Type |
Details |
Score |
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 |
|
|
|
|
•
•
•
•
•
|
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 |
|
•
•
•
•
•
|
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. |
|
•
•
•
•
•
|
HT Experiment |
Series Id: |
GSE82002 |
Experiment Type: |
RNA-Seq |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
|
•
•
•
•
•
|
Publication |
First Author: |
Guo J |
Year: |
2019 |
Journal: |
Nat Cell Biol |
Title: |
AKT methylation by SETDB1 promotes AKT kinase activity and oncogenic functions. |
Volume: |
21 |
Issue: |
2 |
Pages: |
226-237 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
500
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
488
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
526
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
527
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
755
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1308
 |
Fragment?: |
false |
|
•
•
•
•
•
|
HT Experiment |
Series Id: |
E-GEOD-60377 |
Experiment Type: |
RNA-Seq |
Study Type: |
WT vs. Mutant |
Source: |
GEO |
|
•
•
•
•
•
|
Interaction Experiment |
Description: |
Dynamics of Setdb1 expression in early mouse development. |
|
•
•
•
•
•
|
Publication |
First Author: |
Liu T |
Year: |
2017 |
Journal: |
Reproduction |
Title: |
SETDB1 plays an essential role in maintenance of gonocyte survival in pigs. |
Volume: |
154 |
Issue: |
1 |
Pages: |
23-34 |
|
•
•
•
•
•
|
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: |
Zhang H |
Year: |
2014 |
Journal: |
Stem Cells |
Title: |
MiR-7, inhibited indirectly by lincRNA HOTAIR, directly inhibits SETDB1 and reverses the EMT of breast cancer stem cells by downregulating the STAT3 pathway. |
Volume: |
32 |
Issue: |
11 |
Pages: |
2858-68 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ishimoto K |
Year: |
2016 |
Journal: |
PLoS One |
Title: |
Ubiquitination of Lysine 867 of the Human SETDB1 Protein Upregulates Its Histone H3 Lysine 9 (H3K9) Methyltransferase Activity. |
Volume: |
11 |
Issue: |
10 |
Pages: |
e0165766 |
|
•
•
•
•
•
|
Allele |
Name: |
SET domain, bifurcated 1; targeted mutation 1, Shanghai Model Organisms Center |
Allele Type: |
Targeted |
Attribute String: |
Conditional ready, No functional change |
|
•
•
•
•
•
|
Publication |
First Author: |
Ceol CJ |
Year: |
2011 |
Journal: |
Nature |
Title: |
The histone methyltransferase SETDB1 is recurrently amplified in melanoma and accelerates its onset. |
Volume: |
471 |
Issue: |
7339 |
Pages: |
513-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ropa J |
Year: |
2018 |
Journal: |
Oncotarget |
Title: |
PAF1 complex interactions with SETDB1 mediate promoter H3K9 methylation and transcriptional repression of Hoxa9 and Meis1 in acute myeloid leukemia. |
Volume: |
9 |
Issue: |
31 |
Pages: |
22123-22136 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1521
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
230
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
170
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1519
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1173
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
404
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
105
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1521
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
RESF1 is involved in retroelement silencing. It regulates repressive epigenetic modifications associated with SETDB1 []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Blackburn ML |
Year: |
2003 |
Journal: |
Biochim Biophys Acta |
Title: |
Genomic structure and expression of the mouse ESET gene encoding an ERG-associated histone methyltransferase with a SET domain. |
Volume: |
1629 |
Issue: |
1-3 |
Pages: |
8-14 |
|
•
•
•
•
•
|
Allele |
Name: |
gene trap ROSA 26, Philippe Soriano; targeted mutation 2, Atsushi Iwama |
Allele Type: |
Targeted |
Attribute String: |
Conditional ready, Inserted expressed sequence, Reporter |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, targeted mutation |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This domain is often found in the N-terminal region of proteins carrying the SET domain, such as the SETDB1 protein from Humans. SETDB1 is a histone methyltransferase that suppresses gene expression and modulates heterochromatin formation through H3K9me2/3 []. |
|
•
•
•
•
•
|
HT Experiment |
Series Id: |
E-GEOD-77636 |
Experiment Type: |
RNA-Seq |
Study Type: |
WT vs. Mutant |
Source: |
GEO |
|
•
•
•
•
•
|
Strain |
Attribute String: |
mutant strain, congenic, targeted mutation |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This is the second TUDOR domain found in SETDB1 enzymes () from mammals, also known as Eggless in Drosophila []. In Drosophila, SetdB1 (Egg) is important for oogenesis and the silencing of chromosome 4 []. SET domain, bifurcated 1 (SETDB1) is a histone methyltransferase (HMT) that methylates lysine 9 on histone H3 (H3K9). The enzymatic activity of SETDB1, in association with MBD1-containing chromatin-associated factor 1 (MCAF1), converts H3K9me2 to H3K9me3 and represses subsequent transcription. SETDB1 is amplified in cancers such as melanoma and lung cancer, and increased expression of SETDB1 promotes tumorigenesis in a zebrafish melanoma model. In addition, SETDB1 is required for endogenous retrovirus silencing during early embryogenesis, inhibition of adipocyte differentiation, and differentiation of mesenchymal cells into osteoblasts []. The tandem Tudor domains in the N-terminal region are involved in protein-protein interactions []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This is the first TUDOR domain found in SETDB1 enzymes () from animals, also known as Eggless in Drosophila []. In Drosophila, SetdB1 (Egg) is important for oogenesis and the silencing of chromosome 4 []. SET domain, bifurcated 1 (SETDB1) is a histone methyltransferase (HMT) that methylates lysine 9 on histone H3 (H3K9). The enzymatic activity of SETDB1, in association with MBD1-containing chromatin-associated factor 1 (MCAF1), converts H3K9me2 to H3K9me3 and represses subsequent transcription. SETDB1 is amplified in cancers such as melanoma and lung cancer, and increased expression of SETDB1 promotes tumorigenesis in a zebrafish melanoma model. In addition, SETDB1 is required for endogenous retrovirus silencing during early embryogenesis, inhibition of adipocyte differentiation, and differentiation of mesenchymal cells into osteoblasts []. The tandem Tudor domains in the N-terminal region are involved in protein-protein interactions []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Tachibana K |
Year: |
2015 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Analysis of the subcellular localization of the human histone methyltransferase SETDB1. |
Volume: |
465 |
Issue: |
4 |
Pages: |
725-31 |
|
•
•
•
•
•
|
HT Experiment |
|
Experiment Type: |
RNA-Seq |
Study Type: |
WT vs. Mutant |
Source: |
GEO |
|
•
•
•
•
•
|
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gresakova V |
Year: |
2019 |
Journal: |
Exp Cell Res |
Title: |
Fam208a orchestrates interaction protein network essential for early embryonic development and cell division. |
Volume: |
382 |
Issue: |
1 |
Pages: |
111437 |
|
•
•
•
•
•
|
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 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
51
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
745
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
293
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
TASOR is a key component of the HUSH complex, a vertebrate-specific multiprotein complex that mediates epigenetic repression of both exogenous and endogenous genetic elements [, , ]. The HUSH complex regulates H3K9me3 deposition by promoting recruitment of SETDB1 and also recruits MORC2 to compact chromatin [, , ]. The HUSH complex represses L1 retrotransposons and is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed []. TASOR is crucial in early embryonic development [], and contains a catalytically-inactive PARP domain, necessary for epigenetic regulation of target elements. |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhu Y |
Year: |
2018 |
Journal: |
Nature |
Title: |
NP220 mediates silencing of unintegrated retroviral DNA. |
Volume: |
564 |
Issue: |
7735 |
Pages: |
278-282 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bhargava S |
Year: |
2017 |
Journal: |
Sci Rep |
Title: |
The epigenetic modifier Fam208a is required to maintain epiblast cell fitness. |
Volume: |
7 |
Issue: |
1 |
Pages: |
9322 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1610
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1701
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Tchasovnikarova IA |
Year: |
2017 |
Journal: |
Nat Genet |
Title: |
Hyperactivation of HUSH complex function by Charcot-Marie-Tooth disease mutation in MORC2. |
Volume: |
49 |
Issue: |
7 |
Pages: |
1035-1044 |
|
•
•
•
•
•
|
Publication |
First Author: |
Liu N |
Year: |
2018 |
Journal: |
Nature |
Title: |
Selective silencing of euchromatic L1s revealed by genome-wide screens for L1 regulators. |
Volume: |
553 |
Issue: |
7687 |
Pages: |
228-232 |
|
•
•
•
•
•
|
Publication |
First Author: |
Douse CH |
Year: |
2020 |
Journal: |
Nat Commun |
Title: |
TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control. |
Volume: |
11 |
Issue: |
1 |
Pages: |
4940 |
|
•
•
•
•
•
|
Publication |
First Author: |
Xiao X |
Year: |
2016 |
Journal: |
Immunity |
Title: |
The Costimulatory Receptor OX40 Inhibits Interleukin-17 Expression through Activation of Repressive Chromatin Remodeling Pathways. |
Volume: |
44 |
Issue: |
6 |
Pages: |
1271-83 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wu M |
Year: |
2023 |
Journal: |
Cell Rep |
Title: |
Nucleoporin Seh1 maintains Schwann cell homeostasis by regulating genome stability and necroptosis. |
Volume: |
42 |
Issue: |
7 |
Pages: |
112802 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hagelkruys A |
Year: |
2022 |
Journal: |
Sci Adv |
Title: |
The HUSH complex controls brain architecture and protocadherin fidelity. |
Volume: |
8 |
Issue: |
44 |
Pages: |
eabo7247 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pereira RM |
Year: |
2014 |
Journal: |
Nat Commun |
Title: |
Jarid2 is induced by TCR signalling and controls iNKT cell maturation. |
Volume: |
5 |
|
Pages: |
4540 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bao X |
Year: |
2015 |
Journal: |
Cell Res |
Title: |
The p53-induced lincRNA-p21 derails somatic cell reprogramming by sustaining H3K9me3 and CpG methylation at pluripotency gene promoters. |
Volume: |
25 |
Issue: |
1 |
Pages: |
80-92 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This domain is found in eukaryotes, and is approximately 170 amino acids in length. Proteins containing this domain include TASOR and TASOR 2 (also known as FAM208A/B) proteins []. TASOR is a key component of the HUSH complex, a vertebrate-specific multiprotein complex that mediates epigenetic repression of both exogenous and endogenous genetic elements [, , ]. The HUSH complex regulates H3K9me3 deposition by promoting recruitment of SETDB1 and also recruits MORC2 to compact chromatin [, , ]. The HUSH complex represses L1 retrotransposons and is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed []. TASOR is crucial in early embryonic development [], and contains a catalytically-inactive PARP domain, necessary for epigenetic regulation of target elements. |
|
•
•
•
•
•
|
Publication |
First Author: |
Tchasovnikarova IA |
Year: |
2015 |
Journal: |
Science |
Title: |
GENE SILENCING. Epigenetic silencing by the HUSH complex mediates position-effect variegation in human cells. |
Volume: |
348 |
Issue: |
6242 |
Pages: |
1481-1485 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hu G |
Year: |
2023 |
Journal: |
Int J Mol Sci |
Title: |
Atf7ip Inhibits Osteoblast Differentiation via Negative Regulation of the Sp7 Transcription Factor. |
Volume: |
24 |
Issue: |
5 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Nifuji A |
Year: |
2010 |
Journal: |
Exp Cell Res |
Title: |
Nemo-like kinase (NLK) expression in osteoblastic cells and suppression of osteoblastic differentiation. |
Volume: |
316 |
Issue: |
7 |
Pages: |
1127-36 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2382
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
163
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1279
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
148
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
323
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Roloff TC |
Year: |
2003 |
Journal: |
BMC Genomics |
Title: |
Comparative study of methyl-CpG-binding domain proteins. |
Volume: |
4 |
Issue: |
1 |
Pages: |
1 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Methylation at CpG dinucleotide, the most common DNA modification ineukaryotes, has been correlated with gene silencing associated with variousphenomena such as genomic imprinting, transposon and chromosome X inactivation, differentiation, and cancer. Effects of DNA methylation are mediated through proteins which bind to symmetrically methylated CpGs. Such proteins contain a specific domain of ~70 residues, the methyl-CpG-binding domain (MBD), which is linked to additional domains associated with chromatin, such as the bromodomain, the AT hook motif,the SET domain, or the PHD finger. MBD-containing proteins appear to act as structural proteins, which recruit a variety of histone deacetylase (HDAC) complexes and chromatin remodelling factors, leading to chromatin compaction and, consequently, to transcriptional repression. The MBD of MeCP2, MBD1, MBD2, MBD4 and BAZ2 mediates binding to DNA, in case of MeCP2, MBD1 and MBD2 preferentially to methylated CpG. In case of human MBD3 and SETDB1 the MBD has been shown to mediate protein-protein interactions [, ].The MBD folds into an alpha/beta sandwich structure comprising a layer oftwisted beta sheet, backed by another layer formed by the alpha1 helix and ahairpin loop at the C terminus. These layers are both amphipathic, with the alpha1 helix and the beta sheet lying parallel and the hydrophobic faces tightly packed against each other. The beta sheet is composed of two long inner strands (beta2 and beta3) sandwiched by two shorter outer strands (beta1 and beta4) []. |
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Publication |
First Author: |
Elsässer SJ |
Year: |
2015 |
Journal: |
Nature |
Title: |
Histone H3.3 is required for endogenous retroviral element silencing in embryonic stem cells. |
Volume: |
522 |
Issue: |
7555 |
Pages: |
240-244 |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1498
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Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
365
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1753
 |
Fragment?: |
true |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
386
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
386
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
241
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1728
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
102
 |
Fragment?: |
true |
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Publication |
First Author: |
Ohki I |
Year: |
2001 |
Journal: |
Cell |
Title: |
Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA. |
Volume: |
105 |
Issue: |
4 |
Pages: |
487-97 |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
285
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
414
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
484
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1003
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
172
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
130
 |
Fragment?: |
true |
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•
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
181
 |
Fragment?: |
true |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
189
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
261
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
764
 |
Fragment?: |
true |
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