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Search results 301 to 355 out of 355 for Cbx3

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0.024s
Type Details Score
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication        
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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 (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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
Strain
Attribute String: targeted mutation, mutant stock
Publication
First Author: García-Cao M
Year: 2004
Journal: Nat Genet
Title: Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases.
Volume: 36
Issue: 1
Pages: 94-9
Publication
First Author: Benetti R
Year: 2007
Journal: Nat Genet
Title: Telomere length regulates the epigenetic status of mammalian telomeres and subtelomeres.
Volume: 39
Issue: 2
Pages: 243-50
Protein Domain
Type: Domain
Description: Chromodomains serve as chromatin-targeting modules, general protein interaction elements as well as dimerization sites. They are found in many chromatin-associated proteins that bind modified histone tails for chromatin targeting. Chromodomains often recognize modified lysines through their aromatic cage thus targeting proteins to chromatin. Family members such as GEN1 carry a chomodomain which directly contacts DNA and its truncation severely hampers GEN1's catalytic activity. The chromodomain allows GEN1 to correctly position itself against DNA molecules, and without the chromodomain, GEN1's ability to cut DNA was severely impaired. The GEN1 chromodomain was found to be distantly related to the CDY chromodomains and chromobox proteins, particularly to the chromo-shadow domains of CBX1, CBX3 and CBX5. Furthermore, it is conserved from yeast (Yen1) to humans with the only exception being the Caenorhabditis elegans GEN1, which has a much smaller protein size of 443 amino acids compared to yeast Yen1 (759 aa) or human GEN1 (908 aa) [].
Publication
First Author: Ayyanathan K
Year: 2003
Journal: Genes Dev
Title: Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation.
Volume: 17
Issue: 15
Pages: 1855-69
Publication    
First Author: Lee SH
Year: 2015
Journal: Elife
Title: Human Holliday junction resolvase GEN1 uses a chromodomain for efficient DNA recognition and cleavage.
Volume: 4
Protein Domain
Type: Family
Description: SETDB1 is a member of the histone-lysine N-methyltransferase Suvar3-9 subfamily. Members of this subfamily trimethylate 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones []. This enzyme mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. It probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation [].Methyltransferases (EC [intenz:2.1.1.-]) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule [, , ]. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM []. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids [, , ]. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [, , ]. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.
Publication
First Author: Wang H
Year: 2003
Journal: Mol Cell
Title: mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression.
Volume: 12
Issue: 2
Pages: 475-87
Publication
First Author: Aagaard L
Year: 1999
Journal: EMBO J
Title: Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31.
Volume: 18
Issue: 7
Pages: 1923-38
Publication
First Author: Vaquero A
Year: 2007
Journal: Nature
Title: SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation.
Volume: 450
Issue: 7168
Pages: 440-4
Publication
First Author: Peters AH
Year: 2001
Journal: Cell
Title: Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability.
Volume: 107
Issue: 3
Pages: 323-37
Publication
First Author: Peters AH
Year: 2003
Journal: Mol Cell
Title: Partitioning and plasticity of repressive histone methylation states in mammalian chromatin.
Volume: 12
Issue: 6
Pages: 1577-89
Publication
First Author: Rice JC
Year: 2003
Journal: Mol Cell
Title: Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains.
Volume: 12
Issue: 6
Pages: 1591-8
Publication
First Author: Alvarez-Venegas R
Year: 2002
Journal: Gene
Title: SET-domain proteins of the Su(var)3-9, E(z) and trithorax families.
Volume: 285
Issue: 1-2
Pages: 25-37
Publication
First Author: Firestein R
Year: 2000
Journal: Mol Cell Biol
Title: Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9.
Volume: 20
Issue: 13
Pages: 4900-9
Publication
First Author: Ait-Si-Ali S
Year: 2004
Journal: EMBO J
Title: A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells.
Volume: 23
Issue: 3
Pages: 605-15
Publication
First Author: Mal AK
Year: 2006
Journal: EMBO J
Title: Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic differentiation.
Volume: 25
Issue: 14
Pages: 3323-34
Publication
First Author: Carbone R
Year: 2006
Journal: Mol Cell Biol
Title: Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein.
Volume: 26
Issue: 4
Pages: 1288-96
Publication
First Author: Bradley SP
Year: 2006
Journal: J Immunol
Title: The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA.
Volume: 177
Issue: 2
Pages: 1179-88
Protein Domain
Type: Family
Description: Members of this family trimethylate 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. It also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. This enzyme mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats [, , ]. SUV39H1 (the human ortholog) is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation[], regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein [], BMP-induced repression, repression of switch recombination to IgA []and regulation of telomere length [, ]. SUV39H1 is a component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD+/NADP+ ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus []. The activity of this enzyme has been mapped to the SET domain and the adjacent cysteine-rich regions []. The SET domain was originally identified in Su(var)3-9, E(z) and Trithorax genes in Drosophila melanogaster (Fruit fly) []. The sequence conservation pattern and structure analysis of the SET domain provides clues regarding the possible active site residues of the domain. There are three conserved sequence motifs in most of the SET domains. The N-terminal motif (I) has characteristic glycines. The central motif (II) has a distinct pattern of polar and charged residues (Asn, His). The C-terminal conserved motif (III) has a characteristic dyad of polar residues. It has been shown that deregulated SUV39H1 interferes at multiple levels with mammalian higher-order chromatin organisation []and these properties depend primarily on the SET domain [, ]. Methyltransferases (EC [intenz:2.1.1.-]) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule [, , ]. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM []. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids [, , ]. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [, , ]. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.
Publication
First Author: Murayama A
Year: 2008
Journal: Cell
Title: Epigenetic control of rDNA loci in response to intracellular energy status.
Volume: 133
Issue: 4
Pages: 627-39
Publication
First Author: Rea S
Year: 2000
Journal: Nature
Title: Regulation of chromatin structure by site-specific histone H3 methyltransferases.
Volume: 406
Issue: 6796
Pages: 593-9
Protein
Organism: Mus musculus/domesticus
Length: 739  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 908  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1307  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1307  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1308  
Fragment?: false
Publication
First Author: Schluckebier G
Year: 1995
Journal: J Mol Biol
Title: Universal catalytic domain structure of AdoMet-dependent methyltransferases.
Volume: 247
Issue: 1
Pages: 16-20
Publication  
First Author: Kozbial PZ
Year: 2005
Journal: BMC Struct Biol
Title: Natural history of S-adenosylmethionine-binding proteins.
Volume: 5
Pages: 19
Publication
First Author: Wlodarski T
Year: 2011
Journal: PLoS One
Title: Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome.
Volume: 6
Issue: 8
Pages: e23168
Protein
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 412  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 375  
Fragment?: true
Publication
First Author: Schubert HL
Year: 2003
Journal: Trends Biochem Sci
Title: Many paths to methyltransfer: a chronicle of convergence.
Volume: 28
Issue: 6
Pages: 329-35
Publication
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