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Search results 101 to 144 out of 144 for Gar1

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Type Details Score
Allele
Gar1<Gt(IST14708B3)Tigm> | MGI:5257476
 
Name: GAR1 ribonucleoprotein; gene trap IST14708B3, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Protein
Q9CY66-3
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Protein
Q9CY66-2
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: false
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Genotype
Genotype
Symbol: Gar1/Gar1<+>
Background: C57BL/6N-Gar1/Ics
Zygosity: ht
Has Mutant Allele: true
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GO Term
GO:0072588 | box H/ACA RNP complex
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Publication
8766832 | J:34090
First Author: Ardell MD
Year: 1996
Journal: FEBS Lett
Title: The beta subunit of human rod photoreceptor cGMP-gated cation channel is generated from a complex transcription unit.
Volume: 389
Issue: 2
Pages: 213-8
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Publication
8797828 | J:49295
First Author: Balakin AG
Year: 1996
Journal: Cell
Title: The RNA world of the nucleolus: two major families of small RNAs defined by different box elements with related functions.
Volume: 86
Issue: 5
Pages: 823-34
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Protein Domain
IPR040309 | Naf1
Type: Family
Description: Naf1 is an RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex, disappearing during maturation of the complex and being replaced by Gar1 to yield mature H/ACA snoRNPs complex. The core domain of Naf1 is homologous to the core domain of Gar1, suggesting that they share a common Cbf5 binding surface [].
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Publication
17612558 | -
First Author: Leulliot N
Year: 2007
Journal: J Mol Biol
Title: The box H/ACA RNP assembly factor Naf1p contains a domain homologous to Gar1p mediating its interaction with Cbf5p.
Volume: 371
Issue: 5
Pages: 1338-53
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Protein
F6SL78
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Publication
18473479 | -
First Author: Reichow SL
Year: 2008
Journal: Biochemistry
Title: Nop10 is a conserved H/ACA snoRNP molecular adaptor.
Volume: 47
Issue: 23
Pages: 6148-56
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Publication
22085966 | -
First Author: Walbott H
Year: 2011
Journal: Genes Dev
Title: The H/ACA RNP assembly factor SHQ1 functions as an RNA mimic.
Volume: 25
Issue: 22
Pages: 2398-408
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Publication
22117216 | -
First Author: Li S
Year: 2011
Journal: EMBO J
Title: Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita.
Volume: 30
Issue: 24
Pages: 5010-20
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Protein Domain
IPR023532 | Nop10_arc-typ
Type: Family
Description: Nop10 is a component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs). H/ACA snoRNPs are primarily responsible for catalysing the isomerisation of uridine to pseudouridine (Psi) in ribosomal and other cellular RNAs. The protein component of the H/ACA snoRNP consists of Cbf5, Gar1, Nhp2 and Nop10. The complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind. Nop10 has an essential role in the assembly and activity of these particles and binds directly to the Cbf5 to form the minimal active enzyme in archaea. The complex interacts with snoRNAs, Nop10 acting as a molecular adaptor for guiding snoRNP assembly [].
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Protein Domain
IPR039742 | Shq1
Type: Family
Description: The box H/ACA ribonucleoproteins (RNPs) are protein-RNA complexes responsible for pseudouridylation, the most abundant post-transcriptional modification of cellular RNAs []. Each distinct H/ACA RNA assembles with a common set of four proteins, Cbf5 (NAP57 in rodents and dyskerin in humans), Nop10, Nhp2 (L7Ae in archaea) and Gar1 []. Shq1 is an essential assembly factor for H/ACA ribonucleoproteins (RNPs) required for ribosome biogenesis, pre-mRNA splicing, and telomere maintenance []. It interacts with Cbf5 and may function as an assembly chaperone that protects the Cbf5 protein complexes from non-specific RNA binding and aggregation before assembly of H/ACA RNA [].
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Publication
16101307 | -
First Author: Kuorelahti S
Year: 2005
Journal: Biochemistry
Title: Identification in the mold Hypocrea jecorina of the first fungal D-galacturonic acid reductase.
Volume: 44
Issue: 33
Pages: 11234-40
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Protein Domain
IPR038664 | Gar1/Naf1_Cbf5-bd_sf
Type: Homologous_superfamily
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].Naf1 is an RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex, disappearing during maturation of the complex and being replaced by Gar1 to yield mature H/ACA snoRNPs complex. The core domain of Naf1 is homologous to the core domain of Gar1, suggesting that they share a common Cbf5 binding surface [].
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Protein Domain
IPR044495 | AKR3D
Type: Family
Description: This entry represents aldo-keto reductase family 3D, including D-galacturonate reductase Gar1 from Hypocrea jecorina. Gar1 mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH [].In general, the aldo-keto reductase (AKR) protein superfamily members reduce carbonyl substrates such as: sugar aldehydes, keto-steroids, keto-prostaglandins, retinals, quinones, and lipid peroxidation by-products [, ]. However, there are some exceptions, such as the reduction of steroid double bonds catalysed by AKR1D enzymes (5beta-reductases); and the oxidation of proximate carcinogen trans-dihydrodiol polycyclic aromatic hydrocarbons; while the beta-subunits of potassium gated ion channels (AKR6 family) control Kv channel opening [].Structurally, they contain an (alpha/beta)8-barrel motif, display large loops at the back of the barrel which govern substrate specificity, and have a conserved cofactor binding domain. The binding site is located in a large, deep, elliptical pocket in the C-terminal end of the beta sheet, the substrate being bound in an extended conformation. The hydrophobic nature of the pocket favours aromatic and apolar substrates over highly polar ones []. They catalyse an ordered bi bi kinetic mechanism in which NAD(P)H cofactor binds first and leaves last []. Binding of the NADPH coenzyme causes a massive conformational change, reorienting a loop, effectively locking the coenzyme in place. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases [].
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Protein Domain
IPR007504 | H/ACA_rnp_Gar1/Naf1
Type: Family
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].Naf1 is an RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex, disappearing during maturation of the complex and being replaced by Gar1 to yield mature H/ACA snoRNPs complex. The core domain of Naf1 is homologous to the core domain of Gar1, suggesting that they share a common Cbf5 binding surface [].
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Protein
Q3UMQ8
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
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Protein
E9QJT2
Organism: Mus musculus/domesticus
Length: 597  
Fragment?: false
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Publication
16647858 | -
First Author: Meier UT
Year: 2006
Journal: Trends Biochem Sci
Title: How a single protein complex accommodates many different H/ACA RNAs.
Volume: 31
Issue: 6
Pages: 311-5
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Publication
10871366 | -
First Author: Watanabe Y
Year: 2000
Journal: Nucleic Acids Res
Title: Evolutionary appearance of genes encoding proteins associated with box H/ACA snoRNAs: cbf5p in Euglena gracilis, an early diverging eukaryote, and candidate Gar1p and Nop10p homologs in archaebacteria.
Volume: 28
Issue: 12
Pages: 2342-52
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Protein
D3YZ09
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: true
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Protein
Q3TKG5
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: false
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Protein Domain
IPR036756 | H/ACA_rnp_Nop10_sf
Type: Homologous_superfamily
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].In eukaryotes Nop10 is a nucleolar protein that is specifically associated with H/ACA snoRNAs. It is essential for normal 18S rRNA production and rRNA pseudouridylation by the ribonucleoprotein particles containing H/ACA snoRNAs (H/ACA snoRNPs). Nop10 is probably necessary for the stability of these RNPs []. The Nop10 domain structure has a rubredoxin-like fold.
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Protein Domain
IPR007264 | H/ACA_rnp_Nop10
Type: Family
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].In eukaryotes Nop10 is a nucleolar protein that is specifically associated with H/ACA snoRNAs. It is essential for normal 18S rRNA production and rRNA pseudouridylation by the ribonucleoprotein particles containing H/ACA snoRNAs (H/ACA snoRNPs). Nop10 is probably necessary for the stability of these RNPs [].
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Protein
Q9CQS2
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
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Publication
19917616 | -
First Author: Hamma T
Year: 2010
Journal: J Biol Chem
Title: The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification.
Volume: 285
Issue: 2
Pages: 805-9
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Publication
9843512 | -
First Author: Henras A
Year: 1998
Journal: EMBO J
Title: Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs.
Volume: 17
Issue: 23
Pages: 7078-90
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Protein
Q7TMX5
Organism: Mus musculus/domesticus
Length: 569  
Fragment?: false
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Publication
17631273 | -
First Author: Dobbyn HC
Year: 2007
Journal: Biochem Biophys Res Commun
Title: Analysis of pre-mRNA and pre-rRNA processing factor Snu13p structure and mutants.
Volume: 360
Issue: 4
Pages: 857-62
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Publication
14730029 | -
First Author: Dobbyn HC
Year: 2004
Journal: RNA
Title: Analysis of Snu13p mutations reveals differential interactions with the U4 snRNA and U3 snoRNA.
Volume: 10
Issue: 2
Pages: 308-20
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Publication
12215523 | -
First Author: Galardi S
Year: 2002
Journal: Mol Cell Biol
Title: Purified box C/D snoRNPs are able to reproduce site-specific 2'-O-methylation of target RNA in vitro.
Volume: 22
Issue: 19
Pages: 6663-8
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Publication
15044956 | -
First Author: Wang C
Year: 2004
Journal: EMBO J
Title: Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins.
Volume: 23
Issue: 8
Pages: 1857-67
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Protein Domain
IPR002415 | H/ACA_rnp_Nhp2-like
Type: Family
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].This entry represents H/ACA ribonucleoprotein complex subunit NHP2 and similar proteins from eukaryotes, including NHP2-like protein 1 from mammals (SNU13 homologue) and 13 kDa ribonucleoprotein-associated protein (SNU13) from yeast.Nhp2 is part of a complex which catalyses pseudouridylation of rRNA and is required for rRNA biogenesis. This involves the isomerisation of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilise the conformation of rRNAs. Nph2 associates non-specifically with RNA secondary structures instead of directly binding to an specific RNA motif. This protein seem to have evolved from the archaeal ribosomal L7Ae protein family []. Human SNU13 homologue is involved in pre-mRNA splicing as component of the spliceosome []. The protein undergoes a conformational change upon RNA-binding [].SNU13 from Saccharomyces cerevisiae (Baker's yeast) is also a component of the spliceosome and rRNA processing machinery, required for splicing of pre-mRNA and essential for the accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs [, , ].
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Publication
17412961 | -
First Author: Liu S
Year: 2007
Journal: Science
Title: Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.
Volume: 316
Issue: 5821
Pages: 115-20
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Publication
28781166 | -
First Author: Bertram K
Year: 2017
Journal: Cell
Title: Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.
Volume: 170
Issue: 4
Pages: 701-713.e11
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Protein
Q9CRB2
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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Protein
Q9D0T1
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
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Publication
25304492 | -
 
First Author: Penning TM
Year: 2015
Journal: Chem Biol Interact
Title: The aldo-keto reductases (AKRs): Overview.
Volume: 234
Pages: 236-46
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Publication
2498333 | -
First Author: Bohren KM
Year: 1989
Journal: J Biol Chem
Title: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.
Volume: 264
Issue: 16
Pages: 9547-51
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Publication
1447221 | -
First Author: Borhani DW
Year: 1992
Journal: J Biol Chem
Title: The crystal structure of the aldose reductase.NADPH binary complex.
Volume: 267
Issue: 34
Pages: 24841-7
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Publication
1621098 | -
First Author: Wilson DK
Year: 1992
Journal: Science
Title: An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.
Volume: 257
Issue: 5066
Pages: 81-4
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