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Search results 601 to 700 out of 715 for Rrm1

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Type Details Score
Protein
Q52KE1
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
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Publication
23861535 | -
First Author: Bronicki LM
Year: 2013
Journal: RNA
Title: Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction.
Volume: 19
Issue: 8
Pages: 1019-37
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Publication
9516855 | -
First Author: Ross RA
Year: 1997
Journal: Eur J Cancer
Title: HuD, a neuronal-specific RNA-binding protein, is a potential regulator of MYCN expression in human neuroblastoma cells.
Volume: 33
Issue: 12
Pages: 2071-4
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Publication
16927307 | J:112690
First Author: DeschĂȘnes-Furry J
Year: 2006
Journal: Bioessays
Title: The RNA-binding protein HuD: a regulator of neuronal differentiation, maintenance and plasticity.
Volume: 28
Issue: 8
Pages: 822-33
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Publication
8626503 | -
First Author: Ma WJ
Year: 1996
Journal: J Biol Chem
Title: Cloning and characterization of HuR, a ubiquitously expressed Elav-like protein.
Volume: 271
Issue: 14
Pages: 8144-51
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Publication
25584704 | -
First Author: Scheiba RM
Year: 2014
Journal: RNA Biol
Title: The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets.
Volume: 11
Issue: 10
Pages: 1250-61
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Publication
2760983 | -
First Author: Newcomb WW
Year: 1989
Journal: J Virol
Title: Nucleocapsid mass and capsomer protein stoichiometry in equine herpesvirus 1: scanning transmission electron microscopic study.
Volume: 63
Issue: 9
Pages: 3777-83
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Publication
18180367 | -
First Author: Mazroui R
Year: 2008
Journal: J Cell Biol
Title: Caspase-mediated cleavage of HuR in the cytoplasm contributes to pp32/PHAP-I regulation of apoptosis.
Volume: 180
Issue: 1
Pages: 113-27
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Publication
15341728 | -
First Author: Simpson PJ
Year: 2004
Journal: Structure
Title: Structure and RNA interactions of the N-terminal RRM domains of PTB.
Volume: 12
Issue: 9
Pages: 1631-43
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Publication
16179478 | -
First Author: Oberstrass FC
Year: 2005
Journal: Science
Title: Structure of PTB bound to RNA: specific binding and implications for splicing regulation.
Volume: 309
Issue: 5743
Pages: 2054-7
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Publication
22817740 | -
First Author: Kafasla P
Year: 2012
Journal: Biochem Soc Trans
Title: Defining the roles and interactions of PTB.
Volume: 40
Issue: 4
Pages: 815-20
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Protein Domain
IPR034918 | HuD_RRM3
Type: Domain
Description: This entry represents the RNA recognition motif 3 (RRM3) of HuD (also known as ELAV-like protein 4), one of the neuronal members of the Hu family. The neuronal Hu proteins play important roles in neuronal differentiation, plasticity and memory. HuD has been implicated in various aspects of neuronal function, such as the commitment and differentiation of neuronal precursors as well as synaptic remodeling in mature neurons []. HuD also functions as an important regulator of mRNA expression in neurons by interacting with AU-rich RNA element (ARE) and stabilizing multiple transcripts []. Moreover, HuD regulates the nuclear processing/stability of N-myc pre-mRNA in neuroblastoma cells []. Like other Hu proteins, HuD contains three RNA recognition motifs (RRMs). RRM1 and RRM2 may cooperate in binding to an ARE. RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions [].
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Protein Domain
IPR034996 | HuR_RRM2
Type: Domain
Description: This entry represents the RNA recognition motif 2 (RRM2) of HuR, also known as ELAV-like protein 1 (ELAV-1), the ubiquitously expressed Hu family member [, ]. HuR binds to AU-rich RNA element (ARE) in target mRNAs and stabilizes them against degradation. It also regulates the nuclear import of proteins []. It has a variety of biological functions mostly related to the regulation of cellular response to DNA damage and other types of stress. HuR has an anti-apoptotic function during early cell stress response []. HuR may be important in muscle differentiation, adipogenesis, suppression of inflammatory response and modulation of gene expression in response to chronic ethanol exposure and amino acid starvation [].Like other Hu proteins, HuR contains three RNA recognition motifs (RRMs). RRM1 and RRM2 may cooperate in binding to an AU-rich RNA element (ARE). RRM3 may help to maintain the stability of the RNA-protein complex, and might also bind to poly(A) tails or be involved in protein-protein interactions [].
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Protein Domain
IPR035000 | PTBP1_RRM1
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) of polypyrimidine tract-binding protein 1 (PTBP1). PTBP1 (also known as PTB) is involved in numerous post-transcriptional steps in gene expression in both the nucleus and cytoplasm. It can act as a negative regulator of alternative splicing and as an activator of translation driven by IRESs (internal ribosome entry segments) []. It contains four RNA recognition motifs (RRM). RRM1 and RRM2 are independent from each other and separated by flexible linkers. By contrast, there is an unusual and conserved interdomain interaction between RRM3 and RRM4. It is widely held that only RRMs 3 and 4 are involved in RNA binding and RRM2 mediates PTB homodimer formation. However, new evidence shows that the RRMs 1 and 2 also contribute substantially to RNA binding. Moreover, PTB may not always dimerize to repress splicing. It is a monomer in solution [, ].
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Protein
D3YWT1
Organism: Mus musculus/domesticus
Length: 331  
Fragment?: false
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Protein
D3Z3N4
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: false
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Protein
Q3UZ01
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: false
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Publication
8331655 | -
First Author: Nordlund P
Year: 1993
Journal: J Mol Biol
Title: Structure and function of the Escherichia coli ribonucleotide reductase protein R2.
Volume: 232
Issue: 1
Pages: 123-64
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Publication
9558317 | -
First Author: Tong W
Year: 1998
Journal: Biochemistry
Title: Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography.
Volume: 37
Issue: 17
Pages: 5840-8
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Publication
11526233 | -
First Author: Voegtli WC
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer.
Volume: 98
Issue: 18
Pages: 10073-8
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Publication
11802741 | -
First Author: Högbom M
Year: 2002
Journal: Biochemistry
Title: Crystal structure of the di-iron/radical protein of ribonucleotide reductase from Corynebacterium ammoniagenes.
Volume: 41
Issue: 4
Pages: 1381-9
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Publication
9748343 | -
First Author: Eriksson M
Year: 1998
Journal: Biochemistry
Title: Structure of Salmonella typhimurium nrdF ribonucleotide reductase in its oxidized and reduced forms.
Volume: 37
Issue: 38
Pages: 13359-69
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Publication
10980602 | -
First Author: Nakano K
Year: 2000
Journal: Oncogene
Title: A ribonucleotide reductase gene is a transcriptional target of p53 and p73.
Volume: 19
Issue: 37
Pages: 4283-9
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Publication
26089597 | -
 
First Author: Cho EC
Year: 2015
Journal: Mediators Inflamm
Title: RRM2B-Mediated Regulation of Mitochondrial Activity and Inflammation under Oxidative Stress.
Volume: 2015
Pages: 287345
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Publication
18990579 | -
First Author: Lembo D
Year: 2009
Journal: Trends Biochem Sci
Title: Tinkering with a viral ribonucleotide reductase.
Volume: 34
Issue: 1
Pages: 25-32
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Protein Domain
IPR033909 | RNR_small
Type: Family
Description: The beta (small) subunit of ribonucleotide reductase (RNR) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The RNR protein catalyzes the conversion of ribonucleotides to deoxyribonucleotides and is found in all eukaryotes, many prokaryotes, several viruses, and few archaea. The catalytically active form of RNR is a proposed alpha2-beta2 tetramer. The homodimeric alpha subunit (R1) contains the active site and redox active cysteines as well as the allosteric binding sites. The beta subunit (R2) contains a di-iron cluster that, in its reduced state, reacts with dioxygen to form a stable tyrosyl radical and a di-iron(III) cluster. This essential tyrosyl radical is proposed to generate a thiyl radical, located on a cysteine residue in the R1 active site that initiates ribonucleotide reduction. The beta subunit is composed of 10-13 helices, the eight longest helices form an α-helical bundle; some have two addition beta strands [, , , ].The beta-herpesvirus RNR R1 subunit homologues are catalytically inactive; the enzyme seem to function by inhibiting cellular adaptor protein RIP1 to block cellular signaling pathways involved in innate immunity and inflammation [].Yeast is unique in that it assembles both homodimers and heterodimers of RNR. The yeast heterodimer, Y2Y4, contains R2 (Y2) and a R2 homologue (Y4) that lacks the diiron centre and is proposed to only assist in cofactor assembly, and perhaps stabilize R1 (Y1) in its active conformation [, ]. In mammals, the active form of the enzyme is composed of two identical large subunits (RRM1) and two identical small subunits (RRM2 or its homologue RRM2B). RRM1 is the catalytic subunit, and RRM2 and RRM2B the regulatory subunits. RRM2B (also called p53R2) can be induced by p53 [, ].
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Protein Domain
IPR034525 | PSF_RRM1
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) of PSF.PSF is a member of the DBHS (Drosophila behavior human splicing) family. It participates in a wide range of gene regulatory processes and cellular response pathways. It has been shown to affect the alternative splicing of CD45 and Tau and regulate the 3' polyadenylation of mRNAs. It is often localised in the paraspeckles and may be involved in the nuclear retention of mRNAs. It is involved in translation and transcription. It can bind directly to DSBs and play a role in DNA repair. PSF can also be utilized as an essential host factor for viral RNA multiplication and replication [, ]. In addition to the common DHBS core, which encompasses RRM1 and RRM2, the protein-protein interaction NOPS domain and the coiled-coil domain, PSF features additional domains, such as a RGG motif and a proline-rich region in its N terminus []. DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a conserved intervening sequence referred to as a NONA/ParaSpeckle (NOPS) domain, and a ~100 amino acid coiled-coil domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ].
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Protein Domain
IPR034526 | PSF_NOPS
Type: Domain
Description: This entry represents the NOPS domain and the C-terminal coiled-coil region of PSF (also known as SFPQ). The C-terminal coiled-coil region functions in mediating DBHS dimerization, while some surface-exposed basic residues within the NOPS domain may be involved in nucleic acid binding [].PSF is a member of the DBHS (Drosophila behavior human splicing) family. It participates in a wide range of gene regulatory processes and cellular response pathways. It has been shown to affect the alternative splicing of CD45 and Tau and regulate the 3' polyadenylation of mRNAs. It is often localised in the paraspeckles and may be involved in the nuclear retention of mRNAs. It is involved in translation and transcription. It can bind directly to DSBs and play a role in DNA repair. PSF can also be utilized as an essential host factor for viral RNA multiplication and replication [, ]. In addition to the common DHBS core, which encompasses RRM1 and RRM2, the protein-protein interaction NOPS domain and the coiled-coil domain, PSF features additional domains, such as a RGG motif and a proline-rich region in its N terminus []. DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a conserved intervening sequence referred to as a NONA/ParaSpeckle (NOPS) domain, and a ~100 amino acid coiled-coil domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ].
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Protein Domain
IPR034715 | HSV_RIR2
Type: Family
Description: The beta (small) subunit of ribonucleotide reductase (RNR) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The RNR protein catalyzes the conversion of ribonucleotides to deoxyribonucleotides and is found in all eukaryotes, many prokaryotes, several viruses, and few archaea. The catalytically active form of RNR is a proposed alpha2-beta2 tetramer. The homodimeric alpha subunit (R1) contains the active site and redox active cysteines as well as the allosteric binding sites. The beta subunit (R2) contains a di-iron cluster that, in its reduced state, reacts with dioxygen to form a stable tyrosyl radical and a di-iron(III) cluster. This essential tyrosyl radical is proposed to generate a thiyl radical, located on a cysteine residue in the R1 active site that initiates ribonucleotide reduction. The beta subunit is composed of 10-13 helices, the eight longest helices form an α-helical bundle; some have two addition beta strands [, , , ].The beta-herpesvirus RNR R1 subunit homologues are catalytically inactive; the enzyme seem to function by inhibiting cellular adaptor protein RIP1 to block cellular signaling pathways involved in innate immunity and inflammation [].Yeast is unique in that it assembles both homodimers and heterodimers of RNR. The yeast heterodimer, Y2Y4, contains R2 (Y2) and a R2 homologue (Y4) that lacks the diiron centre and is proposed to only assist in cofactor assembly, and perhaps stabilize R1 (Y1) in its active conformation [, ]. In mammals, the active form of the enzyme is composed of two identical large subunits (RRM1) and two identical small subunits (RRM2 or its homologue RRM2B). RRM1 is the catalytic subunit, and RRM2 and RRM2B the regulatory subunits. RRM2B (also called p53R2) can be induced by p53 [, ].This entry includes the ribonucleoside-diphosphate reductase small subunit from Herpesviruses.
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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
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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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 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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Protein
Q60899
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
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Publication
8876648 | J:240311
First Author: Kauppi B
Year: 1996
Journal: J Mol Biol
Title: The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2.
Volume: 262
Issue: 5
Pages: 706-20
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Protein
Q3UR02
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
B1AXZ0
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: false
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Protein
B1AXZ5
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
Q91XI8
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
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Protein
Q91XI9
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
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Protein
B1AXZ6
Organism: Mus musculus/domesticus
Length: 376  
Fragment?: false
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Protein
B1AXZ4
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: false
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Protein
Q564D8
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
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Protein
Q80Y51
Organism: Mus musculus/domesticus
Length: 373  
Fragment?: false
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Protein
Q80UJ0
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
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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
Q8CIN6
Organism: Mus musculus/domesticus
Length: 465  
Fragment?: false
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Protein
Q8JZV4
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
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Protein
Q7TSY6
Organism: Mus musculus/domesticus
Length: 486  
Fragment?: false
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Protein
Q7TN33
Organism: Mus musculus/domesticus
Length: 460  
Fragment?: false
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Protein
D3Z4T1
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
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Protein
D6RHP1
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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Protein
D6RGB9
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
D3YU11
Organism: Mus musculus/domesticus
Length: 481  
Fragment?: false
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Protein
D3Z580
Organism: Mus musculus/domesticus
Length: 394  
Fragment?: false
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Protein
A0A5F8MPH2
Organism: Mus musculus/domesticus
Length: 446  
Fragment?: false
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Protein
A2AG09
Organism: Mus musculus/domesticus
Length: 437  
Fragment?: false
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Protein
F6TN13
Organism: Mus musculus/domesticus
Length: 463  
Fragment?: true
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Protein
A0A0G2JGE2
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
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Publication
15863623 | -
First Author: Clouaire T
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity.
Volume: 102
Issue: 19
Pages: 6907-12
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Publication
15146077 | -
First Author: Will CL
Year: 2004
Journal: RNA
Title: The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome.
Volume: 10
Issue: 6
Pages: 929-41
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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
Q8VIJ6
Organism: Mus musculus/domesticus
Length: 699  
Fragment?: false
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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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Publication
25832716 | -
First Author: Yarosh CA
Year: 2015
Journal: Wiley Interdiscip Rev RNA
Title: PSF: nuclear busy-body or nuclear facilitator?
Volume: 6
Issue: 4
Pages: 351-67
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Publication
27084935 | -
First Author: Knott GJ
Year: 2016
Journal: Nucleic Acids Res
Title: The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold.
Volume: 44
Issue: 9
Pages: 3989-4004
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Protein
Q61701
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
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Protein
P70372
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q6PEE3
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Publication
20200153 | -
First Author: Mazars R
Year: 2010
Journal: J Biol Chem
Title: The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias.
Volume: 285
Issue: 18
Pages: 13364-71
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Protein
P11157
Organism: Mus musculus/domesticus
Length: 390  
Fragment?: false
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Protein
Q60900
Organism: Mus musculus/domesticus
Length: 367  
Fragment?: false
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Protein
Q8BW03
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
D3Z2A4
Organism: Mus musculus/domesticus
Length: 299  
Fragment?: false
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Protein
S4R2S7
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: true
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Protein
Q3TT05
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: true
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Protein
Q8BTQ1
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: true
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Protein
Q3TZL2
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: true
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Protein
S4R2J2
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: true
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Protein
F6RUC3
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Protein
Q3THV8
Organism: Mus musculus/domesticus
Length: 390  
Fragment?: false
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Protein
Q8BVF8
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
S4R2L5
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: true
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Protein
Q8BM84
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
D3Z0D8
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: true
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Protein
Q3UFF9
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom