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 |
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•
•
•
•
•
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Publication |
First Author: |
The Gene Ontology Consortium |
Year: |
2010 |
|
Title: |
Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs |
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•
•
•
•
•
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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 |
|
•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
|
Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations |
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•
•
•
•
•
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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). |
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•
•
•
•
•
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Publication |
First Author: |
Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas |
Year: |
2010 |
|
Title: |
Annotation inferences using phylogenetic trees |
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•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Database and National Center for Biotechnology Information |
Year: |
2000 |
Journal: |
Database Release |
Title: |
Entrez Gene Load |
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•
•
•
•
•
|
Publication |
First Author: |
Allen Institute for Brain Science |
Year: |
2004 |
Journal: |
Allen Institute |
Title: |
Allen Brain Atlas: mouse riboprobes |
|
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•
•
•
•
•
|
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 |
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|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI) |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Consensus CDS project |
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•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Group |
Year: |
2003 |
Journal: |
Database Procedure |
Title: |
Automatic Encodes (AutoE) Reference |
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•
•
•
•
•
|
Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
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•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
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•
•
•
•
•
|
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 |
|
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•
•
•
•
•
|
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 |
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•
•
•
•
•
|
Strain |
Attribute String: |
targeted mutation, mutant stock |
|
•
•
•
•
•
|
Publication |
First Author: |
GarcÃa-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) []. |
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•
•
•
•
•
|
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 |
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•
•
•
•
•
|