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Search results 101 to 175 out of 175 for Nxf1

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0.021s
Type Details Score
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication
First Author: Lindtner S
Year: 2006
Journal: J Biol Chem
Title: RNA-binding motif protein 15 binds to the RNA transport element RTE and provides a direct link to the NXF1 export pathway.
Volume: 281
Issue: 48
Pages: 36915-28
HT Experiment
Series Id: GSE66696
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
Publication
First Author: Kopytova D
Year: 2016
Journal: Nucleic Acids Res
Title: ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association with mRNP and mRNA export in Drosophila.
Volume: 44
Issue: 10
Pages: 4920-33
GO Term
Publication
First Author: Zolotukhin AS
Year: 2009
Journal: Nucleic Acids Res
Title: Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA.
Volume: 37
Issue: 21
Pages: 7151-62
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) of RBM15.RNA-binding motif protein 15 (RBM15), also termed one-twenty two protein 1 (OTT1), is a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE []. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC) []. RBM15 belongs to the Spen (split end) protein family, which contains three N-terminal RNA recognition motifs (RRMs), and a C-terminal SPOC (Spen paralogue and orthologue C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 2 (RRM2) of RBM15.RNA-binding motif protein 15 (RBM15), also termed one-twenty two protein 1 (OTT1), is a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE []. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC) []. RBM15 belongs to the Spen (split end) protein family, which contains three N-terminal RNA recognition motifs (RRMs), and a C-terminal SPOC (Spen paralogue and orthologue C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 3 (RRM3) of RBM15.RNA-binding motif protein 15 (RBM15), also termed one-twenty two protein 1 (OTT1), is a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE []. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC) []. RBM15 belongs to the Spen (split end) protein family, which contains three N-terminal RNA recognition motifs (RRMs), and a C-terminal SPOC (Spen paralogue and orthologue C-terminal) domain.
Protein Domain
Type: Family
Description: Nuclear RNA export factor 3 (NXF3) is a member of the nuclear RNA export factor (NXF) family of proteins, which plays a role in mediating the export of cellular mRNA from the nucleus to the cytoplasm for translation. Like NXF1 and NFX2, NXF3 has the ability to bind and export mRNA from the nucleus to the cytoplasm, but it uses a completely different mechanism []. The expression of NXF3 appears to be restricted to the testis [].
Publication
First Author: Black BE
Year: 1999
Journal: Mol Cell Biol
Title: Identification of an NTF2-related factor that binds Ran-GTP and regulates nuclear protein export.
Volume: 19
Issue: 12
Pages: 8616-24
Publication
First Author: Grant RP
Year: 2002
Journal: Nat Struct Biol
Title: Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1.
Volume: 9
Issue: 4
Pages: 247-51
Publication
First Author: Liker E
Year: 2000
Journal: EMBO J
Title: The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain.
Volume: 19
Issue: 21
Pages: 5587-98
Publication
First Author: Suyama M
Year: 2000
Journal: EMBO Rep
Title: Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins.
Volume: 1
Issue: 1
Pages: 53-8
Publication
First Author: Hobeika M
Year: 2009
Journal: J Biol Chem
Title: Structural requirements for the ubiquitin-associated domain of the mRNA export factor Mex67 to bind its specific targets, the transcription elongation THO complex component Hpr1 and nucleoporin FXFG repeats.
Volume: 284
Issue: 26
Pages: 17575-83
Publication
First Author: Braun IC
Year: 2001
Journal: J Biol Chem
Title: Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export.
Volume: 276
Issue: 23
Pages: 20536-43
Publication
First Author: Yoon DW
Year: 1997
Journal: Immunity
Title: Tap: a novel cellular protein that interacts with tip of herpesvirus saimiri and induces lymphocyte aggregation.
Volume: 6
Issue: 5
Pages: 571-82
Publication
First Author: Bear J
Year: 1999
Journal: Mol Cell Biol
Title: Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirus mRNAs.
Volume: 19
Issue: 9
Pages: 6306-17
Publication
First Author: Kang Y
Year: 1999
Journal: Genes Dev
Title: The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences.
Volume: 13
Issue: 9
Pages: 1126-39
Publication
First Author: Braun IC
Year: 1999
Journal: EMBO J
Title: TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus.
Volume: 18
Issue: 7
Pages: 1953-65
Protein Domain
Type: Domain
Description: The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling []. The structure of the C-terminal domain is composed of four helices []. The structure is related to the UBA domain.The NXF family of mRNA nuclear export factors includes vertebrate NXF1 (also called tip-associated protein or mRNA export factor TAP), NXF2 (also called cancer/testis antigen CT39 or TAP-like protein TAPL-2), Caenorhabditis elegans NXF1 (ceNXF1), Saccharomyces cerevisiae mRNA nuclear export factor Mex67p and similar proteins. NXF proteins can stimulate nuclear export of mRNAs and facilitate the export of unspliced viral mRNA containing the constitutive transport element. An NXF protein is multi-domain with a nuclear localization sequence (NLS), a non-canonical mRNA-binding domain, and four leucine-rich repeats (LLR) at the N-terminal region. Its C-terminal part contains a NTF2-like domain and a ubiquitin-associated (UBA)-like domain, joined by flexible Pro-rich linker. Caenorhabditis elegans NXF1 are essential for the nuclear export of poly(A)+mRNA. In budding yeast, Mex67p binds mRNAs through its adaptor Yra1/REF. It also interacts directly with Nab2, an essential shuttling mRNA-binding protein required for export. Moreover, Mex67p associates with both nuclear pore protein (nucleoporin) FG repeats and Hpr1, a component of the TREX/THO complex linking transcription and export [, , , , , , , , , , , , , , , ].
Publication
First Author: Fribourg S
Year: 2001
Journal: Mol Cell
Title: Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor.
Volume: 8
Issue: 3
Pages: 645-56
Publication
First Author: Grüter P
Year: 1998
Journal: Mol Cell
Title: TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus.
Volume: 1
Issue: 5
Pages: 649-59
Publication
First Author: Bachi A
Year: 2000
Journal: RNA
Title: The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates.
Volume: 6
Issue: 1
Pages: 136-58
Publication
First Author: Yang J
Year: 2001
Journal: Mol Cell
Title: Two closely related human nuclear export factors utilize entirely distinct export pathways.
Volume: 8
Issue: 2
Pages: 397-406
Publication    
First Author: Zhou H
Year: 2017
Journal: Elife
Title: IRAK2 directs stimulus-dependent nuclear export of inflammatory mRNAs.
Volume: 6
Publication    
First Author: Ratnadiwakara M
Year: 2018
Journal: Elife
Title: SRSF3 promotes pluripotency through Nanog mRNA export and coordination of the pluripotency gene expression program.
Volume: 7
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) of RBM15B.RNA binding motif protein 15B (RBM15B, also known as OTT3) is a paralogue of RBM15. Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF [].RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising three N-terminal RNA recognition motifs (RRMs) and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 2 (RRM2) of RBM15B.RNA binding motif protein 15B (RBM15B, also known as OTT3) is a paralogue of RBM15. Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF [].RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising three N-terminal RNA recognition motifs (RRMs) and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 3 (RRM3) of RBM15B.RNA binding motif protein 15B (RBM15B, also known as OTT3) is a paralogue of RBM15. Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF [].RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising three N-terminal RNA recognition motifs (RRMs) and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain.
Publication
First Author: Hautbergue GM
Year: 2008
Journal: Proc Natl Acad Sci U S A
Title: Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP.
Volume: 105
Issue: 13
Pages: 5154-9
Protein
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: false
Publication
First Author: Jun L
Year: 2001
Journal: Curr Biol
Title: NXF5, a novel member of the nuclear RNA export factor family, is lost in a male patient with a syndromic form of mental retardation.
Volume: 11
Issue: 18
Pages: 1381-91
Publication
First Author: Segref A
Year: 1997
Journal: EMBO J
Title: Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores.
Volume: 16
Issue: 11
Pages: 3256-71
Publication
First Author: Zolotukhin AS
Year: 2002
Journal: J Biol Chem
Title: U2AF participates in the binding of TAP (NXF1) to mRNA.
Volume: 277
Issue: 6
Pages: 3935-42
Protein Domain
Type: Family
Description: Mex67 is involved in the export of mRNA from the nucleus to the cytoplasm in Saccharomyces cerevisiae []. Vertebrate TAP (also called NXF1 for nuclear RNA export factor 1) is the orthologue of Mex67 []. TAP belongs to a multigene family with conserved modular architecture []. Other members of the family in humans are NXF2, NXF3, and NFX5. Both TAP(NXF1) and NXF2 bind mRNA and display RNA nuclear export activity []. NXF3 also has the ability to export mRNA from the nucleus to the cytoplasm but it uses a different mechanism []. NXF1 and NXF2 are predominantly nuclear, whereas the cytoplasmic presence of NXF3 and NXF5 suggests that they have a different cellular function [, ].Three functional domains of TAP have been characterised: the RNA-binding domain, the Nuclear Transport Factor 2 (NTF2)-like domain, and the ubiquitin-associated (UBA) domain. The RNA-binding domain (RBD) of TAP is located at its amino terminus and is composed of two RNA recognition motifs (RRMs) and one leucine-rich region [, ]. Once bound to mRNA, TAP escorts the messenger ribonucleoprotein (mRNP) to the nuclear pore, where TAP interacts with nucleoporins via the NTF2-like (NTF2L) and UBA domains [].
Protein
Organism: Mus musculus/domesticus
Length: 89  
Fragment?: true
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Grant RP
Year: 2003
Journal: J Mol Biol
Title: Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution.
Volume: 326
Issue: 3
Pages: 849-58
Publication
First Author: Iglesias N
Year: 2010
Journal: Genes Dev
Title: Ubiquitin-mediated mRNP dynamics and surveillance prior to budding yeast mRNA export.
Volume: 24
Issue: 17
Pages: 1927-38
Protein
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: true
Publication
First Author: Gatfield D
Year: 2002
Journal: J Cell Biol
Title: REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export.
Volume: 159
Issue: 4
Pages: 579-88
Publication
First Author: Tan W
Year: 2005
Journal: Nucleic Acids Res
Title: Identification and characterization of the mouse nuclear export factor (Nxf) family members.
Volume: 33
Issue: 12
Pages: 3855-65
Publication
First Author: Niu H
Year: 2008
Journal: Mamm Genome
Title: Mapping of genetic modifiers of Eya1 ( bor/bor ) in CAST/EiJ and BALB/cJ that suppress cochlear aplasia and associated deafness.
Volume: 19
Issue: 9
Pages: 634-9
Publication
First Author: Nguyen LXT
Year: 2021
Journal: Leukemia
Title: Cytoplasmic DROSHA and non-canonical mechanisms of MiR-155 biogenesis in FLT3-ITD acute myeloid leukemia.
Volume: 35
Issue: 8
Pages: 2285-2298
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
Publication
First Author: Herold A
Year: 2000
Journal: Mol Cell Biol
Title: TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture.
Volume: 20
Issue: 23
Pages: 8996-9008
Protein
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 962  
Fragment?: false
Publication
First Author: Tunnicliffe RB
Year: 2014
Journal: PLoS Pathog
Title: Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF.
Volume: 10
Issue: 2
Pages: e1003907
Protein
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 691  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 475  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 685  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 887  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 282  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 418  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 509  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 620  
Fragment?: false