Type |
Details |
Score |
Publication |
First Author: |
Lee MY |
Year: |
2017 |
Journal: |
PLoS One |
Title: |
Serum response factor regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels. |
Volume: |
12 |
Issue: |
2 |
Pages: |
e0171262 |
|
•
•
•
•
•
|
Publication |
First Author: |
Koshelev M |
Year: |
2010 |
Journal: |
Hum Mol Genet |
Title: |
Heart-specific overexpression of CUGBP1 reproduces functional and molecular abnormalities of myotonic dystrophy type 1. |
Volume: |
19 |
Issue: |
6 |
Pages: |
1066-75 |
|
•
•
•
•
•
|
Publication |
First Author: |
Brockhoff M |
Year: |
2017 |
Journal: |
J Clin Invest |
Title: |
Targeting deregulated AMPK/mTORC1 pathways improves muscle function in myotonic dystrophy type I. |
Volume: |
127 |
Issue: |
2 |
Pages: |
549-563 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ravel-Chapuis A |
Year: |
2017 |
Journal: |
Hum Mol Genet |
Title: |
Misregulation of calcium-handling proteins promotes hyperactivation of calcineurin-NFAT signaling in skeletal muscle of DM1 mice. |
Volume: |
26 |
Issue: |
12 |
Pages: |
2192-2206 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jenquin JR |
Year: |
2019 |
Journal: |
ACS Pharmacol Transl Sci |
Title: |
Combination Treatment of Erythromycin and Furamidine Provides Additive and Synergistic Rescue of Mis-Splicing in Myotonic Dystrophy Type 1 Models. |
Volume: |
2 |
Issue: |
4 |
Pages: |
247-263 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ohsawa N |
Year: |
2015 |
Journal: |
Genes Cells |
Title: |
ABLIM1 splicing is abnormal in skeletal muscle of patients with DM1 and regulated by MBNL, CELF and PTBP1. |
Volume: |
20 |
Issue: |
2 |
Pages: |
121-34 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bisset DR |
Year: |
2015 |
Journal: |
Hum Mol Genet |
Title: |
Therapeutic impact of systemic AAV-mediated RNA interference in a mouse model of myotonic dystrophy. |
Volume: |
24 |
Issue: |
17 |
Pages: |
4971-83 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mahadevan MS |
Year: |
2006 |
Journal: |
Nat Genet |
Title: |
Reversible model of RNA toxicity and cardiac conduction defects in myotonic dystrophy. |
Volume: |
38 |
Issue: |
9 |
Pages: |
1066-70 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kimura T |
Year: |
2005 |
Journal: |
Hum Mol Genet |
Title: |
Altered mRNA splicing of the skeletal muscle ryanodine receptor and sarcoplasmic/endoplasmic reticulum Ca2+-ATPase in myotonic dystrophy type 1. |
Volume: |
14 |
Issue: |
15 |
Pages: |
2189-200 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yuan Y |
Year: |
2007 |
Journal: |
Nucleic Acids Res |
Title: |
Muscleblind-like 1 interacts with RNA hairpins in splicing target and pathogenic RNAs. |
Volume: |
35 |
Issue: |
16 |
Pages: |
5474-86 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ferreboeuf M |
Year: |
2014 |
Journal: |
Hum Mol Genet |
Title: |
Nuclear protein spreading: implication for pathophysiology of neuromuscular diseases. |
Volume: |
23 |
Issue: |
15 |
Pages: |
4125-33 |
|
•
•
•
•
•
|
Publication |
First Author: |
Peng X |
Year: |
2015 |
Journal: |
Biochim Biophys Acta |
Title: |
Celf1 regulates cell cycle and is partially responsible for defective myoblast differentiation in myotonic dystrophy RNA toxicity. |
Volume: |
1852 |
Issue: |
7 |
Pages: |
1490-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yadava RS |
Year: |
2019 |
Journal: |
Hum Mol Genet |
Title: |
MBNL1 overexpression is not sufficient to rescue the phenotypes in a mouse model of RNA toxicity. |
Volume: |
28 |
Issue: |
14 |
Pages: |
2330-2338 |
|
•
•
•
•
•
|
Publication |
First Author: |
Dewald Z |
Year: |
2024 |
Journal: |
Nat Commun |
Title: |
Altered drug metabolism and increased susceptibility to fatty liver disease in a mouse model of myotonic dystrophy. |
Volume: |
15 |
Issue: |
1 |
Pages: |
9062 |
|
•
•
•
•
•
|
Publication |
First Author: |
Da Silva A |
Year: |
2023 |
Journal: |
Sci Adv |
Title: |
N-acetylneuraminate pyruvate lyase controls sialylation of muscle glycoproteins essential for muscle regeneration and function. |
Volume: |
9 |
Issue: |
26 |
Pages: |
eade6308 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lu X |
Year: |
1999 |
Journal: |
Hum Mol Genet |
Title: |
Cardiac elav-type RNA-binding protein (ETR-3) binds to RNA CUG repeats expanded in myotonic dystrophy. |
Volume: |
8 |
Issue: |
1 |
Pages: |
53-60 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sarkar PS |
Year: |
2000 |
Journal: |
Nat Genet |
Title: |
Heterozygous loss of Six5 in mice is sufficient to cause ocular cataracts. |
Volume: |
25 |
Issue: |
1 |
Pages: |
110-4 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein Domain |
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 []. |
|
•
•
•
•
•
|
Protein Domain |
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 []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Tanner MK |
Year: |
2021 |
Journal: |
Nucleic Acids Res |
Title: |
Targeted splice sequencing reveals RNA toxicity and therapeutic response in myotonic dystrophy. |
Volume: |
49 |
Issue: |
4 |
Pages: |
2240-2254 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang LH |
Year: |
2022 |
Journal: |
J Neurosci |
Title: |
Calpain-2 Mediates MBNL2 Degradation and a Developmental RNA Processing Program in Neurodegeneration. |
Volume: |
42 |
Issue: |
25 |
Pages: |
5102-5114 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
486
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
487
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
508
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
460
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
440
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
478
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
443
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
472
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
276
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
92
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
134
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Fueyo-González F |
Year: |
2022 |
Journal: |
Immunity |
Title: |
Interferon-β acts directly on T cells to prolong allograft survival by enhancing regulatory T cell induction through Foxp3 acetylation. |
Volume: |
55 |
Issue: |
3 |
Pages: |
459-474.e7 |
|
•
•
•
•
•
|
Publication |
First Author: |
The Jackson Laboratory |
Year: |
2005 |
Journal: |
Unpublished |
Title: |
Information obtained from The Jackson Laboratory, Bar Harbor, ME |
|
|
|
|
•
•
•
•
•
|