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Search results 301 to 393 out of 393 for Dcps

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Type Details Score
GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_09
Specimen Label: euxassay_013612_09
Detected: true
Specimen Num: 9
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_10
Specimen Label: euxassay_013612_10
Detected: true
Specimen Num: 10
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_11
Specimen Label: euxassay_013612_11
Detected: true
Specimen Num: 11
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_12
Specimen Label: euxassay_013612_12
Detected: true
Specimen Num: 12
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_13
Specimen Label: euxassay_013612_13
Detected: true
Specimen Num: 13
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_14
Specimen Label: euxassay_013612_14
Detected: true
Specimen Num: 14
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_15
Specimen Label: euxassay_013612_15
Detected: true
Specimen Num: 15
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_16
Specimen Label: euxassay_013612_16
Detected: true
Specimen Num: 16
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•
GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_17
Specimen Label: euxassay_013612_17
Detected: true
Specimen Num: 17
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_18
Specimen Label: euxassay_013612_18
Detected: true
Specimen Num: 18
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_19
Specimen Label: euxassay_013612_19
Detected: true
Specimen Num: 19
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GXD Expression
GXD Expression
 
Probe: MGI:4420595
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1625523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4824253
Age: embryonic day 14.5
Image: euxassay_013612_20
Specimen Label: euxassay_013612_20
Detected: true
Specimen Num: 20
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Publication
28700664 | J:246066
First Author: Sundberg JP
Year: 2017
Journal: PLoS One
Title: Systematic screening for skin, hair, and nail abnormalities in a large-scale knockout mouse program.
Volume: 12
Issue: 7
Pages: e0180682
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Publication
- | J:94077
     
First Author: Mutant Mouse Regional Resource Centers
Year: 2004
Journal: Unpublished
Title: Information obtained from the Mutant Mouse Regional Resource Centers (MMRRC)
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Publication
27626380 | J:236599
First Author: Dickinson ME
Year: 2016
Journal: Nature
Title: High-throughput discovery of novel developmental phenotypes.
Volume: 537
Issue: 7621
Pages: 508-514
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Publication
- | J:188991
     
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
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Publication
24194600 | J:228563
First Author: Koscielny G
Year: 2014
Journal: Nucleic Acids Res
Title: The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data.
Volume: 42
Issue: Database issue
Pages: D802-9
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Publication
12520002 | J:91812
First Author: Stryke D
Year: 2003
Journal: Nucleic Acids Res
Title: BayGenomics: a resource of insertional mutations in mouse embryonic stem cells.
Volume: 31
Issue: 1
Pages: 278-81
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Publication
- | J:211773
     
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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Publication
- | J:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
38355793 | J:345621
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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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:141210
     
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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Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:342605
       
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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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
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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Publication
- | J:164563
       
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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Publication
21267068 | J:153498
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
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
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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Publication
- | J:161428
       
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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Publication
- | J:63103
     
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
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
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
- | J:155721
     
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
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
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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Publication
23736298 | J:201094
First Author: Gogliotti RG
Year: 2013
Journal: Hum Mol Genet
Title: The DcpS inhibitor RG3039 improves survival, function and motor unit pathologies in two SMA mouse models.
Volume: 22
Issue: 20
Pages: 4084-101
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Protein
D6RFQ0
Organism: Mus musculus/domesticus
Length: 102  
Fragment?: false
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Publication
32723815 | -
First Author: Fuchs AL
Year: 2020
Journal: Proc Natl Acad Sci U S A
Title: Molecular basis of the selective processing of short mRNA substrates by the DcpS mRNA decapping enzyme.
Volume: 117
Issue: 32
Pages: 19237-19244
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Protein
Q3TBW9
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
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Protein
Q9DAR7
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: false
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Publication
16001405 | -
First Author: Han GW
Year: 2005
Journal: Proteins
Title: Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution.
Volume: 60
Issue: 4
Pages: 797-802
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Protein Domain
IPR008594 | DcpS/DCS2
Type: Family
Description: This entry represents scavenger mRNA decapping enzymes, such as Dcp2 and DcpS. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' mRNA degradation. DcpS uses cap dinucleotides or capped oligonucleotides as substrate to release m(7)GMP (N7-methyl GMP), while Dcp2 uses capped mRNA as substrate in order to hydrolyse the cap to release m(7)GDP (N7-methyl GDP) []. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The family contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues []. The central histidine within the DcpS HIT motif is critical for decapping activityand defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function. This family is related to ().
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Publication
16246173 | -
First Author: Liu H
Year: 2006
Journal: Biochem Soc Trans
Title: Decapping the message: a beginning or an end.
Volume: 34
Issue: Pt 1
Pages: 35-8
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Protein Domain
IPR011145 | Scavenger_mRNA_decap_enz_N
Type: Homologous_superfamily
Description: This superfamily represents the N-terminal domain of scavenger mRNA decapping enzymes, such as Dcp2 and DcpS. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' mRNA degradation. DcpS uses cap dinucleotides or capped oligonucleotides as substrate to release m(7)GMP (N7-methyl GMP), while Dcp2 uses capped mRNA as substrate in order to hydrolyse the cap to release m(7)GDP (N7-methyl GDP) []. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. DcpS exists as a dimer and each monomer is comprised of an N-terminal and a C-terminal region. The two N-termini form into a domain-swapped dimer and carry out substrate binding, cap dinucleotide, and hydrolysis [].
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Publication
28945765 | J:250443
First Author: Cherry JJ
Year: 2017
Journal: PLoS One
Title: In vitro and in vivo effects of 2,4 diaminoquinazoline inhibitors of the decapping scavenger enzyme DcpS: Context-specific modulation of SMN transcript levels.
Volume: 12
Issue: 9
Pages: e0185079
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Protein Domain
IPR011146 | HIT-like
Type: Domain
Description: The histidine triad motif (HIT) consists of the conserved sequence HXHXHXX (where X is a hydrophobic amino acid) at the enzymatic catalytic centre, in which the second histidine is strictly conserved and participates in catalysis with the third histidine [, , ]. Proteins containing HIT domains form a superfamily of nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides [, ]. They are highly conserved from archaea to humans and are involved in galactose metabolism, DNA repair, and tumor suppression []. HIT-containing proteins can be divided in five families based on catalytic specificities, sequence compositions, and structural similarities of its members: Hint family of protein kinase-interacting proteins, the most ancient class in this superfamily. These include adenosine 5'-monophosphoramide hydrolases (e.g. HIT-nucleotide-binding protein, or HINT) [, ]. They also have a conserved zinc-binding motif C-X-X-C (where C is a cysteine residue and X is a hydrophobic residue), and a zinc ion is coordinated by these cysteine residues, together with the first histidine residue [].Fragile HIT protein, or FINT, whose name is due to its high rate of mutation at its locus on chromosome 3 in many cancers has been characterised as a tumor suppressor and plays a role in the hydrolysis of dinucleotide polyphosphates [, ]. HINT and FINT HIT domains have a topology similar to that found in the N-terminal of protein kinases [].GalT family. These include specific nucleoside monophosphate transferases (e.g. galactose-1-phosphate uridylyltransferase, diadenosine tetraphosphate phosphorylase, and adenylyl sulphate:phosphate adenylytransferase). These HIT domains are a duplication consisting of 2 HIT-like motifs. This family binds zinc and iron [, ].Aprataxin, which hydrolyses both dinucleotide polyphosphates and phophoramidates, and is involved in DNA repair systems [, ].mRNA decapping enzyme family. These include enzymes such as DcpS and Dcp2. The HIT-domain is usually C-terminal in these proteins [, ].
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Protein
Q91Y56
Organism: Mus musculus/domesticus
Length: 34  
Fragment?: true
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Protein
Q8K4W1
Organism: Mus musculus/domesticus
Length: 44  
Fragment?: true
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Publication
1016943 | -
First Author: Tomingas R
Year: 1976
Journal: Cancer Lett
Title: Polycyclic aromatic hydrocarbons in human bronchial carcinoma.
Volume: 1
Issue: 4
Pages: 189-95
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Protein Domain
IPR036265 | HIT-like_sf
Type: Homologous_superfamily
Description: The histidine triad motif (HIT) consists of the conserved sequence HXHXHXX (where X is a hydrophobic amino acid) at the enzymatic catalytic centre, in which the second histidine is strictly conserved and participates in catalysis with the third histidine [, , ]. Proteins containing HIT domains form a superfamily of nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides [, ]. They are highly conserved from archaea to humans and are involved in galactose metabolism, DNA repair, and tumor suppression []. HIT-containing proteins can be divided in five families based on catalytic specificities, sequence compositions, and structural similarities of its members: Hint family of protein kinase-interacting proteins, the most ancient class in this superfamily. These include adenosine 5'-monophosphoramide hydrolases (e.g. HIT-nucleotide-binding protein, or HINT) [, ]. They also have a conserved zinc-binding motif C-X-X-C (where C is a cysteine residue and X is a hydrophobic residue), and a zinc ion is coordinated by these cysteine residues, together with the first histidine residue [].Fragile HIT protein, or FINT, whose name is due to its high rate of mutation at its locus on chromosome 3 in many cancers has been characterised as a tumor suppressor and plays a role in the hydrolysis of dinucleotide polyphosphates [, ]. HINT and FINT HIT domains have a topology similar to that found in the N-terminal of protein kinases [].GalT family. These include specific nucleoside monophosphate transferases (e.g. galactose-1-phosphate uridylyltransferase, diadenosine tetraphosphate phosphorylase, and adenylyl sulphate:phosphate adenylytransferase). These HIT domains are a duplication consisting of 2 HIT-like motifs. This family binds zinc and iron [, ].Aprataxin, which hydrolyses both dinucleotide polyphosphates and phophoramidates, and is involved in DNA repair systems [, ].mRNA decapping enzyme family. These include enzymes such as DcpS and Dcp2. The HIT-domain is usually C-terminal in these proteins [, ].This superfamily also includes CDP-diacylglycerol pyrophosphatases, CDH, which play a role in phospholipid metabolism and regulates phosphatidylinositol levels [], the C-terminal CwfJ domains of CWF19-like protein DRN1 from Saccharomyces cerevisiae () which is involved branched RNA metabolism, modulating the turnover of lariat-intron pre-mRNAs by the lariat-debranching enzyme DBR1 and its homologues. This C-terminal Cwfj domains contain evolutionarily conserved cysteine and histidine residues in an arrangement similar to the CCCH-class of zinc fingers [, ].
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Protein
Q9CPS6
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Protein
O89106
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
B0R1E3
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
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Protein
E9PZ91
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: false
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Protein
E9Q3M6
Organism: Mus musculus/domesticus
Length: 57  
Fragment?: true
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Protein
E9Q7F8
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: true
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Protein
F8WH96
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
F6SV10
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: true
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Protein
E9PVU9
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: true
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Publication
15904496 | -
 
First Author: Hopfe M
Year: 2005
Journal: BMC Microbiol
Title: HinT proteins and their putative interaction partners in Mollicutes and Chlamydiaceae.
Volume: 5
Pages: 27
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Publication
15273322 | -
First Author: Liu SW
Year: 2004
Journal: RNA
Title: Functional analysis of mRNA scavenger decapping enzymes.
Volume: 10
Issue: 9
Pages: 1412-22
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Publication
27005423 | -
First Author: McCorvie TJ
Year: 2016
Journal: Hum Mol Genet
Title: Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase.
Volume: 25
Issue: 11
Pages: 2234-2244
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Publication
23373416 | -
First Author: Krakowiak A
Year: 2012
Journal: Postepy Biochem
Title: [Histidine triad protein superfamily--biological function and enzymatic activity].
Volume: 58
Issue: 3
Pages: 302-13
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Publication
19112177 | -
First Author: Cen B
Year: 2009
Journal: J Biol Chem
Title: Histidine triad nucleotide-binding protein 1 up-regulates cellular levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src.
Volume: 284
Issue: 8
Pages: 5265-76
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•
•
•
•
Publication
23659632 | -
First Author: Maize KM
Year: 2013
Journal: FEBS J
Title: Structural characterization of human histidine triad nucleotide-binding protein 2, a member of the histidine triad superfamily.
Volume: 280
Issue: 14
Pages: 3389-98
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•
•
•
•
Publication
30622225 | -
First Author: Jung A
Year: 2019
Journal: Mol Cells
Title: Crystal Structure of Histidine Triad Nucleotide-Binding Protein from the Pathogenic Fungus Candida albicans.
Volume: 42
Issue: 1
Pages: 56-66
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•
•
•
•
Protein
Q8CI33
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
•
•
•
•
•
Protein
Q8BG79
Organism: Mus musculus/domesticus
Length: 887  
Fragment?: false
•
•
•
•
•
Protein
Q3TQJ2
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: false
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•
•
•
•
Publication
24919400 | -
First Author: Garrey SM
Year: 2014
Journal: RNA
Title: A homolog of lariat-debranching enzyme modulates turnover of branched RNA.
Volume: 20
Issue: 8
Pages: 1337-48
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•
•
•
•
Protein
Q9D0S9
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
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•
•
•
•
Protein
P70349
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: false
•
•
•
•
•
Protein
Q5M9J2
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
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•
•
•
•
Publication
12119013 | -
First Author: Brenner C
Year: 2002
Journal: Biochemistry
Title: Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases.
Volume: 41
Issue: 29
Pages: 9003-14
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•
•
•
•
Protein
Q03249
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
•
•
•
•
•
Protein
A2AMS3
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
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•
•
•
•
Protein
A2AMS2
Organism: Mus musculus/domesticus
Length: 375  
Fragment?: false
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•
•
•
•
Protein
Q7TQC5
Organism: Mus musculus/domesticus
Length: 342  
Fragment?: false
•
•
•
•
•
Protein
Q6IR21
Organism: Mus musculus/domesticus
Length: 352  
Fragment?: true
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•
•
•
•
Publication
11884590 | -
First Author: Ohi MD
Year: 2002
Journal: Mol Cell Biol
Title: Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs.
Volume: 22
Issue: 7
Pages: 2011-24
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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