Type |
Details |
Score |
Publication |
First Author: |
Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC) |
Year: |
2014 |
Journal: |
Database Release |
Title: |
Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database |
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•
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•
•
•
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Publication |
First Author: |
DDB, FB, MGI, GOA, ZFIN curators |
Year: |
2001 |
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Title: |
Gene Ontology annotation through association of InterPro records with GO terms |
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•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2003 |
|
Title: |
MGI Sequence Curation Reference |
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•
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•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
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Title: |
Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database |
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•
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Publication |
First Author: |
Adams DJ |
Year: |
2024 |
Journal: |
Nature |
Title: |
Genetic determinants of micronucleus formation in vivo. |
Volume: |
627 |
Issue: |
8002 |
Pages: |
130-136 |
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•
•
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•
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Publication |
First Author: |
GemPharmatech |
Year: |
2020 |
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Title: |
GemPharmatech Website. |
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•
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Publication |
First Author: |
Skarnes WC |
Year: |
2011 |
Journal: |
Nature |
Title: |
A conditional knockout resource for the genome-wide study of mouse gene function. |
Volume: |
474 |
Issue: |
7351 |
Pages: |
337-42 |
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•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI) |
Year: |
2008 |
Journal: |
Database Download |
Title: |
Mouse Gene Trap Data Load from dbGSS |
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•
•
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•
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Publication |
First Author: |
GOA curators |
Year: |
2016 |
|
Title: |
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara |
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•
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•
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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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•
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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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•
•
•
•
•
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Publication |
First Author: |
MGI Genome Annotation Group and UniGene Staff |
Year: |
2015 |
Journal: |
Database Download |
Title: |
MGI-UniGene Interconnection Effort |
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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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•
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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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•
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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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•
•
•
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•
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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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•
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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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•
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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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•
•
•
•
•
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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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•
•
•
•
•
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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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•
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•
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•
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Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
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•
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•
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•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
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•
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•
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HT Experiment |
Series Id: |
GSE50845 |
Experiment Type: |
transcription profiling by array |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
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•
•
•
•
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Publication |
First Author: |
Quinn PM |
Year: |
2019 |
Journal: |
Hum Mol Genet |
Title: |
Loss of CRB2 in Müller glial cells modifies a CRB1-associated retinitis pigmentosa phenotype into a Leber congenital amaurosis phenotype. |
Volume: |
28 |
Issue: |
1 |
Pages: |
105-123 |
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•
•
•
•
•
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Publication |
First Author: |
Botuyan MV |
Year: |
2006 |
Journal: |
Cell |
Title: |
Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. |
Volume: |
127 |
Issue: |
7 |
Pages: |
1361-73 |
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•
•
•
•
•
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Publication |
First Author: |
Sanders SL |
Year: |
2004 |
Journal: |
Cell |
Title: |
Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. |
Volume: |
119 |
Issue: |
5 |
Pages: |
603-14 |
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•
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DO Term |
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•
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DO Term |
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•
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Publication |
First Author: |
Lu R |
Year: |
2013 |
Journal: |
Trends Biochem Sci |
Title: |
Tudor: a versatile family of histone methylation 'readers'. |
Volume: |
38 |
Issue: |
11 |
Pages: |
546-55 |
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•
•
•
•
•
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Protein Domain |
Type: |
Domain |
Description: |
This is the tudor domain found in DNA repair protein Crb2. Structural and functional studies of Crb2 and its mammalian homologue 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1 []. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2 []. |
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•
•
•
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Protein Domain |
Type: |
Family |
Description: |
This entry represents fungal histone-lysine N-methyltransferase Set9 that belongs to the Suv4-20 family. This enzyme catalyzes mono-, di-, and trimethylation of H4K20. It participates in DNA damage response by giving a 'histone mark' required for the recruitment of the checkpoint protein Crb2 to sites of DNA damage [, ]. |
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•
•
•
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•
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Publication |
First Author: |
Wang Y |
Year: |
2009 |
Journal: |
Mol Cell |
Title: |
Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein. |
Volume: |
33 |
Issue: |
4 |
Pages: |
428-37 |
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•
•
•
•
•
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Protein Domain |
Type: |
Domain |
Description: |
This is one of two Tudor-like domains found in the N-terminal region of RapA proteins. RapA is an abundant RNAP-associated protein of 110kDa molecular weight with ATPase activity.It forms a stable complex with the RNAP core enzyme, but not with the holoenzyme. The ATPase activity of RapA increases upon its binding to RNAP []. The N-terminal region of RapA contains two copies of a Tudor-like domains, both folded as a highly bent antiparallel β-sheet. This fold is also found in transcription factor NusG , ribosomal protein L24, human SMN (survival of motor neuron) protein, mammalian DNA repair factor 53BP1, putative fission yeast DNA repair factor Crb2 and bacterial transcription-repair coupling factor known as Mfd. The functional roles of the N-terminal region homologs in these proteins suggest that the Tudor-like domains of RapA may interact with both nucleic acids and RNAP []. |
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•
•
•
•
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Protein Domain |
Type: |
Domain |
Description: |
This is the second of two Tudor-like domains found in the N-terminal region of RapA proteins. RapA is an abundant RNAP-associated protein of 110kDa molecular weight with ATPase activity. It forms a stable complex with the RNAP core enzyme, but not with the holoenzyme. The ATPase activity of RapA increases upon its binding to RNAP []. The N-terminal region of RapA contains two copies of a Tudor-like domains, both folded as a highly bent antiparallel β-sheet. This fold is also found in transcription factor NusG , ribosomal protein L24, human SMN (survival of motor neuron) protein, mammalian DNA repair factor 53BP1, putative fission yeast DNA repair factor Crb2 and bacterial transcription-repair coupling factor known as Mfd. The functional roles of the N-terminal region homologs in these proteins suggest that the Tudor-like domains of RapA may interact with both nucleic acids and RNAP []. |
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•
•
•
•
•
|
Publication |
First Author: |
Shaw G |
Year: |
2008 |
Journal: |
Structure |
Title: |
Structure of RapA, a Swi2/Snf2 protein that recycles RNA polymerase during transcription. |
Volume: |
16 |
Issue: |
9 |
Pages: |
1417-27 |
|
•
•
•
•
•
|
Publication |
First Author: |
Liu B |
Year: |
2015 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Structural basis for transcription reactivation by RapA. |
Volume: |
112 |
Issue: |
7 |
Pages: |
2006-10 |
|
•
•
•
•
•
|
Publication |
First Author: |
Richard M |
Year: |
2006 |
Journal: |
Hum Mol Genet |
Title: |
Towards understanding CRUMBS function in retinal dystrophies. |
Volume: |
15 Spec No 2 |
|
Pages: |
R235-43 |
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•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry includes Suv4-20 family members and its fungal homologue known as Set9. They are a group of histone H4K20 methyltransferases.SET9 methylates 'Lys-20' of histone H4. H4 'Lys-20' methylation is apparently not involved in the regulation of gene expression or heterochromatin function, but participates in DNA damage response by giving a 'histone mark' required for the recruitment of the checkpoint protein Crb2 to sites of DNA damage [, ].Post-translational modification of the core histones H2A, H2B, H3 and H4 play an important part in chromatin biology. Histone H4 lysine 20 methylation (H4K20me) is critical for the biological processes that ensure genome integrity, such as DNA damage repair, DNA replication and chromatin compaction []. Suv4-20 family members are a group of histone H4K20 methyltransferases that play an important role in epigenetic regulation. Lower eukaryotes have a single Suv4-20, while mammals have two closely related Suv4-20 paralogs, SUV420H1 and SUV420H2 []. In mammals H4K20me2 is generated primarily by SUV420H1/KMT5B (which can also produce H4K20me3), while H4K20me3 is mostly generated by SUV420H2/KMT5C []. |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
145
 |
Fragment?: |
false |
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•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
93
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
85
 |
Fragment?: |
true |
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•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
87
 |
Fragment?: |
true |
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•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
110
 |
Fragment?: |
true |
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•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
164
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
212
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
147
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1010
 |
Fragment?: |
false |
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•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1023
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Southall SM |
Year: |
2014 |
Journal: |
Nucleic Acids Res |
Title: |
A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases. |
Volume: |
42 |
Issue: |
1 |
Pages: |
661-71 |
|
•
•
•
•
•
|
Publication |
First Author: |
Tsang LW |
Year: |
2010 |
Journal: |
PLoS One |
Title: |
Comparative analyses of SUV420H1 isoforms and SUV420H2 reveal differences in their cellular localization and effects on myogenic differentiation. |
Volume: |
5 |
Issue: |
12 |
Pages: |
e14447 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jørgensen S |
Year: |
2013 |
Journal: |
Nucleic Acids Res |
Title: |
Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity. |
Volume: |
41 |
Issue: |
5 |
Pages: |
2797-806 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
883
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
468
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
423
 |
Fragment?: |
false |
|
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•
•
•
•
|