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Search results 1 to 63 out of 63 for Nrd1

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Hits by Pathway

Hits by Category

Type Details Score
GO Term
GO:0035649 | Nrd1 complex
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Protein
Q8R1H1
Organism: Mus musculus/domesticus
Length: 498  
Fragment?: true
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Protein
Q8BHG1
Organism: Mus musculus/domesticus
Length: 1161  
Fragment?: false
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Protein Coding Gene
MGI:1201386 | Nrdc
Type: protein_coding_gene
Organism: mouse, laboratory
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SO Term
SO:0002213 | transcription_termination_signal
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Publication
10207106 | J:54714
First Author: Yamamoto H
Year: 1999
Journal: Mol Cell Biol
Title: Isolation of a mammalian homologue of a fission yeast differentiation regulator.
Volume: 19
Issue: 5
Pages: 3829-41
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Publication
27401558 | -
First Author: Lemay JF
Year: 2016
Journal: Genes Dev
Title: The Nrd1-like protein Seb1 coordinates cotranscriptional 3' end processing and polyadenylation site selection.
Volume: 30
Issue: 13
Pages: 1558-72
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Publication
12907709 | -
First Author: Mitsuzawa H
Year: 2003
Journal: Nucleic Acids Res
Title: Rpb7 subunit of RNA polymerase II interacts with an RNA-binding protein involved in processing of transcripts.
Volume: 31
Issue: 16
Pages: 4696-701
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Protein Domain
IPR034894 | Nrd1/Seb1_RRM
Type: Domain
Description: This entry represents the RNA recognition motif (RRM) of budding yeast Nrd1 and fission yeast Seb1. Nrd1 is a novel heterogeneous nuclear ribonucleoprotein (hnRNP)-like RNA-binding protein. It is part of the Nrd1-Nab3-Sen1 (NNS) complex that is involved in the termination and processing of short RNA polymerase II transcripts [].Nrd1 contains an RNA recognition motif (RRM), a short arginine-, serine-, and glutamate-rich segment similar to the regions rich in RE and RS dipeptides (RE/RS domains) in many metazoan splicing factors, and a proline- and glutamine-rich C-terminal domain (P+Q domain) similar to domains found in several yeast hnRNPs. Disruption of NRD1 gene is lethal to yeast cells. Its N-terminal domain is sufficient for viability, which may facilitate interactions with RNA polymerase II where Nrd1 may function as an auxiliary factor. By contrast, the RRM, RE/RS domains, and P+Q domain are dispensable [].Seb1 is an RNA-binding protein essential for cell viability and bound directly to Rpb7 subunit of RNA polymerase II. Seb1 does not function in NNS-like termination. Instead, Seb1 coordinates cotranscriptional 3' end processing and polyadenylation site selection []. It also contains one RRM motif and a region rich in arginine-serine dipeptides (RS domain) [].
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Protein Domain
IPR034195 | Mrn1_RRM1
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) in Mrn1. Proteins containing this motif also include S. pombe Nrd1 (also known as Msa2), which inhibits sexual differentiation []. Mrn1 is an RNA binding protein that localizes both to the nucleus and cytoplasm. It may be involved in the mRNA processing pathway []. Mrn1 contains four copies of a conserved RNA recognition motif (RRM).
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Publication
22431520 | -
First Author: Darby MM
Year: 2012
Journal: Mol Cell Biol
Title: The Saccharomyces cerevisiae Nrd1-Nab3 transcription termination pathway acts in opposition to Ras signaling and mediates response to nutrient depletion.
Volume: 32
Issue: 10
Pages: 1762-75
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Publication
19441079 | -
First Author: Sadvakassova G
Year: 2009
Journal: J Cell Physiol
Title: Regulator of differentiation 1 (ROD1) binds to the amphipathic C-terminal peptide of thrombospondin-4 and is involved in its mitogenic activity.
Volume: 220
Issue: 3
Pages: 672-9
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Publication
9365256 | -
First Author: Ursic D
Year: 1997
Journal: Nucleic Acids Res
Title: The yeast SEN1 gene is required for the processing of diverse RNA classes.
Volume: 25
Issue: 23
Pages: 4778-85
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Protein Domain
IPR026121 | Sen1
Type: Family
Description: This entry includes fungal Sen1. The yeast helicase Sen1 is a subunit of the Nrd1 complex (Nrd1-Nab3-Sen1), which interacts with the exosome to mediate 3' end formation of some mRNAs, snRNAs and snoRNAs []. In Schizosaccharomyces pombe, Sen1 functions as an ATP-dependent 5'->3' DNA/RNA helicase required for the expression and maturation of diverse classes of non-protein-coding RNAs [, ]. It may also play a role in transcription-coupled nucleotide excision repair [].
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Protein Domain
IPR033110 | PTBP3_RRM4
Type: Domain
Description: This entry represents the RNA recognition motif 4 of ROD1 (also known as polypyrimidine tract-binding protein 3, PTBP3), which is an RNA-binding protein highly expressed in hematopoietic cells []. It is a functional homologue of fission yeast Nrd1 and may be involved in differentiation control []. It also plays a role in nonsense-mediated mRNA decay (NMD) []. Several ROD1 isoforms can be generated by alternative splicing and translation initiation []. Rod1 contains four repeats of RNA recognition motifs (RRM).
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Protein Domain
IPR034326 | ROD1_RRM1
Type: Domain
Description: This entry represents the RNA recognition motif 1 of ROD1 (also known as polypyrimidine tract-binding protein 3, PTBP3), which is an RNA-binding protein highly expressed in hematopoietic cells []. It is a functional homologue of fission yeast Nrd1 and may be involved in differentiation control []. It also plays a role in nonsense-mediated mRNA decay (NMD) []. Several ROD1 isoforms can be generated by alternative splicing and translation initiation []. Rod1 contains four repeats of RNA recognition motifs (RRM).
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Publication
27385158 | J:247243
First Author: Nishi K
Year: 2016
Journal: Diabetes
Title: Nardilysin Is Required for Maintaining Pancreatic β-Cell Function.
Volume: 65
Issue: 10
Pages: 3015-27
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Publication
19935654 | J:155532
First Author: Ohno M
Year: 2009
Journal: Nat Neurosci
Title: Nardilysin regulates axonal maturation and myelination in the central and peripheral nervous system.
Volume: 12
Issue: 12
Pages: 1506-13
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Publication
20805243 | -
First Author: Lunde BM
Year: 2011
Journal: Nucleic Acids Res
Title: Structural insights into cis element recognition of non-polyadenylated RNAs by the Nab3-RRM.
Volume: 39
Issue: 1
Pages: 337-46
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Publication
7962083 | -
First Author: Wilson SM
Year: 1994
Journal: J Cell Biol
Title: Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae.
Volume: 127
Issue: 5
Pages: 1173-84
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Publication
7476874 | -
First Author: Sugimoto K
Year: 1995
Journal: Mol Gen Genet
Title: Dosage suppressors of the dominant G1 cyclin mutant CLN3-2: identification of a yeast gene encoding a putative RNA/ssDNA binding protein.
Volume: 248
Issue: 6
Pages: 712-8
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Publication
23028530 | -
First Author: Düring L
Year: 2012
Journal: PLoS One
Title: MRN1 implicates chromatin remodeling complexes and architectural factors in mRNA maturation.
Volume: 7
Issue: 9
Pages: e44373
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Protein Domain
IPR034167 | Nab3_RRM
Type: Domain
Description: This entry represents the RNA recognition motif (RRM) of Nab3p (also known as Hmd1p), an acidic nuclear polyadenylated RNA-binding protein that is essential for cell viability. Nab3p is predominantly localized within the nucleoplasm and essential for growth in budding yeast []. It plays an important role in the maintenance of CLN3 mRNA levels []. It is part of the Nrd1 complex (Nrd1p-Nab3p-Sen1p) that directs the termination and processing of short RNA polymerase II transcripts and regulates cellular response to nutrient availability []. Nab3p contains an N-terminal aspartic/glutamic acid-rich region, a central RNA recognition motif (RRM), and a C-terminal region rich in glutamine and proline residues [].
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Publication
34475109 | J:312347
First Author: Kodama M
Year: 2021
Journal: Cancer Res
Title: Sleeping Beauty Transposon Mutagenesis Identifies Genes Driving the Initiation and Metastasis of Uterine Leiomyosarcoma.
Volume: 81
Issue: 21
Pages: 5413-5424
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Publication
15241417 | -
First Author: Meinhart A
Year: 2004
Journal: Nature
Title: Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors.
Volume: 430
Issue: 6996
Pages: 223-6
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Publication
15665873 | -
First Author: Noble CG
Year: 2005
Journal: Nat Struct Mol Biol
Title: Key features of the interaction between Pcf11 CID and RNA polymerase II CTD.
Volume: 12
Issue: 2
Pages: 144-51
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Publication
8943355 | -
First Author: Steinmetz EJ
Year: 1996
Journal: Mol Cell Biol
Title: Repression of gene expression by an exogenous sequence element acting in concert with a heterogeneous nuclear ribonucleoprotein-like protein, Nrd1, and the putative helicase Sen1.
Volume: 16
Issue: 12
Pages: 6993-7003
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Protein Domain
IPR006569 | CID_dom
Type: Domain
Description: The C-terminal domain (CTD) of the large subunit of RNA polymerase II is aplatform for mRNA processing factors and links gene transcription to mRNAcapping, splicing and polyadenylation. CTD recognition is dependent on thephosphorylation state of the CTD itself, which varies during the course oftranscription but has also been linked to the isomerization state of the CTD'sproline residues. Several RNA-processing factors recognise the CTD by means ofa conserved CTD-interacting domain (CID). Factors with CID domains include theserine/arginine-rich-like factors SCAF4 and SCAF8, Nrd1 (which is implicatedin polyadenylation-independent RNA 3'-end formation) and Pcf11. Pcf11 is aconserved and essential subunit of the yeast cleavage factor 1A, which isrequired for 3'-RNA processing and transcription termination [, ].The CID domain is a right-handed superhelix of eight α-helices forming acompact domain. The CID fold closely resembles that of VHSdomains and is related to armadillo-repeat proteins , except for the two amino-terminal helices. Amino acid residuesin the hydrophobic core of the domain are highly conserved across CID domains[, ].
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Publication
24849253 | J:216321
First Author: Ishizu-Higashi S
Year: 2014
Journal: PLoS One
Title: Deletion of nardilysin prevents the development of steatohepatitis and liver fibrotic changes.
Volume: 9
Issue: 5
Pages: e98017
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Publication
15166138 | -
First Author: Jeong HT
Year: 2004
Journal: Genetics
Title: A novel gene, msa1, inhibits sexual differentiation in Schizosaccharomyces pombe.
Volume: 167
Issue: 1
Pages: 77-91
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Publication
22575643 | -
First Author: Brazão TF
Year: 2012
Journal: FEBS Lett
Title: A new function of ROD1 in nonsense-mediated mRNA decay.
Volume: 586
Issue: 8
Pages: 1101-10
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Publication
15121901 | -
First Author: Ursic D
Year: 2004
Journal: Nucleic Acids Res
Title: Multiple protein/protein and protein/RNA interactions suggest roles for yeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA repair and RNA processing.
Volume: 32
Issue: 8
Pages: 2441-52
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Publication
28408439 | -
First Author: Leonaitė B
Year: 2017
Journal: EMBO J
Title: Sen1 has unique structural features grafted on the architecture of the Upf1-like helicase family.
Volume: 36
Issue: 11
Pages: 1590-1604
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Publication
25940628 | J:306204
First Author: Tan LY
Year: 2015
Journal: Nucleic Acids Res
Title: Generation of functionally distinct isoforms of PTBP3 by alternative splicing and translation initiation.
Volume: 43
Issue: 11
Pages: 5586-600
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Protein
Q9CSU0
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q8VDS4
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
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Protein
Q6NXI6
Organism: Mus musculus/domesticus
Length: 1469  
Fragment?: false
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Protein
Q3TT32
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: true
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Protein
Q9D4Z4
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
Q3TTQ0
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: true
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Protein
A0A0G2JFN1
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
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Protein
F6YB25
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
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Protein
Q8BXA9
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
Q3TZC7
Organism: Mus musculus/domesticus
Length: 279  
Fragment?: true
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Protein
G3X9Z4
Organism: Mus musculus/domesticus
Length: 1553  
Fragment?: false
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Protein
Q69ZY3
Organism: Mus musculus/domesticus
Length: 1641  
Fragment?: true
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Protein
A0A0R4J195
Organism: Mus musculus/domesticus
Length: 325  
Fragment?: false
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Protein
A0A0G2JFW6
Organism: Mus musculus/domesticus
Length: 1386  
Fragment?: true
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Protein
B2RX07
Organism: Mus musculus/domesticus
Length: 1553  
Fragment?: false
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Protein
A0A338P6R5
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
Q80V88
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: false
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Protein
Q8BHD7
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
G3UXA6
Organism: Mus musculus/domesticus
Length: 554  
Fragment?: false
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Protein
G8JL74
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
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Protein
Q8CGZ0
Organism: Mus musculus/domesticus
Length: 936  
Fragment?: false
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Protein
G3UZ01
Organism: Mus musculus/domesticus
Length: 457  
Fragment?: false
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Protein
A0A1D5RL92
Organism: Mus musculus/domesticus
Length: 938  
Fragment?: false
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Protein
Q3TBS5
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: true
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Protein
G5E8I8
Organism: Mus musculus/domesticus
Length: 949  
Fragment?: false
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Protein
Q7TSH6
Organism: Mus musculus/domesticus
Length: 1183  
Fragment?: false
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Protein
Q6DID3
Organism: Mus musculus/domesticus
Length: 1268  
Fragment?: false
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Protein
Q6NV83
Organism: Mus musculus/domesticus
Length: 1029  
Fragment?: false
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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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

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Cambridge CB2 3EH, United Kingdom