the first two RRMs, which are also important for localization in the cytoplasm. The splicing activation or repression activity of CELF-2 on some specific substrates is mediated by RRM1/RRM2. Both, RRM1 and RRM2 of CELF-2, can activate cardiac troponin T (cTNT) exon 5 inclusion. In addition, CELF-2 possesses a typical arginine and lysine-rich nuclear localization signal (NLS) in the C terminus, within RRM3 [].Proteins containing this motif also include Drosophila melanogaster Bruno protein, which plays a central role in regulation ofOskar (Osk) expression in flies. It mediates repression by binding to regulatory Bruno response elements (BREs) in the Osk mRNA 3' UTR []. The full-length Bruno protein contains three RRMs, two located in the N-terminal half of the protein and the third near the C terminus, separated by a linker region.
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Protein
Q9Z0H4
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
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Protein
S4R2U7
Organism: Mus musculus/domesticus
Length: 460  
Fragment?: false
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Protein
A0A0R4J2B0
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: false
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Protein
E9QA47
Organism: Mus musculus/domesticus
Length: 478  
Fragment?: false
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Protein
V9GX43
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: true
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Protein
S4R1S7
Organism: Mus musculus/domesticus
Length: 472  
Fragment?: false
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Protein
Q9D2E2
Organism: Mus musculus/domesticus
Length: 511  
Fragment?: false
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Protein
S4R2S7
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: true
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Protein
S4R2J2
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: true
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Protein
S4R2L5
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: true
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Publication
9787637 | J:50158
First Author: Grishin NV
Year: 1998
Journal: Trends Biochem Sci
Title: The R3H motif: a domain that binds single-stranded nucleic acids.
Volume: 23
Issue: 9
Pages: 329-30
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Publication
17242355 | -
First Author: Villén J
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Large-scale phosphorylation analysis of mouse liver.
Volume: 104
Issue: 5
Pages: 1488-93
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Publication
11042159 | J:68323
First Author: Carninci P
Year: 2000
Journal: Genome Res
Title: Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes.
Volume: 10
Issue: 10
Pages: 1617-30
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Publication
10349636 | J:80645
 
First Author: Carninci P
Year: 1999
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